Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.Cysteine Dioxygenase: An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Cysteine Synthase: An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Sulfhydryl Compounds: Compounds containing the -SH radical.Cystine: A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Cystatins: A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Papain: A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Glutathione: A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.Sulfhydryl Reagents: Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Kinetics: The rate dynamics in chemical or physical systems.Carbon-Sulfur Lyases: Enzymes that catalyze the cleavage of a carbon-sulfur bond by means other than hydrolysis or oxidation. EC 4.4.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Ethylmaleimide: A sulfhydryl reagent that is widely used in experimental biochemical studies.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Serine O-Acetyltransferase: An enzyme that catalyzes the conversion of L-SERINE to COENZYME A and O-acetyl-L-serine, using ACETYL-COA as a donor.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Sulfur: An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.Dithiothreitol: A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.Mesylates: Organic salts or esters of methanesulfonic acid.Dithionitrobenzoic Acid: A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Iodoacetamide: An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Reducing Agents: Materials that add an electron to an element or compound, that is, decrease the positiveness of its valence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Sulfinic Acids: Any of the monobasic inorganic or organic acids of sulfur with the general formula RSO(OH). (From McGraw Hill Dictionary of Scientific and Technical Terms, 4th ed)Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Iodoacetic Acid: A derivative of ACETIC ACID that contains one IODINE atom attached to its methyl group.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Cystathionine gamma-Lyase: A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.Lyases: A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Alkylation: The covalent bonding of an alkyl group to an organic compound. It can occur by a simple addition reaction or by substitution of another functional group.Thioredoxins: Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.Sulfenic Acids: Oxy acids of sulfur with the general formula RSOH, where R is an alkyl or aryl group such as CH3. They are often encountered as esters and halides. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Amino Acids, SulfurBacterial Proteins: Proteins found in any species of bacterium.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Cell Line: Established cell cultures that have the potential to propagate indefinitely.4-Chloromercuribenzenesulfonate: A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.Acetylcysteine: The N-acetyl derivative of CYSTEINE. It is used as a mucolytic agent to reduce the viscosity of mucous secretions. It has also been shown to have antiviral effects in patients with HIV due to inhibition of viral stimulation by reactive oxygen intermediates.Osteonectin: Non-collagenous, calcium-binding glycoprotein of developing bone. It links collagen to mineral in the bone matrix. In the synonym SPARC glycoprotein, the acronym stands for Secreted Protein, Acidic and Rich in Cysteine.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Lipoylation: Covalent attachment of LIPIDS and FATTY ACIDS to other compounds and PROTEINS.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Glutamate-Cysteine Ligase: One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.Oxidoreductases Acting on Sulfur Group Donors: Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Ethyl Methanesulfonate: An antineoplastic agent with alkylating properties. It also acts as a mutagen by damaging DNA and is used experimentally for that effect.Iodoacetates: Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research.Taurine: A conditionally essential nutrient, important during mammalian development. It is present in milk but is isolated mostly from ox bile and strongly conjugates bile acids.Cystatin B: An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Dipeptides: Peptides composed of two amino acid units.Histidine: An essential amino acid that is required for the production of HISTAMINE.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Sulfides: Chemical groups containing the covalent sulfur bonds -S-. The sulfur atom can be bound to inorganic or organic moieties.Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Zinc: A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.Iron-Sulfur Proteins: A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Peroxiredoxins: A family of ubiquitously-expressed peroxidases that play a role in the reduction of a broad spectrum of PEROXIDES like HYDROGEN PEROXIDE; LIPID PEROXIDES and peroxinitrite. They are found in a wide range of organisms, such as BACTERIA; PLANTS; and MAMMALS. The enzyme requires the presence of a thiol-containing intermediate such as THIOREDOXIN as a reducing cofactor.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.CystathionineProtein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Molecular Weight: The sum of the weight of all the atoms in a molecule.Alanine: A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Cross-Linking Reagents: Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.Cystatin A: A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Calpain: Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.Indicators and Reagents: Substances used for the detection, identification, analysis, etc. of chemical, biological, or pathologic processes or conditions. Indicators are substances that change in physical appearance, e.g., color, at or approaching the endpoint of a chemical titration, e.g., on the passage between acidity and alkalinity. Reagents are substances used for the detection or determination of another substance by chemical or microscopical means, especially analysis. Types of reagents are precipitants, solvents, oxidizers, reducers, fluxes, and colorimetric reagents. (From Grant & Hackh's Chemical Dictionary, 5th ed, p301, p499)Glycine: A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Glutaredoxins: A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.Peptide Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Ficain: A sulfhydryl proteinase with cysteine at the active site from ficus latex. Preferential cleavage is at tyrosine and phenylalanine residues. EC 3.4.22.3.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Palmitic Acid: A common saturated fatty acid found in fats and waxes including olive oil, palm oil, and body lipids.Hydrogen Peroxide: A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.PhenanthrolinesMaleimidesSulfurtransferases: Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.Cystathionine beta-Synthase: A multifunctional pyridoxal phosphate enzyme. In the second stage of cysteine biosynthesis it catalyzes the reaction of homocysteine with serine to form cystathionine with the elimination of water. Deficiency of this enzyme leads to HYPERHOMOCYSTEINEMIA and HOMOCYSTINURIA. EC 4.2.1.22.Sulfates: Inorganic salts of sulfuric acid.DiazomethaneEnzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Pyrrolidonecarboxylic Acid: A cyclized derivative of L-GLUTAMIC ACID. Elevated blood levels may be associated with problems of GLUTAMINE or GLUTATHIONE metabolism.Circular Dichroism: A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Cysteamine: A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Point Mutation: A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.S-Nitrosoglutathione: A sulfur-containing alkyl thionitrite that is one of the NITRIC OXIDE DONORS.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Glutathione Disulfide: A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.Nitrosation: Conversion into nitroso compounds. An example is the reaction of nitrites with amino compounds to form carcinogenic N-nitrosamines.Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization: A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.Oxidative Stress: A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Sulfur Compounds: Inorganic or organic compounds that contain sulfur as an integral part of the molecule.Acylation: The addition of an organic acid radical into a molecule.Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Cadmium: An element with atomic symbol Cd, atomic number 48, and atomic weight 114. It is a metal and ingestion will lead to CADMIUM POISONING.Carbon-Oxygen Lyases: Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Protein Engineering: Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.COS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)

An antiviral mechanism of nitric oxide: inhibition of a viral protease. (1/10540)

Although nitric oxide (NO) kills or inhibits the replication of a variety of intracellular pathogens, the antimicrobial mechanisms of NO are unknown. Here, we identify a viral protease as a target of NO. The life cycle of many viruses depends upon viral proteases that cleave viral polyproteins into individual polypeptides. NO inactivates the Coxsackievirus protease 3C, an enzyme necessary for the replication of Coxsackievirus. NO S-nitrosylates the cysteine residue in the active site of protease 3C, inhibiting protease activity and interrupting the viral life cycle. Substituting a serine residue for the active site cysteine renders protease 3C resistant to NO inhibition. Since cysteine proteases are critical for virulence or replication of many viruses, bacteria, and parasites, S-nitrosylation of pathogen cysteine proteases may be a general mechanism of antimicrobial host defenses.  (+info)

Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member. (2/10540)

Peroxiredoxin (PRx) exhibits thioredoxin-dependent peroxidase activity and constitutes a family of proteins. Four members of genes from rat tissues were isolated by PCR using degenerated primers based on the sequences which encode a pair of highly conserved Cys-containing domains, and were then cloned to full-length cDNAs. These included two genes which have previously been isolated in rats, PRx I and PRx II, and two rat homologues of PRx III and PRx IV. We showed, for the first time, the simultaneous expression of all four genes in various rat tissues by Northern blotting. Since a discrepancy exists regarding cellular distribution, we further characterized PRx IV by expressing it in COS-1 cells. This clearly demonstrates that PRx IV is a secretory form and functions within the extracellular space.  (+info)

Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. (3/10540)

Myeloperoxidase (MPO) is the most abundant protein in neutrophils and plays a central role in microbial killing and inflammatory tissue damage. Because most of the non-steroidal anti-inflammatory drugs and other drugs contain a thiol group, it is necessary to understand how these substrates are oxidized by MPO. We have performed transient kinetic measurements to study the oxidation of 14 aliphatic and aromatic mono- and dithiols by the MPO intermediates, Compound I (k3) and Compound II (k4), using sequential mixing stopped-flow techniques. The one-electron reduction of Compound I by aromatic thiols (e.g. methimidazole, 2-mercaptopurine and 6-mercaptopurine) varied by less than a factor of seven (between 1.39 +/- 0.12 x 10(5) M(-1) s(-1) and 9.16 +/- 1.63 x 10(5) M(-1) s(-1)), whereas reduction by aliphatic thiols was demonstrated to depend on their overall net charge and hydrophobic character and not on the percentage of thiol deprotonation or redox potential. Cysteamine, cysteine methyl ester, cysteine ethyl ester and alpha-lipoic acid showed k3 values comparable to aromatic thiols, whereas a free carboxy group (e.g. cysteine, N-acetylcysteine, glutathione) diminished k3 dramatically. The one-electron reduction of Compound II was far more constrained by the nature of the substrate. Reduction by methimidazole, 2-mercaptopurine and 6-mercaptopurine showed second-order rate constants (k4) of 1.33 +/- 0.08 x 10(5) M(-1) s(-1), 5.25 +/- 0.07 x 10(5) M(-1) s(-1) and 3.03 +/- 0.07 x 10(3) M(-1) s(-1). Even at high concentrations cysteine, penicillamine and glutathione could not reduce Compound II, whereas cysteamine (4.27 +/- 0.05 x 10(3) M(-1) s(-1)), cysteine methyl ester (8.14 +/- 0.08 x 10(3) M(-1) s(-1)), cysteine ethyl ester (3.76 +/- 0.17 x 10(3) M(-1) s(-1)) and alpha-lipoic acid (4.78 +/- 0.07 x 10(4) M(-1) s(-1)) were demonstrated to reduce Compound II and thus could be expected to be oxidized by MPO without co-substrates.  (+info)

Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide. (4/10540)

Previous studies showed that CO/H2O oxidation provides electrons to drive the reduction of oxidized hemoglobin (metHb). We report here that Cu(II) addition accelerates the rate of metHb beta chain reduction by CO by a factor of about 1000. A mechanism whereby electron transfer occurs via an internal pathway coupling CO/H2O oxidation to Fe(III) and Cu(II) reduction is suggested by the observation that the copper-induced rate enhancement is inhibited by blocking Cys-beta93 with N-ethylmaleimide. Furthermore, this internal electron-transfer pathway is more readily established at low Cu(II) concentrations in Hb Deer Lodge (beta2His --> Arg) and other species lacking His-beta2 than in Hb A0. This difference is consistent with preferential binding of Cu(II) in Hb A0 to a high affinity site involving His-beta2, which is ineffective in promoting electron exchange between Cu(II) and the beta heme iron. Effective electron transfer is thus affected by Hb type but is not governed by the R left arrow over right arrow T conformational equilibrium. The beta hemes in Cu(II)-metHb are reduced under CO at rates close to those observed for cytochrome c oxidase, where heme and copper are present together in the oxygen-binding site and where internal electron transfer also occurs.  (+info)

Plasma total homocysteine and cysteine in relation to glomerular filtration rate in diabetes mellitus. (5/10540)

BACKGROUND: The plasma concentrations of total homocysteine (tHcy) and total cysteine (tCys) are determined by intracellular metabolism and by renal plasma clearance, and we hypothesized that glomerular filtration is a major determinant of plasma tHcy and tCys. We studied the relationships between the glomerular filtration rate (GFR) and plasma tHcy and tCys in populations of diabetic patients with particularly wide ranges of GFR. METHODS: We measured GFR, urine albumin excretion rate (UAER), plasma tHcy, tCys, methionine, vitamin B12, folate, C-peptide, and routine parameters in 50 insulin-dependent diabetes mellitus (IDDM) and 30 non-insulin-dependent diabetes mellitus (NIDDM) patients. All patients underwent intensive insulin treatment and had a serum creatinine concentration below 115 micromol/liter. RESULTS: Mean plasma tHcy in diabetic patients (0.1 micromol/liter) was lower than in normal persons (11.1 micromol/liter, P = 0.0014). Mean plasma tCys in diabetic patients (266.1 micromol/liter) was also lower than in normal persons (281.9 micromol/liter, P = 0.0005). Seventy-three percent of the diabetic patients had relative hyperfiltration. Plasma tHcy and tCys were closely and independently associated with GFR, serum folate, and serum B12. However, plasma tHcy was not independently associated with any of the 22 other variables tested, including age, serum creatinine concentration, UAER, total daily insulin dose, and glycemic control. CONCLUSIONS: Glomerular filtration rate is an independent determinant of plasma tHcy and tCys concentrations, and GFR is rate limiting for renal clearance of both homocysteine and cysteine in diabetic patients without overt nephropathy. Declining GFR explains the age-related increase in plasma tHcy, and hyperfiltration explains the lower than normal mean plasma tHcy and tCys concentrations in populations of diabetic patients.  (+info)

Variants of ribonuclease inhibitor that resist oxidation. (6/10540)

Human ribonuclease inhibitor (hRI) is a cytosolic protein that protects cells from the adventitious invasion of pancreatic-type ribonucleases. hRI has 32 cysteine residues. The oxidation of these cysteine residues to form disulfide bonds is a rapid, cooperative process that inactivates hRI. The most proximal cysteine residues in native hRI are two pairs that are adjacent in sequence: Cys94 and Cys95, and Cys328 and Cys329. A cystine formed from such adjacent cysteine residues would likely contain a perturbing cis peptide bond within its eight-membered ring, which would disrupt the structure of hRI and could facilitate further oxidation. We find that replacing Cys328 and Cys329 with alanine residues has little effect on the affinity of hRI for bovine pancreatic ribonuclease A (RNase A), but increases its resistance to oxidation by 10- to 15-fold. Similar effects are observed for the single variants, C328A hRI and C329A hRI, suggesting that oxidation resistance arises from the inability to form a Cys328-Cys329 disulfide bond. Replacing Cys94 and Cys95 with alanine residues increases oxidation resistance to a lesser extent, and decreases the affinity of hRI for RNase A. The C328A, C329A, and C328A/C329A variants are likely to be more useful than wild-type hRI for inhibiting pancreatic-type ribonucleases in vitro and in vivo. We conclude that replacing adjacent cysteine residues can confer oxidation resistance in a protein.  (+info)

Metal-catalyzed oxidation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: inactivation and destabilization by oxidation of active-site cysteines. (7/10540)

The in vitro instability of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase [DAHPS(Phe)] from Escherichia coli has been found to be due to a metal-catalyzed oxidation mechanism. DAHPS(Phe) is one of three differentially feedback-regulated isoforms of the enzyme which catalyzes the first step of aromatic biosynthesis, the formation of DAHP from phosphoenolpyruvate and D-erythrose-4-phosphate. The activity of the apoenzyme decayed exponentially, with a half-life of about 1 day at room temperature, and the heterotetramer slowly dissociated to the monomeric state. The enzyme was stabilized by the presence of phosphoenolpyruvate or EDTA, indicating that in the absence of substrate, a trace metal(s) was the inactivating agent. Cu2+ and Fe2+, but none of the other divalent metals that activate the enzyme, greatly accelerated the rate of inactivation and subunit dissociation. Both anaerobiosis and the addition of catalase significantly reduced Cu2+-catalyzed inactivation. In the spontaneously inactivated enzyme, there was a net loss of two of the seven thiols per subunit; this value increased with increasing concentrations of added Cu2+. Dithiothreitol completely restored the enzymatic activity and the two lost thiols in the spontaneously inactivated enzyme but was only partially effective in reactivation of the Cu2+-inactivated enzyme. Mutant enzymes with conservative replacements at either of the two active-site cysteines, Cys61 or Cys328, were insensitive to the metal attack. Peptide mapping of the Cu2+-inactivated enzyme revealed a disulfide linkage between these two cysteine residues. All results indicate that DAHPS(Phe) is a metal-catalyzed oxidation system wherein bound substrate protects active-site residues from oxidative attack catalyzed by bound redox metal cofactor. A mechanism of inactivation of DAHPS is proposed that features a metal redox cycle that requires the sequential oxidation of its two active-site cysteines.  (+info)

Functional importance and local environments of the cysteines in the tetracycline resistance protein encoded by plasmid pBR322. (8/10540)

The properties of the cysteines in the pBR322-encoded tetracycline resistance protein have been examined. Cysteines are important but not essential for tetracycline transport activity. None of the cysteines reacted with biotin maleimide, suggesting that they are shielded from the aqueous phase or reside in a negatively charged local environment.  (+info)

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Cysteine Oxidation Prediction Program Goal: Create a program that will use physicochemical parameters to predict reactive surface cysteine thiols Methods: -Gather examples of proteins susceptible to cysteine oxidation -Extract parameters from Protein Data Bank -Use computer classifier C4.5 to determine rules that will predict if cysteine can become oxidized
Chemical modification using thiol-directed agents and site-directed mutagenesis have been used to investigate the crucial role of an active site cysteine residue within the substrate-binding domain of human type I Ins(1,4,5)P3 5-phosphatase. Irreversible inhibition of enzymic activity is provoked by chemical modification of the enzyme by N-ethylmaleimide (NEM), 5,5´-dithio-2-nitrobenzoic acid, iodoacetate and to a much smaller extent by iodoacetamide. The alkylation reaction by NEM is prevented in the presence of Ins(1,4,5)P3. The results indicate that NEM binds at the active site of the enzyme with a stoichiometry of 0.9 mol of NEM per mol of enzyme. A single [14C]NEM-modified peptide was isolated after α-chymotrypsin proteolysis of the radiolabelled enzyme and reverse-phase HPLC. Sequence analysis of the active site-labelled peptide (i.e. MNTRCPAWCD) demonstrated that Cys348 contained the radiolabel. Furthermore two mutant enzymes were obtained by site-directed mutagenesis of the cysteine ...
As noted, cysteine is characterized by the presence of a thiol (sulphydry) group (-SH). Since thiol groups can undergo reduction (redox) reactions, cysteine can undergo redox reactions. Oxidation of cysteine can produce a disulfide bond with another thiol. A disulfide bond, also called a SS-bond or disulfide bridge, is a single covalent bond derived from the coupling of thiol groups. The overall connectivity is C-S-S-C.. That is, when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond (cys-S-S-cys) between the -SH group. This reaction is reversible, as reduction of this disulphide bond regenerates two cysteine molecules. (Further oxidation can produce sulphfinic or sulfonic acids.). The disulphide bonds of cystine are crucial to defining the structures of many proteins. Disulfide bonds play an important role in the folding and stability of some proteins, by stabilizing the folded form. Extracellularly, by crosslinking proteins, cysteines increase ...
This group of sequences represent the core of p45 (45 kDa) precursor of caspases, which can be processed to produce the active p20 (20 kDa) and p10 (10 kDa) subunits. Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases that belong to the MEROPS peptidase family C14 (caspase family, clan CD) based on the architecture of their catalytic dyad or triad [(PUBMED:11517925)]. Caspases are tightly regulated proteins that require zymogen activation to become active, and once active can be regulated by caspase inhibitors. Activated caspases act as cysteine proteases, using the sulphydryl group of a cysteine side chain for catalysing peptide bond cleavage at aspartyl residues in their substrates. The catalytic cysteine and histidine residues are on the p20 subunit after cleavage of the p45 precursor.. Caspases are mainly involved in mediating cell death (apoptosis) [(PUBMED:10578171), (PUBMED:10872455), (PUBMED:15077141)]. They have two main roles within the apoptosis cascade: ...
Exocytosis, the fusion of a vesicle to a cellular membrane, involves a protein named SNAP-25. This protein, containing two alpha helices connected with a linker region, is localized to the cell membrane via palmitic acids attached to the cysteine residues of its linker region in a process called palmitoylation. Are cysteine residues of the SNAP-25 linker region palmitoylated in an ordered manner and to a particular extent? The answer to this question may give insight into the regulated nature of exocytosis. While it is generally accepted that SNAP-25 must be palmitoylated in order to perform its exocytotic functions, the details surrounding this process are still being discovered, defined, and understood. In these studies we replicate the oxidation, reduction, and palmitoylation of SNAP-25 in vitro. Palmitoylating SNAP-25 in vitro, a process which occurs regularly in vivo, allows us to determine the extent of palmitoylation. In vitro palmitoylation of SNAP-25 was studied both with and without a native
Human fibroblast growth factor-1 (FGF-1) has broad therapeutic potential in regenerative medicine but has undesirable biophysical properties of low thermostability and three buried Cys residues (at positions 16, 83 and117) that interact to promote irreversible protein unfolding under oxidizing conditions. Mutational substitution of such Cys residues eliminates reactive buried thiols but cannot be accomplished simultaneously at all three positions without also introducing further substantial instability. The mutational introduction of a novel Cys residue (Ala66Cys) that forms a stabilizing disulfide bond (i.e., cystine) with one of the extant Cys residues (Cys83) effectively eliminates one Cys while increasing overall stability. This increase in stability offsets the associated instability of remaining Cys substitution mutations and permits production of a Cys-free form of FGF-1 (Cys16Ser/Ala66Cys/Cys117Ala) with only minor overall instability. The addition of a further stabilizing mutation ...
Background: Nitroxyl (HNO) donors increase cardiac inotropy via combined enhancement of SR Ca2+ cycling and myofilament sensitization to Ca2+. HNO reacts with thiols, but the critical -SH targets on the myofilaments are currently unknown.. Aims: Using rat cardiac trabeculae and a new mass spectrometry capture technique based on a modified biotin switch assay, we have identified the sites and the nature of the myofilament modification induced by the novel 1-nitrosocyclohexylacetate (NCA) (a pure HNO releaser) and for comparison the prototypic Angelis (AS).. Results: In steady state activations, NCA (25 μM) increased maximal Ca2+ activated force (Fmax) and decreased [Ca2+]i required for 50% of activation (Ca50): Fmax was 123±18 vs. 95±5 mN/mm2 (p,0.05) and Ca50 0.42±0.01 vs. 0.57±0.03 μmol/L (p,0.004) without affecting cooperativity (Hill, 4.92±0.84 vs. 3.94±0.18, p=NS), confirming and expanding upon previous data obtained with AS. NCA action persisted after skinning, proving that NCA/HNO ...
The prodomain of TACE [TNFα (tumour necrosis factor α)-converting enzyme] is essential for the secretion of the functional enzyme. Previously, we showed that a TACE truncate was not secreted in the absence of the prodomain and that it was subjected to intracellular degradation. In the present study, we show that full-length TACE was also degraded when expressed without the prodomain. We demonstrate that the prodomain can rescue TACEs secretion in trans, suggesting an intramolecular chaperone function. We addressed the question whether a cysteine switch consensus motif is needed for the secretion of active TACE. The cysteine switch mutants [C184A (Cys184→Ala)] of TACE resembled the wild-type functionally and in their sensitivity to inhibitors. Interestingly, TACE zymogen forms expressed in the context of the C184A mutation were susceptible to intracellular degradation, suggesting that the prodomain-bound TACE zymogen may be more accessible to intracellular proteinases when compared with ...
Cross-linking of trans reentrant loops in the Na(+)-citrate transporter CitS of Klebsiella pneumoniae.: The membrane topology model of the Na(+)-citrate transpo
In an eukaryotic cell, DNA molecule exists in the form of chromatin. The repetitive unit of chromatin is a nucleosome, 147 bp of DNA wrapped around histone octamer. Nucleosome position along DNA is important for transcription regulation. Chromatin remodeler ISWI (Drosophila melanogaster) slides nucleosomes along DNA. The aim of this work is to map surface-exposed cysteines in the protein ISWI. The surface-exposed cysteines are easily avaliable for chemical reaction. To probe accessibility of cysteines for chemical reaction, commonly used reagents for spectrophotometric detection of thiols were used: 5,5ʹ-dithiobis- (2-nitrobenzoic acid) and 2-nitro-5-thiocyanatobenzoic acid. To unequivocally identify surfaceexposed cysteines, ISWI was treated with primary alkylating reagent (N-ethylmaleimide), denaturated and treated with secondary alkylating reagent (iodoacetic acid). The two reactions add to the cysteine different modification groups which can be discriminated by mass spectrometry. Half of ...
Solution 17O-NMR application to biological macromolecules is extremely limited. We describe here 17O-NMR observation of the 17O2-oxidized cysteine side chain of human Cu,Zn-superoxide dismutase in solution using selective 17O2 oxidation. 17O-NMR with the aid of 17O-labeling has wide potential to probe the en
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Neurons depend upon neurotransmitter release through regulated exocytosis to accomplish the immense processing performed within the central nervous system. The SNARE hypothesis points to a family of proteins that are thought to enable the membrane fusion that leads to exocytosis. The secondary structure of SNAP-25 is unique among SNARE proteins in that it has two alpha helical SNARE motifs and a cysteine rich (C85, C88, C90, C92) membrane interacting region but notransmembrane domain. The cysteines may be modified by palmitoylation or oxidation but the role of these modifications in vivo is not well understood. Our goal is to elucidate possible regulatory roles of SNAP-25 that relate to its unique structure and these reversible modifications. However, the study of SNAP-25 in reconstituted systems is hampered by a lack of readily available palmitoylated SNAP-25. A method for in vitro palmitoylation of SNAP-25 by HIP14, a neuronal acyltransferase, is described along with the application of a ...
Autor: Riemenschneider, A. et al.; Genre: Zeitschriftenartikel; Im Druck veröffentlicht: 2005; Keywords: arabidopsis thaliana|br/|cysteine|br/|desulfhydrase|br/|h2s|br/|o-acetyl-l-serine|br/|acetylserine thiol lyase|br/|arabidopsis-thaliana|br/|brassica-oleracea|br/|atmospheric h2s|br/|sulfur source|br/|protein|br/|plants|br/|mitochondrial|br/|sulfide|br/|biosynthesis; Titel: Impact of elevated H2S on metabolite levels, activity of enzymes and expression of genes involved in cysteine metabolism
Neurons depend upon neurotransmitter release through regulated exocytosis to accomplish the immense processing performed within the central nervous system. The SNARE hypothesis points to a family of proteins that are thought to enable the membrane fusion that leads to exocytosis. The secondary structure of SNAP-25 is unique among SNARE proteins in that it has two alpha helical SNARE motifs and a cysteine rich (C85, C88, C90, C92) membrane interacting region but notransmembrane domain. The cysteines may be modified by palmitoylation or oxidation but the role of these modifications in vivo is not well understood. Our goal is to elucidate possible regulatory roles of SNAP-25 that relate to its unique structure and these reversible modifications. However, the study of SNAP-25 in reconstituted systems is hampered by a lack of readily available palmitoylated SNAP-25. A method for in vitro palmitoylation of SNAP-25 by HIP14, a neuronal acyltransferase, is described along with the application of a biotinylation
The tertiary structure is the complete three-dimensional structure of a polypeptide chain. Many polypeptides fold into compact, globular structures in which amino acid residues that are distant from each other in primary structure come into close proximity in the folded structure. Because of efficient packing, most water molecules are excluded from the proteins interior. It is the different interactions between the side chains of the amino acids that stabilize the tertiary structure. A major force stabilizing the tertiary structure is the hydrophobic interaction among nonpolar side chains in the core of the protein. Additional stabilizing forces include electrostatic interactions between ionic groups of opposite charge, hydrogen bonds between polar groups, and disulfide bonds . Disulfide (S-S) bonds are formed between the thiol (S-H) groups of two cysteine side chains resulting in a covalent bond between the two side chains. Many physical and chemical agents, including heat, detergents, salts, ...
We have successfully manufactured DES for use as cell culture feeds. L-cysteine hydrochloride monohydrate (L-Cys HCl H2O) and L-tyrosine hydrochloride (L-Tyr HCl) were used to form two DES with Choline Chloride. A range of temperatures and substance ratios to form a stable DES were tested.. Subsequently, the DES feeds were compared in a cell culture fed-batch process using a typical Cyr/Tyr CHO feed for comparison. Our preliminary results suggest that DES could be used as alternative cell culture feeds in the future. Possible advantages of such a strategy would be lower feed volumes required due to ultra-high feed concentration, no extra water (expect hydrate) diluting the content and thus less volume increase in bioreactors and improved bioreactor utilization.. However, there are many open points to study. It would be preferable to use one DES feed including both Cys/Tyr, but such a system showed to be far more complex to manufacture. Stability and bioavailability need to be studied in detail. ...
N-Acetyl Cysteine May Support Dopamine Neurons in Parkinson\s Disease: Preliminary Clinical and Preliminary Clinical and Cell Line Data
Almost all protease families have been associated with plant development, particularly senescence, which is the final developmental stage of every organ before cell death. Proteolysis remobilizes and recycles nitrogen from senescent organs that is required, for example, seed development. Senescence-associated expression of proteases has recently been characterized using large-scale gene expression analysis seeking to identify and characterize senescence-related genes. Increasing activities of proteolytic enzymes, particularly cysteine proteases, are observed during the senescence of legume nodules, in which a symbiotic relationship between the host plant and bacteria (Rhizobia) facilitate the fixation of atmospheric nitrogen. It is generally considered that cysteine proteases are compartmentalized to prevent uncontrolled proteolysis in nitrogen-fixing nodules. In addition, the activities of cysteine proteases are regulated by endogenous cysteine protease inhibitors called cystatins. These small proteins
Cysteine Other name(s): a-amino-b-thiolpropionic acid Unsubstantiated claims Please note that this section reports on claims that have not yet been substantiated through studies. Cysteine may help treat arthritis ( L -cysteine) and hardening of the arteries. It may also help treat certain lung diseases. These include bronchitis, emphysema, and tuberculosis. It may help protect the lungs from cigarette smoke. Cysteine is said to help protect the liver from alcohol and prevent hangovers. It may also reduc...
SiliaBond® Cysteine (Si-Cys) is the silica bound equivalent of the amino acid Cysteine. By attaching the molecule to the backbone via the amino group, the thiol group remains free and accessible for higher metal scavenging efficiency.
The elucidation of signalling pathways relies heavily upon the identification of protein kinase substrates. Recent investigations have demonstrated the efficacy of chemical genetics using ATP analogues and modified protein kinases for specific substrate labelling. Here we combine N(6) -(cyclohexyl)ATPγS with an analogue-sensitive cdk2 variant to thiophosphorylate its substrates and demonstrate a pH-dependent, chemoselective, one-step alkylation to facilitate the detection or isolation of thiophosphorylated peptides.
From NCBI Gene: This gene is one of several cytokine genes clustered on the q-arm of chromosome 17. Chemokines are a superfamily of secreted proteins involved in immunoregulatory and inflammatory processes. The superfamily is divided into four subfamilies based on the arrangement of N-terminal cysteine residues of the mature peptide. This chemokine is a member of the CC subfamily which is characterized by two adjacent cysteine residues. This cytokine displays chemotactic activity for monocytes and basophils but not for neutrophils or eosinophils. It has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis and atherosclerosis. It binds to chemokine receptors CCR2 and CCR4. [provided by RefSeq, Jul 2013]
The ABC protein ABCE1, formerly named RNase L inhibitor RLI1, is one of the most conserved proteins in evolution and is expressed in all organisms except eubacteria. Because of its fundamental role in translation initiation and/or ribosome biosynthesis, ABCE1 is essential for life. Its molecular mechanism has, however, not been elucidated. In addition to two ABC ATPase domains, ABCE1 contains a unique N-terminal region with eight conserved cysteines, predicted to coordinate iron-sulfur clusters. Here we present detailed information on the type and on the structural organization of the Fe-S clusters in ABCE1. Based on biophysical, biochemical, and yeast genetic analyses, ABCE1 harbors two essential diamagnetic [4Fe-4S](2+) clusters with different electronic environments, one ferredoxin-like (CPX(n)CX(2)CX(2)C; Cys at positions 4-7) and one unique ABCE1-type cluster (CXPX(2)CX(3)CX(n)CP; Cys at positions 1, 2, 3, and 8). Strikingly, only seven of the eight conserved cysteines coordinating the Fe-S
Citation: Natilla, A., Hammond, R. 2013. Analysis of the solvent accessibility of cysteine residues on maize rayado fino virus virus-like particles produced in Nicotiana benthamiana plants and cross-linking of peptides to VLPs. Journal of Visualized Experiments. 72:e50084. Interpretive Summary: Agricultural losses due to plant and animal diseases necessitate the development of reagents for detection and control of the pathogens that cause the disease. Plant viruses and virus-like particles are able to assemble themselves in unique ways. Mimicking and exploiting virus biological, chemical, and physical properties holds promise to provide solutions to some of the worlds most pressing challenges in agriculture and medicine; however, in order to utilize viruses for the new applications, they must be modified from their natural form to impart the new functions. In this report, we describe the steps to determine which properties of the virus can be modified and the methods used to chemically modify ...
The IUPHAR/BPS Guide to Pharmacology. Alanine/serine/cysteine transporter 2 - Alanine/serine/cysteine transporter subfamily. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of drug targets.
Dr. Loesers primary research goal is to discover the basic mechanisms relevant to joint tissue destruction in osteoarthritis. Osteoarthritis (OA) is the leading cause of pain and disability in older adults. A better mechanistic understanding of OA is needed in order to develop interventions that can slow or stop disease progression before advanced joint tissue destruction occurs.. Dr. Loesers lab uses a combination of in vitro experiments using human joint tissue cells and in vivo experiments in rodent models to study cell signaling pathways that regulate anabolic and catabolic activity responsible for joint tissue remodeling and destruction. The lab is particularly interested in determining how reactive oxygen species regulate chondrocyte signaling downstream of integrins, cytokines, and growth factors through the oxidation of specific cysteine residues in kinases and phosphatases as well as other intracellular proteins. The lab is studying how oxidative stress that occurs with aging and ...
The oligomeric state and activation mechanism that enable p75 NTR to mediate these effects have recently been called into question. In this new study, we have investigated mutant mice lacking the p75NTR death domain (DD) or a highly conserved transmembrane (TM) cysteine residue (Cys 259) implicated in receptor dimerization and activation. Neuronal death induced by proneurotrophins or epileptic seizures was assessed and compared with responses in p75NTR knock-out mice and wild-type animals. Proneurotrophins induced apoptosis of cultured hippocampal and cortical neurons from wild-type mice, but mutant neurons lacking p75NTR, only the p75NTR DD, or just Cys259 were all equally resistant to proneurotrophin-induced neuronal death. Homo-FRET anisotropy experiments demonstrated that both NGF and proNGF induce conformational changes in p75 NTR that are dependent on the TM cysteine. In vivo, neuronal death induced by pilocarpine-mediated seizures was significantly reduced in the hippocampus and ...
Critical residues for signalling by the Aer PAS domain have been identified (Bibikov et al., 2000; Repik et al., 2000; Burón-Barral et al., 2006; Watts et al., 2006a). Null Aer mutants have a signal-off conformation that produces a counterclockwise (CCW) rotational bias of the flagellar motors. The signal from Aer PAS enhances the signal-on conformation of the signalling domain (Fig. 1), imposing a clockwise (CW) bias on the motors. Thirteen cysteine PAS mutants had defective input-output control and were not rescued by simultaneous production of the Tar, Trg and Tap chemoreceptors (Repik et al., 2000; Watts et al., 2006a). Cysteine replacements at Arg57, His58 and Asp60 abolished FAD binding to Aer. These residues surround the pocket in which FAD is predicted to bind (Fig. 3). Residues Arg57, His58 and Asp60 are unique to the Aer _ PAS (FAD-binding) subfamily and are conserved in members of the subfamily, but not in other PAS domains (L. Ulrich, W. Black and I. Zhulin, pers. comm.). This ...
This locus encodes a member of the nicotinic acetylcholine receptor family of proteins. Members of this family of proteins form pentameric complexes comprised of both alpha and beta subunits. This locus encodes an alpha-type subunit, as it contains characteristic adjacent cysteine residues. The encoded protein is a ligand-gated ion channel that likely plays a role in neurotransmission. Polymorphisms in this gene have been associated with an increased risk of smoking initiation and an increased susceptibility to lung cancer. Alternatively spliced transcript variants have been described. [provided by RefSeq, Nov 2009 ...
MIP-3 alpha is a CC chemokine that is expressed in the liver, lymph nodes, appendix, PBL and lung and signals through the CCR6 receptor. MIP-3 alpha is chemotactic towards lymphocytes and dendritic cells. Additionally, it promotes the adhesion of memory CD4+ T cells and inhibits colony formation of bone marrow myeloid immature progenitors. Recombinant murine MIP-3 alpha is a 7.9 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines ...
MIP-3 alpha is a CC chemokine that is expressed in the liver, lymph nodes, appendix, PBL and lung and can signal through the CCR6 receptor. MIP-3 alpha is chemotactic towards lymphocytes and dendritic cells. Additionally, it promotes the adhesion of memory CD4+ T cells and inhibits colony formation of bone marrow myeloid immature progenitors. Recombinant human MIP-3 alpha is an 8.0 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines ...
A number of N-acetyl-S-glycosyl cysteine derivatives have been prepared through the development of a general and simply applicable synthetic pathway, by modifying existing literature methods. The coupling of N-acetyl-L-cysteine and a carbohydrate is desirable as it may improve the efficacy of the labile N-acetyl-L-cysteine as a drug. The S-glycosyl cysteines prepared are as follows: N-acetyl-S-D-glucopyranosyl-L-cysteine, alpha and beta-anomers, N-acetyl-S-beta-D-ribopyranosyl-L-cysteine, N-acetyl-S-alpha-D-mannopyranosyl-L-cysteine and N-acetyl-O-methyl-S-(2,3,4,6-tetra-O-benzoyl-beta-D-galactopyranosyl)-L-cysteine. The coupling reaction was designed to yield both a and beta-anomers in the same step, and this was observed in the synthesis of the glucose derivatives. However, the other carbohydrates chosen appear to couple more selectively. The preparation of N-acetyl-O-methyl-S-alpha-D-glucopyranosyl-L-cysteine was also carried out by a different method, but this proved to be more involved and ...
The sessions here will examine the mechanisms and consequences of protein modification, including misfolding, bacterial takeover and cysteine modifications.
Previous Q1-E1 cysteine cross-linking studies have focused on extracellular protein-protein interactions in intact cells, where the environment is oxidizing and the membrane potential of the cell provides control of complex conformation. In the present work, we focused on the juxtamembranous part of the E1 C terminus because this domain adopts a helical structure, where both laboratory-made and long QT mutations cluster to one face of the helix predicted to face the cytoplasmic side of the Q1 channel (Rocheleau et al., 2006). To identify these Q1-E1 protein interactions, we oxidized hypotonically lysed cells, which provided cytoplasmic access to the complex in a membranous environment. Although these conditions enabled us to screen hundreds of pairs of Q1-E1 residues, our approach comes with a caveat: hypotonic lysis destroys the electrochemical gradient and TM potential. Thus, at 0 mV the activation gate machinery of the channel is predicted to be undergoing large movements while equilibrating ...
Proteins are long chain of amino acids that are tightly folded in on themselves. The order and chemical properties of the acids determine the locations of the folds, which in turn determine the function of the protein. Cysteine is "hydrophobic"; it interacts poorly with water and so it is usually on the inside of a protein. And because stress changes the shape of these folded proteins, Discher reasoned that measuring the degree to which cysteine is exposed would in effect measure how stressed the protein and cells containing it are. Dischers team simulated the shear forces originating from the beating heart, which forcefully pumps blood and ultimately pulls apart the folds that keep cysteine on the inside of proteins at the red blood cell membrane, allowing it to bind with a fluorescent marker dye. The team could visually confirm that more stressed cells were more fluorescent under the microscope but actually tested the levels of marked cysteine using mass spectrometry. "Just like a polymer ...
Solgar L Cysteine 500 mg Kosher Cysteine Kosher Amino Acids. We carry cheap and discount vitamins, supplements pills, capsules, tablets, softgels, natural, organic and herbal products.
[80 Pages Report] Check for Discount on Global L- Cysteine Market Data Survey Report 2025 report by HeyReport. Summary Cysteine (abbreviated as Cys or C) is an a-...
Allen339, member , July 11th, 2019 CASP14 caspase 14, apoptosis-related cysteine peptidase BackgroundCaspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis.1 The precursor form of all.... view details ...
18841-42-4 - MAFDYIDMXCXBRB-WUCPZUCCSA-N - beta-Mercaptolactate cysteine disulfide - Similar structures search, synonyms, formulas, resource links, and other chemical information.
Synthetic peptide corresponding to amino acids 2-15 of human LC3B, conjugated to KLH via a C-terminal cysteine residue. The corresponding sequence differs by one amino acid in rat and mouse. (ZFIN Staff ...
A simple fluorescent probe based on an ortho-hydroxyaldehyde-functionalized coumarin showed selective responses to homocysteine and cysteine by fluorescence turn-on.
I have a solution for puzzle 627 with lots of cysteines that when loaded and wiggled crashes using devprev. The end of the log.txt file is below and the full log.txt file should be attached. If you would like the solution file, which file listed in the logfile is the correct one and how do I get it to a developer? I dont know if this is related to the crash in Feedback https://fold.it/portal/node/991395.. core.conformation.Conformation: current variant for 79 ...
Cysteine | C3H7NO2S | CID 5862 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists, and more.
Biohit Oyj, the Finnish company behind a cysteine chewing gum unveiled this week that could help reduce the risk of oral cancer in smokers and drinkers, is looking for partners to help realise the full potential of its technology in the supplements and food sectors.
The main benefits of cysteine include the prevention of cancer growths in some of the bodys tissues, the treatment of poisoning...
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Structures of the C-terminal CLTD subdomains of the Intimin and Invasin passenger domains.The cysteine residues are depicted by spheres with the C-terminal cyst
Greetings Netters, I was asking what is NTCB?.... I get in three hours 5 answers and all pointing to 2-nitro-5-thiocyanobenzoic acid.... to make chemical cleavage at cysteine. I know it has to do with protein/peptid sequence analysis.... but my memory dont served me..... Thank you very much for the prompt responses. Indeed the internet is really great.... Best of luck peter ...
Complete information for RUBCN gene (Protein Coding), RUN And Cysteine Rich Domain Containing Beclin 1 Interacting Protein, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Residues 59-98 rank in the 91.29th percentile to Block BL01035A, described as PTS EIIB domain proteins cysteine phosphorylation site proteins proteins. Block A has a rank of 1, however there is no significant alignment or similarity to block B ...
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View mouse Serpina6 Chr12:103646630-103657212 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Opens the Highlight Feature Bar and highlights feature annotations from the FEATURES table of the record. The Highlight Feature Bar can be used to navigate to and highlight other features and provides links to display the highlighted region separately. Links in the FEATURES table will also highlight the corresponding region of the sequence. More... ...
L-cysteine Hydrochloride Review, Benefits, Side Effects and Uses. Anhydrous and Monohydrate formulas for solubility plus dosages and how to take.
About the cover: A, BSO effects on oltipraz- or 2-(allylthio)pyrazine-inducible mEH and rGSTA2 mRNAs. B, the inhibition of oltipraz- or 2-(allylthio)pyrazine-inducible mEH and rGSTA2 mRNA expression by cysteine. See the article by Kim et al. in this issue on page 667. ...
pep:known chromosome:VEGA66:12:104112780:104121808:1 gene:OTTMUSG00000035420 transcript:OTTMUST00000090572 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Serpina3a description:novel serine (or cysteine) peptidase inhibitor, clade A, member ...
Jostra Bently part numbers 311033-000 C130S C330S C440S C120S 341233-000 341244-000 C-480S 331033-000 321444-000 C330S 301009-000 341333-000 341333-000 SFC10 342333-000
1S/C19H15NO8S/c21-16(22)2-1-7-20-19(25)10-3-5-12-14(8-10)18(24)15-9-11(29(26,27)28)4-6-13(15)17(12)23/h3-6,8-9H,1-2,7H2,(H,20,25)(H,21,22)(H,26,27,28 ...
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Previously, bovine rhodopsin has been shown to be palmitoylated at cysteine residues 322 and 323. Here we report on palmitoylation of bovine opsin in COS-1 cells following expression of the synthetic wild-type opsin gene and several of its cysteine mutants in the presence of [3H]palmitic acid. Two moles of palmitic acid are introduced per wild-type opsin molecule in thioester linkages. Palmitoylation is abolished when both Cys-322 and Cys-323 are replaced by serine residues. Replacement of Cys-322 by serine prevents palmitoylation at Cys-323, whereas replacement of the latter with serine allows palmitoylation at Cys-322. Opsin mutants that evidently do not contain a Cys-110/Cys-187 disulfide bond and presumably remain in the endoplasmic reticulum are not palmitoylated. Replacement of Cys-140 or Cys-185 reduces the extent of palmitoylation of the opsin. Lack of palmitoylation at Cys-322 and/or Cys-323 does not affect 11-cis-retinal binding, absorption maximum or extinction coefficient of the ...
TY - JOUR. T1 - Autoxidation of cysteine generates hydrogen peroxide. T2 - Cytotoxicity and attenuation by pyruvate. AU - Nath, Karl A. AU - Salahudeen, Abdulla K.. PY - 1993. Y1 - 1993. N2 - The reactivity of cys-teine presents a paradox: although regarded as an antioxidant, cysteine interacts with oxygen in a metal-catalyzed reaction to produce reactive species. Because ischemia provokes the appearance of millimolar amounts of cysteine and increased amounts of transition metals, we studied whether cysteine, in the presence of transition metals, consumes oxygen, generates hydrogen peroxide, and is toxic. Using fluorescence cytometry, we provide direct evidence that hydrogen peroxide is copiously generated during cysteine autoxidation. Pyruvate attenuates such generation of hydrogen peroxide and cytotoxicity. Cysteine oxidation is stimulated by an EDTA-chelatable diethyldithiocarbamate-chelatable constituent of kidney extract; this suggests that copper is the catalytically active metal. The ...
We have devised a generally applicable strategy for analysis of protein structure and have applied it to examine the structure of the transmembrane portion of the Tar receptor of Escherichia coli. The basis of our approach is the use of disulfide cross-linking to identify residues that are within close proximity. To generate and test large numbers of cysteine pairs, we used an unusual method of mutagenesis by which cysteine substitutions can be created randomly at a number of targeted codons. Cysteine-substituted proteins encoded by mutagenized genes may be screened directly for disulfide formation within oligomers or, alternatively, different pools of genes may be randomly recombined to generate gene populations with substitutions in multiple regions. Thus, it is possible to detect a variety of disulfide cross-links between and within individual protein molecules. Interactions between the four membrane-spanning stretches of the Tar dimer were probed by measuring the tendency of 48 cysteine ...
Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). , -Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site. ...
Caspases (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death (including apoptosis, pyroptosis and necroptosis) and inflammation. They are named caspases due to their specific cysteine protease activity - a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 11 or 12 confirmed caspases in humans[note 1] and 10 in mice, carrying out a variety of cellular functions.. The role of these enzymes in programmed cell death was first identified in 1993, with their functions in apoptosis well characterised. This is a form of programmed cell death, occurring widely during development, and throughout life to maintain cell homeostasis. Activation of Caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding ...
3VUM: Seven cysteine-deficient mutants depict the interplay between thermal and chemical stabilities of individual cysteine residues in mitogen-activated protein kinase c-Jun N-terminal kinase 1
3VUM: Seven cysteine-deficient mutants depict the interplay between thermal and chemical stabilities of individual cysteine residues in mitogen-activated protein kinase c-Jun N-terminal kinase 1
Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range ...
Many proteins that are exported from the cytosol pass through a membrane channel into the ER in eukaryotes or the extracellular space in prokaryotes (for reviews see Rapoport et al., 1996; Pohlschroder et al., 1997; Matlack et al., 1998; Johnson and van Waes, 1999). The channel is formed by a heterotrimeric complex of proteins called the Sec61 complex in eukaryotes and the SecY complex in bacteria and archaea. The channel has a hydrophilic interior, as shown by electrophysiology and fluorescence lifetime measurements (Simon and Blobel, 1991; Crowley et al., 1994). Previous models assumed that the channel is formed at the interface between three or four copies of the Sec61/SecY complex (Hanein et al., 1996; Beckmann et al., 1997; Hamman et al., 1997; Manting et al., 2000; Menetret et al., 2000). However, the recently solved X-ray structure of the SecY complex from M. jannaschii is of a monomer with no exterior hydrophilic surfaces in the membrane (van den Berg et al., 2004); thus, the channel ...
Nitric oxide can modify cysteine residues on proteins and produce an S-nitrosylated derivative (see the review by Lane et al.). Gu et al. report that such a modification of matrix metalloproteinase-9 (MMP-9) activates the enzyme. MMP-9 nitrosylation and activation were observed in rodent brain tissue upon stroke, and treatment of cultured neurons with NO-activated MMP-9 caused apoptosis. This activation pathway may contribute to neuronal cell death that is associated with the extracellular matrix disruption observed in cerebral ischemia and neurodegenerative diseases. P. Lane, G. Hao, S. S. Gross, S-Nitrosylation is emerging as a specific and fundamental posttranslational protein modification: Head-to-head comparison with O-phosphorylation. Sciences STKE (2001), http://stke.sciencemag.org/cgi/content/full/sigtrans;2001/86/re1 [Abstract] [Full Text] Z. Gu, M. Kaul, B. Yan, S. J. Kridel, J. Cui, A. Strongin, J. W. Smith, R. C. Liddington, S. A. Lipton, S-Nitrosylation of matrix ...
TY - JOUR. T1 - Sulphoxythiocarbamates modify cysteine residues in HSP90 causing degradation of client proteins and inhibition of cancer cell proliferation. AU - Zhang, Y.. AU - Dayalan Naidu, S.. AU - Samarasinghe, K.. AU - Van Hecke, G. C.. AU - Pheely, A.. AU - Boronina, T. N.. AU - Cole, R. N.. AU - Benjamin, I. J.. AU - Cole, P. A.. AU - Ahn, Y-H. AU - Dinkova-Kostova, A. T.. PY - 2014/1/7. Y1 - 2014/1/7. N2 - BackgroundHeat shock protein 90 (HSP90) has a key role in the maintenance of the cellular proteostasis. However, HSP90 is also involved in stabilisation of oncogenic client proteins and facilitates oncogene addiction and cancer cell survival. The development of HSP90 inhibitors for cancer treatment is an area of growing interest as such agents can affect multiple pathways that are linked to all hallmarks of cancer. This study aimed to test the hypothesis that targeting cysteine residues of HSP90 will lead to degradation of client proteins and inhibition of cancer cell ...
Article, see p 1308. In the study by Murphy et al,13 this group combined the classic biotin switch assay with the isotopic cysteine-reactive tandem mass tag (CysTMT) reagent to not only identify specific Cys residues that were SNO-modified in the heart but also determine the occupancy of SNO modification for each site. The use of thiol-reactive isotopic affinity (mass) tags is not new. The earliest isotope-labeled affinity tags were developed by Aebersolds group14 and reacted with the free thiol groups; however, these were conceived for general protein quantification rather than the targeted analysis of Cys PTMs. Cohen et al15 first pursued a Cys-specific application of isotope-coded affinity tags (ICAT) in cardiac muscle to investigate the extent of oxidative Cys modifications upon peroxide treatment. CysTMT tags are the most recent development in thiol-targeted isotopic mass tags and can be multiplexed with up to 6 different samples in a single MS analysis.12 More recently, our group, in ...
C/EBP homologous protein (CHOP) is a transcription factor that is elevated in adipose tissue across many models of diabetes and metabolic stress. Although increased CHOP levels are associated with the terminal response to endoplasmic reticulum stress and apoptosis, there is no evidence for CHOP mediated apoptosis in the adipose tissue during diabetes. CHOP protein levels increase in parallel with protein succination, a fumarate derived cysteine modification, in the adipocyte during metabolic stress. We investigated the factors contributing to sustained CHOP proteins levels in the adipocyte, with an emphasis on the regulation of CHOP protein turnover by metabolite-driven modification of Keap1 cysteines. CHOP protein stability was investigated in conditions of nutrient stress due to high glucose or elevated fumarate (fumarase knockdown model); where cysteine succination is specifically elevated. CHOP protein turnover is significantly reduced in models of elevated glucose and fumarate with a ∼30% ...
Formylglycine-generating enzyme (FGE) catalyzes the oxidation of a specific cysteine residue in nascent sulfatase polypeptides to formylglycine (FGly). This FGly is part of the active site of all sulfatases and is required for their catalytic activity. Here we demonstrate that residues 34-68 constitute an N-terminal extension of the FGE catalytic core that is dispensable for in vitro enzymatic activity of FGE but is required for its in vivo activity in the endoplasmic reticulum (ER), i.e. for generation of FGly residues in nascent sulfatases. In addition, this extension is needed for the retention of FGE in the ER. Fusing a KDEL retention signal to the C terminus of FGE is sufficient to mediate retention of an N-terminally truncated FGE but not sufficient to restore its biological activity. Fusion of FGE residues 1-88 to secretory proteins resulted in ER retention of the fusion protein. Moreover, when fused to the paralog of FGE (pFGE), which itself lacks FGly-generating activity, the FGE ...
Cells respond to oxidants and electrophiles by activating receptor/transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2) to coordinate the induction of cytoprotective genes critical for defense against oxidative and other stresses. Activation involves blocking the ubiquitination-proteasomal degradation of Nrf2. Modification of cysteine thiol groups by inducers in the linker regio
Homocysteine is usually broken down into the amino acid cysteine. Cysteine is one of the amino acids needed by the cells to make intracellular glutathione. If your body does not convert homocysteine to cysteine the intracellular glutathione conversion will not take place. ...
GPR37, also known as parkin-associated endothelin-like receptor (Pael-R), is an orphan G protein-coupled receptor (GPCR) that aggregates intracellularly in a juvenile form of Parkinsons disease. However, little is known about the structure or function of this receptor. Here, in order to better understand the functioning of this receptor, we focused on the GPR37 C-terminal tail, in particular on a cystein-enriched region. Thus, we aimed to reveal the role of these residues on receptor plasma membrane expression and function, and also whether the presence of this cysteine-rich domain is linked to the previously described receptor-mediated cytotoxicity. Interestingly, while the deletion of six cysteine residues within this region did not affect receptor internalization it promoted GPR37 plasma membrane expression and signaling. Furthermore, the removal of the C-terminal cysteine-rich domain protected against GPR37-mediated apoptosis and cell death. Overall, we identified a GPR37 domain, namely the ...
TY - JOUR. T1 - Assembly and molecular architecture of the phosphoinositide 3-kinase p85α homodimer. AU - LoPiccolo, Jaclyn. AU - Kim, Seung Joong. AU - Shi, Yi. AU - Wu, Bin. AU - Wu, Haiyan. AU - Chait, Brian T.. AU - Singer, Robert H.. AU - Sali, Andrej. AU - Brenowitz, Michael D.. AU - Bresnick, Anne R.. AU - Backer, Jonathan M.. PY - 2015/12/18. Y1 - 2015/12/18. N2 - Phosphoinositide 3-kinases (PI3Ks) are a family of lipid kinases that are activated by growth factor and G-protein-coupled receptors and propagate intracellular signals for growth, survival, proliferation, and metabolism. p85α, a modular protein consisting of five domains, binds and inhibits the enzymatic activity of class IA PI3K catalytic subunits. Here, we describe the structural states of the p85α dimer, based on data from in vivo and in vitro solution characterization. Our in vitro assembly and structural analyses have been enabled by the creation of cysteine-free p85α that is functionally equivalent to native p85α. ...
C alpha-formylglycine (FGly) is the catalytic residue of sulfatases in eukaryotes. It is generated by a unique post-translational modification catalysed by the FGly-generating enzyme (FGE) in the endoplasmic reticulum. FGE oxidizes a cysteine residue within the conserved CxPxR sequence motif of nascent sulfatase polypeptides to FGly. Here we show that this oxidation is strictly dependent on molecular oxygen (O-2) and consumes 1 mol O-2 per mol FGly formed. For maximal activity FGE requires an O-2 concentration of 9% (105 mu M). Sustained FGE activity further requires the presence of a thiol-based reductant such as DTT. FGly is also formed in the absence of DTT, but its formation ceases rapidly. Thus inactivated FGE accumulates in which the cysteine pair Cys336/Cys341 in the catalytic site is oxidized to form disulfide bridges between either Cys336 and Cys341 or Cys341 and the CxPxR cysteine of the sulfatase. These results strongly suggest that the Cys336/Cys341 pair is directly involved in the ...
When peptides contain multiple cysteine residues, challenges arise due to the random formation of disulfide bridges between them.
A green and efficient adsorbent for adsorption of palladium ions was prepared from 2,3-dialdehyde cellulose (DAC) originating from nanocellulose from the green algae Cladophora. The DAC was functional
Blood plasma samples from HIV-1-infected persons contain elevated glutamate concentrations up to 6-fold the normal level and relatively low concentrations of acid-soluble thiol (i.e. decreased cysteine concentrations). The intracellular glutathione concentration in peripheral blood-mononuclear cells …
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Copper ion (Cu(2+)) and L-cysteine (L-Cys) detection is critically important since an abnormal level of Cu(2+) or L-Cys is an indicator for many diseases. In this paper, we demonstrate an off-on approach for highly sensitive and selective detection of Cu(2+) and L-Cys using carbon dots (CDs) as fluorescent probes. CDs were prepared by using mesoporous silica (MS) spheres as nanoreactors. The binding ability of CDs towards metal ions was examined by comparing the fluorescence intensities of CDs before and after the addition of the metal ions. The addition of Cu(2+) cations leads to their absorption on the surface of CDs and the significant fluorescence quench of CDs (turn-off). The resulting in CDs-Cu(2+) system was found to be sensitive to L-Cys. The addition of L-Cys not only serves to shelter the CDs effectively from being quenched, but also to reverse the quenching and restore the fluorescence (turn-on) due to its ability to remove Cu(2+) from the surface of CDs. This method is facile, ...
Cysteine Complex is a combination of n-acetyl cysteine, alpha lipoic acid, pomegranate extract, broccoli extracts, indole-3-carbinol and molybdenum.
Glutathione, a protein made from the amino acids cysteine, glutamic acid, and glycine, is one of the most important elements within the bodys system that fights free radicals. Glutathione also keeps some biological molecules in a reduced (less dangerous state,) such as chemicals and pesticides, so that the body can better excrete them.
Glutathione, a protein made from the amino acids cysteine, glutamic acid, and glycine, is one of the most important elements within the bodys system that fights free radicals. Glutathione also keeps some biological molecules in a reduced (less dangerous state,) such as chemicals and pesticides, so that the body can better excrete them.
Glutathione, a protein made from the amino acids cysteine, glutamic acid, and glycine, is one of the most important elements within the bodys system that fights free radicals. Glutathione also keeps some biological molecules in a reduced (less dangerous state,) such as chemicals and pesticides, so that the body can better excrete them.
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine ...
My name is Mika Covington and I live with Cystinosis. I am 23 years old and hope to live 23 more. I was born with Cystinosis and diagnosed around age 10 months. Cystinosis is a rare metabolic disease that causes cells to crystallize causing early cell death. This happens because the amino acid cysteine accumulates…
Background: Reactive species have been regarded as by-products of cellular metabolism, which cause oxidative damage contributing to aging and neurodegenerative diseases. However, accumulated evidence support the notion that reactive species mediate intracellular and extracellular signals that regulate physiological functions including posttranslational protein modifications. Cysteine thiol groups of proteins are particularly susceptible to oxidative modifications by oxygen, nitrogen and sulfur species generating different products with critical roles in the cellular redox homeostasis. At physiological conditions, reactive species can function not only as intracellular second messengers with regulatory roles in many cellular metabolic processes but also as part of an ancestral biochemical network that controls cellular survival, regeneration, and death ...
According to a research team led by led by scientists at University of Utah Health aging can stem from too much of a good thing. Elevated levels of an important nutrient- the amino acid cysteine - jump starts the agi... ...
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We have shown that the E172Q and E172C mutations of L247T α7 nicotinic receptors eliminate receptor stimulation by the presence of permeable divalent cations. ACh dose responses of E172Q/L247T α7 nAChRs were inhibited by the presence of Ca2+, Ba2+, or Sr2+, and E172C/L247T α7 nAChRs were insensitive to the presence of these ions. E172Q/L247T α7 nAChRs did not display the high level of basal activity that is a characteristic of L247T α7 receptors and were not activated by the antagonist DHβE. E172C/L247T α7 receptors were blocked by the thiol-modifying reagent MTSET, indicating that E172 is accessible to permeant ions. These data support the conclusion drawn from a chimera of α7 nicotinic receptors and 5-HT3 receptors that E172 is essential for the modulation of α7 receptors by Ca2+ and other permeant divalent cations (19). The data are also consistent with a model of α7 receptors based on the crystal structure of AChBP (6) that places E172 near the inner surface of the vestibule, where ...
Copyright 2017 by Aaron Antcliff. In accordance with Title 17 of the United States Code, Copyright Law of the United States of America, this material is copyrighted, and any further reproduction or distribution is prohibited without the permission of the copyright owner ...
Rationale: S-nitrosylation (SNO), an oxidative post-translational modification of cysteine residues, responds to changes in the cardiac redox-environment. Classic biotin switch assay and its derivatives are the most common methods used for detecting SNO. In this approach, the labile SNO group is selectively replaced with a single stable tag. To date, a variety of thiol-reactive tags have been introduced. However, these methods have not produced a consistent dataset which suggests an incomplete capture by a single tag and potentially the presence of different cysteine subpopulations. Objective: To investigate potential labeling bias in the existing methods with a single tag to detect SNO, explore if there are distinct cysteine subpopulations, and then, develop a strategy to maximize the coverage of SNO proteome. Methods and Results: We obtained SNO-modified cysteine datasets for wild-type and S-nitrosoglutathione reductase (GSNOR) knock-out mouse hearts (GSNOR is a negative regulator of GSNO ...
TY - JOUR. T1 - Redox control of the transsulfuration and glutathione biosynthesis pathways.. AU - Deplancke, Bart. AU - Gaskins, H. Rex. PY - 2002/1. Y1 - 2002/1. N2 - Intracellular reduction-oxidation status is increasingly recognized as a primary regulator of cellular growth and development. The relative reduction-oxidation state of the cell depends primarily on the precise balance between concentrations of reactive oxygen species and the cysteine-dependent antioxidant thiol buffers glutathione and thioredoxin, which by preferentially reacting with reactive oxygen species, protect other intracellular molecules from oxidative damage. The transsulfuration pathway constitutes the major route of cysteine biosynthesis, and may thus be central in controlling the intracellular reduction-oxidation state and the balance between self-renewal and differentiation programs. This review discusses new findings on reciprocal reduction-oxidation modulation of enzymes involved in the transsulfuration and ...
TY - JOUR. T1 - Technetium-99m ethyl cysteinate dimer (ECD) cerebral accumulation and symptom and sign severity during hypothyroidism. AU - Schraml, Frank V.. AU - Beason-Held, Lori L.. PY - 2010. Y1 - 2010. N2 - OBJECTIVE: The purpose of this study was to correlate hypothyroid-related symptomatology with regional cerebral blood flow (rCBF) during hypothyroidism. MATERIALS AND METHODS: Nine thyroidectomized patients underwent neuropsychological testing and single photon emission computed tomography (SPECT) of their brains with technetium-99m (Tc-99m) ethyl cysteinate dimer (ECD), a lipophilic cerebral blood flow radiotracer, while hypothyroid, and again following thyroid hormone replacement. Neuropsychological test scores and TSH levels while hypothyroid were correlated with rCBF in hypothyroid-affected areas of the brain. RESULTS: Correlations were found during hypothyroidism between the noted parameters and ECD radiotracer accumulation in the following respective regions, all of which ...
TY - JOUR. T1 - Effect of L-cysteine on the long-term depletion of brain indoles caused by p-chloroamphetamine and d-fenfluramine in rats Relation to brain drug concentrations. AU - Invernizzi, Roberto. AU - Fracasso, Claudia. AU - Caccia, Silvio. AU - Di Clemente, Angelo. AU - Garattini, Silvio. AU - Samanin, Rosario. PY - 1989/4/12. Y1 - 1989/4/12. N2 - The effect of L-cysteine on the depletion of serotonin and 5-hydroxyindoleacetic acid concentrations caused by p-chloroamphetamine and d-fenfluramine was studied in various brain regions one week after drug injection. p-Chloroamphetamine (2.5 and 5 mg/kg i.p.) and d-fenfluramine (13.4 mg/kg i.p.) significantly reduced serotonin and 5-hydroxyindoleacetic acid levels in the striatum, hippocampus and cortex, particularly in the latter areas. L-cysteine (500 mg/kg i.p.), administered 30 min before and 5 h after p-chloroamphetamine or d-fenfluramine, significantly reduced the effect of either drug on the concentrations of both indoles without ...
TY - JOUR. T1 - Two pathways for cysteine biosynthesis in Leishmania major. AU - Williams, Roderick A. M.. AU - Westrop, Gareth D.. AU - Coombs, Graham H.. PY - 2009/6/15. Y1 - 2009/6/15. N2 - Genome mining and biochemical analyses have shown that Leishmania major possesses two pathways for cysteine synthesis - the de novo biosynthesis pathway comprising SAT (serine acetyltransferase) and CS (cysteine synthase) and the RTS (reverse trans-sulfuration) pathway comprising CBS (cystathionine beta-synthase) and CGL (cystathionine gamma-lyase). The LmjCS (L. major CS) is similar to the type A CSs of bacteria and catalyses the synthesis of cysteine using O-acetylserine and Sulfide with K(m)s of 17.5 and 0.13 mm respectively. LmjCS can use sulfide provided by the action of MST (mercaptopyruvate Sulfurtransferase) oil 3-MP (3-mercaptopyruvate). LmJCS forms a bi-enzyme complex with Leishmania SAT (and Arabidopsis SAT), with residues LYs(222), His(226) and Lys(227) of LmjCS being involved in the complex ...
The Moco (molybdenum cofactor) sulfurase ABA3 from Arabidopsis thaliana catalyses the sulfuration of the Moco of aldehyde oxidase and xanthine oxidoreductase, which represents the final activation step of these enzymes. ABA3 consists of an N-terminal NifS-like domain that exhibits L-cysteine desulfurase activity and a C-terminal domain that binds sulfurated Moco. The strictly conserved Cys430 in the NifS-like domain binds a persulfide intermediate, which is abstracted from the substrate L-cysteine and finally needs to be transferred to the Moco of aldehyde oxidase and xanthine oxidoreductase. In addition to Cys⁴³⁰, another eight cysteine residues are located in the NifS-like domain, with two of them being highly conserved among Moco sulfurase proteins and, at the same time, being in close proximity to Cys⁴³⁰. By determination of the number of surface-exposed cysteine residues and the number of persulfide-binding cysteine residues in combination with the sequential substitution of each ...
A 0·5 kb fragment of Streptomyces venezuelae ISP5230 genomic DNA was amplified by PCR using primers based on consensus sequences of cysteine synthase isozyme A from bacteria. The deduced amino acid sequence of the PCR product resembled not only cysteine synthase sequences from prokaryotes and eukaryotes but also eukaryotic cystathionine β-synthase sequences. Probing an Str. venezuelae genomic library with the PCR product located a hybridizing colony from which pJV207 was isolated. Sequencing and analysis of the Str. venezuelae DNA insert in pJV207 detected two ORFs. The deduced amino acid sequence of ORF1 matched both cysteine synthase and cystathionine β-synthase sequences in GenBank, but its size favoured assignment as a cystathionine β-synthase. ORF2 in the pJV207 insert was unrelated in function to ORF1; in its sequence the deduced product resembled acetyl-CoA transferases, but disruption of the ORF did not cause a detectable phenotypic change. Disruption of ORF1 failed to elicit cysteine
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"cysteine - Definition of cysteine in English by Oxford Dictionaries". Oxford Dictionaries - English. Retrieved 15 April 2018.. ... Cysteine (symbol Cys or C;[3] /ˈsɪstiiːn/)[4] is a semiessential[5] proteinogenic amino acid with the formula HO2CCH(NH2)CH2SH ... For example, the reaction of cysteine with sugars in a Maillard reaction yields meat flavors.[26] L-Cysteine is also used as a ... N-Acetyl-L-cysteine is a derivative of cysteine wherein an acetyl group is attached to the nitrogen atom. This compound is sold ...
Cysteine-rich domain[edit]. Frizzled proteins include cysteine-rich domain that is conserved in diverse proteins, including ... This domain contains ten conserved cysteines that form five disulphide bridges. Group members[edit]. The following is a list of ... Sequence similarity between the cysteine-rich domain of Frizzled and several receptor tyrosine kinases, which have roles in ... Crystal structure of the cysteine-rich domain of mouse frizzled 8 (mfz8)[1] ...
Cysteine[edit]. The genes required for the synthesis of cysteine are coded for on the cys regulon. The integration of sulfur is ... 3-Phosphoglycerates: serine, glycine, cysteine[edit]. Serine[edit]. Serine is the first amino acid in this family to be ... In addition, the amino acids arginine, cysteine, glycine, glutamine, histidine, proline, serine, and tyrosine are considered ... There are two other negative regulators of cysteine. These are the molecules sulfide and thiosulfate, they act to bind to CysB ...
cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase. *Glutathione synthetase. *Gamma-glutamyl transpeptidase. * ...
cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase. *Glutathione synthetase. *Gamma-glutamyl transpeptidase. * ...
The original FASTA/Pearson format is described in the documentation for the FASTA suite of programs. It can be downloaded with any free distribution of FASTA (see fasta20.doc, fastaVN.doc or fastaVN.me-where VN is the Version Number). In the original format, a sequence was represented as a series of lines, each of which was no longer than 120 characters and usually did not exceed 80 characters. This probably was to allow for preallocation of fixed line sizes in software: at the time most users relied on Digital Equipment Corporation (DEC) VT220 (or compatible) terminals which could display 80 or 132 characters per line.[citation needed] Most people preferred the bigger font in 80-character modes and so it became the recommended fashion to use 80 characters or less (often 70) in FASTA lines. Also, the width of a standard printed page is 70 to 80 characters (depending on the font). Hence, 80 characters became the norm.[citation needed] The first line in a FASTA file started either with a "," ...
cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase. *Glutathione synthetase. *Gamma-glutamyl transpeptidase. * ...
cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase. *Glutathione synthetase. *Gamma-glutamyl transpeptidase. * ...
Cysteine Cys C MT-TC 5,761-5,826 H Glutamic acid Glu E MT-TE 14,674-14,742 H ...
Two enzymes convert L-amino acids to D-amino acids. D-Amino-acid racemase, a PLP-dependent enzyme, racemizes amino acids via the formation of the alpha-iminoacids, where the stereogenic center is lost. L-amino-acid oxidases convert L-amino acids to the alpha-ketoacids, which are susceptible to reductive amination. Some amino acids are prone to racemization, one example being lysine, which racemizes via formation pipecolic acid. In peptides, L-amino acid residues slowly racemize, resulting in the formation of some D-amino acid residues. Racemization occurs via deprotonation of the methyne that is alpha to the amido group. Rates increase with pH. Many D-amino acids found in higher organisms are derived from microbial sources. The D-alanine in peptidoglycans that comprise bacterial cell walls helps its host resist attack by proteolytic enzymes. Several antibiotics, e.g. bacitracin, contain D-amino acid residues.[1] ...
conversion to cysteine: Cystathionine. *α-Ketobutyric acid+Cysteine. threonine→. *α-Ketobutyric acid ...
conversion to cysteine: Cystathionine. *alpha-Ketobutyric acid+Cysteine. threonine→. *α-Ketobutyric acid ...
conversion to cysteine: Cystathionine. *α-Ketobutyric acid+Cysteine. threonine→. *α-Ketobutyric acid ...
... or cysteine to activate it as a nucleophile. In a histidine proton shuttle, histidine is used to quickly shuttle protons. It ...
There are inhibitory amino acids (IAA) or excitatory amino acids (EAA). Some EAA are L-Glutamate, L-Aspartate, L-Cysteine, and ...
While most amino acids are oxidized in the liver, BCAAs are primarily oxidized in the skeletal muscle and other peripheral tissues.[4] The effects of BCAA administration on muscle growth in rat diaphragm was tested, and concluded that not only does a mixture of BCAAs alone have the same effect on growth as a complete mixture of amino acids, but an amino acid mixture with all but BCAAs has no effect on rat diaphragm muscle growth.[16] Administration of either isoleucine or valine alone had no effect on muscle growth, although administration of leucine alone appears to be nearly as effective as the complete mixture of BCAAs. Leucine indirectly activates p70 S6 kinase as well as stimulates assembly of the eIF4F complex, which are essential for mRNA binding in translational initiation.[16] P70 S6 kinase is part of the mammalian target of rapamycin complex (mTOR) signaling pathway, and has been shown to allow adaptive hypertrophy and recovery of rat muscle.[17] At rest protein infusion stimulates ...
conversion to cysteine: Cystathionine. *alpha-Ketobutyric acid+Cysteine. threonine→. *α-Ketobutyric acid ...
Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization ...
Glycerate 3-phosphate is also a precursor for serine, which, in turn, can create cysteine and glycine through the homocysteine ...
These asthmatic effects are proposed to be caused by the oxidation of cysteine residues, as well as methionine residues.[10] ...
L-cysteine (E920). *L-cystine (E921). *Potassium persulfate (E922). *Ammonium persulfate (E923) ...
L-cysteine (E910). *Montan wax (E912). *Lanolin (E913). *Oxidised polyethylene wax (E914) ...
L-cysteine (E920). *L-cystine (E921). *Potassium persulfate (E922). *Ammonium persulfate (E923) ...
DNAJC5: Cysteine string protein. *EDEM2: ER degradation-enhancing alpha-mannosidase-like 2 ...
Due to cysteine's low pKa, the importance of the Asp to catalysis varies and several cysteine proteases are effectively Cys-His ... The second most studied triad is the Cysteine-Histidine-Aspartate motif.[2] Several families of cysteine proteases use this ... requires serine to be re-protonated whereas cysteine can leave as S−. Sterically, the sulfur of cysteine also forms longer ... Shown are the serine triad of chymotrypsin[e] and the cysteine triad of TEV protease.[a] (PDB: 1LVM, 1GG6​) ...
Active site cysteine residues are the functional unit in cysteine protease catalytic triads. Cysteine residues may also react ... Cysteine and cystineEdit. As the functional group of the amino acid cysteine, the thiol group plays a very important role in ... When the thiol groups of two cysteine residues (as in monomers or constituent units) are brought near each other in the course ... A physical manifestation of cysteine-cystine equilibrium is provided by hair straightening technologies.[34] ...
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In addition, a mutated form of Prx1p containing the absolutely conserved cysteine as the only cysteine residue also shows ... conserved cysteine residues. Moreover, 2-Cys Prxs, also named thioredoxin peroxidases, have peroxide reductase activity with ...
Cysteine dioxygenase (CDO) is a mononuclear ferrous enzyme located at a branch-point in cysteine metabolism and catalyzes the ... Spectroscopic and kinetic investigation of two unusual structural features found in eukaryotic cysteine dioxygenase. View/. ... Purified CDO in the resting state was capable of binding L-cysteine but incapable of binding nitric oxide; however, when ... Consistent with the oxidation, purified CDO displayed no activity beyond the background oxidation of L-cysteine. Activity was ...
Degradation of cysteine and homocysteine 9 Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1 ... Methylated cysteine dioxygenase-1 gene promoter in the serum is a potential biomarker for hepatitis B virus-related ... Frequent inactivation of cysteine dioxygenase type 1 contributes to survival of breast cancer cells and resistance to ... Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range. ...
Calpastatin (CAST) is a calpain inhibitor, a calcium-dependent cysteine protease that is widely distributed in higher order ...
"cysteine - Definition of cysteine in English by Oxford Dictionaries". Oxford Dictionaries - English. Retrieved 15 April 2018.. ... Cysteine (symbol Cys or C;[3] /ˈsɪstiiːn/)[4] is a semiessential[5] proteinogenic amino acid with the formula HO2CCH(NH2)CH2SH ... For example, the reaction of cysteine with sugars in a Maillard reaction yields meat flavors.[26] L-Cysteine is also used as a ... N-Acetyl-L-cysteine is a derivative of cysteine wherein an acetyl group is attached to the nitrogen atom. This compound is sold ...
Cysteine, Sulfur-containing nonessential amino acid. In peptides and proteins, the sulfur atoms of two cysteine molecules are ... Cysteine, Sulfur-containing nonessential amino acid. In peptides and proteins, the sulfur atoms of two cysteine molecules are ... amino acid: Cysteine oxidation. The thiol (sulfur-containing) group of cysteine is highly reactive. The most common reaction of ... Oxidation of two molecules of cysteine forms cystine, a molecule that contains a disulfide bond. When two cysteine residues… ...
Cysteine definition, a crystalline amino acid, C 3 H 7 O 2 NS, a component of nearly all proteins, obtained by the reduction of ... cysteine in Medicine Expand. cysteine cys·te·ine (sĭstē-ēn, -ĭn, sĭ-stēĭn). n. Abbr. Cys An alpha-amino acid found in most ... Eggs, he says, are a good source of cysteine, an amino acid that helps the liver break down alcohol faster. ...
... is a N-acetyl-L-amino acid (CHEBI:21545) N-acetyl-L-cysteine (CHEBI:28939) is a L-cysteine ... N-acetyl-L-cysteine (CHEBI:28939) is a acetylcysteine (CHEBI:22198) N-acetyl-L-cysteine (CHEBI:28939) is conjugate acid of N- ... S-substituted N-acetyl-L-cysteine (CHEBI:47911) has functional parent N-acetyl-L-cysteine (CHEBI:28939). N-acetyl-L-cysteinate ... N-acetyl-L-cysteine (CHEBI:28939) has role antiviral drug (CHEBI:36044) N-acetyl-L-cysteine (CHEBI:28939) has role human ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Other names: Cysteine, L-; «beta»-Mercaptoalanine; Cystein; Cysteine; Half-cystine; L-(+)-Cysteine; L-Alanine, 3-mercapto-; NSC ...
Other names: L-HSCH2CH(NH2)COOH; Cysteine, DL- * Permanent link for this species. Use this link for bookmarking this species ...
Cysteine can be converted to cystine and taurine. Cystine itself is a disulfide, containing two cysteine molecules. Cysteine is ... L-cysteine also forms another amino acid, L-cystine, which is important in hair and nail tissues.. L-cysteine supplementation ... Tagged asamino acidAnti-agingantioxidantcysteinecystinedetoxificationglutathioneL-Cysteine ... POSSIBLE USES OF L-CYSTEINE. Smokers*. Smokers cough/bronchitis. Air pollution. Exposure to chemicals. Psoriasis (aids skin ...
Cysteine and Cystine are sulfur-containing amino acids that are synthesized in the liver and are involved in multiple metabolic ... Cysteine can be converted to cystine and taurine. Cystine itself is a disulfide, containing two cysteine molecules. Cysteine is ... L-cysteine also forms another amino acid, L-cystine, which is important in hair and nail tissues. L-cysteine supplementation ... POSSIBLE USES OF L-CYSTEINE. Smokers*. Smokers cough/bronchitis. Air pollution. Exposure to chemicals. Psoriasis (aids skin ...
Brands A-Z Now Foods L-Cysteine Categories Supplements Amino Acids L-Cysteine ... Now Foods, L-Cysteine 1 Results (showing 1 - 1) Visit Manufacturers Website » ...
L-Cysteine is also used as a processing aid for baking. In the field of personal care, cysteine is used for permanent wave ... N-Acetyl-L-cysteine is a derivative of cysteine wherein an acetyl group is attached to the nitrogen atom. This compound is sold ... Again, the cysteine is used for breaking up the disulfide bonds in the hairs keratin. Cysteine is a very popular target for ... While free cysteine residues do occur in proteins, most are covalently bonded to other cysteine residues to form disulfide ...
Cysteine (thing). See all of Cysteine, there are 3 more in this node. ...
Professional guide for Cysteine. Includes: pharmacology, pharmacokinetics, contraindications, interactions, adverse reactions ... Infants: Metabolic acidosis has occurred in infants related to the "hydrochloride" component of cysteine; each 1 mmol cysteine ... of cysteine may be needed; each 40 mg cysteine (equal to every 1 g amino acid when used in the recommended ratio) adds 0.228 ... Cysteine may be considered an essential amino acid in infants.. Use: Labeled Indications. Nutritional supplement: Additive to ...
Cysteine is a type of amino acid thats combined in your body with glutamic acid and glycine to make glutathione. Glutathione ... Cysteine supplements are associated with no specific medical conditions, but the modified form known as N-acetyl cysteine, or ... Cysteine is considered a "nonessential" amino acid, meaning that your body can create it and you dont need to get it from your ... Cysteine is a type of amino acid thats combined in your body with glutamic acid and glycine to make glutathione. Glutathione ...
N-acetyl-L-cysteine (NAC) is a form of cysteine where an acetyl group is attached to cysteines nitrogen atom; it is sold as a ... Cystine is an oxidized form of cysteine, involving two cysteine residues liked by a disulfide bond. Cysteine is named after ... That is, when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond (cys-S-S-cys ... The cysteine derivative N-acetyl cysteine (NAC) is often used as a cough medicine as it breaks up the disulfide bonds in the ...
For decades, cysteine-based reactions with maleimides and alkyl halides are the primary methods for selectively tagging ... These cysteine arylation reactions are applied to the synthesis of macrocyclic peptides and antibody-drug conjugates (ADCs). ... The goal of this thesis is to develop new cysteine arylation reactions to generate sulfur-sp² carbon bonds on proteins. These ... These traditional reactions generate sulfur-sp³ carbon bonds between the cysteine thiol and the labeling reagents. ...
... , Cysteine Stone, Cysteine Nephrolithiasis, Cystine Calculi, Cystine Stone, Cystine Nephrolithiasis, Cystinuria ... Cysteine Calculi. Aka: Cysteine Calculi, Cysteine Stone, Cysteine Nephrolithiasis, Cystine Calculi, Cystine Stone, Cystine ... Cysteine dissolves poorly at normal Urine pH. *Calculi form at cysteine concentration ,250 mg/day ... Diuresis: reduce cysteine ,300 mg/L. *Alkalinize urine (especially if Urine pH is low, acidic). *Maintain Urine pH ,5.5 (6.5 - ...
In human cysteine metabolism, L-cysteine is consumed in several ways as shown below. L-cysteine is also consumed in methionine ... L-cysteine is the product of several processes as well. In addition to the reactions below, L-cysteine is also a product of ... Cysteine metabolism refers to the biological pathways that consume or create cysteine. The pathways of different amino acids ...
See the reference protein sequence for Farnesyl cysteine-carboxyl methyltransferase, mediates the carboxyl methylation step ... Komagataella phaffii GS115 Farnesyl cysteine-carboxyl methyltransferase, mediates the carboxyl methylation step during C-termin ... Komagataella phaffii GS115 Farnesyl cysteine-carboxyl methyltransferase, mediates the carboxyl methylation step during C-termin ... Komagataella phaffii GS115 Farnesyl cysteine-carboxyl methyltransferase, mediate... ...
... Guest Editors: Christian Appenzeller-Herzog, Kenji Inaba, and Agnès Delaunay ... Cysteine-10 on 17β-Hydroxysteroid Dehydrogenase 1 Has Stabilizing Interactions in the Cofactor Binding Region and Renders ... Cell Biology of Cysteine-Based Molecular Switches, Christian Appenzeller-Herzog, Kenji Inaba, and Agnès Delaunay-Moisan ...
  • Involvement of the Cys-Tyr cofactor on iron binding in the active site of human cysteine dioxygenase. (nih.gov)
  • The spectrum of CDO expressed in cell lysate was consistent with Fe(II) and the lysate displayed considerable catalytic activity for cysteine oxidation. (auburn.edu)
  • Cysteine dioxygenase (CDO) is a mononuclear ferrous enzyme located at a branch-point in cysteine metabolism and catalyzes the oxidation of L-cysteine using both atoms of dioxygen. (auburn.edu)
  • Branched-chain amino acids inhibit the TGF-beta-induced down-regulation of taurine biosynthetic enzyme cysteine dioxygenase in HepG2 cells. (nih.gov)
  • Prognostic Significance of Promoter DNA Hypermethylation of cysteine dioxygenase 1 (CDO1) Gene in Primary Breast Cancer. (nih.gov)
  • Consistent with the oxidation, purified CDO displayed no activity beyond the background oxidation of L-cysteine. (auburn.edu)
  • Models of the active site revealed that the amino acid cysteine occurs at a particular location (dubbed C289) in the two insects, but not in people. (thefreelibrary.com)
  • N-acetyl cysteine (NAC) is a specially modified form of the dietary amino acid cysteine. (epnet.com)
  • Biohit has worked closely with scientists at the University of Helsinki who have been studying the neutralising effects of the amino acid cysteine on acetaldehyde, a carcinogen that is dissolved from tobacco into the saliva and from alcohol by microbes in the mouth. (nutraingredients.com)
  • A new study in the journal Chest concludes that the amino acid cysteine may be a biomarker for the development of obstructive sleep apnea (OSA). (highlighthealth.com)
  • Cysteine is unique among amino acids in that it contains sulfur, which helps it to maintain protein structure in your body. (livestrong.com)
  • Your body makes cysteine from methionine and other amino-acid building blocks, and you also get small amounts of the substance from eating high-protein foods, says the University of Michigan Health System. (livestrong.com)
  • See the reference protein sequence for Farnesyl cysteine-carboxyl methyltransferase, mediates the carboxyl methylation step during C-termin (XP_002492338.1). (nih.gov)
  • ADAM19 autolysis is activated by LPS and promotes non-classical secretion of cysteine-rich protein 2. (nih.gov)
  • Title: Cysteine-rich intestinal protein 2 (CRIP2) acts as a repressor of NF-kappaB-mediated proangiogenic cytokine transcription to suppress tumorigenesis and angiogenesis. (nih.gov)
  • Cysteine S-nitrosylation (SNO) has important physiological roles related to maintaining protein activity, influencing protein conformation, and signaling apoptotic pathways. (springer.com)
  • Avoid use of L-cysteine if patient is receiving at least 3 gram/kg per day of protein. (drugs.com)
  • Cysteine is a source of disulfide linkage in protein and is associated with sulfur transport. (sigmaaldrich.com)
  • L-Cysteine Base is natural amino acid which is considered as building block for protein synthesis in body and also assists in boosting energy levels. (tradeindia.com)
  • Their team also included graduate student Smita Iyer and immunologist Mauricio Rojas, who found that a high level of oxidized cysteine drives white blood cells to send out inflammatory messages in the form of the protein IL-1 beta. (thaindian.com)
  • N-Acetyl Cysteine (NAC) by SciFit is the N-acetyl derivative of the protein amino acid L-cysteine. (illpumpyouup.com)
  • Pure Encapsulations N-Acetyl-l-Cysteine is a free-form amino acid derived from protein and extensively purified. (purecapspro.com)
  • Modification of cysteine thiol groups by inducers in the linker region of Kelch-like ECH-associated protein-1 (Keap1), which congregates Nrf2 into the Keap1/Cul3 E3 complex for ubiquitination, is important but not sufficient for activation of Nrf2. (cdc.gov)
  • Here we describe oxidized cysteine-selective combined precursor isotopic labeling and isobaric tagging (OxcyscPILOT), a high-throughput method for the identification and quantification of endogenous peptide SNO sites relative to the entire cysteine proteome. (springer.com)
  • L-Cysteine is used as a precursor in food, pharmaceutical and personal care products. (fishersci.ca)
  • Some cough medicines contain cysteine as a way to assist in removing mucus from a person's respiratory system, helping the person to stop coughing. (wisegeek.com)
  • Some medicines used to treat bronchitis and Chronic Obstructive Pulmonary Disease ( COPD ) also contain cysteine, using its ability to break apart excessive mucus manufactured by the body as a symptom of both conditions. (wisegeek.com)
  • The real potential for cysteine lies in gastrointestinal health, and the introduction of capsules, known as BioCyst (also in collaboration with Fennobon) is planned in about nine months time. (nutraingredients.com)
  • Beyond gum and capsules, Biohit also holds the patent for cysteine and some other compounds in food. (nutraingredients.com)
  • Below are reviews of Cysteine Complex - 60 Capsules by bodykind customers. (bodykind.com)
  • Cysteine in sufficient levels will bind with metals-preferentially, the heavy metals lead, mercury, and cadmium bond most strongly-thus, cysteine aids the body's elimination of them. (healthy.net)
  • The cysteine bonds with the poisonous products of the acetaminophen that are present in the body's liver. (wisegeek.com)
  • L-Cysteine is also one of the body's main sources of sulfur. (vitaminworld.com)
  • LC189 N-Acetyl-L-cysteine for biochemistry Order number Packaging Quantity Price € AC27189 Plastic bottle 25 g 17.37 AC27189 Plastic bottle 100 g 58.5 AC27189 Plastic bottle 1 kg 440.10 AC27189 Plastic bottle 10 kg inquire Product information Synonyms 2-Acetamido-3-mercaptopropionic. (tradeindia.com)
  • The thiol side chain in cysteine often participates in enzymatic reactions, as a nucleophile . (wikipedia.org)
  • The cysteine thiol group is also a nucleophile (a reagent that forms a chemical bond to its reaction partner by donating both bonding electrons), and can undergo nucleophilic addition and nucleophilic substitution reactions. (newworldencyclopedia.org)
  • These traditional reactions generate sulfur-sp³ carbon bonds between the cysteine thiol and the labeling reagents. (mit.edu)
  • These cysteine arylation reactions are applied to the synthesis of macrocyclic peptides and antibody-drug conjugates (ADCs). (mit.edu)
  • present and experimentally verify an algorithm that can identify which cysteines act in redox reactions by searching for sporadic selenocysteine-Cys pairs in sequence databases. (sciencemag.org)
  • Most people receive sufficient levels of cysteine in their regular diet, except for some vegetarians. (wisegeek.com)
  • Plasma levels of cysteine were significantly increased by cysteine supplementation but not by N-acetylcysteine supplementation. (cochrane.org)
  • Induction and activation of cysteine oxidase of rat liver II. (alfa.com)
  • Your search returned 9 cysteine rich transmembrane module containing 1 Antibodies across 6 suppliers. (biocompare.com)
  • This is in agreement with the stronger in vitro feedback inhibition of free SAT by cysteine compared with CSC-bound SAT and explains the high OAS export rate of WT mitochondria in the presence of cysteine. (mendeley.com)
  • We now report that specific cysteine protease inhibitors kill Leishmania parasites in vitro , at concentrations that do not overtly affect mammalian host cells. (pnas.org)
  • Cysteine supplements are associated with no specific medical conditions, but the modified form known as N-acetyl cysteine, or NAC, has potential benefits for many different ailments. (livestrong.com)
  • What Is the Scientific Evidence for N-Acetyl Cysteine? (epnet.com)
  • The goal of the proposed study is to evaluate the efficacy and safety of N-Acetyl Cysteine (NAC) in trichotillomania. (clinicaltrials.gov)
  • What other names is N-acetyl Cysteine known by? (rxlist.com)
  • N-acetyl cysteine comes from the amino acid L-cysteine. (rxlist.com)
  • N-acetyl cysteine has many uses as medicine. (rxlist.com)
  • People take N-acetyl cysteine by mouth to counteract acetaminophen (Tylenol) and carbon monoxide poisoning. (rxlist.com)
  • Some people use N-acetyl cysteine orally for long-term bronchitis, chronic obstructive pulmonary disease (COPD), cystic fibrosis, hay fever, human immunodeficiency virus (HIV), a lung condition called fibrosing alveolitis, autism, head and neck cancer, colorectal cancer, and lung cancer. (rxlist.com)
  • Some people use N-acetyl cysteine to improve fertility and immunity to flu and H1N1 (swine) flu. (rxlist.com)
  • N-acetyl cysteine is applied to the skin to treat a genetic condition known as lamellar ichthyosis. (rxlist.com)
  • Healthcare providers give N-acetyl cysteine intravenously (by IV) for acetaminophen (Tylenol) overdose, acrylonitrile poisoning, amyotrophic lateral sclerosis (ALS, Lou Gehrig's disease), kidney failure in the presence of liver disease (hepatorenal syndrome), pancreas swelling (pancreatitis), chest pain in combination with nitroglycerin, heart attack in combination with nitroglycerin and streptokinase, and for helping to prevent multi-organ failure leading to death. (rxlist.com)
  • Intravenously, N-acetyl cysteine may also be used to improve recovery after surgery, decrease heart rhythm problems after surgery, treat a genetic condition known as adrenoleukodystrophy (ALD), improve exercise performance, treat acute respiratory distress syndrome (ARDS), improve lung function in patients with sepsis, and prevent kidney damage due to certain X-ray dyes. (rxlist.com)
  • N-acetyl cysteine is sometimes used rectally for conditions known as meconium ileus and meconium ileus equivalent. (rxlist.com)
  • N-acetyl cysteine is sometimes inhaled (breathed into the lungs) or delivered through a tube in the throat to treat certain lung disorders such as asthma, pneumonia, chronic obstructive pulmonary disease (COPD), bronchitis, emphysema, cystic fibrosis, and others. (rxlist.com)
  • What Are the Benefits of N-Acetyl-Cysteine? (livestrong.com)
  • This study intends to verify the interference of N acetyl cysteine in the progression of chronic kidney disease in patients with Nephropathic Cystinosis. (clinicaltrials.gov)
  • Therefore, this study is conducted to verify the interference of the stress oxidative in the progression of the renal disease with the use of an oxidant drug, N acetyl cysteine (NAC). (clinicaltrials.gov)
  • N-acetyl cysteine appears to be a safe and moderately effective augmentation strategy in chronic schizophrenia. (greenmedinfo.com)
  • When taking N-Acetyl cysteine it is recommended that two to three times as much vitamin C be taken at the same time. (iherb.com)
  • N-acetyl-cysteine or NAC drug may prevent many age-related health problems when used at much lower levels, suggests new research conducted on rats published in the journal Redox Biology. (medindia.net)
  • I came across something about a doctor in minnesota using N-Acetyl-Cysteine to help people with hair pulling. (healthboards.com)
  • The generic N-Acetyl Cysteine is manufactured by 4 companies. (medindia.net)
  • Please also note that Medindia's database currently has 4 Brands of Generics of N-Acetyl Cysteine listed . (medindia.net)
  • New - Nutrient Complex with broccoli sprout, n-acetyl cysteine, alpha lipoic acid and molybdenum. (biocare.co.uk)
  • Cysteine Complex is a specialist combination of n-acetyl cysteine, alpha lipoic acid, pomegranate extract, broccoli extracts, indole-3-carbinol and molybdenum. (biocare.co.uk)
  • Cysteine Complex will replace our popular product LIV-D. We've improved the formulation by reducing the dosages of alpha lipoic acid and N-acetyl cysteine and adding other nutrients in to make it more balanced. (biocare.co.uk)
  • N-Acetyl Cysteine (NAC) is a stable form of the non-essential amino acid L-Cysteine. (puritan.com)
  • N-acetyl cysteine (NAC) supplements are among the most popular amino acid supplements out there. (swansonvitamins.com)
  • N-acetyl cysteine also promotes healthy liver function, as it helps to naturally detoxify this important organ. (swansonvitamins.com)
  • When it is taken in the form of supplement then it is formed in the form of N-Acetyl Cysteine (NAC). (planetayurveda.com)
  • The reversible inhibitors ZLIII43A and ZLIII115A are derivatives of oxalic bis[(2-hydroxy-1-naphthyl)methylene]hydrazide, a cysteine protease inhibitor lead compound found in a computer graphics screen of the Fine Chemicals Directory ( 9 ). (pnas.org)
  • The second approach utilizes organometallic palladium reagents to chemoselectively install electron-neutral and electron-rich aryls on cysteine thiols. (mit.edu)
  • Using bispalladium reagents, macrocyclic peptides bearing aryl linkers are synthesized via crosslinking of two cysteine thiols. (mit.edu)
  • Male patient discussing the use of cysteine supplements. (livestrong.com)
  • Although you can take supplements of cysteine, it is recommended to meet the needs of this amino acid through a balanced diet . (botanical-online.com)
  • Women who are pregnant or breastfeeding should not use cysteine supplements. (lifebridgehealth.org)
  • Biohit Oyj, the Finnish company behind a cysteine chewing gum unveiled this week that could help reduce the risk of oral cancer in smokers and drinkers, is looking for partners to help realise the full potential of its technology in the supplements and food sectors. (nutraingredients.com)
  • The other potential benefits of cysteine consumption, whether naturally through diet or through supplements, is a long list. (wisegeek.com)
  • L-cysteine supplementation will be discussed in the specific programs in Part Four of this book. (healthy.net)
  • However, there is insufficient evidence to assess the risks of cysteine supplementation, especially regarding metabolic acidosis, which has been reported during the first two weeks of cysteine chloride administration. (cochrane.org)
  • Five small trials evaluated short-term cysteine supplementation of cysteine-free PN. (cochrane.org)
  • Nitrogen retention was significantly increased by cysteine supplementation (4 trials) (WMD 31.8 mg/kg/day, 95% confidence interval +8.2, +55.4, n = 95, including 73 preterm infants). (cochrane.org)
  • Using the same model system, the bio-antimutagenic effect of the sulfhydryl compound L-cysteine against DIHQ was established. (greenmedinfo.com)
  • When combined with parenteral amino acid solutions, cysteine is relatively unstable. (drugs.com)
  • Premier Inc . ( PINC ), through its ProvideGx ™ program, is now supplying cysteine hydrochloride injection to providers, a critical drug for pediatric and adult patients that require total parenteral nutrition (TPN). (yahoo.com)
  • Cysteine hydrochloride is indicated to meet the nutritional needs of newborn infants requiring total parenteral nutrition (TPN), as well as adult and pediatric patients with severe liver disease who may require TPN. (yahoo.com)
  • The cysteine thiol group is nucleophilic and easily oxidized. (wikipedia.org)
  • First, through a nucleophilic aromatic substitution (SNAr) mechanism, fluorinated aromatic reagents are used for the regioselective arylation of a single cysteine in the presence of many. (mit.edu)
  • American Regent has L-cysteine hydrochloride injection on back order due to manufacturing delays. (drugs.com)
  • American Regent has L-cysteine hydrochloride injection 10 mL and 50 mL vials on long-term back order and the company cannot estimate a release date. (drugs.com)
  • This FDA-approved New Drug Application (NDA) for cysteine hydrochloride injection is held by Exela Pharma Sciences, LLC, a U.S.-based manufacturer. (yahoo.com)
  • Current supplies of cysteine hydrochloride injection are imported from Canada under special FDA rules that allow shortage drugs to be sourced abroad if no domestic supplies are available. (yahoo.com)
  • This partnership is expected to allow Premier members to have uninterrupted access to the only domestic, FDA-approved version of cysteine hydrochloride injection - a first in the industry," said Premier's President, Michael J. Alkire. (yahoo.com)
  • Inhibition of Leishmania cysteine protease activity was accompanied by defects in the parasite's lysosome/endosome compartment resembling those seen in lysosomal storage diseases. (pnas.org)
  • In studies with Leishmania mexicana , elimination of selected cysteine protease genes by homologous recombination showed that null mutants of the cpL gene array designated "cpb" had reduced virulence in highly susceptible BALB/c mice, and they produced no lesions at all in C57BL/6 or CBA/Ca mice ( 3 , 4 ). (pnas.org)
  • Here we report on palmitoylation of bovine opsin in COS-1 cells following expression of the synthetic wild-type opsin gene and several of its cysteine mutants in the presence of [3H]palmitic acid. (pnas.org)
  • A gene on chromosome 4q34 that encodes a so-called effector caspase belonging to the cysteine-aspartic acid protease (caspase) family which, once activated by proteolytic processing, plays a central role in the execution phase of apoptosis, as well as various stages of embryological development. (thefreedictionary.com)
  • But Cysteine provides excellent and reversible reducing conditions while working with oxidoreductases. (bio.net)
  • We have identified both reversible and irreversible cysteine protease inhibitors that meet these criteria. (pnas.org)
  • Gu L, Robinson RA (2016) Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases. (springer.com)
  • An N -acetyl- L -amino acid that is the N -acetylated derivative of the natural amino acid L -cysteine. (ebi.ac.uk)
  • Its derivative, N-acetyl-L-cysteine is used as a dietary supplement. (fishersci.ca)
  • Any L-cysteine derivative obtained by conversion of the thiol group into a sulfide. (mcw.edu)
  • In this work, we discuss the current knowledge on connexin redox regulation and we propose the hypothesis that extracellular cysteines could be important for sensing changes in redox potential. (frontiersin.org)
  • Our research shows a direct mechanistic link between the oxidative stress biomarker (cysteine redox potential) and pro-inflammatory cytokines, which have been linked to multiple age-related and chronic diseases," says Jones. (thaindian.com)
  • Our group and others have already established that cysteine redox potential is oxidized with aging and with a number of health risk factors. (thaindian.com)
  • This suggests that one could target cysteine redox potential as a means to decrease chronic proinflammatory signaling as an intervention for age-related diseases and for the acute inflammation of sepsis or lung injury," he adds. (thaindian.com)
  • In this step, a fragment of the substrate is released with an amine terminus, the histidine residue in the protease is restored to its deprotonated form, and a thioester intermediate linking the new carboxy-terminus of the substrate to the cysteine thiol is formed. (wikipedia.org)
  • During the study, the researchers used a mouse model of sepsis to test the effects of dietary cysteine on reducing inflammation. (thaindian.com)
  • In a subsequent study of healthy, but overweight adult volunteers with an average age of 62, IL-1 beta levels also rose and fell in association with the amount of dietary cysteine. (thaindian.com)
  • Cysteine delivered to the stomach in BioCyst capsults forms a stable compound with carcinogenic acetaldehyde, making the acetaldehyde inactive. (nutraingredients.com)
  • These people argue that cysteine helps the body transform acetaldehyde, which is a product of the consumption of alcohol, into a less-harmful substance called acetic acid. (wisegeek.com)
  • Eggs, he says, are a good source of cysteine , an amino acid that helps the liver break down alcohol faster. (dictionary.com)
  • Cysteine is said to help protect the liver from alcohol and prevent hangovers. (lifebridgehealth.org)
  • Although no conclusive lab testing has proven the benefits of cysteine when it comes to the consumption of alcohol, some claim it can cure a person's hangover or protect the liver from damage normally caused by consuming large quantities of alcohol. (wisegeek.com)
  • This reaction between the toxic metabolite of acetaminophen, N-acetyl-p-benzoquinoneimine, and liver cells is stopped by N-acetyl-L-cysteine binding to the toxic part of acetaminophen instead. (reference.com)
  • Cysteine may decrease the chance of liver disease and brittle bones. (cochrane.org)
  • Although classified as a non essential amino acid , in rare cases, cysteine may be essential for infants, the elderly, and individuals with certain metabolic diseases or who suffer from malabsorption syndromes . (wikipedia.org)
  • Cysteine may be considered an essential amino acid in infants. (drugs.com)
  • Cysteine is a non-essential amino acid that can be found in eggs, pork, oats, red peppers and several other food sources. (wisegeek.com)