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DisulfidesSulfhydryl CompoundsGlutaredoxinsGlutathione DisulfideCysteineDithiothreitolProtein Disulfide-IsomerasesCystamineOxidation-ReductionCystineGlutathioneThioredoxinsDithionitrobenzoic AcidMalate Dehydrogenase (NADP+)Protein Disulfide Reductase (Glutathione)IodoacetamideProtein FoldingDiamideOxidoreductasesHeterocyclic Compounds, Bridged-RingOxidoreductases Acting on Sulfur Group DonorsProtein ConformationDithioerythritolReceptors, Amino AcidMercaptoethanolAmino Acid SequenceIsomerasesSulfidesKineticsThioredoxin-Disulfide ReductaseSulfhydryl ReagentsIodoacetatesMolecular Sequence DataIodoacetic AcidMercaptoethylaminesIodobenzoatesAlkylationEthylmaleimideConalbuminSulfinic AcidsChromatography, High Pressure LiquidPhosphinesRibonuclease, PancreaticModels, MolecularPantetheineSucralfateCobra Neurotoxin ProteinsReducing AgentsSperm MaturationProtein EngineeringEscherichia coliProtein Structure, SecondaryCatalysisRecombinant ProteinsProtein DenaturationMass SpectrometryNeurophysinsRhodiumStructure-Activity RelationshipS-NitrosothiolsProteinsProtein Structure, TertiarySodium HydroxideMutagenesis, Site-DirectedMacromolecular SubstancesMolecular StructureCattlePeptide MappingProtein BindingGlutathione ReductaseAprotininBinding SitesHydrogen-Ion ConcentrationTrypsin InhibitorsPeptide FragmentsNADH, NADPH OxidoreductasesDimerizationPeptidesCrystallography, X-RayElectrophoresis, Polyacrylamide GelCross-Linking ReagentsHydrogen PeroxideTrypsinMolecular ChaperonesModels, ChemicalHydrochloric AcidIsomerismPeroxiredoxinsGuanidineEndoplasmic ReticulumSubstrate SpecificityAmino Acid SubstitutionMolecular WeightNADPCircular DichroismMalate DehydrogenaseCatalytic DomainMuramidaseModels, StructuralStomach Diseases
Disulfides
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Sulfhydryl Compounds
Compounds containing the -SH radical.
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.
Glutathione Disulfide
A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.
Cysteine
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
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.
Protein Disulfide-Isomerases
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
Cystamine
A radiation-protective agent that interferes with sulfhydryl enzymes. It may also protect against carbon tetrachloride liver damage.
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).
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.
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.
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.
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.
Malate Dehydrogenase (NADP+)
Protein Disulfide Reductase (Glutathione)
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.
Iodoacetamide
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.
Protein Folding
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Diamide
A sulfhydryl reagent which oxidizes sulfhydryl groups to the disulfide form. It is a radiation-sensitizing agent of anoxic bacterial and mammalian cells.
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)
Heterocyclic Compounds, Bridged-Ring
A class of organic compounds which contain two rings that share a pair of bridgehead carbon atoms.
Oxidoreductases Acting on Sulfur Group Donors
Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.
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).
Dithioerythritol
A compound that, along with its isomer, Cleland's reagent (DITHIOTHREITOL), is used for the protection of sulfhydryl groups against oxidation to disulfides and for the reduction of disulfides to sulfhydryl groups.
Receptors, Amino Acid
Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.
Mercaptoethanol
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.
Isomerases
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Sulfides
Chemical groups containing the covalent sulfur bonds -S-. The sulfur atom can be bound to inorganic or organic moieties.
Kinetics
The rate dynamics in chemical or physical systems.
Thioredoxin-Disulfide Reductase
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5
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.
Iodoacetates
Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research.
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.
Iodoacetic Acid
A derivative of ACETIC ACID that contains one IODINE atom attached to its methyl group.
Mercaptoethylamines
Iodobenzoates
Benzoic acid esters or salts substituted with one or more iodine atoms.
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.
Ethylmaleimide
A sulfhydryl reagent that is widely used in experimental biochemical studies.
Conalbumin
A glycoprotein albumin from hen's egg white with strong iron-binding affinity.
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)
Chromatography, High Pressure Liquid
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Phosphines
Inorganic or organic compounds derived from phosphine (PH3) by the replacement of H atoms. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Ribonuclease, Pancreatic
An enzyme that catalyzes the endonucleolytic cleavage of pancreatic ribonucleic acids to 3'-phosphomono- and oligonucleotides ending in cytidylic or uridylic acids with 2',3'-cyclic phosphate intermediates. EC 3.1.27.5.
Models, Molecular
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Pantetheine
An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.
Sucralfate
A basic aluminum complex of sulfated sucrose.
Cobra Neurotoxin Proteins
Toxins, contained in cobra (Naja) venom that block cholinergic receptors; two specific proteins have been described, the small (short, Type I) and the large (long, Type II) which also exist in other Elapid venoms.
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)
Sperm Maturation
The maturing process of SPERMATOZOA after leaving the testicular SEMINIFEROUS TUBULES. Maturation in SPERM MOTILITY and FERTILITY takes place in the EPIDIDYMIS as the sperm migrate from caput epididymis to cauda epididymis.
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.
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.
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.
Catalysis
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Recombinant Proteins
Proteins prepared by recombinant DNA technology.
Protein Denaturation
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
Mass Spectrometry
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Neurophysins
Carrier proteins for OXYTOCIN and VASOPRESSIN. They are polypeptides of about 10-kDa, synthesized in the HYPOTHALAMUS. Neurophysin I is associated with oxytocin and neurophysin II is associated with vasopressin in their respective precursors and during transportation down the axons to the neurohypophysis (PITUITARY GLAND, POSTERIOR).
Rhodium
Rhodium. A hard and rare metal of the platinum group, atomic number 45, atomic weight 102.905, symbol Rh. (Dorland, 28th ed)
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.
S-Nitrosothiols
A group of organic sulfur-containing nitrites, alkyl thionitrites. S-Nitrosothiols include compounds such as S-NITROSO-N-ACETYLPENICILLAMINE and S-NITROSOGLUTATHIONE.
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.
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.
Sodium Hydroxide
A highly caustic substance that is used to neutralize acids and make sodium salts. (From Merck Index, 11th ed)
Mutagenesis, Site-Directed
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Macromolecular Substances
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
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.
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.
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.
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.
Glutathione Reductase
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.
Aprotinin
A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)
Binding Sites
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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)
Trypsin Inhibitors
Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.
Peptide Fragments
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
NADH, NADPH Oxidoreductases
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
Dimerization
The process by which two molecules of the same chemical composition form a condensation product or polymer.
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.
Crystallography, X-Ray
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Electrophoresis, Polyacrylamide Gel
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
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.
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.
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.
Molecular Chaperones
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
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.
Hydrochloric Acid
A strong corrosive acid that is commonly used as a laboratory reagent. It is formed by dissolving hydrogen chloride in water. GASTRIC ACID is the hydrochloric acid component of GASTRIC JUICE.
Isomerism
The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
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.
Guanidine
A strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant. (From Martindale, the Extra Pharmacopoeia, 30th ed and Merck Index, 12th ed) It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC.
Endoplasmic Reticulum
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 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.
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.
Molecular Weight
The sum of the weight of all the atoms in a molecule.
NADP
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
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)
Malate Dehydrogenase
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
Catalytic Domain
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Muramidase
A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.
Models, Structural
A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed)
Stomach Diseases
Pathological processes involving the STOMACH.
Cell Membrane
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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.
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).
Oxygen
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.

The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules. (1/5505)

The disulfide-bonded loop of chromogranin B (CgB), a regulated secretory protein with widespread distribution in neuroendocrine cells, is known to be essential for the sorting of CgB from the trans-Golgi network (TGN) to immature secretory granules. Here we show that this loop, when fused to the constitutively secreted protein alpha1-antitrypsin (AT), is sufficient to direct the fusion protein to secretory granules. Importantly, the sorting efficiency of the AT reporter protein bearing two loops (E2/3-AT-E2/3) is much higher compared with that of AT with a single disulfide-bonded loop. In contrast to endogenous CgB, E2/3-AT-E2/3 does not undergo Ca2+/pH-dependent aggregation in the TGN. Furthermore, the disulfide-bonded loop of CgB mediates membrane binding in the TGN and does so with 5-fold higher efficiency if two loops are present on the reporter protein. The latter finding supports the concept that under physiological conditions, aggregates of CgB are the sorted units of cargo which have multiple loops on their surface leading to high membrane binding and sorting efficiency of CgB in the TGN.  (+info)

Chaperone activity with a redox switch. (2/5505)

Hsp33, a member of a newly discovered heat shock protein family, was found to be a very potent molecular chaperone. Hsp33 is distinguished from all other known molecular chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function. In vitro and in vivo experiments suggest that Hsp33 protects cells from oxidants, leading us to conclude that we have found a protein family that plays an important role in the bacterial defense system toward oxidative stress.  (+info)

Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions. (3/5505)

Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I and IGF-II are unable to form and maintain their native disulfide bonds at redox conditions that are similar to the situation in the secretory vesicles in vivo and (ii) that the presence of protein disulfide isomerase does not overcome this problem. The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance.  (+info)

In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli. (4/5505)

We have found that the in vivo folding of periplasmic Escherichia coli Cu,Zn superoxide dismutase is assisted by DsbA, which catalyzes the efficient formation of its single disulfide bond, whose integrity is essential to ensure full catalytic activity to the enzyme. In line with these findings, we also report that the production of recombinant Xenopus laevis Cu,Zn superoxide dismutase is enhanced when the enzyme is exported in the periplasmic space or is expressed in thioredoxin reductase mutant strains. Our data show that inefficient disulfide bond oxidation in the bacterial cytoplasm inhibits Cu,Zn superoxide dismutase folding in this cellular compartment.  (+info)

Scrotal heat stress induces altered sperm chromatin structure associated with a decrease in protamine disulfide bonding in the stallion. (5/5505)

A variety of testicular insults can induce changes in the structure of spermatozoal chromatin, resulting in spermatozoal DNA that is more susceptible to acid-induced denaturation. The degree of change in the DNA can be measured using the sperm chromatin structure assay (SCSA). The SCSA measures the relative amounts of single- and double-stranded DNA after staining with the metachromatic dye, acridine orange. Here we used a stallion model (n = 4) to study the effects of scrotal heat stress on spermatozoal DNA. This model was created by insulating stallion testes for 48 h and collecting sperm daily thereafter for 60 days. Changes in the SCSA were then correlated with protamine disulfide content and protamine types and levels. Results of the SCSA indicated that the susceptibility of spermatozoal DNA to denaturation was dependent on the spermatogenic cell stage that the ejaculated sperm was in at the time of the heat stress. Spermatozoa with altered DNA had a decrease in the extent of disulfide bonding that was associated with an increase in the susceptibility of DNA to denaturation. However, there were no detectable changes in either the protamine type or level. Thus, in this model, decreased disulfide bonding is associated with an increased susceptibility of spermatozoal DNA to denaturation in the absence of protamine changes.  (+info)

An intact sperm nuclear matrix may be necessary for the mouse paternal genome to participate in embryonic development. (6/5505)

We have been interested in determining the minimally required elements in the sperm head that are necessary in order for the paternal genome to participate in embryogenesis. We used an ionic detergent, mixed alkyltrimethylammonium bromide (ATAB), plus dithiothreitol (DTT) to remove the acrosome and almost all of the perinuclear theca, leaving only the sperm nucleus morphologically intact. We also tested the stability of the sperm nuclear matrix by the ability to form nuclear halos. Sperm nuclei washed in freshly prepared 0.5% ATAB + 2 mM DTT completely decondensed when extracted with salt, but nuclei washed in the same buffer that was 1 wk old, and then extracted with salt, produced nuclear halos, indicating stable nuclear matrices. When we treated sperm heads with freshly prepared ATAB+DTT and injected them into oocytes, none of the oocytes developed into live offspring. In contrast, sperm heads treated in the same way but with 1-wk-old ATAB+DTT solution could support development of about 30% of the oocytes to live offspring. Electron microscopy demonstrated that most of the perinuclear theca had been removed in both cases. These data suggest that at least in the mouse, the only component of the spermatozoa that is crucial for participation in embryologic development is the sperm nucleus with a stable nuclear matrix.  (+info)

The internal Cys-207 of sorghum leaf NADP-malate dehydrogenase can form mixed disulphides with thioredoxin. (7/5505)

The role of the internal Cys-207 of sorghum NADP-malate dehydrogenase (NADP-MDH) in the activation of the enzyme has been investigated through the examination of the ability of this residue to form mixed disulphides with thioredoxin mutated at either of its two active-site cysteines. The h-type Chlamydomonas thioredoxin was used, because it has no additional cysteines in the primary sequence besides the active-site cysteines. Both thioredoxin mutants proved equally efficient in forming mixed disulphides with an NADP-MDH devoid of its N-terminal bridge either by truncation, or by mutation of its N-terminal cysteines. They were poorly efficient with the more compact WT oxidised NADP-MDH. Upon mutation of Cys-207, no mixed disulphide could be formed, showing that this cysteine is the only one, among the four internal cysteines, which can form mixed disulphides with thioredoxin. These experiments confirm that the opening of the N-terminal disulphide loosens the interaction between subunits, making Cys-207, located at the dimer contact area, more accessible.  (+info)

Hairpin-shaped DNA duplexes with disulfide bonds in sugar-phosphate backbone as potential DNA reagents for crosslinking with proteins. (8/5505)

Convenient approaches were described to incorporate -OP(=O)O(-)-SS-O(-)(O=)PO- bridges in hairpin-shaped DNA duplexes instead of regular phosphodiester linkages: (i) H2O2- or 2,2'-dipyridyldisulfide-mediated coupling of 3'- and 5'-thiophosphorylated oligonucleotides on complementary template and (ii) more selective template-guided autoligation of a preactivated oligonucleotide derivative with an oligomer carrying a terminal thiophosphoryl group. Dithiothreitol was found to cleave completely modified internucleotide linkage releasing starting oligonucleotides. The presence of complementary template as an intrinsic element of the molecule protects the hairpin DNA analog from spontaneous exchange of disulfide-linked oligomer fragments and makes it a good candidate for auto-crosslinking with cysteine-containing proteins.  (+info)

The Interdomain Disulfide Bond of a Homogeneous Rabbit Pneumococcal Antibody Light Chain | The Journal of ImmunologyThe Interdomain Disulfide Bond of a Homogeneous Rabbit Pneumococcal Antibody Light Chain | The Journal of Immunology
Rabbit light chain 3315, prepared from a homogeneous antipneumococcal antibody, was subjected to hydrolysis by pepsin without prior reduction and alkylation of the intrachain disulfide bonds. Gel filtration of the hydrolysate on Sephadex G-10, G-15, and G-25 and ion exchange chromatography on SP-Sephadex yielded several disulfide bridge peptides. These were fully reduced and alkylated and sequenced by Edman degradation. The peptides were located in the light chain sequence determined in independent studies from our laboratory.. The half-cystine residues in this κB rabbit chain are located at positions 23, 80, 88, 134, 171, 194, and 214. The extra disulfide bridge extends between residues 80 and 171, thus joining the variable and constant domains. This is consistent with x-ray diffraction crystallographic studies showing that the corresponding residues in human light chains are separated by a distance compatible with disulfide bond formation.. ...
http://www.jimmunol.org/content/115/5/1422
Engineering an Improved IgG4 Molecule with Reduced Disulfide Bond Heterogeneity and Increased Fab Domain Thermal Stability -...Engineering an Improved IgG4 Molecule with Reduced Disulfide Bond Heterogeneity and Increased Fab Domain Thermal Stability -...
The integrity of antibody structure, stability, and biophysical characterization are becoming increasingly important as antibodies receive increasing scrutiny from regulatory authorities. We altered the disulfide bond arrangement of an IgG4 molecule by mutation of the Cys at the N terminus of the heavy chain constant domain 1 (CH1) (Kabat position 127) to a Ser and introduction of a Cys at a variety of positions (positions 227-230) at the C terminus of CH1. An inter-LC-CH1 disulfide bond is thus formed, which mimics the disulfide bond arrangement found in an IgG1 molecule. The antibody species present in the supernatant following transient expression in Chinese hamster ovary cells were analyzed by immunoblot to investigate product homogeneity, and purified product was analyzed by a thermofluor assay to determine thermal stability. We show that the light chain can form an inter-LC-CH1 disulfide bond with a Cys when present at several positions on the upper hinge (positions 227-230) and that such ...
https://kar.kent.ac.uk/29892/
Disulfide - WikipediaDisulfide - Wikipedia
Thiolates, not thiols, attack disulfide bonds. Hence, thiol-disulfide exchange is inhibited at low pH (typically, below 8) where the protonated thiol form is favored relative to the deprotonated thiolate form. (The pKa of a typical thiol group is roughly 8.3, but can vary due to its environment.) Thiol-disulfide exchange is the principal reaction by which disulfide bonds are formed and rearranged in a protein. The rearrangement of disulfide bonds within a protein generally occurs via intra-protein thiol-disulfide exchange reactions; a thiolate group of a cysteine residue attacks one of the proteins own disulfide bonds. This process of disulfide rearrangement (known as disulfide shuffling) does not change the number of disulfide bonds within a protein, merely their location (i.e., which cysteines are bonded). Disulfide reshuffling is generally much faster than oxidation/reduction reactions, which change the number of disulfide bonds within a protein. The oxidation and reduction of protein ...
https://en.wikipedia.org/wiki/Disulfide_bond
Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium...Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium...
Correct folding and disulfide bond formation is essential for the function of many secreted proteins including bacterial toxins, and their formation is facilitated by d is ulfide b ond forming (Dsb) oxidoreductase proteins, which usually contain a conserved thioredoxin (TRX) fold [1]. Protein disulfide bonds can serve structural roles, and thus are often buried in the core of a protein. However, in the case of Dsb proteins, partially exposed disulfide bonds in the TRX-fold CXXC motif have catalytic roles in protein folding, electron transport and bioenergetics in a variety of organisms [2, 3].. The Dsb proteins of Escherichia coli are the best characterized, and reside in its periplasm to correctly fold disulfide bond containing secreted and cell-wall proteins [4]. E. coli DsbA (Ec-DsbA) catalyzes the oxidation of disulfide bonds in reduced, unfolded proteins [5, 6], and is then re-oxidized by ubiquinone via E. coli DsbB (Ec-DsbB), an inner membrane transmembrane protein, which in turn is ...
https://bmcstructbiol.biomedcentral.com/articles/10.1186/1472-6807-13-23
Impact of SCILL catalysts for the S-S coupling of thiols to disulfides - Faraday Discussions (RSC Publishing) DOI:10.1039...Impact of SCILL catalysts for the S-S coupling of thiols to disulfides - Faraday Discussions (RSC Publishing) DOI:10.1039...
Disulfide bonds play an important role in the folding and stability of many proteins.1-4 For example, S-S bonds are formed following the oxidative folding process between the thiol groups of cysteine, which can also hold different subunits of larger protein complexes together such as antibodies.5 These are also found in keratin in hair.6 In the refining of crude oil, oxidative desulfurization (ODS) of thiols forms the corresponding disulfides7 which then undergo further oxidation to thiosulfinates, disulfoxides, sulfinyl sulfones or disulfones. Disulfides are also used as vulcanizing agents for rubber8 and elastomers,9 in drugs,10 and in the design of rechargeable lithium batteries,11 for example. Traditionally, disulfides are produced through the oxidation of thiols in the presence of homogeneous catalysts including tributylammonium chlorochromate,12 metal phthalocyanines,13 cobalt(II) phthalocyanine tetrasodium sulfonate attached to poly(vinylamine),14 porphyrazinatocobalt(II) complex15 and ...
http://pubs.rsc.org/en/content/articlehtml/2018/fd/c7fd00159b
Refolding by disulfide isomerization - the mixed disulfide between ribonuclease t-1 and glutathione as a model refolding...Refolding by disulfide isomerization - the mixed disulfide between ribonuclease t-1 and glutathione as a model refolding...
Protein folding, associated with isomerization of disulfide bonds, was studied using the mixed disulfide between glutathione and reduced ribonuclease T-1 (GS-RNase T-1) as a stable soluble and homogenous starting material; conditions were selected to model those within the lumen of the endoplasmic reticulum where native disulfide bonds are formed in protein biosynthesis, Folding was initiated by addition of free glutathione (GSH +/- GSSG) to promote thiol-disulfide interchange and was monitored by intrinsic protein fluorescence, appearance of native ribonuclease activity, HPLC, and nonreducing SDS-PAGE, All the analyses indicated that native RNase T-1 was recovered in high yield in a variety of redox conditions, Appearance of native activity followed first-order kinetics; kinetic analysis of the intrinsic fluorescence changes indicated an additional rapid process in some conditions, interpreted as the formation of a nonnative intermediate state. Analysis by HPLC and SDS-PAGE also indicated the ...
https://kar.kent.ac.uk/19005/
Mitochondrial intermembrane space import and assembly protein 40Mitochondrial intermembrane space import and assembly protein 40
Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17 or MICU1 (PubMed:16185709, PubMed:26387864, PubMed:19182799, PubMed:21059946, PubMed:23186364). Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS) (PubMed:16185709, PubMed:19182799, PubMed:21059946). Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria (PubMed:16185709, PubMed:19182799, PubMed:21059946). The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS (PubMed:16185709, PubMed:19182799, PubMed:21059946). Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay system (PubMed:23186364). Mediates formation of disulfide bond in MICU1 ...
https://pharos.nih.gov/idg/targets/Q8N4Q1
Injectable self-healing hydrogels formed via thiol/disulfide exchange of thiol functionalized F127 and dithiolane modified PEG ...Injectable self-healing hydrogels formed via thiol/disulfide exchange of thiol functionalized F127 and dithiolane modified PEG ...
Injectable self-healing hydrogels have found broad applications in drug delivery, tissue engineering and controlled 3D cell culture. Recently, cyclic disulfides were found to be useful in cross-linking and stabilizing liposomes by disulfide exchange polymerization, benefiting from the enhanced reactivity of
http://pubs.rsc.org/en/content/articlelanding/2017/tb/c7tb00746a
TCDB » SEARCHTCDB » SEARCH
5.A.1 The Disulfide Bond Oxidoreductase D (DsbD) Family The best characterized member of the DsbD family is DsbD of E. coli (Katzen and Beckwith, 2000; Krupp et al., 2001). The DsbD protein is membrane-embedded with a putative N-terminal TMS plus 8 additional TMSs. The smallest homologues (190 aas with 6 putative TMSs) are found in archaea while the largest are found in both Gram-negative bacteria (758 aas with 9 putative TMSs) and Gram-positive bacteria (695 aas with 6 putative TMSs). In the E. coli DsbD system, electrons are transferred from NADPH in the cytoplasm to periplasmic dithiol/disulfide-containing proteins via an electron transfer chain that sequentially involves NADPH, thioredoxin reductase (TrxB), present in the cytoplasm, thioredoxin (TrxA), also in the cytoplasm, DsbD, the integral membrane constituent of the system, and the periplasmic electron acceptors, DsbC, DsbE (CcmG) and DsbG. All of these last three proteins can donate electrons to oxidized disulfide-containing proteins ...
http://www.tcdb.org/search/result.php?tc=5.A.1
The Salmonella SPI1 Type Three Secretion System Responds to Periplasmic Disulfide Bond Status via the Flagellar Apparatus and...The Salmonella SPI1 Type Three Secretion System Responds to Periplasmic Disulfide Bond Status via the Flagellar Apparatus and...
The inability to form disulfide bonds in the periplasm affects the assembly of complex machinery in the cell envelope. Indeed, loss of DsbA, the primary disulfide bond oxidase in the periplasm, has been shown to block type III secretion in serovar Typhimurium, S. flexneri, P. aeruginosa, and Y. pestis and motility in E. coli and serovar Typhimurium (10, 18, 28, 34, 48, 64) (Fig. 5). But does loss of function indicate a simple defect in assembly? Here we have shown that, in addition to a structural or functional defect conferred by mutations in dsbA, there is a distinct regulatory response. The SPI1 T3SS regulatory circuit responds to the state of disulfide bonds in the periplasm and adjusts expression of the machine components. Our results suggest that loss of DsbA affects SPI1 through four distinct yet overlapping pathways (Fig. 1). First, DsbA inhibits activation of the RcsCDB system (45). Activation of RcsCDB in a dsbA mutant inhibits hilA expression (50) through HilD. Activated RcsCDB also ...
https://jb.asm.org/content/190/1/87?ijkey=e497254db47cba26c05146d5061b75a6e5130fd5&keytype2=tf_ipsecsha
Antibodies - The School of Biomedical Sciences Wiki
structure and there are five types. It is these heavy chains which enable antibodies to be separated into the five classes (or isotypes) of immunoglobins; IgG, IgA, IgD, IgM and IgE. The way in which the two heavy chains are connected to one another is through disulfide bonds, they are then connected to a light chain by disulfide bonds as well. This therefore creates two identical antigen-binding sites[4]. The regions of the heavy chain includes three constant domains, which are the same for all antibodies, and the one variable domain. The light chains are also composed of a constant domain and a variable domain. The variable regions of the antibodies are where the antigen binding site is located and the constant domain is responsible for the outcome of the antigen[5]. The Fc region is the part of the antibody that binds to cell surface receptors on cells such as macrophages. Finally, the Fab region is primarily known as the location for the antigen binding site[6]. The domains of antibodies are ...
https://teaching.ncl.ac.uk/bms/wiki/index.php?title=Antibodies&diff=prev&oldid=17492
Antibodies - The School of Biomedical Sciences Wiki
structure and there are five types. It is these heavy chains which enable antibodies to be separated into the five classes (or isotypes) of immunoglobins; IgG, IgA, IgD, IgM and IgE. The way in which the two heavy chains are connected to one another is through disulfide bonds, they are then connected to a light chain by disulfide bonds as well. This therefore creates two identical antigen-binding sites[4]. The regions of the heavy chain includes three constant domains, which are the same for all antibodies, and the one variable domain. The light chains are also composed of a constant domain and a variable domain. The variable regions of the antibodies are where the antigen binding site is located and the constant domain is responsible for the outcome of the antigen[5]. The Fc region is the part of the antibody that binds to cell surface receptors on cells such as macrophages. Finally, the Fab region is primarily known as the location for the antigen binding site[6]. The domains of antibodies are ...
https://teaching.ncl.ac.uk/bms/wiki/index.php?title=Antibodies&oldid=17492
V-PLEX Human IL-13 Kit | Meso Scale DiscoveryV-PLEX Human IL-13 Kit | Meso Scale Discovery
Human interleukin-12p70 (IL-13) is a 15.8 kDa, glycosylated monomeric cytokine with two internal disulfide bonds. It is secreted by a variety of immune cells. IL-13 is involved in a number of biological processes, such as positive regulation of B-cell proliferation, macrophage activation, immunoglobulin production, protein secretion, and phosphorylation of Stat6 protein. IL-13 initially interacts with IL-13 Rα1 to form a low-affinity complex. The formation of this complex triggers association with IL-4 Rα to form a high-affinity complex that also functions as the type 2 IL-4 receptor complex. IL-13 also binds with high affinity to IL-13 Rα2, which is expressed as a soluble intracellular protein, and also on the cell surface. It is involved in a number of disorders including allergic rhinitis, inflammatory bowel disease, and colorectal cancer. The Human IL-13 Kit provides the assay-specific components for the quantitative determination of endogenous IL-13 in human urine, serum, plasma, and ...
https://www.mesoscale.com/en/products/v-plex-human-il-13-kit-k151odd/
Determination of transmembrane protein structure by disulfide cross-linking: The Escherichia coli Tar receptor - CaltechAUTHORSDetermination of transmembrane protein structure by disulfide cross-linking: The Escherichia coli Tar receptor - CaltechAUTHORS
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 ...
https://authors.library.caltech.edu/9212/
U-PLEX Human IL-13 Assay | Meso Scale DiscoveryU-PLEX Human IL-13 Assay | Meso Scale Discovery
MSD offers a range of individual assays utilizing U-PLEX Antibody Sets that provide a rapid and convenient method for measuring biomarkers in complex matrices. The individual assays are offered on MSD GOLD Small Spot Streptavidin Plates and use the same antibody sets and diluents as the U-PLEX multiplex assays. This allows for efficient transfer between the individual assay and a higher throughput multiplex configuration. Typical of assays developed on the MSD platform, the individual assays have high sensitivity, excellent precision, provide up to five-logs of linear dynamic range, and require minimal sample volume. Interleukin-13 (IL-13) is a glycosylated immunoregulatory cytokine with two internal disulfide bonds. IL-13 is secreted by a variety of immune cells. IL-13 is involved in a number of biological processes, such as positive regulation of B-cell proliferation, macrophage activation, immunoglobulin production, protein secretion, and phosphorylation of Stat6 protein. IL-13 initially ...
https://www.mesoscale.com/en/products/u-plex-human-il-13-assay-k151ubk/
Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY ...Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY ...
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 ...
http://jcb.rupress.org/content/169/2/219
RCSB PDB - 1MXP: Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB Literature Report PageRCSB PDB - 1MXP: Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB Literature Report Page
1MXP: A New Level of Conotoxin Diversity, a Non-native Disulfide Bond Connectivity in alpha -Conotoxin AuIB Reduces Structural Definition but Increases Biological Activity.
http://www.rcsb.org/pdb/explore/litView.do?structureId=1MXP
PEROXIDASE - CAS - 9003-99-0 (02195371) - MP BiomedicalsPEROXIDASE - CAS - 9003-99-0 (02195371) - MP Biomedicals
Horseradish peroxidase is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. It is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. HRP labeled immunoglobulins are used as probes for the demonstration of tissue antigens and in enzyme immunoassay (EIA) systems for determination of soluble and insoluble antigens. HRP is the most desired label for antibodies since it is the smallest and most stable of the three most popular enzyme labels (HRP, alkaline phosphatase, and B-galactosidase) and its glycosylation leads to lower non-specific binding. It is also useful for tracing neural connections. These include motor and sensory innervation of peripheral organs, and connections of peripheral nerves, ganglia and individual dorsal roots. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed ...
http://www.mpbio.com/product.php?pid=02195371&country=223
Disruption of disulfide restriction at integrin knees induces activation and ligand-independent signaling of α4β7 | Journal of...Disruption of disulfide restriction at integrin knees induces activation and ligand-independent signaling of α4β7 | Journal of...
A major finding of our present study is that integrin α4β7 can be activated by selectively breaking two conserved disulfide bonds, α4C589-C594 and β7C494-C526, located at the knees of integrin. Interestingly, integrin activated by this mechanism has a unique active conformation that is different from the global conformation induced by Mn2+ stimulation. In addition, activated α4β7 integrin can spontaneously cluster on the cell membrane and trigger integrin outside-in signaling independent of ligand binding.. All integrins contain a large number of disulfide bonds that are generally believed to facilitate protein folding and stabilize three-dimensional structures (Calvete et al., 1991). The two disulfide bonds at the knees of integrin α4β7 are exposed to solution, making them easily accessible to reducing agents. In this study, these two disulfide bonds were selectively reduced by 0.1 mM DTT, which induced the activation of integrin α4β7 and triggered outside-in signaling. Accumulating ...
http://jcs.biologists.org/content/126/21/5030
Inhibiting rotavirus infection by membrane-impermeant thiol/disulfide exchange blockers and antibodies against protein...Inhibiting rotavirus infection by membrane-impermeant thiol/disulfide exchange blockers and antibodies against protein...
Sigma-Aldrich offers abstracts and full-text articles by [Martha N Calderon, Carlos A Guerrero, Orlando Acosta, Susana Lopez, Carlos F Arias].
https://www.sigmaaldrich.com/catalog/papers/22398681
A Second Disulfide Bridge from the N-Terminal Domain to Extracellular Loop 2 Dampens Receptor Activity in GPR39 †A Second Disulfide Bridge from the N-Terminal Domain to Extracellular Loop 2 Dampens Receptor Activity in GPR39 †
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https://www.infona.pl/resource/bwmeta1.element.acs-doi-10_1021_bi8005016
Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro. - Walter Lab
Immunoglobulin heavy-chain binding protein (BiP, GRP-78) associates tightly in the endoplasmic reticulum (ER) with newly synthesized proteins that are incompletely assembled, have mutant structures, or are incorrectly glycosylated. The function of BiP has been suggested to be to prevent secretion of incorrectly folded or incompletely assembled protein, to promote folding or assembly of proteins, or to solubilize protein aggregates within the ER lumen. Here we examine the interaction of BiP with newly synthesized polypeptides in an in vitro protein translation-translocation system. We find that BiP forms tight complexes with nonglycosylated yeast invertase and incorrectly disulphide-bonded prolactin, but does not associate detectably with either glycosylated invertase or correctly disulphide-bonded prolactin. Moreover, BiP associates detectably only with completed chains of prolactin, not with chains undergoing synthesis. We conclude that BiP recognizes and binds with high affinity in vitro to ...
http://walterlab.ucsf.edu/publication/520/heavy-chain-binding-protein-recognizes-aberrant-polypeptides-translocated-in-vitro/
Oxidation state-dependent protein-protein interactions in disulfide cascades. - Oxford Neuroscience
Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms.
https://www.neuroscience.ox.ac.uk/publications/138824
SMART: EGF Lam domain annotationSMART: EGF Lam domain annotation
Laminins [(PUBMED:2404817)] are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation. They are composed of distinct but related alpha, beta and gamma chains. The three chains form a cross-shaped molecule that consist of a long arm and three short globular arms. The long arm consist of a coiled coil structure contributed by all three chains and cross-linked by interchain disulphide bonds. Beside different types of globular domains each subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines [(PUBMED:2666164)]. The tertiary structure [(PUBMED:8648630), (PUBMED:8648631)] of this domain is remotely similar in its N-terminal to that of the EGF-like module. It is known as a LE or laminin-type EGF-like domain. The number of copies of the LE domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found. A schematic ...
http://smart.embl.de/smart/do_annotation.pl?DOMAIN=EGF_Lam&START=1144&END=1188&E_VALUE=6.64e-11&TYPE=SMART&BLAST=CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPAC
SMART: EGF Lam domain annotationSMART: EGF Lam domain annotation
Laminins [(PUBMED:2404817)] are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation. They are composed of distinct but related alpha, beta and gamma chains. The three chains form a cross-shaped molecule that consist of a long arm and three short globular arms. The long arm consist of a coiled coil structure contributed by all three chains and cross-linked by interchain disulphide bonds. Beside different types of globular domains each subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines [(PUBMED:2666164)]. The tertiary structure [(PUBMED:8648630), (PUBMED:8648631)] of this domain is remotely similar in its N-terminal to that of the EGF-like module. It is known as a LE or laminin-type EGF-like domain. The number of copies of the LE domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found. A schematic ...
http://smart.embl.de/smart/do_annotation.pl?DOMAIN=EGF_Lam&START=376&END=425&E_VALUE=5.56e-13&TYPE=SMART&BLAST=CECDPDGAVQGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFANPKGC
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch. - PubMed - NCBIIntermolecular disulfide bond to modulate protein function as a redox-sensing switch. - PubMed - NCBI
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
https://www.ncbi.nlm.nih.gov/pubmed/20177947?dopt=Abstract
Publication : USDA ARSPublication : USDA ARS
Citation: Meng, Y., Moscou, M., Wise, R.P. 2008. Blufensin1 Negatively Impacts Basal Defense in Response to Barley Powdery Mildew. Plant Physiology. 149(1):271-285. Interpretive Summary: Plant diseases are among the greatest deterrents to crop production worldwide. Pathogenic fungi, viruses, bacteria, insects, and nematodes impact agronomic and horticultural crops, as well as commercial and recreational forests. ARS researchers have isolated a novel regulator of disease defense. The new monocot-specific gene encodes a family of small cysteine-rich peptides, designated blufensins. BLUFENSIN1 (BLN1) is highly induced during infection by pathogenic fungi and contains both structural and sequence similarities to knottins, a diverse family of small disulfide-rich proteins characterized by a unique disulfide through disulfide knot. This discovery, also supported by the National Science Foundation-Plant Genome Research Program, establishes a previously unrecognized role for small peptides as negative ...
https://www.ars.usda.gov/research/publications/publication/?seqNo115=238538
Sephiroth 20140618 - Disulfide Connectivity PredictionSephiroth 20140618 - Disulfide Connectivity Prediction
Sephiroth 20140618 :: DESCRIPTION Sephiroth is a disulfide connectivity pattern predictor based on evolutionary information retrieved from Multiple Sequence Alignments (MSAs). ::DEVELOPER (IB)² - Interuniver
http://www.mybiosoftware.com/sephiroth-20140618-disulfide-connectivity-prediction.html
Cyclic Peptides BrochureCyclic Peptides Brochure
Disulfide bridges are an important structural element in many proteins and peptides. This brochure is a guideline how to plan and execute the synthesis of peptides with one or several disulfide bridges.
https://www.iris-biotech.de/cyclic-peptides-brochure
RCSB PDB for 1MDKRCSB PDB for 1MDK
1MDK: Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.
http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=1MDK
Journal:JBSD:39 - Proteopedia, life in 3DJournal:JBSD:39 - Proteopedia, life in 3D
colored in yellow) [6] [7] [8] [9]. One structural feature of Pin-II IRD is a disordered loop with triple stranded β sheet scaffold. The disordered solvent exposed reactive loop is anchored by the four conserved disulfide bonds (C4-C41, C7-C25, C8-C37 and C14-C50) [10] [11]. Among the four disulfide bonds, C8-C37 has been found to be very crucial for maintaining active conformation, whereas C4-C41 has an important role in maintaining the flexibility of the reactive loop [12]. Thus, any selective loss of disulfide bond is expected to have evolutionary significance leading to functional differentiation of inhibitors [13]. [A] Functionality: To assess the effect of aa variations on activity and structural stability different biochemical studies and 20 ns MD simulations was performed on IRD structures. Inhibition kinetic studies displayed a sigmoidal pattern with increasing concentrations of the inhibitors suggesting reversible and competitive inhibition with tight binding. IRD-9 turned out to be a ...
http://proteopedia.org/wiki/index.php/Journal:JBSD:39
Rosetta: core::scoring::disulfides::CentroidDisulfideNeighborIterator Class ReferenceRosetta: core::scoring::disulfides::CentroidDisulfideNeighborIterator Class Reference
An iterator over the disulfide bonds a residue forms. When scoring a pose, a long range energy container must be able to iterate over all the residues which interact with a particular residue. For disulfide bonds, this is either zero or one items depending on whether the residue specified forms a disulfide bond or not.. ...
https://www.rosettacommons.org/manuals/latest/core+protocols/d0/d94/classcore_1_1scoring_1_1disulfides_1_1_centroid_disulfide_neighbor_iterator.html
MHC molecules lead many lives | EMBO ReportsMHC molecules lead many lives | EMBO Reports
The meeting was introduced by P. Pontarotti (Marseille, France), who discussed the evolutionary genetics of the MHC based on the ideas of gene co‐option and exon shuffling as the drivers of new functions for existing structures. These ideas about the evolution of the MHC suggest that conserved regions brought into new structures could retain their old (binding) functions. N. Bulleid (Manchester, UK) introduced the topic of MHC class I biosynthesis, describing a semi‐permeable cell system with an intact endoplasmic reticulum that allowed him to address the timing and partners involved in the formation of disulphide bonds between MHC class I and endoplasmic reticulum molecules. He also emphasized the role of the endoplasmic reticulum redox environment and the importance of a transmembrane cysteine residue in associating nascent class I molecules with their appropriate partners. This talk connected to later talks that highlighted misfolding and aberrant disulphide‐bond formation in disease. ...
http://embor.embopress.org/content/10/1/30
Current Price Of The Bond Assignment | Homework For You - MyHomeworkWritersCurrent Price Of The Bond Assignment | Homework For You - MyHomeworkWriters
1. Consider an annual coupon bond with a face value of $1000, annual coupon rate of 7.5%, three years to maturity and initial YTM of y = 0.091. (a) Compute
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Dollar Price Of The Bond Assignment | Homework For You - MyHomeworkWritersDollar Price Of The Bond Assignment | Homework For You - MyHomeworkWriters
5. Union Local School District has bonds outstanding with a coupon rate of 4% paid semiannually (8%, annually) and 20 years to maturity. The yield to maturity
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non-reductive gel to check the disulfide bond - Protein and Proteomicsnon-reductive gel to check the disulfide bond - Protein and Proteomics
I didnt even use oxidative environment to trigger disulfide bond formation. Only 1xPBS incubation for 30 min at room temperature, then I saw the dimer on western blot.....Of course this dimer also appears in oxidative enviroment group, but since I can get it using PBS, why bother using oxidative agents?....Afterwards I found out that this dimer doesnt break at RT with DTT or ME, and does break when boiling without DTT ...
http://www.protocol-online.org/biology-forums/posts/18824more1.html
KAKEN - Research Projects | Bond Engineering at Nano-Interfaces using Nanoparticle Plasmas (KAKENHI-PLANNED-21110005)KAKEN - Research Projects | Bond Engineering at Nano-Interfaces using Nanoparticle Plasmas (KAKENHI-PLANNED-21110005)
Principal Investigator：SHIRATANI Masaharu, Project Period (FY)：2009-07-23 - 2014-03-31, Research Category：Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area), Project Area：Creation of Science of Plasma Nano-Interface Interactions
https://kaken.nii.ac.jp/grant/KAKENHI-PLANNED-21110005/
Labile disulfide bonds are common at the leucocyte cell surface - Oxford Neuroscience
We use cookies to ensure that we give you the best experience on our website. If you click Continue well assume that you are happy to receive all cookies and you wont see this message again. Click Find out more for information on how to change your cookie settings ...
https://www.neuroscience.ox.ac.uk/publications/228587
H-Cys-ala-oh)2,(disulfide bond) - Alfa ChemistryH-Cys-ala-oh)2,(disulfide bond) - Alfa Chemistry
(H-Cys-ala-oh)2,(disulfide bond)/ACM20898219 can be provided in Alfa Chemistry. We are dedicated to provide our customers the best products and services.
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H-Ala-cys-ser-ser-ser-pro-ser-lys-his-cys-gly-oh,(disulfide bond) - Alfa ChemistryH-Ala-cys-ser-ser-ser-pro-ser-lys-his-cys-gly-oh,(disulfide bond) - Alfa Chemistry
H-Ala-cys-ser-ser-ser-pro-ser-lys-his-cys-gly-oh,(disulfide bond)/ACM888486235 can be provided in Alfa Chemistry. We are dedicated to provide our customers the best products and services.
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Which statement is true? A. a molecule having a covalent bond can be ionic B. a molecule having a covalent bond is always polar...
✅ Question: Which statement is true? A. a molecule having a covalent bond can be ionic B. a molecule having a covalent bond is always polar C. a molecule having a covalent bond may be polar or nonpolar D. a molecule having a covalent bond i =s always nonpolar
https://www.studyhawks.com/question/what-is-the-difference-between-a-paraphrase-and-a-summary-a-a-summary-restates-the-same-information-in-a-different-way-whereas-a-paraphrase-only-r-851266/
Sydney Research Online: Large-scale capture of peptides containing reversibly oxidized cysteines by thiol-disulfide exchange...
This work has been made available to the staff and students of the University of Sydney for the purposes of research and study only. It constitutes material that is held by the University for the purposes of reporting for HERDC and the ERA. This work may not be downloaded, copied and distributed to any third party ...
https://sro.library.usyd.edu.au/handle/10765/95720
Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon - UCL DiscoveryRecognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon - UCL Discovery
UCL Discovery is UCLs open access repository, showcasing and providing access to UCL research outputs from all UCL disciplines.
http://discovery.ucl.ac.uk/1371748/
Glutathione | Profiles RNSGlutathione | Profiles RNS
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 ...
https://profiles.wakehealth.edu/display/87865
ccp4bb] PhD UCL/National Institute of Biological Standards and Control (NIBSC)
The very excellent Dr Clive Metcalfe (an ex-post-doc with me) of NIBSC has a PhD project with Prof Paul Dalby at UCL looking at disulphide bond reduction in monoclonal antibodies ...
http://www.ccp4.ac.uk/jobs/msg00259.html
Enzymes - NanoTemper TechnologiesEnzymes - NanoTemper Technologies
Enzymes execute a wide variety of functions. For example, they regulate signal transduction via kinases and phosphatases. ATPases generate muscle contraction and active transport. Several enzymes can work together in a specific metabolic pathway (e.g., glycolysis). The common characteristic of enzymes is that they catalyze the chemical modification of specific substrates. Depending on their cellular sub-localization, enzymes can have various preferences toward the presence of reducing agents in biochemical assays. Redox regulation is, like phosphorylation, a covalent regulatory system that controls normal cell function. For example, mitochondria contain the most reducing compartment and are highly sensitive to oxidation. The secretory pathway contains oxidative systems which introduce disulfides into proteins for transport. As opposed to secretory mechanisms, uptake and activation through the endocytic pathway involve reduction of disulfides.. If it is necessary to keep the enzyme of interest ...
https://nanotempertech.com/nanopedia/enzymes/
A straightforward synthetic access to symmetrical glycosyl disulfides and biological evaluation thereofA straightforward synthetic access to symmetrical glycosyl disulfides and biological evaluation thereof
A free platform for explaining your research in plain language, and managing how you communicate around it - so you can understand how best to increase its impact.
https://www.growkudos.com/publications/10.1039%25252Fc1ob05619k/reader
About Us ⇓<...About Us ⇓<...
Encourage interaction within the local institute to start building relationships between students in different years of the program. Stronger bonds form when students see each other on a daily basis around campus and once they are established, these bonds can carry over between institutes ...
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B.1.427/B.1.429 variant of SARS-CoV-2 evades neutralization via disulfide bond rearrangement - crisprsocietyB.1.427/B.1.429 variant of SARS-CoV-2 evades neutralization via disulfide bond rearrangement - crisprsociety
A new paper discusses an intriguing new mechanism of immune evasion traceable to specific mutations in the B.1.427/B.1.429 variant of the severe acute…
https://thecrisprsociety.com/2021/07/07/b1427b1429-variant-of-sars-cov-2-evades-neutralization-via-disulfide-bond-rearrangement-aspx/
Double Bond Formation - DnaTube.com - Scientific Video and Animation SiteDouble Bond Formation - DnaTube.com - Scientific Video and Animation Site
Double Bond Formation video This Scientific content most probably shows video related to topic: Double Bond Formation. However in few cases, video content could be different than the title.
https://www.dnatube.com/video/5047/Double-Bond-Formation
DisulfideDisulfide
... disulfide species". A disulfide ensemble is a grouping of all disulfide species with the same number of disulfide bonds, and is ... Disulfides where the two R groups are the same are called symmetric, examples being diphenyl disulfide and dimethyl disulfide. ... This process of disulfide rearrangement (known as disulfide shuffling) does not change the number of disulfide bonds within a ... for disulfide species having one, two, etc. disulfide bonds. Thus, the (26-84) disulfide species belongs to the 1S ensemble, ...
https://en.wikipedia.org/wiki/Disulfide
Hydrogen disulfideHydrogen disulfide
... hydrogen disulfide adds to alkenes to give disulfides and thiols. The deuterated form of hydrogen disulfide DSSD, has a similar ... Hydrogen disulfide has been described as "having a severe and irritating odour" that is similar to camphor or SCl2, causing " ... Hydrogen disulfide is the inorganic compound with the formula H2S2. This hydrogen chalcogenide is a pale yellow volatile liquid ... Hydrogen disulfide can be synthesised by dissolving alkali metal or alkaline earth metal polysulfides in water. When the ...
https://en.wikipedia.org/wiki/Hydrogen_disulfide
Glutathione disulfideGlutathione disulfide
... (GSSG) is a disulfide derived from two glutathione molecules. In living cells, glutathione disulfide is ... generate glutathione disulfide through thiol-disulfide exchange with protein disulfide bonds or other low molecular mass ... Antioxidant enzymes, such as glutathione peroxidases and peroxiredoxins, generate glutathione disulfide during the reduction of ... Organic disulfides, Excitatory amino acid receptor ligands, Neurotransmitters). ...
https://en.wikipedia.org/wiki/Glutathione_disulfide
Palladium disulfidePalladium disulfide
... is a chemical compound of palladium and sulfur with the chemical formula PdS2. Palladium disulfide is ... PdS2 contains sulfur-sulfur bonds so it can be thought of as a disulfide that formally consists of S22− and Pd2+ ions. It ... Pyrite Marcasite Platinum disulfide Platinum diselenide Greenwood, Norman N.; Earnshaw, Alan (1997). Chemistry of the Elements ... then washing the crude product with carbon disulfide. This procedure yields PdS2 free of PdS. ...
https://en.wikipedia.org/wiki/Palladium_disulfide
Platinum disulfidePlatinum disulfide
... is the inorganic compound with the formula PtS2. It is a black, semiconducting solid, which is insoluble in ... S. Soled, A. Wold (1979). "Platinum Disulfide and Platinum Ditelluride". Inorganic Syntheses. 19: 49-51. doi:10.1002/ ...
https://en.wikipedia.org/wiki/Platinum_disulfide
Molybdenum disulfideMolybdenum disulfide
... (or moly) is an inorganic compound composed of molybdenum and sulfur. Its chemical formula is MoS 2. The ... Molybdenum disulfide is stable in air and attacked only by aggressive reagents. It reacts with oxygen upon heating forming ... In appearance and feel, molybdenum disulfide is similar to graphite. It is widely used as a dry lubricant because of its low ... 2 S 2Cl 2 Molybdenum disulfide is a host for formation of intercalation compounds. This behavior is relevant to its use as a ...
https://en.wikipedia.org/wiki/Molybdenum_disulfide
Diallyl disulfideDiallyl disulfide
Allyl propyl disulfide allyl disulfide Diallyl disulfide at Sigma Aldrich Block, Eric (2010). Garlic and Other Alliums: The ... Diallyl disulfide is also a starting material for the synthesis of allicin. In the food industry, diallyl disulfide is used to ... When diallyl disulfide is heated it decomposes giving a complex mixture. The carbon-sulfur bond of diallyl disulfide is 16 kcal ... By activating the TRPA1 ion channel, diallyl disulfide leads to a short-term lowering of blood pressure. Diallyl disulfide is a ...
https://en.wikipedia.org/wiki/Diallyl_disulfide
Iridium disulfideIridium disulfide
... is the binary inorganic compound with the formula IrS2. Prepared by the direct reaction of the elements, the ... Munson, Ronald A. (February 1968). "The synthesis of iridium disulfide and nickel diarsenide having the pyrite structure" (PDF ...
https://en.wikipedia.org/wiki/Iridium_disulfide
Titanium disulfideTitanium disulfide
... was chosen because it is the lightest and cheapest chalcogenide. Titanium disulfide also has the fastest ... The microstructure of the titanium disulfide greatly affects the intercalation and deintercalation kinetics. Titanium disulfide ... Titanium disulfide is a semimetal, meaning there is small overlap of the conduction band and valence band. The properties of ... Thiols and organic disulfides can be employed in place of hydrogen sulfide. A variety of other titanium sulfides are known. ...
https://en.wikipedia.org/wiki/Titanium_disulfide
Carbon disulfideCarbon disulfide
Concerns about carbon disulfide exposure have a long history.: 79 Around 1900, carbon disulfide came to be widely used in the ... Carbon disulfide production also emits carbon disulfide. As of 2004[update], about 250 g of carbon disufide is emitted per ... "Chemical profile: carbon disulfide from ICIS.com". Retrieved June 15, 2013. "Carbon Disulfide". Akzo Nobel. Archived from the ... The primary source of carbon disulfide in the environment is rayon factories. Most global carbon disulfide emissions come from ...
https://en.wikipedia.org/wiki/Carbon_disulfide
Germanium disulfideGermanium disulfide
... or Germanium(IV) sulfide is the inorganic compound with the formula GeS2. It is a white high-melting ... Germanium disulfide was the first germanium compound found by Clemens Winkler, during the analysis of argyrodite. The fact that ... Germanium disulfide is created by reacting hydrogen sulfide with germanium tetrachloride in a concentrated hydrochloric acid ... The compound is a 3-dimensional polymer, in contrast to silicon disulfide, which is a one-dimensional polymer. The Ge-S ...
https://en.wikipedia.org/wiki/Germanium_disulfide
Tungsten disulfideTungsten disulfide
... is an inorganic chemical compound composed of tungsten and sulfur with the chemical formula WS2. This ... WS2 also catalyses hydrogenation of carbon dioxide: CO2 + H2 → CO + H2O Tungsten disulfide is the first material which was ... "AMS2530A: Tungsten Disulfide Coating, Thin Lubricating Film, Binder-Less Impingement Applied". SAE International. Retrieved ... Science Daily (2013-01-016) Lalwani, Gaurav (September 2013). "Tungsten disulfide nanotubes reinforced biodegradable polymers ...
https://en.wikipedia.org/wiki/Tungsten_disulfide
Thiuram disulfideThiuram disulfide
Wang, Yu; Liao, J.-H. (1989). "Deformation Density Studies of Tetramethylthiuram Disulfide and Tetraethylthiuram Disulfide". ... Thiuram disulfides are a class of organosulfur compounds with the formula (R2NCSS)2. Many examples are known, but popular ones ... They are disulfides obtained by oxidation of the dithiocarbamates. These compounds are used in sulfur vulcanization of rubber ... Treatment of thiuram disulfides with triphenylphosphine or cyanide salts gives the thiuram sulfide: (R2NCSS)2 + PPh3 → (R2NCS) ...
https://en.wikipedia.org/wiki/Thiuram_disulfide
Uranium disulfideUranium disulfide
... is an inorganic chemical compound of uranium in oxidation state +4 and sulfur in oxidation state -2. It is ...
https://en.wikipedia.org/wiki/Uranium_disulfide
Selenium disulfideSelenium disulfide
... is available as a generic medication and over the counter. Selenium disulfide is sold as an antifungal agent ... Selenium disulfide acts as a keratolytic and antifungal agent. Selenium disulfide was approved for medical use in the United ... Selenium disulfide may also discolor metallic jewellery. Case reports of temporary diffuse hair loss with selenium disulfide ... However, hair loss has not been reported with topical selenium disulfide in several large studies. Selenium disulfide should ...
https://en.wikipedia.org/wiki/Selenium_disulfide
Silicon disulfideSilicon disulfide
... is the inorganic compound with the formula SiS2. Like silicon dioxide, this material is polymeric, but it ...
https://en.wikipedia.org/wiki/Silicon_disulfide
Dimethyl disulfideDimethyl disulfide
... (DMDS) is an organic chemical compound with the molecular formula CH3SSCH3 which is the simplest disulfide. ... Dimethyl disulfide is a widespread natural odoriferous compound emitted from many sources such as bacteria, fungi, plants and ... 2], OSHA Dimethyl Disulfide (DMDS) Archived 2011-09-29 at the Wayback Machine, Arkema, Inc. "DMDS for agricultural soil ... "Registration of Paladin and Paladin EC containing the new active ingredient dimethyl disulfide" (PDF). New York State ...
https://en.wikipedia.org/wiki/Dimethyl_disulfide
Niobium disulfideNiobium disulfide
... is the chemical compound with the formula NbS2. It is a black layered solid that can be exfoliated into ... Wikimedia Commons has media related to Niobium disulfide. Lide, D. R., ed. (2005). CRC Handbook of Chemistry and Physics (86th ...
https://en.wikipedia.org/wiki/Niobium_disulfide
Diphenyl disulfideDiphenyl disulfide
Like most organic disulfides, the C-S-S-C core of Ph2S2 is non-planar with a dihedral angle approaching 85°. Ph2S2 is mainly ... Diphenyl disulfide is usually prepared by the oxidation of thiophenol: 2 PhSH + I2 → Ph2S2 + 2 HI Hydrogen peroxide can also be ... "Diphenyl disulfide". pubchem.ncbi.nlm.nih.gov. Retrieved 13 December 2021. Ravikumar,K. S.; Kesavan, V.; Crousse, B.; Bonnet- ... Diphenyl disulfide is the chemical compound with the formula (C6H5S)2. This colorless crystalline material is often abbreviated ...
https://en.wikipedia.org/wiki/Diphenyl_disulfide
Zirconium disulfideZirconium disulfide
Like the closely related titanium disulfide, ZrS2 is prepared by heating sulfur and zirconium metal. It can be purified by ...
https://en.wikipedia.org/wiki/Zirconium_disulfide
Rhenium disulfideRhenium disulfide
... is an inorganic compound of rhenium and sulfur with the formula ReS2. It has a layered structure where atoms ... Murray, H. H.; Kelty, S. P.; Chianelli, R. R.; Day, C. S. (September 1994). "Structure of Rhenium Disulfide". Inorganic ... ISBN 3-432-87823-0. Rahman, Mohammad; Davey, Kenneth; Qiao, Shi-Zhang (2017). "Advent of 2D Rhenium Disulfide (ReS2): ...
https://en.wikipedia.org/wiki/Rhenium_disulfide
Hafnium disulfideHafnium disulfide
... is an inorganic compound of hafnium and sulfur. It is a layered dichalcogenide with the chemical formula is ... Hafnium disulfide powder can be produced by reacting hydrogen sulfide and hafnium oxides at 500-1300 °C. Wikimedia Commons has ... media related to Hafnium disulfide. Haynes, William M., ed. (2011). CRC Handbook of Chemistry and Physics (92nd ed.). Boca ...
https://en.wikipedia.org/wiki/Hafnium_disulfide
Allyl propyl disulfideAllyl propyl disulfide
... is an organosulfur compound with the chemical formula C3H5S2C3H7. It is a volatile pale-yellow liquid ... Organic disulfides, Allyl compounds, All stub articles, Organic compound stubs). ...
https://en.wikipedia.org/wiki/Allyl_propyl_disulfide
Carbon disulfide hydrolaseCarbon disulfide hydrolase
It catalyzes the hydrolysis of carbon disulfide. Carbon disulfide occurs naturally in the mudpots of volcanic solfataras. It is ... Carbon disulfide hydrolase is an enzyme with a molecular mass of 23,576 Da. The enzyme is hexadecameric. ...
https://en.wikipedia.org/wiki/Carbon_disulfide_hydrolase
Protein-disulfide reductaseProtein-disulfide reductase
In enzymology, a protein-disulfide reductase (EC 1.8.1.8) is an enzyme that catalyzes the chemical reaction protein dithiol + ... Other names in common use include protein disulphide reductase, insulin-glutathione transhydrogenase, disulfide reductase, and ... whereas its 4 products are protein disulfide, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, ... NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } protein disulfide + NAD(P)H + H+ The 3 substrates of this enzyme are protein ...
https://en.wikipedia.org/wiki/Protein-disulfide_reductase
Trypanothione-disulfide reductaseTrypanothione-disulfide reductase
In enzymology, a trypanothione-disulfide reductase (EC 1.8.1.12) is an enzyme that catalyzes the chemical reaction ... whereas its 3 products are trypanothione disulfide, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, ... a newly discovered member of the family of disulfide-containing flavoprotein reductases". Biochemistry. 25 (12): 3519-26. doi: ... trypanothione + NADP+ ⇌ {\displaystyle \rightleftharpoons } trypanothione disulfide + NADPH + H+ Thus, the two substrates of ...
https://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase
Disulfide oxidoreductase DDisulfide oxidoreductase D
... reversibly forming two disulfide bonds. Although DsbA displays no proofreading activity for repair of wrongly paired disulfides ... The Disulfide bond oxidoreductase D (DsbD) family is a member of the Lysine Exporter (LysE) Superfamily. A representative list ... Homologues include: (1) several thiol-disulfide exchange proteins (i.e., TC# 5.A.1.1.1) (2) the cytochrome c-type biogenesis ... In the E. coli DsbD system, electrons are transferred from NADPH in the cytoplasm to periplasmic dithiol/disulfide-containing ...
https://en.wikipedia.org/wiki/Disulfide_oxidoreductase_D
CoA-disulfide reductaseCoA-disulfide reductase
Other names in common use include CoA-disulfide reductase (NADH2), NADH2:CoA-disulfide oxidoreductase, CoA:NAD+ oxidoreductase ... CoA-disulfide + NAD(P)H + H+ The 3 substrates of this enzyme are CoA, NAD+, and NADP+, whereas its 4 products are CoA-disulfide ... "Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide ... In enzymology, a CoA-disulfide reductase (EC 1.8.1.14) is an enzyme that catalyzes the chemical reaction 2 CoA + NAD(P)+ ⇌ {\ ...
https://en.wikipedia.org/wiki/CoA-disulfide_reductase
Protein disulfide-isomeraseProtein disulfide-isomerase
... has also been suggested to play a role in the formation of regulatory disulfide bonds in ... The reduced (dithiol) form of protein disulfide-isomerase is able to catalyze a reduction of a misformed disulfide bridge of a ... Therefore, protein disulfide-isomerase is capable of catalyzing the post-translational modification disulfide exchange. In the ... Due to the role of protein disulfide-isomerase in a number of disease states, small molecule inhibitors of protein disulfide- ...
https://en.wikipedia.org/wiki/Protein_disulfide-isomerase
Bis(trifluoromethyl) disulfideBis(trifluoromethyl) disulfide
... (TFD) is a fluorinated organosulfur compound that was used as a fumigant. It is also an ... disulfide". "Reaction of metal fluorides with thiophosgene and perchloromethyl mercaptan". "Progressive Pulmonary Pathology of ... Organic disulfides, Trifluoromethylthio compounds, Pulmonary agents, Fumigants, All stub articles, Organohalide stubs). ...
https://en.wikipedia.org/wiki/Bis(trifluoromethyl)_disulfide
Carbon Disulfide | NIOSH | CDCCarbon Disulfide | NIOSH | CDC
Carbon disulfide is a colorless liquid with an ether-like odor. Exposure can cause dizziness, poor sleep, headache, anxiety, ... Carbon disulfide (CS2) is a colorless liquid with an ether-like odor. Exposure can cause dizziness, poor sleep, headache, ... Carbon disulfide is used in many industries. Its used to make rubber, viscose rayon, cellophane, and carbon tetrachloride. ... Some examples of workers at risk of being exposed to carbon disulfide include the following:. *Factory workers who work where ...
https://www.cdc.gov/niosh/topics/carbon-disulfide/default.html
Carbon Disulfide | ToxFAQs™ | ATSDR
Carbon disulfide has been found in at least 210 of the 1,430 National Priorities List sites identified by the Environmental ... Exposure to carbon disulfide can occur by breathing it in the air and by drinking water or eating foods that contain it. ... What is carbon disulfide?. Pure carbon disulfide is a colorless liquid with a pleasant odor that is like the smell of ... How can carbon disulfide affect my health?. At very high levels, carbon disulfide may be life-threatening because of its ...
https://wwwn.cdc.gov/TSP/ToxFAQs/ToxFAQsDetails.aspx?faqid=473&toxid=84
Occupational Exposure to Carbon Disulfide (77-156) | NIOSH | CDCOccupational Exposure to Carbon Disulfide (77-156) | NIOSH | CDC
Appendix I - Air Sampling Method for Carbon Disulfide. X. Appendix II - Analytical Method for Carbon Disulfide. 77-156F.PDF (28 ... I. Recommendations for a Carbon Disulfide Standard. 77-156B.PDF (21 pages, 697K)pdf icon. ... Criteria for a Recommended Standard: Occupational Exposure to Carbon Disulfide. ... Appendix III - Method of Biologic Monitoring for Carbon Disulfide: Iodine-Azide Test. ...
https://www.cdc.gov/niosh/docs/77-156/default.html
Carbon disulfideCarbon disulfide
2002)‎. Carbon disulfide. World Health Organization. https://extranet.who.int/iris/restricted/handle/10665/42554 ...
https://extranet.who.int/iris/restricted/handle/10665/42554
disulfide bridgedisulfide bridge
... s are a common mechanism used in nature to stabilize many proteins. Such disulfide bridges are often found ... In eukaryotic organisms, formation of disulfide bridges occurs within the organelle called the endoplasmic reticulum. ... Other articles where disulfide bridge is discussed: amino acid: Cysteine oxidation: …is referred to as a disulfide bridge. ... Disulfide bridges are a common mechanism used in nature to stabilize many proteins. Such disulfide bridges are often found ...
https://www.britannica.com/science/disulfide-bridge
Dieuropium disulfideDieuropium disulfide
The National Institute of Standards and Technology (NIST) uses its best efforts to deliver a high quality copy of the Database and to verify that the data contained therein have been selected on the basis of sound scientific judgment. However, NIST makes no warranties to that effect, and NIST shall not be liable for any damage that may result from errors or omissions in the Database ...
https://webbook.nist.gov/cgi/cbook.cgi?ID=C62462515&Units=CAL
Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductaseUnprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase
... there exists a group that is able to transfer reducing equivalents from FAD to a redox-active disulfide bridge, which further ... Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase Proc Natl Acad Sci U S A. 2017 Nov ... We have tentatively named the flavoprotein "DDOR" (diflavin-linked disulfide oxidoreductase) and propose that its activity is ... Keywords: Rossmann fold; flavoprotein; redox active disulfide; sulfhydryl; transfer of reducing equivalents. ...
https://pubmed.ncbi.nlm.nih.gov/29133410/
Copy this link to clipboardCopy this link to clipboard
2-D Molybdenum Disulfide Shows Piezoelectric Properties Researchers believe the demonstration could lead to self-powered, atom- ... "The materials community is excited about molybdenum disulfide, and demonstrating the piezoelectric effect in it adds a new ... material molybdenum disulfide (MoS2) exhibits piezoelectricity and the piezotronic effect. ...
https://spectrum.ieee.org/for-first-time-molybdenum-disulfide-exhibits-piezoelectric-properties
ELECTRONIC CONDUCTION PROCESS IN 1T-TANTALUM DISULFIDE. - Nokia Bell LabsELECTRONIC CONDUCTION PROCESS IN 1T-TANTALUM DISULFIDE. - Nokia Bell Labs
Nokia sites use cookies to improve and personalize your experience and to display advertisements. The sites may also include cookies from third parties. By using this site, you consent to the use of cookies. Learn more ...
https://www.bell-labs.com/institute/publications/bl8091027/
Nomination Summary for Carbon disulfide (N85002)Nomination Summary for Carbon disulfide (N85002)
Nomination Summary for Nomination Summary for Carbon disulfide (N85002). Nomination Summary for Carbon disulfide (N85002). ...
https://ntp.niehs.nih.gov/getinvolved/nominate/summary/nm-n85002.html
RCSB PDB - 3FKF: thiol-disulfide oxidoreductase from Bacteroides fragilis NCTC 9343RCSB PDB - 3FKF: thiol-disulfide oxidoreductase from Bacteroides fragilis NCTC 9343
thiol-disulfide oxidoreductase. A, B, C, D. 148. Bacteroides fragilis NCTC 9343. Mutation(s): 0 Gene Names: BF9343_4170, ... thiol-disulfide oxidoreductase from Bacteroides fragilis NCTC 9343. Duke, N.E.C., Freeman, L., Tesar, C., Joachimiak, A.. To be ... thiol-disulfide oxidoreductase from Bacteroides fragilis NCTC 9343. *PDB DOI: 10.2210/pdb3FKF/pdb ... thiol-disulfide oxidoreductase from Bacteroides fragilis NCTC 9343 ...
https://www.rcsb.org/structure/3fkf
Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity | Nature CommunicationsDisulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity | Nature Communications
Here, the authors use atomic force microscopy to study the properties of titin disulfide bonds, showing that disulfide ... Using single-molecule atomic force microscopy, we show that disulfide isomerization reactions within Ig domains enable a third ... Oxidation of Ig domains leads to non-canonical disulfide bonds that stiffen titin while enabling force-triggered isomerization ... of titins I-band Ig domains contain a conserved cysteine triad that can engage in disulfide isomerization reactions. We ...
https://www.nature.com/articles/s41467-017-02528-7?error=cookies_not_supported&code=6d1989f2-a9f9-4ade-946e-19bdecf7732a
Skip to PropertiesSkip to Properties
Disulfide, Iodine Intercalated I2:MoS2 bulk & research qty manufacturer. Properties, SDS, Applications, Price. Free samples ... About Molybdenum(IV) Disulfide, Iodine Intercalated. Iodine Intercalated Molybdenum(IV) Disulfide is a unique 2D material ... Molybdenum(IV) Disulfide, Iodine Intercalated Synonyms. Iodine-doped molybdenum disulfide, Molybdenum sulfide iodide, I2 ... Customers For Molybdenum(IV) Disulfide, Iodine Intercalated Have Also Viewed. Tungsten(IV) Disulfide, Iodine Intercalated ...
https://www.americanelements.com/molybdenum-iv-disulfide-iodine-intercalated
Surprising Discoveries about 2D Molybdenum Disulfide | Lab ManagerSurprising Discoveries about 2D Molybdenum Disulfide | Lab Manager
Surprising Discoveries about 2D Molybdenum Disulfide. Berkeley Lab researchers use award-winning campanile probe on promising ... Molybdenum disulfide is a 2D semiconductor that features high electrical conductance comparable to that of graphene, but, ... probe they developed to make some surprising discoveries about molybdenum disulfide, a member of a family of semiconductors, ... Schuck and his colleagues also discovered that the disordered edge region in molybdenum disulfide crystals harbors a sulfur ...
https://www.labmanager.com/news/surprising-discoveries-about-2d-molybdenum-disulfide-11473
Molybdenum Disulfide Market - Request Customization FormMolybdenum Disulfide Market - Request Customization Form
Molybdenum Disulfide Market By Form (Powder, Crystals), By Application (Greases, Pastes, Oil and Synthetic Fluid, Water ... Molybdenum Disulfide Market. Molybdenum Disulfide Market By Form (Powder, Crystals), By Application (Greases, Pastes, Oil and ...
https://www.reportsanddata.com/request-customization-form/2487
Disulfide bond - Proteopedia, life in 3DDisulfide bond - Proteopedia, life in 3D
In the Tools Tab of FirstGlance in Jmol, click on Disulfides/S/Se.. to be shown the disulfide bonds in a protein structure. ... DiANNA: a web server for disulfide connectivity prediction *DISULFIND: Cysteines Disulfide Bonding State and Connectivity ...
https://proteopedia.org/wiki/index.php/Disulfide_bond
Disulfides as synergists for 2, 4-d - Patent US-2668103-A - PubChemDisulfides as synergists for 2, 4-d - Patent US-2668103-A - PubChem
US-2668103-A chemical patent summary.
https://pubchem.ncbi.nlm.nih.gov/patent/US-2668103-A
Diallyl disulfide inhibits TGF‑β1‑induced upregulation of Rac1Diallyl disulfide inhibits TGF‑β1‑induced upregulation of Rac1
... and β‑catenin in epithelial‑mesenchymal transition and tumor ... Diallyl disulfide inhibits TGF‑β1‑induced upregulation of Rac1 and β‑catenin in epithelial‑mesenchymal transition and tumor ... Diallyl disulfide inhibits TGF‑β1‑induced upregulation of Rac1 and β‑catenin in epithelial‑mesenchymal transition and tumor ... The present study investigated the effects of diallyl disulfide (DADS) on TGF‑β1‑induced EMT, invasion and growth of gastric ...
https://greenmedinfo.com/article/diallyl-disulfide-inhibits-tgf-1-induced-upregulation-rac1-and-catenin-epithel
Improved Disulfide-Reducing Reagent - ChemistryViewsImproved Disulfide-Reducing Reagent - ChemistryViews
Improved Disulfide-Reducing Reagent. Author: ChemistryViews.org. The conversion between dithiols and disulfides is important in ... Disulfide-reducing agents are widely used in this field, either to protect free thiols or reduce disulfide bridges in peptides ... 2-(Dibenzylamino)butane-1,4-dithiol (DABDT), a Friendly Disulfide-Reducing Reagent Compatible with a Broad Range of Solvents,. ... and colleagues have developed a new disulfide-reducing agent, 2-(dibenzylamino)butane-1,4-dithiol (DABDT, pictured). This ...
https://www.chemistryviews.org/details/news/11201386/Improved_Disulfide-Reducing_Reagent/
Glycidyl azide polymer-based polyurethane vitrimers with disulfide chain extenders - Polymer Chemistry (RSC Publishing)Glycidyl azide polymer-based polyurethane vitrimers with disulfide chain extenders - Polymer Chemistry (RSC Publishing)
Glycidyl azide polymer-based polyurethane vitrimers with disulfide chain extenders Y. Hu, G. Tang, Y. Luo, S. Chi and X. Li, ... Herein, we report the preparation of a series of GAP-based PU vitrimers (GAPUVs), with GAP, 2-hydroxyethyl disulfide (HEDS), ... More interestingly, the incorporation of dynamic disulfide bonds in the network not only endowed the GAPUVs with decent ... the thermo-exchangeable disulfide linkage in the GAPUVs allowed the full recovery of the loaded fillers by simply heating the ...
https://pubs.rsc.org/en/Content/ArticleLanding/2021/PY/D1PY00441G
The superiority of single-layer molybdenum disulfide for water desalinationThe superiority of single-layer molybdenum disulfide for water desalination
... (Nanowerk Spotlight) Most available desalination ...
https://www.nanowerk.com/spotlight/spotid=55569.php
Molybdenum Disulfide The latest Qatar News,Qatar Technology,Qatar IndusMolybdenum Disulfide The latest Qatar News,Qatar Technology,Qatar Indus
Molybdenum disulfide (MoS2) is known as the "king of lubrication" and has its unique advant Molybdenum disulfide is a solid ... Molybdenum Disulfide MoS2 Powder CAS 1317-33-5. Item No.: TR-MoS2 Molybdenum disulfide is the main component of molybdenite. ... Lubrication of Molybdenum Disulfide MoS2. Molybdenum disulfide is a solid powder made from natural molybdenum concentrate ... What is Molybdenum Disulfide?. Since the beginning of this year, people around the world have felt the pressure of rising ...
https://www.actionext.com/tags/Molybdenum-Disulfide.html
Molybdenum Disulfide MoS2 Powder CAS 1317-33-5Molybdenum Disulfide MoS2 Powder CAS 1317-33-5
Molybdenum disulfide is the main component of molybdenite. Black solid powder with a metallic luster. Chemical formula MoS₂, ... Molybdenum disulfide is also known as "the king of advanced solid lubricants".. Molybdenum disulfide is a solid powder made ... About Molybdenum Disulfide MoS2 Powder:. Molybdenum disulfide (MoS2) is the main component of molybdenite. Black solid powder ... Applications of Molybdenum Disulfide MoS2 Powder:. Molybdenum disulfide is diamagnetic, can convert linear photoconductors and ...
https://www.it-chuiko.com/Products/Molybdenum-Disulfide-MoS2-Powder-CAS-1317-33-5.html
Tungsten disulfide has high catalytic activity Mis-aisa-The latest News,Tech,Industry,EnvironmentTungsten disulfide has high catalytic activity Mis-aisa-The latest News,Tech,Industry,Environment
Tungsten disulfide is an inorganic compound with a molecular formula of WS2 and a molecular weight of 247.97.It is a small gray ... Tungsten disulfide has high catalytic activity. Tungsten disulfide is an inorganic compound with a molecular formula of WS2 and ... Tungsten disulfide is an inorganic compound with a molecular formula of WS2 and a molecular weight of 247.97.It is a small gray ... Tungsten disulfide has high catalytic activity_Mis-aisa-The latest News,Tech,Industry,Environment ...
https://www.mis-asia.com/tags/Tungsten-disulfide-has-high-catalytic-activity.html
Phylogenetic and expression analysis of protein disulfide isomerase unravels good reference genes for gene expression studies...Phylogenetic and expression analysis of protein disulfide isomerase unravels good reference genes for gene expression studies...
Protein disulfide isomerase (PDI) is an important enzyme for protein folding in endoplasmic reticulum. The PDI gene family has ... Phylogenetic and expression analysis of protein disulfide isomerase unravels good reference genes for gene expression studies ... "Phylogenetic and expression analysis of protein disulfide isomerase unravels good reference genes for gene expression studies ... "Phylogenetic and expression analysis of protein disulfide isomerase unravels good reference genes for gene expression studies ...
https://bioone.org/journals/canadian-journal-of-plant-science/volume-98/issue-5/cjps-2017-0302/Phylogenetic-and-expression-analysis-of-protein-disulfide-isomerase-unravels-good/10.1139/cjps-2017-0302.short
Signatures of defect-localized charged excitons in the photoluminescence of monolayer molybdenum disulfideSignatures of defect-localized charged excitons in the photoluminescence of monolayer molybdenum disulfide
... In: Physical Review ...
https://epub.ub.uni-muenchen.de/68059/
tungsten disulfide nmfbihop.com | Nanomaterials, Chemical Products, Btungsten disulfide nmfbihop.com | Nanomaterials, Chemical Products, B
Tungsten disulfide WS2 can be used as a solid lubricant.Its performance is better than that of molybdenum disulfide, with lower ... Global tungsten disulfide market trend 2024-2028 Tungsten disulfide vs. tungsten diselenide by Newsnmfbihop. ... Global MoS2 powder market trend 2023-2026 Why can molybdenum disulfide and tungsten disulfide be used as lubricants? by ... Tungsten disulfide nanoparticles and coatings Whether youre a professional, an amateuror seeking a low-cost way to keep your ...
https://www.nmfbihop.com/tags/tungsten+disulfide.html
Electric Switching of the Charge-Density-Wave and Normal Metallic Phases in Tantalum Disulfide Thin-Film Devices - NASA/ADSElectric Switching of the Charge-Density-Wave and Normal Metallic Phases in Tantalum Disulfide Thin-Film Devices - NASA/ADS
Electric Switching of the Charge-Density-Wave and Normal Metallic Phases in Tantalum Disulfide Thin-Film Devices *Geremew, A. ...
https://ui.adsabs.harvard.edu/abs/2019arXiv190306050G/abstract
Molybdenum Disulfide MoS2MoS2BondsCarbonProteinsProteinMonolayer molybdenum disulfidePeptidesDimethylIsomeraseIntramolecular disulfidePowderSubstancesNanomaterialsExtracellularBridgesDiallylOxidoreductaseInorganic substanceBindsCysteineGlutathione reductaseReactionLinkageInsolubleLubricationFrictionLubricantsFormCrystalsPreparationSelectivelyMolecularMonomerBondContentMarket trend
Molybdenum Disulfide MoS27
  • Molybdenum disulfide (MoS2) is known as the "king of lubrication" and has its unique advant Molybdenum disulfide is a solid powder made from natural molybdenum concentrate powder, which is the modern Since the beginning of this year, people around the world have felt the pressure of rising prices. (actionext.com)
  • Molybdenum disulfide (MoS2) is the main component of molybdenite. (it-chuiko.com)
  • Feel free to send an inquiry to get the latest price if you would like to buy Molybdenum Disulfide MoS2 Powder in bulk. (it-chuiko.com)
  • Molybdenum disulfide MoS2 is an important solid lubricant, especially suitable for high temperature and high pressure. (1-4dioxane.com)
  • In this work, a highly efficient, molybdenum disulfide (MoS2) based near infrared (NIR) heterojunction photodetector is fabricated on a Si substrate using a cost-effective and simple drop casting method. (preprints.org)
  • Mass layoffs on the internet have created a host of socioeconomic issues, including molybdenum disulfide MoS2. (jeromechampagne2015.com)
  • Molybdenum disulfide MoS2 is an inorganic substance with the chemical formula MoS2, which is the main component of molybdenite. (jeromechampagne2015.com)
MoS25
  • Item No.: TR-MoS2 Molybdenum disulfide is the main component of molybdenite. (actionext.com)
  • Global MoS2 powder market trend 2023-2026 Why can molybdenum disulfide and tungsten disulfide be used as lubricants? (nmfbihop.com)
  • Molybdenum disulfide has the chemical formula MoS2 and is used as a dry lubricant in greases, dispersions, friction materials and bond coatings. (1-4dioxane.com)
  • Molybdenum disulfide is an inorganic substance with the chemical formula MoS2, which is the main component of molybdenum ore. (jeromechampagne2015.com)
  • Molybdenum disulfide has excellent properties and broad application prospects, so a lot of research has been done on the preparation and application of nano-MoS2 at home and abroad. (jeromechampagne2015.com)
Bonds14
  • Oxidation of Ig domains leads to non-canonical disulfide bonds that stiffen titin while enabling force-triggered isomerization reactions to more extended states of the domains. (nature.com)
  • Disulfides are covalent bonds that cannot be cleaved by forces in the physiologically relevant picoNewton (pN) range. (nature.com)
  • to be shown the disulfide bonds in a protein structure. (proteopedia.org)
  • More interestingly, the incorporation of dynamic disulfide bonds in the network not only endowed the GAPUVs with decent mechanical properties, but also marked healing ability upon mild heating and thermo-reprocessability. (rsc.org)
  • Analysis for disulfide bonds in peptides and proteins. (uni-konstanz.de)
  • The introduction of disulfide bonds into periplasmic proteins is a critical process in many Gram-negative bacteria. (cam.ac.uk)
  • The formation and regulation of protein disulfide bonds have been linked to the production of virulence factors. (cam.ac.uk)
  • The well characterized disulfide bond-forming (DSB) proteins play a key role by introducing or isomerizing disulfide bonds between cysteines in substrate proteins. (cam.ac.uk)
  • Dsb proteins control the formation and rearrangement of disulfide bonds during the folding of secreted and membrane proteins in bacteria. (edu.au)
  • Cysteines contain sulfur atoms that form connections, called disulfide bonds, with other cysteines. (medlineplus.gov)
  • Disulfide bonds help a protein fold by connecting cysteines in different regions of the protein. (medlineplus.gov)
  • When cysteines within the TNFR1 protein are replaced with other amino acids, the disulfide bonds are not formed, and the protein is misfolded. (medlineplus.gov)
  • BTC (Betacellulin) is an EGF related growth factor containing 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. (goldbio.com)
  • Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties. (bvsalud.org)
Carbon55
  • Carbon disulfide (CS 2 ) is a colorless liquid with an ether-like odor. (cdc.gov)
  • Workers may be harmed by carbon disulfide. (cdc.gov)
  • Carbon disulfide is used in many industries. (cdc.gov)
  • If you work in an industry that uses carbon disulfide, please read chemical labels and the accompanying Safety Data Sheets for hazard information. (cdc.gov)
  • The following resources provide information about occupational exposure to carbon disulfide. (cdc.gov)
  • A useful search term for carbon disulfide includes "carbon bisulfide," "carbon sulfide," and "carbon disulphide. (cdc.gov)
  • NIOSHTIC-2 search results on carbon disulfide -NIOSHTIC-2 is a searchable database of worker safety and health publications, documents, grant reports, and journal articles supported in whole or in part by NIOSH. (cdc.gov)
  • Immediately Dangerous to Life or Health Concentrations (IDLH) of Carbon Disulfide -NIOSH reviews relevant scientific data and researches methods for developing IDLH values. (cdc.gov)
  • Carbon Disulfide: Rubber and Plastics Chemical Manufacturing -The NIOSH Worker Notification Program notifies workers and other stakeholders about the findings of these research studies. (cdc.gov)
  • DHHS (NIOSH) Publication No. 77-156 (1977)-This report increases awareness and recommends work practices to reduce exposures to carbon disulfide in the workplace. (cdc.gov)
  • Carbon Disulfide (No. 1600) -Sampling and measurement data from NMAM, fourth edition. (cdc.gov)
  • Occupational Health Guideline for Carbon Disulfide -This guideline helps stakeholders conduct effective occupational safety and health programs. (cdc.gov)
  • This fact sheet answers the most frequently asked health questions about carbon disulfide. (cdc.gov)
  • Exposure to carbon disulfide can occur by breathing it in the air and by drinking water or eating foods that contain it. (cdc.gov)
  • Carbon disulfide has been found in at least 210 of the 1,430 National Priorities List sites identified by the Environmental Protection Agency (EPA). (cdc.gov)
  • What is carbon disulfide? (cdc.gov)
  • Pure carbon disulfide is a colorless liquid with a pleasant odor that is like the smell of chloroform. (cdc.gov)
  • The impure carbon disulfide that is usually used in most industrial processes is a yellowish liquid with an unpleasant odor, like that of rotting radishes. (cdc.gov)
  • Carbon disulfide evaporates at room temperature, and the vapor is more than twice as heavy as air. (cdc.gov)
  • In nature, small amounts of carbon disulfide are found in gases released to the earth's surface as, for example, in volcanic eruptions or over marshes. (cdc.gov)
  • Commercial carbon disulfide is made by combining carbon and sulfur at very high temperatures. (cdc.gov)
  • What happens to carbon disulfide when it enters the environment? (cdc.gov)
  • The amount of carbon disulfide released into the air through natural processes is difficult to judge because it is so small. (cdc.gov)
  • Carbon disulfide evaporates rapidly when released to the environment. (cdc.gov)
  • Most carbon disulfide in the air and surface water is from manufacturing and processing activities. (cdc.gov)
  • Carbon disulfide does not stay dissolved in water very long, and it also moves through soils fairly quickly. (cdc.gov)
  • Carbon disulfide does not appear to be taken up in significant amounts by the organisms living in water. (cdc.gov)
  • How might I be exposed to carbon disulfide? (cdc.gov)
  • The people most often exposed to carbon disulfide are workers in plants that use carbon disulfide in their manufacturing processes. (cdc.gov)
  • People may also be exposed through skin contact with soil, water, or other substances that contain carbon disulfide. (cdc.gov)
  • How can carbon disulfide affect my health? (cdc.gov)
  • At very high levels, carbon disulfide may be life-threatening because of its effects on the nervous system. (cdc.gov)
  • People who breathed carbon disulfide near an accident involving a railroad car showed changes in breathing and some chest pains. (cdc.gov)
  • However, these workers may have been exposed to other chemicals besides carbon disulfide. (cdc.gov)
  • Studies in animals indicate that carbon disulfide can affect the normal functions of the brain, liver, and heart. (cdc.gov)
  • After pregnant rats breathed carbon disulfide in the air, some of the newborn rats died or had birth defects. (cdc.gov)
  • High concentrations of carbon disulfide have caused skin burns when the chemical accidentally touched people's skin. (cdc.gov)
  • How likely is carbon disulfide to cause cancer? (cdc.gov)
  • The Department of Health and Human Services (DHHS), the International Agency for Research on Cancer (IARC), and the EPA have not classified carbon disulfide for carcinogenicity. (cdc.gov)
  • There are no definitive data in humans or animals that indicate a carcinogenic potential for carbon disulfide. (cdc.gov)
  • Is there a medical test to show whether I've been exposed to carbon disulfide? (cdc.gov)
  • One chemical test using urine can be done to tell whether the levels of breakdown substances from carbon disulfide are higher than normal. (cdc.gov)
  • However, the test is not specific for carbon disulfide exposure. (cdc.gov)
  • It also requires special equipment and cannot tell you exactly how much carbon disulfide you were exposed to or predict whether harmful effects will occur. (cdc.gov)
  • 1988. Neurological examination, computerized- tomography, cerebral blood-flow and neuropsychological examination in workers with long-term exposure to carbon disulfide. (cdc.gov)
  • 1990. Carbon disulfide exposure and neurotoxic sequelae among viscose rayon workers. (cdc.gov)
  • 1992. Regional cerebral blood flow after long-term exposure to carbon disulfide. (cdc.gov)
  • 1966. The question of pathogenesis, specific prevention, and therapy of carbon disulfide intoxication. (cdc.gov)
  • Toxicology of carbon disulfide. (cdc.gov)
  • 1980. Measurements of emission rates of carbon disulfide from biogenic sources and its possible importance to the stratospheric aerosol layer. (cdc.gov)
  • 1989. Determination of room temperature OH rate constants for acetylene, ethylene dichloride, ethylene dibromide, p-dichlorobenzene, and carbon disulfide. (cdc.gov)
  • Rate constants for the reaction of hydroxyl radicals with carbonyl sulfide, carbon disulfide and dimethyl thioether over the temperature range 299-430 K. (cdc.gov)
  • It dissolves readily in chloroform, carbon tetrachloride, or carbon disulfide. (americanelements.com)
  • In this research article, a systematic study has been carried out to investigate the mechanical properties of carbon fabric reinforced epoxy (C-E) composites, having alumina (Al 2 O 3 ) in one instance and molybdenum disulfide (MoS 2 ) of two different loadings in the epoxy matrix resin The study has revealed that with 60 wt. (inderscience.com)
  • It is soluble in hot water and insoluble in ether, chloroform or carbon disulfide. (robocup2009.org)
Proteins8
  • Disulfide bridges are a common mechanism used in nature to stabilize many proteins. (britannica.com)
  • Such disulfide bridges are often found among extracellular proteins that are secreted from cells. (britannica.com)
  • Within this protein superfamily, there exists a group that is able to transfer reducing equivalents from FAD to a redox-active disulfide bridge, which further reduces disulfide bridges in target proteins to regulate their structure and function. (nih.gov)
  • Expression of proteins containing disulfides in the native state can make a lot of trouble when expressed using standard vectors and strains for cytoplasmic expression. (uni-konstanz.de)
  • Determination of thiols and disulfides in proteins. (uni-konstanz.de)
  • This finding suggests that, rather than catalyzing disulfide rearrangement in unfolded substrates, DsbG may preferentially act later in the folding process to catalyze disulfide rearrangement in folded or partially folded proteins. (edu.au)
  • In another fraction methyl mercaptan is covalently bound to proteins in a disulfide linkage and is released by reaction with dithiothreitol. (cdc.gov)
  • with sufficient oxidation, extra sulfenic acid groups are made available for covalent, disulfide coupling to sulfhydryl groups of proteins or peptides. (figshare.com)
Protein11
  • However, our experimental data show that the protein does not transfer reducing equivalents from flavins to disulfides as in NTRs but functions in the opposite direction. (nih.gov)
  • Protein disulfide isomerase (PDI) is an important enzyme for protein folding in endoplasmic reticulum. (bioone.org)
  • Method according to Thannhauser: determination of disulfides and thiols The amount of disulfides in a protein is assessed by determination of thiols generated through cleavage of disulfides by sulfite. (uni-konstanz.de)
  • 5. Dilute protein in 1ml reaction buffer at a final concentration of 10-40 µM disulfide. (uni-konstanz.de)
  • Protein disulfide isomerase (PDI), an endoplasmic reticulum protein vital for protein folding, also possesses essential extracellular functions, including regulation of thrombus formation. (aacrjournals.org)
  • The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity. (cam.ac.uk)
  • The equilibrium unfolding of the derivative involves a stable intermediate, which is also similar to the molten globule state of the disulfide intact protein. (eurekamag.com)
  • To elucidate the physiological roles and regulation of a protein disulfide isomerase (PDI) from the fission yeast Schizosaccharomyces pombe, the full-length PDI gene was ligated into the shuttle vector pRS316, resulting in pPDI10. (umn.edu)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Protein Disulfide Isomerase A2 (PDIA2) in samples from tissue homogenates or other biological fluids. (glideruniversity.org)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Protein Disulfide Isomerase A2 (PDIA2) in Tissue homogenates and other biological fluids. (glideruniversity.org)
  • The slide, entitled, "Ricin Molecule", describes the molecule as a 66kDa heterodimer, bonded by a disulfide bridge, the B-chain (34kDa) binds to cell surface receptors, while the toxin-receptor complex is taken into the cell, the A-chain ((32kDa) has endonuclease activity, and inhibits DNA replication and protein synthesis at low levels (cytotoxin). (cdc.gov)
Monolayer molybdenum disulfide1
  • The paper is titled " Visualizing nanoscale excitonic relaxation properties of disordered edges and grain boundaries in monolayer molybdenum disulfide . (labmanager.com)
Peptides1
  • Disulfide-reducing agents are widely used in this field, either to protect free thiols or reduce disulfide bridges in peptides. (chemistryviews.org)
Dimethyl1
  • Hydrogen sulfide (H2S), dimethyl sulfide ([CH3]2S), and dimethyl disulfide ([CH3]2S2) are other reduced sulfur compounds that may occur along with methyl mercaptan and are commonly determined along with it. (cdc.gov)
Isomerase1
  • DsbG, a member of this family, has disulfide bond isomerase and chaperone activity. (edu.au)
Intramolecular disulfide1
  • It has also been proposed that oxidative stress can limit the elasticity of titin through intramolecular disulfide formation of the cardiac-specific, unstructured N2B region 10 . (nature.com)
Powder1
  • Molybdenum disulfide is the main component of molybdenite, which is a black solid powder with metallic luster and is an important solid lubricant. (1-4dioxane.com)
Substances1
  • Most of the molybdenum disulfide coating raw materials extracted are in the form of non-renewable substances, placing a heavy burden on the environment, society and climate. (abbaworld.com)
Nanomaterials1
  • Tungsten disulfide nanotubes (INTs-WS2) are extremely hydrophobic and chemically inert inorganic nanomaterials. (pulsus.com)
Extracellular2
  • Using sequence similarity analyses, these authors proposed that 40% of the I-band Ig domains contain cysteines at positions that form the classical disulfide bond connecting β-strands B and F in extracellular Ig domains such as antibodies. (nature.com)
  • The extracellular disulfide loop motif of the inhibitory glycine receptor does not form the agonist binding site. (aspetjournals.org)
Bridges2
  • In eukaryotic organisms, formation of disulfide bridges occurs within the organelle called the endoplasmic reticulum. (britannica.com)
  • Two CD95-Fc polypeptide chains are covalently connected by disulfide bridges in the hinge region of the Fc domain to form active APG101. (who.int)
Diallyl3
  • Diallyl disulfide inhibits TGF‑β1‑induced upregulation of Rac1 and β‑catenin in epithelial‑mesenchymal transition and tumor growth of gastric cancer. (greenmedinfo.com)
  • The present study investigated the effects of diallyl disulfide (DADS) on TGF‑β1‑induced EMT, invasion and growth of gastric cancer cells. (greenmedinfo.com)
  • It has previously been demonstrated that diallyl disulfide (DADS) was capable of attenuating liver dysfunction, as DADS supplementation had a positive impact on liver regeneration, proliferation and oxidative damage. (spandidos-publications.com)
Oxidoreductase1
  • We have tentatively named the flavoprotein "DDOR" (diflavin-linked disulfide oxidoreductase) and propose that its activity is linked to a thiol-based transfer of reducing equivalents in bacterial membranes. (nih.gov)
Inorganic substance1
Binds1
  • A disulfide opioid pentapeptide that selectively binds to the DELTA OPIOID RECEPTOR . (bvsalud.org)
Cysteine2
  • Using sequence and structural analyses, we show that 21% of titin's I-band Ig domains contain a conserved cysteine triad that can engage in disulfide isomerization reactions. (nature.com)
  • most of the remainder is the disulfide dimer of captopril and captopril-cysteine disulfide. (nih.gov)
Glutathione reductase1
  • Glutathione stabilizes ROS, and after being converted (oxidizing) to glutathione disulfide, it is reduced back to GSH by glutathione reductase. (medscape.com)
Reaction1
  • Catalysis of the reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+. (yeastrc.org)
Linkage1
  • Additionally, the thermo-exchangeable disulfide linkage in the GAPUVs allowed the full recovery of the loaded fillers by simply heating the composite in a solvent. (rsc.org)
Insoluble1
  • Molybdenum disulfide is insoluble in water, dilute acid and concentrated sulfuric acid. (it-chuiko.com)
Lubrication1
  • Tungsten disulfide is an extremely smooth dry film lubrication coating. (nmfbihop.com)
Friction1
  • Tungsten Sulfide (WS2) or Tungsten Disulfide is a very smooth dry film friction coating. (grinderpro.com)
Lubricants2
  • Tungsten disulfide nanoparticles and coatings Whether you're a professional, an amateuror seeking a low-cost way to keep your machine functioning smoothly, there's numerous options for the use of lubricants and paints. (nmfbihop.com)
  • Tungsten disulfide particles as well as coatings No matter if you're a professional or an amateur, or simply seeking a low-cost solution to keep your machine functioning at its best, there's many options for painting and lubricants. (godhatestheworld.com)
Form1
  • Molybdenum disulfide and alkyl lithium react under control to form an intercalation compound (interlayer compound) LixMoS2. (it-chuiko.com)
Crystals2
  • The Campanile probe's remarkable resolution enabled us to identify significant nanoscale optoelectronic heterogeneity in the interior regions of monolayer crystals of molybdenum disulfide, and an unexpected, approximately 300 nanometer wide, energetically disordered edge region," says James Schuck, a staff scientist with Berkeley Lab's Materials Sciences Division. (labmanager.com)
  • In their new study, Schuck, Bao, Borys and their co-authors used the Campanile probe to spectroscopically map nanoscale excited-state/relaxation processes in monolayer crystals of molybdenum disulfide that were grown by chemical vapor deposition (CVD). (labmanager.com)
Preparation1
  • Herein, we report the preparation of a series of GAP-based PU vitrimers (GAPUVs), with GAP, 2-hydroxyethyl disulfide (HEDS), and trimethylolpropane (TMP) as the soft segment, chain extender and crosslinker, respectively. (rsc.org)
Selectively1
  • The unfolding and refolding of a derivative of alpha-lactalbumin, in which the disulfide bond between Cys6 and Cys120 is selectively reduced and S-carboxymethylated, are investigated by equilibrium and kinetic circular dichroism measurements. (eurekamag.com)
Molecular1
  • Working at the Molecular Foundry , a DOE Office of Science User Facility, the scientific team used the "Campanile" probe they developed to make some surprising discoveries about molybdenum disulfide, a member of a family of semiconductors, called "transition metal dichalcogenides (TMDCs), whose optoelectronic properties hold great promise for future nanoelectronic and photonic devices. (labmanager.com)
Monomer1
  • PCC6803 obtained by X-ray crystallography showed two juxtaposed FAD molecules per monomer in redox communication with an active disulfide bridge in a variant of the fold adopted by NTRs. (nih.gov)
Bond3
  • The stabilization of the native state by the disulfide has been interpreted in terms of a decrease in chain entropy in the unfolded state and elimination of the strain imposed on the disulfide bond in the native state. (eurekamag.com)
  • The molten globule state is also stabilized by the disulfide bond, although the degree of stabilization of the molten globule state is smaller than of the native state. (eurekamag.com)
  • To determine whether this effect of disulfide bond formation was unique to rat liver nuclei, nuclear matrix/cytoskeleton structures were prepared in situ by sequentially treating monolayers of tissue culture cells with Nonidet-P40, DNase I and RNase A, and 1.6 M NaCl (S. H. Kaufmann and J. H. Shaper (1991) Exp. (elsevier.com)
Content1
  • Molybdenum disulfide has a high content of active sulfur, which is easy to cause corrosion to copper. (it-chuiko.com)
Market trend1
  • Global Molybdenum disulfide market trend 2023-2029 What is Molybdenum Disulfide? (1-4dioxane.com)