Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Cystatins: A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.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.Papain: A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.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.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.HIV Protease: Enzyme of the human immunodeficiency virus that is required for post-translational cleavage of gag and gag-pol precursor polyproteins into functional products needed for viral assembly. HIV protease is an aspartic protease encoded by the amino terminus of the pol gene.Calpain: Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Dipeptides: Peptides composed of two amino acid units.Caspase 1: A long pro-domain caspase that has specificity for the precursor form of INTERLEUKIN-1BETA. It plays a role in INFLAMMATION by catalytically converting the inactive forms of CYTOKINES such as interleukin-1beta to their active, secreted form. Caspase 1 is referred as interleukin-1beta converting enzyme and is frequently abbreviated ICE.Protease La: 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.Cysteine Dioxygenase: An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.Spirometra: A genus of tapeworms of the family Diphyllobothriidae, which are parasites of fish-eating cats, dogs, and birds. Infection in man is caused by eating undercooked fish. The larval form is called SPARGANUM.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.Caspases: 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.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.ATP-Dependent Proteases: 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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Cysteine Synthase: An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.Kinetics: The rate dynamics in chemical or physical systems.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.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Paragonimus: A genus of lung flukes of the family Troglotrematidae infecting humans and animals. This genus consists of several species one of which is PARAGONIMUS WESTERMANI, a common lung fluke in humans.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Helminth Proteins: Proteins found in any species of helminth.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Streptococcus pyogenes: A species of gram-positive, coccoid bacteria isolated from skin lesions, blood, inflammatory exudates, and the upper respiratory tract of humans. It is a group A hemolytic Streptococcus that can cause SCARLET FEVER and RHEUMATIC FEVER.Lysosomes: 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)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.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Bromelains: Protein-digesting and milk-clotting enzymes found in PINEAPPLE fruit juice and stem tissue. Enzymes from the two sources are distinguished as fruit bromelain and stem bromelain. This enzyme was formerly listed as EC 3.4.22.4.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Bacterial Proteins: Proteins found in any species of bacterium.Cystatin B: An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.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)Cystatin A: A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Proteolysis: 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.Protease Nexins: Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.Oligopeptides: Peptides composed of between two and twelve amino acids.Apoptosis: 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.Cathepsin W: A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.Protozoan Proteins: Proteins found in any species of protozoan.Leupeptins: 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.Sulfhydryl Compounds: Compounds containing the -SH radical.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.Caspase 3: 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.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.Cystatin C: An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.Ubiquitin-Specific Proteases: Members of the peptidase C19 family which regulate signal transduction by removing UBIQUITIN from specific protein substrates via a process known as deubiquitination or deubiquitylation.Amino Acid Chloromethyl Ketones: Inhibitors of SERINE ENDOPEPTIDASES and sulfhydryl group-containing enzymes. They act as alkylating agents and are known to interfere in the translation process.Serpins: A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.Caspase 6: 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.Coumarins: Synthetic or naturally occurring substances related to coumarin, the delta-lactone of coumarinic acid.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Molecular Weight: The sum of the weight of all the atoms in a molecule.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.Cathepsin Z: A ubiquitously-expressed cysteine peptidase that exhibits carboxypeptidase activity. It is highly expressed in a variety of immune cell types and may play a role in inflammatory processes and immune responses.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Vinyl CompoundsCystine: 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.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.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Cystatin M: A cystatin subtype that has a diverse tissue distribution, target specificity, and functions as an endogenous inhibitor of lysosomal cysteine proteases.Paragonimiasis: Infection with TREMATODA of the genus PARAGONIMUS.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.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.Haemonchus: A genus of parasitic nematode worms which infest the duodenum and stomach of domestic and wild herbivores, which ingest it with the grasses (POACEAE) they eat. Infestation of man is accidental.Leishmania mexicana: A parasitic hemoflagellate of the subgenus Leishmania leishmania that infects man and animals including rodents. The Leishmania mexicana complex causes both cutaneous (LEISHMANIASIS, CUTANEOUS) and diffuse cutaneous leishmaniasis (LEISHMANIASIS, DIFFUSE CUTANEOUS) and includes the subspecies amazonensis, garnhami, mexicana, pifanoi, and venezuelensis. L. m. mexicana causes chiclero ulcer, a form of cutaneous leishmaniasis (LEISHMANIASIS, CUTANEOUS) in the New World. The sandfly, Lutzomyia, appears to be the vector.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).SulfonesProtein 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.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.Caspase 2: A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Activation of this enzyme can occur via the interaction of its caspase recruitment domain with CARD SIGNALING ADAPTOR PROTEINS. Caspase 2 plays a role in APOPTOSIS by cleaving and activating effector pro-caspases. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Ficain: A sulfhydryl proteinase with cysteine at the active site from ficus latex. Preferential cleavage is at tyrosine and phenylalanine residues. EC 3.4.22.3.Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Haemonchiasis: Infection with nematodes of the genus HAEMONCHUS, characterized by digestive abnormalities and anemia similar to that from hookworm infestation.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Iodoacetamide: An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.Caspase Inhibitors: Endogenous and exogenous compounds and that either inhibit CASPASES or prevent their activation.Trypanosoma cruzi: The agent of South American trypanosomiasis or CHAGAS DISEASE. Its vertebrate hosts are man and various domestic and wild animals. Insects of several species are vectors.Entamoeba histolytica: A species of parasitic protozoa causing ENTAMOEBIASIS and amebic dysentery (DYSENTERY, AMEBIC). Characteristics include a single nucleus containing a small central karyosome and peripheral chromatin that is finely and regularly beaded.Arthropod Proteins: Proteins synthesized by organisms belonging to the phylum ARTHROPODA. Included in this heading are proteins from the subdivisions ARACHNIDA; CRUSTACEA; and HORSESHOE CRABS. Note that a separate heading for INSECT PROTEINS is listed under this heading.Aspartic Acid Endopeptidases: A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Protein PrecursorsOxidation-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).Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Blotting, Western: 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.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Antigens, Dermatophagoides: Antigens from the house dust mites (DERMATOPHAGOIDES), mainly D. farinae and D. pteronyssinus. They are proteins, found in mite feces or mite extracts, that can cause ASTHMA and other allergic diseases such as perennial rhinitis (RHINITIS, ALLERGIC, PERENNIAL) and atopic dermatitis (DERMATITIS, ATOPIC). More than 11 groups of Dermatophagoides ALLERGENS have been defined. Group I allergens, such as Der f I and Der p I from the above two species, are among the strongest mite immunogens in humans.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.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.DiazomethaneIodoacetic Acid: A derivative of ACETIC ACID that contains one IODINE atom attached to its methyl group.Pancreatic Elastase: 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.Plasmodium falciparum: A species of protozoa that is the causal agent of falciparum malaria (MALARIA, FALCIPARUM). It is most prevalent in the tropics and subtropics.Porphyromonas gingivalis: A species of gram-negative, anaerobic, rod-shaped bacteria originally classified within the BACTEROIDES genus. This bacterium produces a cell-bound, oxygen-sensitive collagenase and is isolated from the human mouth.Sparganosis: Infection of animals, including fish and man, with a developmental stage of Diphyllobothrium. This stage has recently been referred to as a plerocercoid but the name sparganum has persisted. Therefore, infection of fish or other animals with the plerocercoid larvae is sparganosis. Fish-eating mammals, including man, are the final hosts.Caspase 10: A long pro-domain caspase that contains a death effector domain in its pro-domain region. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS. Caspase 10 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Exotoxins: Toxins produced, especially by bacterial or fungal cells, and released into the culture medium or environment.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Immunoblotting: 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.RNA, Messenger: 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.Chymotrypsin: 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.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Viral Proteins: Proteins found in any species of virus.Vacuoles: Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.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.Parasites: Invertebrate organisms that live on or in another organism (the host), and benefit at the expense of the other. Traditionally excluded from definition of parasites are pathogenic BACTERIA; FUNGI; VIRUSES; and PLANTS; though they may live parasitically.Salivary Cystatins: A group of closely-related cystatins found in SALIVA.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Subtilisins: A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Recombinant Fusion Proteins: 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.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.Chromatography, Ion Exchange: Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.Virulence: The degree of pathogenicity within a group or species of microorganisms or viruses as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host. The pathogenic capacity of an organism is determined by its VIRULENCE FACTORS.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Endopeptidase Clp: 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.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Caspase 7: A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 3 and CASPASE 10. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Metalloproteases: Proteases which use a metal, normally ZINC, in the catalytic mechanism. This group of enzymes is inactivated by metal CHELATORS.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.Caseins: A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.Host-Parasite Interactions: The relationship between an invertebrate and another organism (the host), one of which lives at the expense of the other. Traditionally excluded from definition of parasites are pathogenic BACTERIA; FUNGI; VIRUSES; and PLANTS; though they may live parasitically.SemicarbazonesCell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Epoxy Compounds: Organic compounds that include a cyclic ether with three ring atoms in their structure. They are commonly used as precursors for POLYMERS such as EPOXY RESINS.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Chymopapain: A cysteine endopeptidase isolated from papaya latex. Preferential cleavage at glutamic and aspartic acid residues. EC 3.4.22.6.Temperature: 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.Hemoglobins: The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.DNA Fragmentation: Splitting the DNA into shorter pieces by endonucleolytic DNA CLEAVAGE at multiple sites. It includes the internucleosomal DNA fragmentation, which along with chromatin condensation, are considered to be the hallmarks of APOPTOSIS.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.Molecular Probes: A group of atoms or molecules attached to other molecules or cellular structures and used in studying the properties of these molecules and structures. Radioactive DNA or RNA sequences are used in MOLECULAR GENETICS to detect the presence of a complementary sequence by NUCLEIC ACID HYBRIDIZATION.Trypanosoma congolense: A species of Trypanosome hemoflagellates that is carried by tsetse flies and causes severe anemia in cattle. These parasites are also found in horses, sheep, goats, and camels.Ananas: A plant genus of the family BROMELIACEAE known for the edible fruit that is the source of BROMELAINS.Viral Nonstructural Proteins: Proteins encoded by a VIRAL GENOME that are produced in the organisms they infect, but not packaged into the VIRUS PARTICLES. Some of these proteins may play roles within the infected cell during VIRUS REPLICATION or act in regulation of virus replication or VIRUS ASSEMBLY.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Signal Transduction: 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.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Kininogens: Endogenous peptides present in most body fluids. Certain enzymes convert them to active KININS which are involved in inflammation, blood clotting, complement reactions, etc. Kininogens belong to the cystatin superfamily. They are cysteine proteinase inhibitors. HIGH-MOLECULAR-WEIGHT KININOGEN; (HMWK); is split by plasma kallikrein to produce BRADYKININ. LOW-MOLECULAR-WEIGHT KININOGEN; (LMWK); is split by tissue kallikrein to produce KALLIDIN.Rabbits: 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.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.Cathepsin D: 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).HeLa Cells: 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.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Hemagglutinins: Agents that cause agglutination of red blood cells. They include antibodies, blood group antigens, lectins, autoimmune factors, bacterial, viral, or parasitic blood agglutinins, etc.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Adhesins, Bacterial: Cell-surface components or appendages of bacteria that facilitate adhesion (BACTERIAL ADHESION) to other cells or to inanimate surfaces. Most fimbriae (FIMBRIAE, BACTERIAL) of gram-negative bacteria function as adhesins, but in many cases it is a minor subunit protein at the tip of the fimbriae that is the actual adhesin. In gram-positive bacteria, a protein or polysaccharide surface layer serves as the specific adhesin. What is sometimes called polymeric adhesin (BIOFILMS) is distinct from protein adhesin.Carbon-Nitrogen Lyases: Enzymes that catalyze the cleavage of a carbon-nitrogen bond by means other than hydrolysis or oxidation. Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. EC 4.3.Life Cycle Stages: The continuous sequence of changes undergone by living organisms during the post-embryonic developmental process, such as metamorphosis in insects and amphibians. This includes the developmental stages of apicomplexans such as the malarial parasite, PLASMODIUM FALCIPARUM.Models, Biological: 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.Liliaceae: A monocot family within the order Liliales. This family is divided by some botanists into other families such as Convallariaceae, Hyacinthaceae and Amaryllidaceae. Amaryllidaceae, which have inferior ovaries, includes CRINUM; GALANTHUS; LYCORIS; and NARCISSUS and are known for AMARYLLIDACEAE ALKALOIDS.Mice, Inbred C57BLTrypanosoma: A genus of flagellate protozoans found in the blood and lymph of vertebrates and invertebrates, both hosts being required to complete the life cycle.Trypsin Inhibitors: Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.Opisthorchis: A genus of trematode liver flukes of the family Opisthorchidae. It consists of the following species: O. felineus, O. noverca (Amphimerus noverca), and O. viverrini. The intermediate hosts are snails, fish, and AMPHIBIANS.Ethylmaleimide: A sulfhydryl reagent that is widely used in experimental biochemical studies.Caspase 14: A short pro-domain caspase that is almost exclusively expressed in the EPIDERMIS and may play a role in the differentiation of epidermal KERATINOCYTES.Caspase 8: A long pro-domain caspase that contains a death effector domain in its pro-domain region. Caspase 8 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS.Mice, Knockout: Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.Pichia: Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.Histidine: An essential amino acid that is required for the production of HISTAMINE.Drug Design: The molecular designing of drugs for specific purposes (such as DNA-binding, enzyme inhibition, anti-cancer efficacy, etc.) based on knowledge of molecular properties such as activity of functional groups, molecular geometry, and electronic structure, and also on information cataloged on analogous molecules. Drug design is generally computer-assisted molecular modeling and does not include pharmacokinetics, dosage analysis, or drug administration analysis.Paragonimus westermani: A species of lung fluke infecting humans and other animals, and found chiefly in Asia and the Far East.Carbon-Sulfur Lyases: Enzymes that catalyze the cleavage of a carbon-sulfur bond by means other than hydrolysis or oxidation. EC 4.4.KetonesCalcium: 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.Exopeptidases: A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.
Otubains are deubiquitinating cysteine proteases (DUBs; see MIM 602519) that belong to the ovarian tumor (OTU) protein ... a new family of cysteine proteases in the ubiquitin pathway". EMBO Rep. 4 (5): 517-22. doi:10.1038/sj.embor.embor824. PMC ... 2004). "Sequence organization and matrix attachment regions of the human serine protease inhibitor gene cluster at 14q32.1". ...
... are cysteine proteases related by amino acid sequence to trypsin-like serine proteases. Picornain 3C is encoded by ... Picornavirus belongs to the family Picornaviridae. Picornavirus virions are nonenveloped and the +ssRNA nonsegmented genome is ... Caspase stands for cysteine-aspartic acid protease and play an essential role in the apoptotic pathway of the cell. Protease 2A ... Hepatitis A 3C proteinase is a member of the cysteine proteases that are responsible for the infectivity and maturation of HAV ...
... is a lysosomal enzyme that belongs to the papain family of cysteine proteases. While a role in antigen presentation ... Cathepsin S is a member of the peptidase C1 family and is a lysosomal cysteine protease that may participate in the degradation ... The mechanism by which cathepsin S leads to itch and pain is consistent with the capacity of this cysteine protease to activate ... This is because the cysteine enzyme can no longer act together with other proteases to break up the brain extracellular matrix ...
... belongs to a family of caspases, cysteine-aspartic proteases involved in apoptosis and cytokine signalling. Apoptotic ... the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". ... the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". ... This variant is used as the reference sequence, and it has full cysteine protease activity. Isoform 2 doesn't include exons 3, ...
... belongs to a family of lysosomal cysteine proteases and plays an important role in intracellular proteolysis. ... "The cysteine protease cathepsin B is a key drug target and cysteine protease inhibitors are potential therapeutics for ... Hook G, Hook V, Kindy M (2011). "The cysteine protease inhibitor, E64d, reduces brain amyloid-β and improves memory deficits in ... Hook V, Kindy M, Hook G (February 2007). "Cysteine protease inhibitors effectively reduce in vivo levels of brain beta-amyloid ...
It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic ... the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. ... which may serve as an activation platform for the protease, although it may also be activated in the absence of PIDD. Overall, ...
Peptidase 1 is a cysteine protease belonging to the C1 protein family, with a structure similar to that of papain. Initially, ... As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the ... "Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine protease activity". Biochem. Biophys. Res. ... By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that ...
... a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many ... This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a type II transmembrane ... "Entrez Gene: TMPRSS2 transmembrane protease, serine 2". Yu J, Yu J, Mani RS, Cao Q, Brenner CJ, Cao X, Wang X, Wu L, Li J, Hu M ... The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage. The biological ...
... and cysteine proteases very similar to papain. The soy cotyledon storage proteins, important for human nutrition, can be ... Legume proteins, such as soy and pulses, belong to the globulin family of seed storage proteins called legumin and vicilins, or ... and cysteine proteases very similar to papain. The soy cotyledon storage proteins, important for human nutrition, can be ... "A high-order structure of plant storage proprotein allows its second conversion by an asparagine-specific cysteine protease, a ...
... , also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and ... mountain papaya (Vasconcellea cundinamarcensis). Papain belongs to a family of related proteins with a wide variety of ... After ten minutes, the tissue should be treated with a protease inhibitor solution to stop the protease action. Left untreated ... "Novel cysteine proteinase inhibitors homologous to the proregions of cysteine proteinases". Curr Protein Pept Sci. 3 (2): 231- ...
... and belongs to a family of cysteine proteases called caspases. It is an inflammatory caspase, along with caspase 1, caspase 4 ...
... a cysteine protease with the proregion covalently linked to the active site cysteine". Journal of Molecular Biology. 295 (4): ... These cysteine proteinases belong to the papain family and represent a major component of the lysosomal proteolytic system.In ... It is a member of the cysteine cathepsin protease family, which has 11 members. As one of the 11 cathepsins, cathepsin Z ... Nägler DK, Zhang R, Tam W, Sulea T, Purisima EO, Ménard R (September 1999). "Human cathepsin X: A cysteine protease with unique ...
The first four groups are cysteine proteases, whereas the last group are Zn metalloproteases. USP20 belongs to the USP group ... is a cysteine protease deubiquitinating enzyme (DUB). The catalytic site of USP20, like other DUBs, contains conserved cysteine ... ovarian tumour proteases (OTU), Machado-Joseph disease proteases (MJD), and JAB1/MPN/MOV34 proteases (JAMM/MPN+). ... Ubiquitin-specific protease 20 (USP20), also known as ubiquitin-binding protein 20 and VHL protein-interacting deubiquitinating ...
... and belongs to a family of cysteine proteases called caspases. The function of caspase 4 is not fully known, but it is believed ...
The WFDC domain, or WAP signature motif, contains eight cysteines forming four disulfide bonds at the core of the protein, and ... This gene belongs to the centromeric cluster. GRCh38: Ensembl release 89: ENSG00000175121 - Ensembl, May 2017 GRCm38: Ensembl ... "A locus on human chromosome 20 contains several genes expressing protease inhibitor domains with homology to whey acidic ... functions as a protease inhibitor. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric ...
... (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase ... Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin ... Once activated by cathepsin C, the proteases are capable of degrading various extracellular matrix components, which can lead ... exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases". The EMBO ...
These activities were caused by an intracellular cysteine protease not associated with the lysosome and having an optimum ... A calpain (/ˈkælpeɪn/; EC 3.4.22.52, EC 3.4.22.53) is a protein belonging to the family of calcium-dependent, non-lysosomal ... and the cysteine protease of papaya, papain. Shortly thereafter, the activity was found to be attributable to two main isoforms ... "Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?". ...
... is performed by the Atg8 conjugation system comprising the cysteine protease ATG4 (belonging to the caspase family), as well as ... In the first step, the Gly116 residue of Atg8 binds to a cysteine residue of ATG7 via a thioester bond in an ATP-dependent ...
Abisi S, Burnand KG, Waltham M, Humphries J, Taylor PR, Smith A (December 2007). "Cysteine protease activity in the wall of ... Cystatin C belongs to the type 2 cystatin gene family. Glomerular filtration rate (GFR), a marker of kidney health, is most ... Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory ... It encodes the most abundant extracellular inhibitor of cysteine proteases. It is found in high concentrations in biological ...
This family of serine protease inhibitors belongs to MEROPS inhibitor family I19, clan IW. They inhibit chymotrpsin, a ... Each of these inhibitor domains carries a six-cysteine motif - see below. The first family members to be identified were ... The inhibitor unit of pacifastin is a conserved pattern of six cysteine residues (Cys1 - Xaa9-12 - Cys2 - Asn - Xaa - Cys3 - ... A number of the transferrin family members are also serine peptidases, and belong to MEROPS peptidase family S60 (INTERPRO). ...
Protease serine- cysteine- aspartic- metallo- Enzyme Proteolysis Catalytic triad Convergent evolution The Proteolysis Map ... Five families belonging to two separate superfamilies are currently recognised: the Ntn fold proteosomes (superfamily PB) and ... Protease inhibitor (pharmacology) Protease inhibitor (biology) TopFIND - database of protease specificity, substrates, products ... Threonine proteases are a family of proteolytic enzymes harbouring a threonine (Thr) residue within the active site. The ...
... putative cysteine protease (PRSC), putative MCP, and putative minor capsid protein (mCP). These genes are also referred to as ... All host viruses of the known virophages belong to the group of nucleocytoplasmic large DNA viruses. Studies have been done to ...
The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of ... Cystatins mainly inhibit peptidase enzymes (another term for proteases) belonging to peptidase families C1 (papain family) and ... van Wyk SG, Du Plessis M, Cullis CA, Kunert KJ, Vorster BJ (November 2014). "cysteine protease and cystatin expression and ... found some 19 different cystatins similar to oryzacystatin-I in the soybean along with related cysteine proteases. Chicken ...
Classes of proteases are: Aspartic protease inhibitors Cysteine protease inhibitors Metalloprotease inhibitors Serine protease ... The inhibitor I29 domain, which belongs to MEROPS peptidase inhibitor family I29, is found at the N-terminus of a variety of ... It contains inhibitors of multiple cysteine and serine protease families. Their mechanism of action relies on undergoing a ... Inhibitor family I42 includes chagasin, a reversible inhibitor of papain-like cysteine proteases. Chagasin has a beta-barrel ...
TNMD belongs to the new family of type II transmembrane glycoproteins. The gene is localized on the X chromosome and accounts ... The last exon of TNMD gene encodes the conserved C-terminal cysteine-rich domain, which makes up the part of the protein ... Unlike chondromodulin-1, TNMD does not have a processing signal for furin protease. The extracellular part, prior the putative ... This domain consists of a homologous sequence of approximately 100 amino acids containing a pair of conserved cysteine residues ...
The single cysteine residue of A1AT in position 256 (UniProtKB nomenclature) is found to be covalently linked to a free single ... A protease inhibitor, it is also known as alpha1-proteinase inhibitor (A1PI) or alpha1-antiproteinase (A1AP) because it ... Alpha-1-antitrypsin or α1-antitrypsin (A1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded in ... Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices. Mutations ...
Otubains are deubiquitinating cysteine proteases (DUBs; see MIM 602519) that belong to the ovarian tumor (OTU) protein ... a new family of cysteine proteases in the ubiquitin pathway". EMBO Rep. 4 (5): 517-22. doi:10.1038/sj.embor.embor824. PMC ... 2004). "Sequence organization and matrix attachment regions of the human serine protease inhibitor gene cluster at 14q32.1". ...
Cysteine protease involved in xylem tracheary element (TE) autolysis during xylogenesis in roots. Participates in micro ... Belongs to the peptidase C1 family.PROSITE-ProRule annotation. ,p>Manual validated information which has been generated by the ... Cysteine protease XCP1Curated (EC:3.4.22.-). Alternative name(s):. Xylem cysteine peptidase 11 Publication. ,p>Manually curated ... Cysteine protease XCP1Add BLAST. 219. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view. ...
Picornain 3C are cysteine proteases related by amino acid sequence to trypsin-like serine proteases. Picornain 3C is encoded by ... Picornavirus belongs to the family Picornaviridae. Picornavirus virions are nonenveloped and the +ssRNA nonsegmented genome is ... Caspase stands for cysteine-aspartic acid protease and play an essential role in the apoptotic pathway of the cell. Protease 2A ... Hepatitis A 3C proteinase is a member of the cysteine proteases that are responsible for the infectivity and maturation of HAV ...
... cysteine proteases, serine proteases, aspartic proteases and metallo-proteases. This review will cover only cysteine proteases ... cysteine proteases, serine proteases, aspartic proteases and metallo-proteases. This review will cover only cysteine proteases ... Cysteine protease inhibitors are available that can block the active site but no such inhibitor available yet that can be ... Cysteine protease inhibitors are available that can block the active site but no such inhibitor available yet that can be ...
Caspases belong to a particular class of proteases, known as cysteine proteases. Proteases are classified either by the ... Cysteine proteases are defined by the latter grouping and all have the amino acid cysteine in their active site. ... The enzymes involved in this activity are a subtype of a class of proteases-enzymes that degrade other proteins. There are ... They are based around measuring the protease activity as the zymogen is processed to an active enzyme. Caspase activity ...
CCHFV encodes a cysteine protease belonging to the ovarian tumor (OTU) family which is involved in host immune suppression. ... Certain RNA viruses, such as CCHFV, encode cysteine proteases of the ovarian tumor (OTU) family that antagonize interferon (IFN ... pestis strains belonging to Antiqua biovar in the Tien Shan Mountains. ... of the OTU to cellular ubiquitin are required for the generation of recombinant CCHFV containing a mutated catalytic cysteine. ...
Caspases, a family of cysteine proteases, are critical mediators of neuronal apoptosis and neurodegeneration [33]. Cleavage of ... Nrf2, a regulator of endogenous antioxidant defense which belonging to CNC-bZIP transcription factors, plays as a chief ... To clarify the mechanisms, proteases inhibitors or siRNA were used. Protein levels were investigated by western blotting. ... Bax and Bcl-2 belong to the Bcl-2 family, Bcl-2 is an anti-apoptotic protein, and Bax is a pro-apoptotic protein. ...
Two residues that belong to another monomer but form hydrogen bonds (red) with either N24 or Y25 are shown in orange (D281) and ... Here, we now report that 2 lysosomal cysteine proteases present in lymphoblasts are able to degrade l-asparaginase. Cathepsin B ... A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug l. -asparaginase ... A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug l. -asparaginase ...
... cysteine-dependent aspartate-specific protease). Caspases are among the most specific of proteases, recognizing at least four ... These homologous endopeptidases belong to the large family of proteins called caspases ( ... M. Drag and G. S. Salvesen, "Emerging principles in protease-based drug discovery," Nature Reviews Drug Discovery, vol. 9, no. ... Most of the morphological changes associated with apoptosis are caused by a set of proteases that are specifically activated in ...
This small protein belongs to a recently defined family of cysteine protease inhibitors. Although resembling well-known ... This small protein belongs to a recently defined family of cysteine protease inhibitors. Although resembling well-known ... This small protein belongs to a recently defined family of cysteine protease inhibitors. Although resembling well-known ... Crystal Structure of the Parasite Protease Inhibitor Chagasin in Complex with a Host Target Cysteine Protease.. Ljunggren, Anna ...
Calpains belong to a family of calcium-dependent cysteine proteases [4]. Among 15 family members, only calpain 1 and calpain 2 ... Stalker TJ, Gong Y, Scalia R (2005) The calcium-dependent protease calpain causes endothelial dysfunction in type 2 diabetes. ...
1984, 1985) reported the presence of two types of cysteine protease inhibitors in colostrum, belonging to the kininogen and ... 1995) purified a third type of cysteine protease inhibitor from colostrum, but information relating to its taxonomy is not ... Plasmin, a serine protease derived from plasminogen, is the principal indigenous proteinase in milk (Fox and Kelly 2006a, b). ... 2006) reported that the activity of the acid milk protease, cathepsin D, is significantly lower in colostrum than in milk. ...
Neither hydrocortisone nor cysteine protease inhibitors weakened the cytokine production.. Our findings suggest that proteases ... Trypsin belongs to the group of serine proteases and serves a positive control stimulus. ... Inhibition of cytokine synthesis was performed using a glucocorticoid, a serine protease inhibitor, and a cysteine protease ... Units of total protease, serine protease, metalloprotease, and thiol protease activity in four different S. aureus strains and ...
... is an important proteolytic mixture that contains enzymes belonging to the cysteine proteases of the papain family. Numerous ... AnanasBromelainsChemical FractionationCysteine EndopeptidasesCysteine ProteasesPlant ExtractsPlant ProteinsPlant Stems ... The cysteine proteinases of the pineapple plant.. *Bromelain, a cysteine protease from pineapple (Ananas comosus) stem, is an ... All forms are completely inhibited by specific cysteine and cysteine/serine protease inhibitors, but not by specific serine and ...
Cathepsin B belongs to a family of lysosomal cysteine proteases and plays an important role in intracellular proteolysis. ...
The second group of genes belonged to the family of cysteine-proteases (cruzipain) expressed in all of the different forms of ... after the release of pro-inflammatory bradykinin peptide by the parasite proteases during infection [54]. Thirdly, a recent ...
A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family ... Adenovirus protease had been indicated to resemble the cysteine protease, ubiquitin-like protein protease 1 (Ulp1) in yeast (Li ... The two-domain architecture of IpaH and the presence of a cysteine residue in the CTD (IpaH-CTD) suggested IpaH may belong to ... and designates them as such to the C55 family of cysteine proteases (Orth et al., 2000; Barrett and Rawlings, 2001). Each ...
Peptidase_C1; Papain family cysteine protease. RefSeqs of Annotated Genomes: Homo sapiens Updated Annotation Release ... The following sections contain reference sequences that belong to a specific genome build. Explain ... cysteine-type endopeptidase activity IBA Inferred from Biological aspect of Ancestor. more info ... Title: Cysteine cathepsins B, X and K expression in peri-arteriolar glioblastoma stem cell niches. ...
Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. A ... The following sections contain reference sequences that belong to a specific genome build. Explain ... CysPc; Calpain-like thiol protease family. cd04046. Location:555 → 678. C2_Calpain; C2 domain present in Calpain proteins. ... calcium-dependent cysteine-type endopeptidase activity IBA Inferred from Biological aspect of Ancestor. more info ...
All mammalian transglutaminases (TGases) belong to a superfamily of cysteine proteases, have structural homology and possess ... All mammalian transglutaminases (TGases) belong to a superfamily of cysteine proteases, have structural homology and possess ... The catalytic mechanism is evolutionarily related to that of cysteine proteases. The active site thiol reacts with a glutamine ... between endo-glutamyl residues belonging to two different proteins or to the same proteins [7,15]. This catalytic activity, ...
Mammalian asparaginyl endopeptidase (AEP) or legumain is a recently identified lysosomal cysteine protease belonging to clan CD ... The plasmid-encoded toxin (Pet) from enteroaggregative Escherichia coli is a serine protease autotransporter that acts as an ...
Here, we describe new, highly specific Ub iso-peptidases, that have no sequence homology to known DUBs, but which belong to the ... Otubains: a new family of cysteine proteases in the ubiquitin pathway EMBO Rep. 2003 May;4(5):517-22. doi: 10.1038/sj.embor. ... Functional analysis of otubains shows that the OTU domain contains an active cysteine protease site. ... a heterogeneous group of cysteine proteases that cleave proteins precisely at the Ub-protein bond. Two families of DUBs have ...
Caspase-3 protein belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a ... Nicholson, D.W. and Thornberry, N.A. (1997). Caspases: killer proteases. Trends in Biochemical Sciences 22: 299-306. ... protease inhibitors, salts, reducing agents, denaturants, and chelating agents may be added to the reagent.. Features of the B- ...
This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a serine protease domain, ... a transmembrane domain, an LDL receptor-like domain, and a scavenger receptor cysteine-rich domain. Serine proteases are known ... transmembrane protease, serine 3. MGI:2155445 Go Annotations as Summary Text (Tabular View) (GO Graph). Summary from NCBI ...
... wherein Z is a cysteine protease binding moiety; X and Y are S, O or optionally substituted N; and R.sub.1 is optionally ... The present invention relates to cysteine protease inhibitors of the general formula (I): ##STR1## ... Lysosomal cysteine proteases or cathepsins (including cathepsins B, C, H, L, S, O and O2/K) belong to the papain superfamily of ... cysteine endopeptidase(Ostertagia), cysteine endopeptidase (pea), cysteine endopeptidase (Plasmodium), cysteine protease tpr ( ...
  • Picornain 3C (EC 3.4.22.28, Picornain 3C is a protease and endopeptidase enzyme found in the picornavirus, that cleaves peptide bonds of non- terminal sequences. (wikipedia.org)
  • A new bioRxiv * study by a research group from the University of California Irvine shows in vitro activity and non-toxicity of the first-in-class cyclic peptide that inhibits the main protease of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) - laying the groundwork for its use in the treatment of coronavirus disease (COVID-19). (news-medical.net)
  • It is therefore expected that the peptide hydrolase activity of NsPCS, i.e., the deglycination of GSH, resembles the general and well known mechanism of papain-like cysteine proteases. (biology-online.org)
  • A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. (ebi.ac.uk)
  • a) First, interaction of a positively charged WLM domain with DNA may induce conformational changes facilitating displacement of the negatively charged C-terminal peptide with an inhibitory cysteine from the active site. (nih.gov)
  • It is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. (biomol.com)
  • Generally, serine proteases such as trypsin and tryptase are considered to play a role in inflammation and immunity under physiological and pathophysiological conditions by cleavage of protease-activated receptors (PARs) and subsequent activation of various signal transduction cascades such as the mobilization of calcium from endoplasmatic reticula ( 11 ). (jimmunol.org)
  • Using AEP-mediated cleavage sequences, we modeled the effects of the protease on ASNase and created a number of recombinant ASNase products. (jci.org)
  • Moreover, there are no known human proteases that exhibit similar cleavage specificity as M pro , suggesting that the development of inhibitors that specifically target this protease and are not coupled with off-target toxicity is a viable option. (news-medical.net)
  • Unique Cleavage Specificity of `Prohormone thiol Protease` Related to Proenkephalin Processing," FEBS Lett. (patentgenius.com)
  • A conformational change within the serpin interrupts the cleavage reaction, deforming the protease active site and preventing dissociation. (portlandpress.com)
  • a) Modification of the regulatory cysteine by thiram (Th) or APMA displaces the cysteine from the active site Zn, activates the metalloprotease and induces in-cis Wss1 cleavage. (nih.gov)
  • The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain and releases the transcription factor from the Golgi membrane. (abcam.com)
  • Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7. (abcam.com)
  • The results suggest that VP4 cleaves the (Ser/Thr)-X-Ala↓(Ser/Ala)-Gly motif, a target sequence with similarities to bacterial leader peptidases and herpesvirus protease cleavage sites. (asm.org)
  • Ensuing studies demonstrated that PPAF‐II forms a homo‐oligomer upon cleavage by the upstream protease and that the clip domain of PPAF‐II functions as a module for binding phenoloxidase through the central cleft, while the clip domain of a catalytically active easter‐type SP plays an essential role in the rapid activation of its protease domain. (embopress.org)
  • Poliovirus 3C protease replication occurs in the cytoplasm, yet is able to inhibit transcription in the nucleus without any nuclear localization. (wikipedia.org)
  • Previous biochemical studies showed that both recombinant EPI1 and EPI10 inhibit and interact with the pathogenesis-related (PR) P69B subtilisin-like serine protease of tomato. (osu.edu)
  • We now report the mechanism and kinetics of this unusual inhibition of a cysteine proteinase by a member of the serpin superfamily previously thought to inhibit serine proteinase only. (embl.de)
  • Proteases are classified either by the substrates they use or by the nature of their active site. (wisegeek.com)
  • Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells (PubMed:15537383, PubMed:26018085, PubMed:25122198). (genecards.org)
  • Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. (ebi.ac.uk)
  • Most of the virus-encoded proteases are related to the chymotrypsin-like cellular proteases with a distinctive double β-barrel fold, but only a few, like the Alphavirus capsid protease and the Flaviviridae NS3 proteases, contain the His-Asp-Ser catalytic triad found in the cellular world ( 14 , 31 ). (asm.org)
  • 1998). Similar to other potyviruses, TW-TN3 RNA was presumed coding a single large polyprotein that undergoes proteolytic processing by virus-encoded proteases to yield several mature gene products (Shukla et al. (sinica.edu.tw)