Proteolysis. Medical search

Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.

Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.

A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.

The process of cleaving a chemical compound by the addition of a molecule of water.

Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.

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.

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.

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.

A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.

A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins.

A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).

Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.

The sum of the weight of all the atoms in a molecule.

A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.

The rate dynamics in chemical or physical systems.

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.

A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.

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.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

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.

An ATP-dependent protease found in prokaryotes, CHLOROPLASTS, and MITOCHONDRIA. It is a soluble multisubunit complex that plays a role in the degradation of many abnormal proteins.

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).

Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Proteins prepared by recombinant DNA technology.

An enzyme that catalyzes the hydrolysis of keratin, and of other proteins with subtilisin-like specificity. It hydrolyses peptide amides. Endopeptidase K is from the mold Tritirachium album Limber. (Enzyme Nomenclature, 1992) EC 3.4.21.64.

A group of acylated oligopeptides produced by Actinomycetes that function as protease inhibitors. They have been known to inhibit to varying degrees trypsin, plasmin, KALLIKREINS, papain and the cathepsins.

ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.

A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.

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.

Proteases that contain proteolytic core domains and ATPase-containing regulatory domains. They are usually comprised of large multi-subunit assemblies. The domains can occur within a single peptide chain or on distinct subunits.

Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).

A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.

A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.

A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.

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.

Established cell cultures that have the potential to propagate indefinitely.

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.

A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-

A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)

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.

A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.

Endopeptidases that are specific for AMYLOID PROTEIN PRECURSOR. Three secretase subtypes referred to as alpha, beta, and gamma have been identified based upon the region of amyloid protein precursor they cleave.

An E3 ubiquitin ligase primarily involved in regulation of the metaphase-to-anaphase transition during MITOSIS through ubiquitination of specific CELL CYCLE PROTEINS. Enzyme activity is tightly regulated through subunits and cofactors, which modulate activation, inhibition, and substrate specificity. The anaphase-promoting complex, or APC-C, is also involved in tissue differentiation in the PLACENTA, CRYSTALLINE LENS, and SKELETAL MUSCLE, and in regulation of postmitotic NEURONAL PLASTICITY and excitability.

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.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

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.

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.

The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.

An essential branched-chain amino acid important for hemoglobin formation.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

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.

A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.

A family of membrane-anchored glycoproteins that contain a disintegrin and metalloprotease domain. They are responsible for the proteolytic cleavage of many transmembrane proteins and the release of their extracellular domain.

Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.

Proteins found in any species of bacterium.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.

A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Transport proteins that carry specific substances in the blood or across cell membranes.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.

The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.

A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.

Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.

A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.

Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.

Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.

Physiologically inactive substances that can be converted to active enzymes.

A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.

Physiological changes that occur in bodies after death.

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)

Proteases which use a metal, normally ZINC, in the catalytic mechanism. This group of enzymes is inactivated by metal CHELATORS.

A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.

A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.

An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.

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)

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 7; CASPASE 8; and CASPASE 10. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.

Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.

A prokaryotic ATP-dependent protease that plays a role in the degradation of many abnormal proteins. It is a tetramer of 87-kDa subunits, each of which contains a proteolytic site and a ATP-binding site.

The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.

Histidine substituted in any position with one or more methyl groups.

Cdh1 is an activator of the anaphase-promoting complex-cyclosome, and is involved in substrate recognition. It associates with the complex in late MITOSIS from anaphase through G1 to regulate activity of CYCLIN-DEPENDENT KINASES and to prevent premature DNA replication.

The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.

A proteolytic enzyme that converts PLASMINOGEN to FIBRINOLYSIN where the preferential cleavage is between ARGININE and VALINE. It was isolated originally from human URINE, but is found in most tissues of most VERTEBRATES.

A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.

An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).

A family of structurally-related proteins that were originally identified by their ability to complex with cyclin proteins (CYCLINS). They share a common domain that binds specifically to F-BOX MOTIFS. They take part in SKP CULLIN F-BOX PROTEIN LIGASES, where they can bind to a variety of F-BOX PROTEINS.

A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.

The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.

Peptides composed of two amino acid units.

Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.

The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.

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.

An enzyme inhibitor that inactivates IRC-50 arvin, subtilisin, and the fatty acid synthetase complex.

Derangement in size and number of muscle fibers occurring with aging, reduction in blood supply, or following immobilization, prolonged weightlessness, malnutrition, and particularly in denervation.

Proteins found in any species of fungus.

Proteins obtained from ESCHERICHIA COLI.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

Elements of limited time intervals, contributing to particular results or situations.

An extracellular receptor specific for UROKINASE-TYPE PLASMINOGEN ACTIVATOR. It is attached to the cell membrane via a GLYCOSYLPHOSPHATIDYLINOSITOL LINKAGE and plays a role in the co-localization of urokinase-type plasminogen activator with PLASMINOGEN.

The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.

A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.

The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.

Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

Precursor of plasmin (FIBRINOLYSIN). It is a single-chain beta-globulin of molecular weight 80-90,000 found mostly in association with fibrinogen in plasma; plasminogen activators change it to fibrinolysin. It is used in wound debriding and has been investigated as a thrombolytic agent.

A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.

Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes.

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.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.

The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

A highly conserved subunit of the anaphase-promoting complex (APC-C) containing multiple 34-amino-acid tetratricopeptide repeats. These domains, also found in Apc3, Apc6, and Apc7, have been shown to mediate protein-protein interactions, suggesting that Apc8 may assist in coordinating the juxtaposition of the catalytic and substrate recognition module subunits relative to coactivators and APC-C inhibitors.

A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.

N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.

Securin is involved in the control of the metaphase-anaphase transition during MITOSIS. It promotes the onset of anaphase by blocking SEPARASE function and preventing proteolysis of cohesin and separation of sister CHROMATIDS. Overexpression of securin is associated with NEOPLASTIC CELL TRANSFORMATION and tumor formation.

A cyclin subtype that is transported into the CELL NUCLEUS at the end of the G2 PHASE. It stimulates the G2/M phase transition by activating CDC2 PROTEIN KINASE.

Peptides composed of between two and twelve amino acids.

A proteolytic enzyme obtained from Streptomyces griseus.

Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.

A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.

A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.

The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.

An essential amino acid. It is often added to animal feed.

Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.

A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.

Contractile tissue that produces movement in animals.

Presence of warmth or heat or a temperature notably higher than an accustomed norm.

Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.

Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.

The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.

Compounds that inhibit the function or proteolytic action of the PROTEASOME.

The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.

Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).

One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

The phase of cell nucleus division following METAPHASE, in which the CHROMATIDS separate and migrate to opposite poles of the spindle.

A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.

Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.

Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.

A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.

Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.

An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.

Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.

The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

The process by which two molecules of the same chemical composition form a condensation product or polymer.

Peptide hydrolases that contain at the active site a SERINE residue involved in catalysis.

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)

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.

Integral membrane protein of Golgi and endoplasmic reticulum. Its homodimer is an essential component of the gamma-secretase complex that catalyzes the cleavage of membrane proteins such as NOTCH RECEPTORS and AMYLOID BETA-PEPTIDES precursors. PSEN1 mutations cause early-onset ALZHEIMER DISEASE type 3 that may occur as early as 30 years of age in humans.

A family of F-box domain proteins that contain sequences that are homologous to the beta subunit of transducin (BETA-TRANSDUCIN). They play an important role in the protein degradation pathway by becoming components of SKP CULLIN F-BOX PROTEIN LIGASES, which selectively act on a subset of proteins including beta-catenin and IkappaBbeta.

A single-pass type I membrane protein. It is cleaved by AMYLOID PRECURSOR PROTEIN SECRETASES to produce peptides of varying amino acid lengths. A 39-42 amino acid peptide, AMYLOID BETA-PEPTIDES is a principal component of the extracellular amyloid in SENILE PLAQUES.

A high-molecular-weight plasma protein, produced by endothelial cells and megakaryocytes, that is part of the factor VIII/von Willebrand factor complex. The von Willebrand factor has receptors for collagen, platelets, and ristocetin activity as well as the immunologically distinct antigenic determinants. It functions in adhesion of platelets to collagen and hemostatic plug formation. The prolonged bleeding time in VON WILLEBRAND DISEASES is due to the deficiency of this factor.

An enzyme the catalyzes the degradation of insulin, glucagon and other polypeptides. It is inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not phosphoramidon. (Eur J Biochem 1994;223:1-5) EC 3.4.24.56.

Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.

Highly conserved proteins that specifically bind to and activate the anaphase-promoting complex-cyclosome, promoting ubiquitination and proteolysis of cell-cycle-regulatory proteins. Cdc20 is essential for anaphase-promoting complex activity, initiation of anaphase, and cyclin proteolysis during mitosis.

The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)

A family of zinc-dependent metalloendopeptidases that is involved in the degradation of EXTRACELLULAR MATRIX components.

Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)

Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.

Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.

A transmembrane domain-containing matrix metalloproteinase. It is synthesized as an inactive zymogen that is activated by the action of PROPROTEIN CONVERTASES such as FURIN. Matrix metalloproteinase 14 plays a direct role in the cleavage of proteins in the pericellular environment. In addition, it can function indirectly by enzymatically activating the proprotein form of MATRIX METALLOPROTEINASE 15.

A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.

CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)

Sites on an antigen that interact with specific antibodies.

A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

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.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.

A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.

Proteins found in any species of virus.

A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere.

Over-expression, rapid preparation and some properties of c-terminal BARc region in PICK1. (1/2649)

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Cyclophilin D is required for mitochondrial removal by autophagy in cardiac cells. (2/2649)

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Building and remodeling synapses. (3/2649)

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Beta-arrestin: a signaling molecule and potential therapeutic target for heart failure. (4/2649)

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Depletion of Beclin-1 due to proteolytic cleavage by caspases in the Alzheimer's disease brain. (5/2649)

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Pregabalin suppresses calcium-mediated proteolysis and improves stroke outcome. (6/2649)

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Regulation of PINK1-Parkin-mediated mitophagy. (7/2649)

Parkinson disease (PD) is a devastating disorder of the nervous system for which no cure exists. Although the exact mechanisms involved in the pathogenesis of PD are unclear, very recently, a novel cellular process has been identified that promises great future potential. Two PD-associated genes have been found to converge on the emerging mitophagy pathway that links the two major cellular dysfunctions implicated in the pathogenesis of PD. Thereby, PINK1 and Parkin physically associate and functionally cooperate to identify and label damaged mitochondria for selective degradation via autophagy. PD-associated mutations in both genes disrupt mitophagy although through different mechanisms, revealing a sequential multistep process. Further key players that tie into this process have been identified and provide the framework for future research aiming at a complete dissection of this neuroprotective pathway. This may not only yield novel targets for therapeutic intervention in PD, but possibly for other neurodegenerative disorders as well. (+info)

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1. (8/2649)

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There are events that follow protein biosynthesis such as proteolysis and protein-folding. Proteolysis refers to the cleavage ... "proteolysis , chemistry , Britannica". www.britannica.com. Retrieved 2022-05-17. Duan G, Walther D (February 2015). "The roles ... Ciechanover A (January 2005). "Proteolysis: from the lysosome to ubiquitin and the proteasome". Nature Reviews. Molecular Cell ...

https://en.wikipedia.org/wiki/Protein_biosynthesis

The reason for proteolysis is to provide the relevant tissue with a feedstock for gluconeogenesis; see glucogenic amino acids. ... Simmons PS, Miles JM, Gerich JE, Haymond MW (February 1984). "Increased proteolysis. An effect of increases in plasma cortisol ... Elevated levels of cortisol, if prolonged, can lead to proteolysis (breakdown of proteins) and muscle wasting. ...

https://en.wikipedia.org/wiki/Cortisol

Golubkov VS, Strongin AY (2007). "Proteolysis-driven oncogenesis". Cell Cycle. 6 (2): 147-50. doi:10.4161/cc.6.2.3706. PMID ...

https://en.wikipedia.org/wiki/Interstitial_collagenase

Suzuki K (1 March 2000). "Protein C inhibitor (PAI-3): structure and multi-function". Fibrinolysis and Proteolysis. 14 (2): 133 ...

https://en.wikipedia.org/wiki/Protein_C_inhibitor

Fibrinolysis and Proteolysis. 11: 39-44. doi:10.1016/S0268-9499(97)80069-0. Portal: Biology (Protein pages needing a picture, ...

https://en.wikipedia.org/wiki/Staphylokinase

Proteolysis in Cell Functions. IOS Press. pp. 88-95. ISBN 978-90-5199-322-6. McDonald JK, Reilly TJ, Zeitman BB, Ellis S (1968 ...

https://en.wikipedia.org/wiki/Puromycin

ISBN 978-0-387-68233-4. {{cite book}}: ,last1= has generic name (help) editor, David A. Dougan (2013). Regulated proteolysis in ... ISBN 3-642-46304-5. {{cite book}}: ,first1= has generic name (help) editor, David A. Dougan (2013). Regulated proteolysis in ...

https://en.wikipedia.org/wiki/Streptomyces_hawaiiensis

UPS proteolysis plays a major role in responses of cancer cells to stimulatory signals that are critical for the development of ... The mechanism of proteolysis by the β subunits of the 20S core particle is through a threonine-dependent nucleophilic attack. ... Which of these processes is the rate-limiting step in the overall proteolysis reaction depends on the specific substrate; for ... The proteasomal activation of NF-κB by processing p105 into p50 via internal proteolysis is one major example. Some proteins ...

https://en.wikipedia.org/wiki/Proteasome

Proteolysis Stennicke, Henning R.; Breddam, Klaus (2013-01-01). Rawlings, Neil D.; Salvesen, Guy (eds.). Handbook of ...

https://en.wikipedia.org/wiki/Glutamyl_endopeptidase_I

Krieglstein, K. G.; Henschen, A. H.; Weller, U.; Habermann, E. (15 November 1991). "Limited proteolysis of tetanus toxin. ...

https://en.wikipedia.org/wiki/Kerstin_Krieglstein

They are stable to proteolysis. These characteristics underpin theis biologically activity and utility in medicinal chemistry. ...

https://en.wikipedia.org/wiki/2,5-Diketopiperazine

Low level of p27Kip-1 protein is often found in various cancers and is due to overactivation of ubiquitin-mediated proteolysis ... A heat-stable polypeptide present in these extracts, ATP-dependent proteolysis factor 1 (APF-1), was found to become covalently ... Lysine 48-linked polyubiquitin chains target proteins for destruction, by a process known as proteolysis. Multi-ubiquitin ... Wilkinson KD (October 2005). "The discovery of ubiquitin-dependent proteolysis". Proceedings of the National Academy of ...

https://en.wikipedia.org/wiki/Ubiquitin

Intramembrane proteolysis was proposed in the 1990s by researchers studying Alzheimer's disease, such as Dennis Selkoe, as a ... Brown, MS; Ye, J; Rawson, RB; Goldstein, JL (18 February 2000). "Regulated intramembrane proteolysis: a control mechanism ... Kühnle, Nathalie; Dederer, Verena; Lemberg, Marius K. (15 August 2019). "Intramembrane proteolysis at a glance: from signalling ... Wolfe, MS; Kopan, R (20 August 2004). "Intramembrane proteolysis: theme and variations". Science. 305 (5687): 1119-23. doi: ...

https://en.wikipedia.org/wiki/Intramembrane_protease

Löfvenberg L, Backman L (1999). "Calpain-induced proteolysis of beta-spectrins". FEBS Lett. 443 (2): 89-92. doi:10.1016/S0014- ...

https://en.wikipedia.org/wiki/SPTBN1

Rogg, L. E.; Bartel, B. (November 2001). "Auxin signaling: derepression through regulated proteolysis". Developmental Cell. 1 ( ...

https://en.wikipedia.org/wiki/Derepression

... and proteolysis; thyroid peroxidase activity; and hormone release. TSHR is involved in regulating seasonal reproduction in ...

https://en.wikipedia.org/wiki/Thyrotropin_receptor

Randall W. King; Raymond J. Deshaies; Jan-Michael Peters; Marc W. Kirschner (1996). "How proteolysis drives the cell cycle". ... and proteolysis are necessary. However, experiments using budding yeast cells with cdc28-as1, an INM-PP1 (ATP analog)-sensitive ... A Family of Substrate-Specific Activators of APC-Dependent Proteolysis". Science. 278 (5337): 460-463. Bibcode:1997Sci...278.. ... did shorten the Cdk1-inhibition period required for triggering irreversible mitotic exit indicating that cyclin proteolysis ...

https://en.wikipedia.org/wiki/Biochemical_switches_in_the_cell_cycle

... and proteolysis are necessary. However, experiments using budding yeast cells with cdc28-as1, an INM-PP1 (ATP analog)-sensitive ... "How proteolysis drives the cell cycle". Science. 274 (5293): 1652-1659. Bibcode:1996Sci...274.1652K. doi:10.1126/science. ... A Family of Substrate-Specific Activators of APC-Dependent Proteolysis". Science. 278 (5337): 460-463. Bibcode:1997Sci...278.. ... did shorten the Cdk1-inhibition period required for triggering irreversible mitotic exit indicating that cyclin proteolysis ...

https://en.wikipedia.org/wiki/Mitotic_exit

King RW, Deshaies RJ, Peters JM, Kirschner MW (December 1996). "How proteolysis drives the cell cycle". Science. 274 (5293): ... King RW, Deshaies RJ, Peters JM, Kirschner MW (December 1996). "How proteolysis drives the cell cycle". Science. 274 (5293): ... "Degradation of B-Myb by ubiquitin-mediated proteolysis: involvement of the Cdc34-SCF(p45Skp2) pathway". Oncogene. 19 (26): 2986 ... "Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis". ...

https://en.wikipedia.org/wiki/CDC34

Nanotechnology The Proteolysis Map Smith JW. Allostery and proteolysis: two novel modes of regulating integrin function. Matrix ...

https://en.wikipedia.org/wiki/Jeffrey_W._Smith

Monitto CL, Dong SM, Jen J, Sidransky D (2005). "Characterization of a human homologue of proteolysis-inducing factor and its ... PIF is involved in muscular proteolysis. Dermcidin is a secreted protein that is subsequently processed into mature peptides of ... The full-length protein produces derived peptides as proteolysis-inducing factor (PIF) and other anti-microbial peptides, ... 2006). "The cachectic mediator proteolysis inducing factor activates NF-kappaB and STAT3 in human Kupffer cells and monocytes ...

https://en.wikipedia.org/wiki/Dermcidin

King RW, Deshaies RJ, Peters JM, Kirschner MW (December 1996). "How proteolysis drives the cell cycle". Science. 274 (5293): ... and their key role in eukaryotic cell-cycle regulation that established the importance of ubiquitin-mediated proteolysis in ... a family of substrate-specific activators of APC-dependent proteolysis". Science. 278 (5337): 460-3. Bibcode:1997Sci...278.. ...

https://en.wikipedia.org/wiki/Anaphase-promoting_complex

Proteolysis has been indicated as one of the first and most sustained activities involved in the formation of new blood vessels ... Uncontrolled proteolysis also is attributed to the disruption of vascular development and premature deaths in murine embryos ... If not for this control excessive proteolysis could lead to damage of the tissue and the loss of anchorage points for migrating ... Saksela, O (1985). "Plasminogen activation and regulation of pericellular proteolysis". Biochim. Biophys. Acta. 823 (1): 35-65 ...

https://en.wikipedia.org/wiki/Proteases_in_angiogenesis

The Proteolysis Map "the definition of calpain". Dictionary.com. Retrieved 23 April 2018. Ohno S, Emori Y, Imajoh S, Kawasaki H ... Increase in concentration of calcium in the cell results in calpain activation, which leads to unregulated proteolysis of both ... Calpain Info with links in the Cell Migration Gateway Alzheimers and calpain protease, PMAP The Proteolysis Map-animation. ... The calcium-dependent activity, intracellular localization, and the limited, specific proteolysis on its substrates, ...

https://en.wikipedia.org/wiki/Calpain

"Proteolysis and Lipolysis of Goat Milk Cheese". Journal of Dairy Science. 84 (1): E84-E92. doi:10.3168/jds.S0022-0302(01)70202- ...

https://en.wikipedia.org/wiki/List_of_goat_cheeses

in 1962, he and his uncle offered a new explanation for tooth decay, the "proteolysis-chelation theory." (He later referred to ... The theory which they named "proteolysis-chelation theory" rooted in Scatz's original research in 1955. The full framework of ... Schatz, A.; Martin, J. J.; Schatz, V. (1972). "The chelation and proteolysis-chelation theories of dental caries: their origin ... Schatz, A.; Martin, J. J. (1962). "The proteolysis-chelation theory of dental caries". Journal of the American Dental ...

https://en.wikipedia.org/wiki/Albert_Schatz_(scientist)

Peptones are derived from animal milk or meat digested by proteolysis. In addition to containing small peptides, the resulting ... Some ribosomal peptides are subject to proteolysis. These function, typically in higher organisms, as hormones and signaling ...

https://en.wikipedia.org/wiki/Peptide

Matrix metalloproteinase The Proteolysis Map Shen, Yuequan; Joachimiak, Andrzej; Rosner, Marsha Rich; Tang, Wei-Jen (2006-10-19 ... Minde DP, Maurice MM, Rüdiger SG (2012). "Determining biophysical protein stability in lysates by a fast proteolysis assay, ...

https://en.wikipedia.org/wiki/Metalloproteinase

146 Ongoing proteolysis also contributes to conditioning. Hypoxanthine, a breakdown product of ATP, contributes to the meat's ...

https://en.wikipedia.org/wiki/Meat

Rao L, Perez D, White E (1997). "Lamin proteolysis facilitates nuclear events during apoptosis". J. Cell Biol. 135 (6 Pt 1): ... Caspase 6 has been shown to interact with Caspase 8. The Proteolysis Map Caspase GRCh38: Ensembl release 89: ENSG00000138794 - ...

https://en.wikipedia.org/wiki/Caspase_6

In fact, the amount of total muscle proteolysis varies daily in humans deprived of food3. Furthermore, Lange et al. ... identified increased serum alanine values in mice fed with a high-fat diet for 10 weeks, possibly via muscle proteolysis35. ... reported that the stimulation of muscle proteolysis requires increased endogenous GC and impaired insulin signaling27. The ... Ketogenic diet induces skeletal muscle atrophy via reducing muscle protein synthesis and possibly activating proteolysis in ...

https://www.nature.com/articles/s41598-019-56166-8?error=cookies_not_supported&code=3c4dde44-ca39-4ead-94e2-6108c74ea0f6

... ubiquitination of IFNAR1 and proteolysis. The non-catalytic role of Tyk2 in sustaining the steady-state IFNAR1 level at the ...

https://research.pasteur.fr/en/publication/tyk2-activity-promotes-ligand-induced-ifnar1-proteolysis/

Cottrell, G. S. (2013) Roles of proteolysis in regulation of G protein-coupled receptor function. British Journal of ... This review discusses the different roles proteolysis plays in regulating G protein-coupled receptors (GPCRs). At the cell- ... the discovery of new regulatory mechanisms involving proteolysis that control GPCRs may provide additional targets to modulate ...

https://centaur.reading.ac.uk/30250/

Intramembrane proteolysis is now widely recognized as an important physiological pathway required for reverse signaling and ... Failure of shedding of Bri3 is accompanied by a lack of intramembrane proteolysis by SPPL2b. Surprisingly, a low molecular ... We demonstrate that similar to -secretase substrates, intramembrane proteolysis of Bri2 (Itm2b) is greatly facilitated by an ... Serial deletions revealed that the length of the ectodomain negatively correlates with efficient intramembrane proteolysis. ...

https://cipsm.de/publications/research-area-f/substrate-requirements-for-sppl2b-dependent-regulated-intramembrane-proteolysis/

The role of Siah proteins in regulating proteolysis and cell cycle inhibition. *Janes, Peter (Primary Chief Investigator (PCI)) ...

https://research.monash.edu/en/projects/the-role-of-siah-proteins-in-regulating-proteolysis-and-cell-cycl

ZHOU, Hong-Ming et al. Urokinase-type plasminogen activator and its receptor synergize to promote pathogenic proteolysis. In: ... Urokinase-type plasminogen activator (uPA) is a potent catalyst of extracellular proteolysis, which also binds to a high- ... Thus, combined overexpression of uPA and uPAR acts in synergy to promote pathogenic extracellular proteolysis. ... Urokinase-type plasminogen activator and its receptor synergize to promote pathogenic proteolysis. ...

https://archive-ouverte.unige.ch/unige:3897

Effect of high-pressure treatment of milk for cheese manufacture on proteolysis, lipolysis, texture and functionality of ... Effect of high-pressure treatment of milk for cheese manufacture on proteolysis, lipolysis, texture and functionality of ... Effect of high-pressure treatment of milk for cheese manufacture on proteolysis, lipolysis, texture and functionality of ... Effect of high-pressure treatment of milk for cheese manufacture on proteolysis, lipolysis, texture and functionality of ...

https://osuseafoodlab.oregonstate.edu/biblio/effect-high-pressure-treatment-milk-cheese-manufacture-proteolysis-lipolysis-texture-and

... as indicated by dichloroacetate-enhanced proteolysis of the Notch ligand, Jagged1. Despite altering proteolysis of the amyloid ... The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the ... In conclusion, dichloroacetate can inhibit amyloidogenic and promote non-amyloidogenic proteolysis of the amyloid precursor ... further research into its mechanism of action with respect to APP proteolysis may lead to the development of therapies for ...

https://eprints.lancs.ac.uk/id/eprint/164650/

These results indicate that WF has similar effects to those of proteolysis-inducing factor, but is less potent than the latter ... In this work, we used cytotoxicity and enzymatic assays and morphological analysis to examine the effects of a proteolysis- ... Yano, C.L., Ventrucci, G., Field, W.N. et al. Metabolic and morphological alterations induced by proteolysis-inducing factor ... Todorov PT, Field WN, Tisdale MJ: Role of a proteolysis-inducing factor (PIF) in cachexia induced by a human melanoma (G361). ...

https://bmccancer.biomedcentral.com/articles/10.1186/1471-2407-8-24

Use your RU credentials (u/z-number and password) to log in with SURFconext to upload a file for processing by the repository team ...

https://repository.ubn.ru.nl/handle/2066/27496

Proteolysis, metalloproteinases, and inflammation. In AAA, the aortic media appears to degrade by way of a proteolytic process ...

https://www.medscape.com/answers/1979501-30945/what-is-the-difference-in-mortality-rates-between-elective-and-emergency-repair-of-abdominal-aortic-aneurysm-aaa

... to interfere with proteolysis in ischemic myocardium was also evaluated. Leupeptin (10 or 40 mg/kg) inhibited proteolysis in a ... to interfere with proteolysis in ischemic myocardium was also evaluated. Leupeptin (10 or 40 mg/kg) inhibited proteolysis in a ... to interfere with proteolysis in ischemic myocardium was also evaluated. Leupeptin (10 or 40 mg/kg) inhibited proteolysis in a ... to interfere with proteolysis in ischemic myocardium was also evaluated. Leupeptin (10 or 40 mg/kg) inhibited proteolysis in a ...

https://jhu.pure.elsevier.com/en/publications/role-of-cellular-proteinases-in-acute-myocardial-infarction-i-pro-3

Proteolysis and protein fragments. In some types of amyloidosis (eg, always in AA, often in AL and ATTR), the amyloid ... Whether the proteolysis occurs before or after tissue deposition is unclear in patients in whom beta protein fragments are ... What is the role of proteolysis in the pathogenesis of amyloidosis?. Which immunocytochemical studies are performed in the ... Gelsolin domain 2 Ca2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of finnish type. J Mol ...

https://emedicine.medscape.com/article/335414

The positive transcription factor of the 5S RNA gene proteolyses during direct exchange between 5S DNA sites. E B Kmiec, E B ... E B Kmiec, A Worcel; The positive transcription factor of the 5S RNA gene proteolyses during direct exchange between 5S DNA ... Unexpectedly, the direct exchange of factor between 5S DNA sites leads to proteolysis at the C-terminal arm of TFIIIA. ...

https://rupress.org/jcb/article/103/3/673/13484/The-positive-transcription-factor-of-the-5S-RNA

Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo. In: Nature. 2003 ; Vol. 423, No ... Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo. Nature. 2003 Jun 12;423(6941): ... Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo. / Kanemaki, M; Sanchez-Diaz, A ... Dive into the research topics of Functional proteomic identification of DNA replication proteins by induced proteolysis in ...

https://discovery.dundee.ac.uk/en/publications/functional-proteomic-identification-of-dna-replication-proteins-b

Ubiquitin and proteolysis. Journal of Biosciences. 2016 Sept; 41(3): 325-329. ...

https://imsear.searo.who.int/handle/123456789/181594

Peripheral and integral membrane proteins analyzed by proteolysis and TX114 ... Sodium carbonate extraction/Triton X-114 phase separation and mild proteolysis (proteinase K, PK) of intact exosomes is used in ... appear bound to the outer exosome surface since they are sensitive to PK proteolysis. The finding that outer surface-localized ... Peripheral and integral membrane proteins analyzed by proteolysis and TX114. ...

https://opal.latrobe.edu.au/articles/journal_contribution/Surfaceome_of_exosomes_secreted_from_the_colorectal_cancer_cell_line_SW480_Peripheral_and_integral_membrane_proteins_analyzed_by_proteolysis_and_TX114/13685470/1

DESCRIPTION (provided by applicant): The dorsoventral axis of the Drosophila embryo is established by ventral activation of the Toll signaling pathway, resulting in the graded nuclear uptake of the Dorsal transcription factor. Pathway activation relies on a ventral cue synthesized during oogenesis through the action of Pipe, a putative heparan sulfate 2-O- sulfotransferase, on an unknown carbohydrate substrate. In the embryo, the ligand for the receptor Toll is generated by a proteolytic processing reaction involving 4 members of a serine protease cascade, Nude1, Gastrulation Defective (GD), Snake and Easter. Published work has shown that early cascade events occur independently of pipe activity and are not ventrally restricted, while new data shows that activation of the Easter protease requires pipe and is probably ventrally restricted. These observations establish that spatial control occurs within the protease cascade. To investigate the mechanism by which pipe regulates the cascade, three ...

https://augusta.pure.elsevier.com/en/projects/spatial-control-of-proteolysis-in-dorsoventral-polarity

Adults with obesity and knee plus hand OA have distinct fecal metabolomes characterized by increased products of proteolysis, ... Title : Fecal Metabolomics Reveals Products of Dysregulated Proteolysis and Altered Microbial Metabolism in Obesity-Related ... These metabolic perturbations indicate a possible role of dysregulated proteolysis in OA. ... Fecal Metabolomics Reveals Products of Dysregulated Proteolysis and Altered Microbial Metabolism in Obesity-Related ...

https://stacks.cdc.gov/view/cdc/112965

... involved in proteolysis; interacts with the proteasome; contains an N-terminal Ub-like (UBL) and a C-terminal Ub-associated ( ...

https://www.yeastgenome.org/locus/S000004889

Intramembrane proteolysis, Alzheimer´s disease, Parkinsons disease, type-2 diabetes, γ-secretase, signal peptide peptidase , ... Atherogenic LOX-1 signaling is controlled by SPPL2-mediated intramembrane proteolysis. Mentrup T, Theodorou K, Cabrera-Cabrera ... Phagosomal signalling of the C-type lectin receptor Dectin-1 is terminated by intramembrane proteolysis. ...

https://www.i-proteolysis.de/people/regina-fluhrer-1/

Limited proteolysis of MUPs. MUPs. Wu, C., Robertson, D.H.L., Hubbard, S.J. Gaskell, S.J. & Beynon, R.J. (1999) Proteolysis of ... Limited proteolysis of native proteins. Ellison, D., Hinton, J., Hubbard, S.J. & Beynon, R.J. (1995) Limited proteolysis of ... Prevention of proteolysis. Proteomics. Beynon RJ, Oliver S. (2004) Avoidance of proteolysis in extracts. Methods Mol Biol. 244: ... Limited proteolysis. Hubbard, S. J. & Beynon, R. J. (2001). Proteolysis of native proteins as a structural probe. In ...

http://www.phbuffers.org/PDF/files/tag-proteolysis.html

Given the growing potential for treatment-induced disease, side effects must be treated as potential symptoms for a second diagnosis. Rigorous, differentiating confirmation must be performed, diagnosis made and "treatment" applied, the latter being significantly complicated due to ongoing treatment for the primary or initial disease. Eliminating the likelihood of treatment-induced disease in early-stage drug discovery has enormous benefits but can only become a reality if clinical indicators can be reliably converted into molecular risk factors for a specific disease. Within a broad context, translation of clinical observations into the capacities of the research laboratory comprises a wholly new biomarker discovery area.. ...

https://www.4open-sciences.org/articles/fopen/full_html/2022/01/fopen220009/F5.html

Nakano, S., Zheng, G., Nakano, M. M., & Zuber, P. (2002). Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis. ... Nakano, S, Zheng, G, Nakano, MM & Zuber, P 2002, Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis, Journal of ... An in vitro proteolysis experiment using purified proteins demonstrated that Spx was degraded by ClpCP but only in the presence ... An in vitro proteolysis experiment using purified proteins demonstrated that Spx was degraded by ClpCP but only in the presence ...

https://ohsu.pure.elsevier.com/en/publications/multiple-pathways-of-spx-yjbd-proteolysis-in-bacillus-subtilis-2

Several alternatives to agrin for this function are suggested, including focal pericellular proteolysis and integrin signaling ... 4.3.2. Proteolysis as Mediator of Synapse Maintenance. Finally, it should be noted that even if focal proteolysis ultimately ... If focal proteolysis is a key mechanism in mediating cell-cell interaction at the NMJ, this would hardly be a novel phenomenon ... Focal Pericellular Proteolysis. As discussed in Section 3.2.2, synapse formation in the amphibian in vitro system is invariably ...

https://www.mdpi.com/2073-4409/8/11/1448

In vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysis. The ... In vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysis. / Peng, Bi ... In vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysis.. ... title = "In vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysis.", ...

https://researchexperts.utmb.edu/en/publications/in-vitro-protein-complex-formation-with-cytoskeleton-anchoring-do

The amino-terminal one-third of the influenza virus PA protein is responsible for the induction of proteolysis. J Virol. 1996; ...

https://wwwnc.cdc.gov/eid/article/12/9/06-0276-t1

We hypothesized that OPG expression is increased in human AAAs and is associated with proteolysis. Methods and Results: AAA ... Osteoprotegerin is associated with aneurysm diameter and proteolysis in abdominal aortic aneurysm disease ... Osteoprotegerin is associated with aneurysm diameter and proteolysis in abdominal aortic aneurysm disease. Arteriosclerosis, ...

https://researchonline.jcu.edu.au/21583/

PROTACs, otherwise known as PROteolysis TArgeting Chimera, emerged as a novel therapeutic modality in drug development and ...

https://labtesting.wuxiapptec.com/tag/proteolysis-targeting-chimera/

Intramembrane proteolysis is now widely recognized as an important physiological pathway required for reverse signaling and membrane protein degradation. (cipsm.de)
We demonstrate that similar to -secretase substrates, intramembrane proteolysis of Bri2 (Itm2b) is greatly facilitated by an initial shedding event mediated by ADAM-10. (cipsm.de)
Serial deletions revealed that the length of the ectodomain negatively correlates with efficient intramembrane proteolysis. (cipsm.de)
Failure of shedding of Bri3 is accompanied by a lack of intramembrane proteolysis by SPPL2b. (cipsm.de)
Surprisingly, a low molecular weight membrane-retained stub of Bri3 also fails to be processed by SPPL2b, indicating that shedding per se is not sufficient for subsequent intramembrane proteolysis. (cipsm.de)
Extensive domain swapping analysis reveals that primary sequence determinants within the intracellular domain and the transmembrane domain together with short luminal juxtamembrane sequences are required for efficient intramembrane proteolysis. (cipsm.de)
Phagosomal signalling of the C-type lectin receptor Dectin-1 is terminated by intramembrane proteolysis. (i-proteolysis.de)
Atherogenic LOX-1 signaling is controlled by SPPL2-mediated intramembrane proteolysis. (i-proteolysis.de)
QARIP: a web server for quantitative proteomic analysis of regulated intramembrane proteolysis. (skoltech.ru)
Regulated intramembrane proteolysis (RIP) is a critical mechanism for intercellular communication and regulates the function of membrane proteins through sequential proteolysis. (skoltech.ru)
RIP typically starts with ectodomain shedding of membrane proteins by extracellular membrane-bound proteases followed by intramembrane proteolysis of the resulting membrane-tethered fragment. (skoltech.ru)
Here we present the QARIP (Quantitative Analysis of Regulated Intramembrane Proteolysis) web server which matches identified peptides to the protein transmembrane topology. (skoltech.ru)
Dive into the research topics of 'QARIP: a web server for quantitative proteomic analysis of regulated intramembrane proteolysis. (skoltech.ru)
Taking a position on intramembrane proteolysis. (bvsalud.org)

However, the possibility remains that ischemia selectively accelerates the breakdown of vital proteins, a phenomenon that may not be detected by measuring overall proteolysis. (elsevier.com)
Budding yeast strains have been constructed in which essential proteins of unknown function have been fused to a 'heat-inducible-degron' cassette that targets the protein for proteolysis at 37 degreesC (ref. 4). (dundee.ac.uk)
Proteolysis of native proteins as a structural probe. (phbuffers.org)
An in vitro proteolysis experiment using purified proteins demonstrated that Spx was degraded by ClpCP but only in the presence of one of the ClpC adapter proteins, MecA or YpbH. (elsevier.com)
Regulated proteolysis controls the quality and quantity of proteins. (grantome.com)
The bioavailability of IGFs is regulated by the proteolysis of IGF-binding proteins. (authorea.com)
Supplemental glutamine can help promote cell volumization, the mechanism of drawing of water INSIDE muscle cells which can help increase muscle hydration, increase protein synthesis (the making of proteins), and decrease proteolysis (the breakdown of protein). (firstendurance.ca)

Binding of uPA may influence pericellular proteolysis and/or activate intracellular signal transduction. (unige.ch)

Association between seven single nucleotide polymorphisms involved in inflammation and proteolysis and abdominal aortic aneurysm. (cdc.gov)

IFNalpha promotes the phosphorylation of IFNAR1 on Ser535, followed by recruitment of the E3 ubiquitin ligase, beta-TrCP2 (beta-transducin repeats-containing protein 2), ubiquitination of IFNAR1 and proteolysis. (pasteur.fr)
This review discusses the different roles proteolysis plays in regulating G protein-coupled receptors (GPCRs). (reading.ac.uk)
In the current study, we investigated whether the orphan drug, dichloroacetate, could alter amyloid precursor protein proteolysis. (lancs.ac.uk)
Similar enhancement of ADAM-mediated amyloid precursor protein processing by dichloroacetate was observed in unrelated cell lines and the effect was not exclusive to the amyloid precursor protein as an ADAM substrate, as indicated by dichloroacetate-enhanced proteolysis of the Notch ligand, Jagged1. (lancs.ac.uk)
Despite altering proteolysis of the amyloid precursor protein, dichloroacetate did not significantly affect the expression/activity of α-, β- or γ-secretases. (lancs.ac.uk)
In conclusion, dichloroacetate can inhibit amyloidogenic and promote non-amyloidogenic proteolysis of the amyloid precursor protein. (lancs.ac.uk)
The material was named proteolysis-inducing factor (PIF), because of its ability to directly induce protein loss in murine myotubes and isolated muscle preparations, and because this was the name given to an unidentified factor in human serum, which was capable of inducing proteolysis in isolated muscle preparations [ 11 ]. (biomedcentral.com)
Many mechanisms of protein function contribute to amyloidogenesis, including "nonphysiologic proteolysis, defective or absent physiologic proteolysis, mutations involving changes in thermodynamic or kinetic properties, and pathways that are yet to be defined. (medscape.com)
The putative proteolysis by ClpXP might require another adapter protein. (elsevier.com)
In vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysis. (utmb.edu)
Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP). (anl.gov)
The increases in proteolysis correlate well with increases in steady state uPA mRNA levels and with increased levels of uPAR protein. (cdc.gov)
Protein inactivation in mycobacteria by controlled proteolysis and its application to deplete the beta subunit of RNA polymerase. (cornell.edu)

Our results show that sequential proteolysis of LexA is conserved in S. aureus and that the NTD may differentially regulate a subset of genes in the SOS regulon. (gva.es)

In the present study, we show that catalytic activation of Tyk2 is not essential for IFNAR1 internalization, but is required for ligand-induced IFNAR1 serine phosphorylation, ubiquitination and efficient lysosomal proteolysis. (pasteur.fr)
Conversely, in the presence or absence of DNA, Xic3 was stable in the Xenopus interphase egg extract and did not exhibit a shift indicative of phosphorylation.Conclusions: During interphase, Xic2 is targeted for DNA- and PCNA-dependent proteolysis that is negatively regulated by CDK2 phosphorylation. (uthscsa.edu)

The neutral proteases activated by calcium ions, called calpains, are partially responsible for postmortem proteolysis, leading to a progressive increase in meat tenderness. (usp.br)

Chemical composition, microbiology and proteolysis were studied during the ripening. (inonu.edu.tr)

Urokinase-type plasminogen activator (uPA) is a potent catalyst of extracellular proteolysis, which also binds to a high-affinity plasma membrane receptor (uPAR). (unige.ch)
Thus, combined overexpression of uPA and uPAR acts in synergy to promote pathogenic extracellular proteolysis. (unige.ch)

To determine whether future studies on the effects of proteolytic inhibition on infarct size are feasible, the ability of the proteinase inhibitors antipain, leupeptin, pepstatin and chymostatin, given in vivo, to interfere with proteolysis in ischemic myocardium was also evaluated. (elsevier.com)

Limited proteolysis and proton NMR spectroscopy of Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex. (ox.ac.uk)

Endothelial cells were exposed to chrysotile (12001295), crocidolite (12001284), or refractory-ceramic-fiber-1 (RCF-1) in an effort to determine whether asbestos induced endothelial cell activation is associated with altered proteolysis and expression of urokinase-like- plasminogen-activator (uPA) and urokinase-like-plasminogen-activator- receptor (uPAR). (cdc.gov)
Thus vitronectin serves to regulate proteolysis initiated by plasminogen activation. (en-academic.com)

This process is called proteolysis, and presenilin 1 is described as the proteolytic subunit of γ-secretase. (medlineplus.gov)

Moving on from basic biology, international chapter authors examine a range of pathological conditions associated with proteolysis, including inflammation, wound healing, and cancer. (elsevier.com)

Microparticle-enhanced nephelometric immunoassay of residual β-CN, performed in reaction supernatants, indicated there is no significant influence of β-CN fragments (β-CN f(1-105 / 7) and mixture of C-terminal peptides β-CN (29-209), (106-209), (108-209)) on the proteolysis of the whole β-CN. (dairy-journal.org)

In this work, we used cytotoxicity and enzymatic assays and morphological analysis to examine the effects of a proteolysis-inducing factor (PIF)-like molecule purified from ascitic fluid of Walker tumour-bearing rats (WF), which has been suggested to be responsible for muscle atrophy, on cultured C 2 C 12 muscle cells. (biomedcentral.com)
To test the hypothesis that cellular proteinases contribute to ischemic myocellular death, measurements were made of tyrosine release (an index of overall proteolysis) from incubated slices of nonischemic and ischemic myocardium obtained at various times after coronary artery occlusion in rats. (elsevier.com)

Kinetic study of β-CN proteolysis indicated a perceptible loss of enzyme activity in plasmin-Sepharose conjugate compared to free plasmin (V max = 3.8 10 -2 and 53.5 10 -2 OD unit / min, K m = 1.2 10 -4 et 6.2 10 -4 mol / l, respectively). (dairy-journal.org)

In this study, we used T cells expressing cleavable or non-cleavable L-selectin and determined the impact of L-selectin proteolysis on T cell activation in virus-infected mice. (uea.ac.uk)
Following virus infection of mice, L-selectin proteolysis promoted early clonal expansion of cytotoxic T cells resulting in an 8-fold increase over T cells unable to cleave L-selectin. (uea.ac.uk)

We isolated a structural domain from both the bacterial-expressed C-terminal cytoplasmic region of human occludin and native cellular occludin, extracted from epithelial (Madin-Darby canine kidney) or endothelial (human brain) cells, by limited proteolysis with trypsin. (utmb.edu)

Therefore, we considered other roles for L-selectin proteolysis during T cell activation. (uea.ac.uk)

These results demonstrate that whatever proteolysis is occurring during acute myocardial infarction is largely mediated by cathepsins A, B, D, L and H and by calciumactivated neutral protease (that is, the enzymes sensitive to the inhibitors used). (elsevier.com)

These results indicate that WF has similar effects to those of proteolysis-inducing factor, but is less potent than the latter. (biomedcentral.com)

The incorporation of whey cheese in the manufacture of mould-ripened Civil cheese altered the gross composition and adversely affected proteolysis in the cheeses. (inonu.edu.tr)
The inoculated P.roqueforti moulds appeared to grow slowly on those cheeses, and little proteolysis was evident in all cheese treatments during the first 90days of ripening. (inonu.edu.tr)

Although the use of peptidase inhibitors has already brought success in the treatment of diseases such as hypertension, the discovery of new regulatory mechanisms involving proteolysis that control GPCRs may provide additional targets to modulate dysregulated GPCR signaling in disease. (reading.ac.uk)

Because antipain, leupeptin and pepstatin significantly suppress such proteolysis, these agents might be useful in further assessing any potential contribution of cellular proteinases to the production of ischemic myocellular death. (elsevier.com)

PROTACs, otherwise known as PROteolysis TArgeting Chimera, emerged as a novel therapeutic modality in drug development and currently show promising clinical results for tackling some of the most complex diseases. (wuxiapptec.com)
Based on these results, we propose that ADAM17-dependent proteolysis of L-selectin should be considered a regulator of T-cell activation at sites of immune activity. (uea.ac.uk)

Electrophoretic study of the reaction mixtures showed that the proteolysis of β-CN f( 1-105 / 7) by immobilized or free plasmin, producing β-CN f(29-105 / 7), succeeds the reaction of the whole β-CN. (dairy-journal.org)

The increase in flexibility of the linker domain upon IGF-1 binding may explain the IGF-dependent modulation of proteolysis of IGFBP2 in this domain. (authorea.com)

These data represent the first assessment of myocardial proteolysis throughout the development of ischemic death, and suggest that cellular proteinases do not play a causal role in this process. (elsevier.com)
We confirm an essential and non-redundant role for ADAM17 in TCR-induced proteolysis of L-selectin in mouse and human T cells and show that L-selectin cleavage does not regulate T cell activation measured by CD69 or TCR internalisation. (uea.ac.uk)

Ubiquitin-dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: killing three birds with one stone. (cdc.gov)

Proteolysis failed to increase in ischemic myocardium throughout the first 24 hours of occlusion, when irreversible damage develops, indicating that cellular proteinases do not undergo generalized activation in this phase. (elsevier.com)

Given the small size and blood-brain-barrier permeability of the drug, further research into its mechanism of action with respect to APP proteolysis may lead to the development of therapies for slowing the progression of Alzheimer's disease. (lancs.ac.uk)

We hypothesized that OPG expression is increased in human AAAs and is associated with proteolysis. (edu.au)

The positive transcription factor of the 5S RNA gene proteolyses during direct exchange between 5S DNA sites. (rupress.org)
Unexpectedly, the direct exchange of factor between 5S DNA sites leads to proteolysis at the C-terminal arm of TFIIIA. (rupress.org)
During the aging of the meat, proteolysis is the major factor that contributes to the increased tenderness. (usp.br)

In-situ zymography for uPA activity in exposed cultures demonstrated that these fibers produce localized increases in proteolysis. (cdc.gov)

In addition, this study provides a new experimental model that affords serial assessments of regional myocardial proteolysis during the evolution of myocardial infarction. (elsevier.com)

Anatomy23

Organisms8

Diseases2

Chemicals and Drugs147

Analytical, Diagnostic and Therapeutic Techniques and Equipment25

Phenomena and Processes49

Information Science3

Health Care2

Over-expression, rapid preparation and some properties of c-terminal BARc region in PICK1. (1/2649)

Cyclophilin D is required for mitochondrial removal by autophagy in cardiac cells. (2/2649)

Building and remodeling synapses. (3/2649)

Beta-arrestin: a signaling molecule and potential therapeutic target for heart failure. (4/2649)

Depletion of Beclin-1 due to proteolytic cleavage by caspases in the Alzheimer's disease brain. (5/2649)

Pregabalin suppresses calcium-mediated proteolysis and improves stroke outcome. (6/2649)

Regulation of PINK1-Parkin-mediated mitophagy. (7/2649)

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1. (8/2649)

Proteolysis

Peptide Hydrolases

Endopeptidases

Hydrolysis

Calpain

Trypsin

Amino Acid Sequence

Molecular Sequence Data

Proteasome Endopeptidase Complex

Peptide Fragments

Cysteine Endopeptidases

Ubiquitins

Chymotrypsin

Electrophoresis, Polyacrylamide Gel

Protease Inhibitors

Serine Endopeptidases

Molecular Weight

Thermolysin

Kinetics

Protein Processing, Post-Translational

Multienzyme Complexes

Ubiquitin

Protein Binding

Binding Sites

Protein Structure, Tertiary

Endopeptidase Clp

Protein Conformation

Cysteine Proteinase Inhibitors

Substrate Specificity

Recombinant Proteins

Endopeptidase K

Leupeptins

Metalloendopeptidases

Cathepsins

Proteins

ATP-Dependent Proteases

Ubiquitin-Protein Ligase Complexes

Ubiquitin-Protein Ligases

SKP Cullin F-Box Protein Ligases

Ligases

Mutation

Cell Line

Membrane Proteins

Papain

Subtilisins

Lysosomes

Peptide Mapping

Fibrinolysin

Amyloid Precursor Protein Secretases

Anaphase-Promoting Complex-Cyclosome

Escherichia coli

Amino Acids

Cattle

Peptides

Muscle Proteins

Leucine

Enzyme Activation

Macromolecular Substances

Pancreatic Elastase

ADAM Proteins

Blotting, Western

Bacterial Proteins

Base Sequence

Phosphorylation

Cathepsin B

Models, Molecular

Carrier Proteins

Sequence Homology, Amino Acid

Recombinant Fusion Proteins

Cell Membrane

Aspartic Acid Endopeptidases

Cells, Cultured

Immunoblotting

Cell Cycle Proteins

Cathepsin L

Protein Denaturation

Models, Biological

Enzyme Precursors

F-Box Proteins

Postmortem Changes