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.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.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.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.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.Neprilysin: Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Thiorphan: A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.PHEX Phosphate Regulating Neutral Endopeptidase: A membrane-bound metalloendopeptidase that may play a role in the degradation or activation of a variety of PEPTIDE HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Genetic mutations that result in loss of function of this protein are a cause of HYPOPHOSPHATEMIC RICKETS, X-LINKED DOMINANT.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.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.Glycopeptides: Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Neurotensin: A biologically active tridecapeptide isolated from the hypothalamus. It has been shown to induce hypotension in the rat, to stimulate contraction of guinea pig ileum and rat uterus, and to cause relaxation of rat duodenum. There is also evidence that it acts as both a peripheral and a central nervous system neurotransmitter.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Kinetics: The rate dynamics in chemical or physical systems.Dipeptides: Peptides composed of two amino acid units.Lysostaphin: A 25-kDa peptidase produced by Staphylococcus simulans which cleaves a glycine-glcyine bond unique to an inter-peptide cross-bridge of the STAPHYLOCOCCUS AUREUS cell wall. EC 3.4.24.75.Aspartic Acid Endopeptidases: A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.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.Sulfhydryl Compounds: Compounds containing the -SH radical.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Transcription Factor AP-1: A multiprotein complex composed of the products of c-jun and c-fos proto-oncogenes. These proteins must dimerize in order to bind to the AP-1 recognition site, also known as the TPA-responsive element (TRE). AP-1 controls both basal and inducible transcription of several genes.Proto-Oncogene Proteins c-jun: Cellular DNA-binding proteins encoded by the c-jun genes (GENES, JUN). They are involved in growth-related transcriptional control. There appear to be three distinct functions: dimerization (with c-fos), DNA-binding, and transcriptional activation. Oncogenic transformation can take place by constitutive expression of c-jun.Dronabinol: A psychoactive compound extracted from the resin of Cannabis sativa (marihuana, hashish). The isomer delta-9-tetrahydrocannabinol (THC) is considered the most active form, producing characteristic mood and perceptual changes associated with this compound.Cannabis: The plant genus in the Cannabaceae plant family, Urticales order, Hamamelidae subclass. The flowering tops are called many slang terms including pot, marijuana, hashish, bhang, and ganja. The stem is an important source of hemp fiber.Receptor, Cannabinoid, CB1: A subclass of cannabinoid receptor found primarily on central and peripheral NEURONS where it may play a role modulating NEUROTRANSMITTER release.Cannabinoids: Compounds having the cannabinoid structure. They were originally extracted from Cannabis sativa L. The most pharmacologically active constituents are TETRAHYDROCANNABINOL; CANNABINOL; and CANNABIDIOL.Marijuana Smoking: Inhaling and exhaling the smoke from CANNABIS.Receptors, Cannabinoid: A class of G-protein-coupled receptors that are specific for CANNABINOIDS such as those derived from CANNABIS. They also bind a structurally distinct class of endogenous factors referred to as ENDOCANNABINOIDS. The receptor class may play a role in modulating the release of signaling molecules such as NEUROTRANSMITTERS and CYTOKINES.Cannabidiol: Compound isolated from Cannabis sativa extract.ElastinPancreatic 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.Leukocyte Elastase: 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.Histocompatibility Antigens Class II: Large, transmembrane, non-covalently linked glycoproteins (alpha and beta). Both chains can be polymorphic although there is more structural variation in the beta chains. The class II antigens in humans are called HLA-D ANTIGENS and are coded by a gene on chromosome 6. In mice, two genes named IA and IE on chromosome 17 code for the H-2 antigens. The antigens are found on B-lymphocytes, macrophages, epidermal cells, and sperm and are thought to mediate the competence of and cellular cooperation in the immune response. The term IA antigens used to refer only to the proteins encoded by the IA genes in the mouse, but is now used as a generic term for any class II histocompatibility antigen.Antigen Presentation: The process by which antigen is presented to lymphocytes in a form they can recognize. This is performed by antigen presenting cells (APCs). Some antigens require processing before they can be recognized. Antigen processing consists of ingestion and partial digestion of the antigen by the APC, followed by presentation of fragments on the cell surface. (From Rosen et al., Dictionary of Immunology, 1989)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.Antigens, Differentiation, B-Lymphocyte: Membrane antigens associated with maturation stages of B-lymphocytes, often expressed in tumors of B-cell origin.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.Proteome: The protein complement of an organism coded for by its genome.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.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.

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. (1/6256)

The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The first subdomain is an alpha-helix-beta-strand arrangement, whereas the second subdomain has a predominantly beta-strand arrangement. The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. This enables inhibitors based on the thyroglobulin type-1 domain fold, in contrast to the rather non-selective cystatins, to exhibit specificity for their target enzymes.  (+info)

C/EBPalpha regulates generation of C/EBPbeta isoforms through activation of specific proteolytic cleavage. (2/6256)

C/EBPalpha and C/EBPbeta are intronless genes that can produce several N-terminally truncated isoforms through the process of alternative translation initiation at downstream AUG codons. C/EBPbeta has been reported to produce four isoforms: full-length 38-kDa C/EBPbeta, 35-kDa LAP (liver-enriched transcriptional activator protein), 21-kDa LIP (liver-enriched transcriptional inhibitory protein), and a 14-kDa isoform. In this report, we investigated the mechanisms by which C/EBPbeta isoforms are generated in the liver and in cultured cells. Using an in vitro translation system, we found that LIP can be generated by two mechanisms: alternative translation and a novel mechanism-specific proteolytic cleavage of full-length C/EBPbeta. Studies of mice in which the C/EBPalpha gene had been deleted (C/EBPalpha-/-) showed that the regulation of C/EBPbeta proteolysis is dependent on C/EBPalpha. The induction of C/EBPalpha in cultured cells leads to induced cleavage of C/EBPbeta to generate the LIP isoform. We characterized the cleavage activity in mouse liver extracts and found that the proteolytic cleavage activity is specific to prenatal and newborn livers, is sensitive to chymostatin, and is completely abolished in C/EBPalpha-/- animals. The lack of cleavage activity in the livers of C/EBPalpha-/- mice correlates with the decreased levels of LIP in the livers of these animals. Analysis of LIP production during liver regeneration showed that, in this system, the transient induction of LIP is dependent on the third AUG codon and most likely involves translational control. We propose that there are two mechanisms by which C/EBPbeta isoforms might be generated in the liver and in cultured cells: one that is determined by translation and a second that involves C/EBPalpha-dependent, specific proteolytic cleavage of full-length C/EBPbeta. The latter mechanism implicates C/EBPalpha in the regulation of posttranslational generation of the dominant negative C/EBPbeta isoform, LIP.  (+info)

An antiviral mechanism of nitric oxide: inhibition of a viral protease. (3/6256)

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

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (4/6256)

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport.  (+info)

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. (5/6256)

The role of conformation-based quality control in the early secretory pathway is to eliminate misfolded polypeptides and unassembled multimeric protein complexes from the endoplasmic reticulum, ensuring the deployment of only functional molecules to distal sites. The intracellular fate of terminally misfolded human alpha1-antitrypsin was examined in hepatoma cells to identify the functional role of asparagine-linked oligosaccharide modification in the selection of glycoproteins for degradation by the cytosolic proteasome. Proteasomal degradation required physical interaction with the molecular chaperone calnexin. Altered sedimentation of intracellular complexes following treatment with the specific proteasome inhibitor lactacystin, and in combination with mannosidase inhibition, revealed that the removal of mannose from attached oligosaccharides abrogates the release of misfolded alpha1-antitrypsin from calnexin prior to proteasomal degradation. Intracellular turnover was arrested with kifunensine, implicating the participation of endoplasmic reticulum mannosidase I in the disposal process. Accelerated degradation occurred in a mannosidase-independent manner and was arrested by lactacystin, in response to the posttranslational inhibition of glucosidase II, demonstrating that the attenuated removal of glucose from attached oligosaccharides functions as the underlying rate-limiting step in the proteasome-mediated pathway. A model is proposed in which the removal of mannose from multiple attached oligosaccharides directs calnexin in the selection of misfolded alpha1-antitrypsin for degradation by the proteasome.  (+info)

Possible involvement of proteasomes (prosomes) in AUUUA-mediated mRNA decay. (6/6256)

We have identified a cellular target for proteasomal endonuclease activity. Thus, 20 S proteasomes interact with the 3'-untranslated region of certain cytoplasmic mRNAs in vivo, and 20 S proteasomes isolated from Friend leukemia virus-infected mouse spleen cells were found to be associated with a mRNA fragment showing great homology to the 3'-untranslated region of tumor necrosis factor-beta mRNA that contains AUUUA sequences. We furthermore demonstrate that 20 S proteasomes destabilize oligoribonucleotides corresponding to the 3'-untranslated region of tumor necrosis factor-alpha, creating a specific cleavage pattern. The cleavage reaction is accelerated with increasing number of AUUUA motifs, and major cleavage sites are localized at the 5' side of the A residues. These results strongly suggest that 20 S proteasomes could be involved in the destabilization of cytokine mRNAs such as tumor necrosis factor mRNAs and other short-lived mRNAs containing AUUUA sequences.  (+info)

Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia. (7/6256)

The formation of a persistently active cAMP-dependent protein kinase (PKA) is critical for establishing long-term synaptic facilitation (LTF) in Aplysia. The injection of bovine catalytic (C) subunits into sensory neurons is sufficient to produce protein synthesis-dependent LTF. Early in the LTF induced by serotonin (5-HT), an autonomous PKA is generated through the ubiquitin-proteasome-mediated proteolysis of regulatory (R) subunits. The degradation of R occurs during an early time window and appears to be a key function of proteasomes in LTF. Lactacystin, a specific proteasome inhibitor, blocks the facilitation induced by 5-HT, and this block is rescued by injecting C subunits. R is degraded through an allosteric mechanism requiring an elevation of cAMP coincident with the induction of a ubiquitin carboxy-terminal hydrolase.  (+info)

Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance. (8/6256)

PML/RARalpha is the leukemogenetic protein of acute promyelocytic leukemia (APL). Treatment with retinoic acid (RA) induces degradation of PML/RARalpha, differentiation of leukaemic blasts, and disease remission. However, RA resistance arises during RA treatment of APL patients. To investigate the phenomenon of RA resistance in APL, we generated RA-resistant sublines from APL-derived NB4 cells. The NB4.007/6 RA-resistant subline does not express the PML/RARalpha protein, although its mRNA is detectable at levels comparable to those of the parental cell line. In vitro degradation assays showed that the half-life of PML/RARalpha is less than 30 minutes in NB4.007/6 and longer than 3 hours in NB4. Treatment of NB4.007/6 cells with the proteasome inhibitors LLnL and lactacystin partially restored PML/RARalpha protein expression and resulted in a partial release of the RA-resistant phenotype. Similarly, forced expression of PML/RARalpha, but not RARalpha, into the NB4/007.6 cells restored sensitivity to RA treatment to levels comparable to those of the NB4 cells. These results indicate that constitutive degradation of PML/RARalpha protein may lead to RA resistance and that PML/RARalpha expression is crucial to convey RA sensitivity to APL cells.  (+info)

*Peptidase 1 (mite)

This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. The various forms of peptidase 1 ... which bind to the cysteine active site and block substrate access. The major kiwifruit cysteine proteinase inhibitor KCPI1 has ... As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the ... By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that ...

*Cathepsin V

... is a human lysosomal cysteine endopeptidase. Cathepsin L2 Brömme, D.; Li, Z.; Barnes, M.; Mehler, E. (1999). "Human ... Santamaría, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; López-Otín, C. (1998). "Cathepsin L2, a novel human cysteine ...

*Cathepsin X

Shows weak endopeptidase activity Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). Nägler, D.K.; ... Nägler, D.K.; Ménard, R. (1998). "Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion ... Santamaría, I.; Velasco, G.; Pendás, A.M.; Fueyo, A.; López-Otín, C. (1998). "Cathepsin Z, a novel human cysteine proteinase ... Cathepsin X (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ...

*Nepenthesin

Takahashi K, Nishii W, Shibata C (2012). "The digestive fluid of Drosera indica contains a cysteine endopeptidase ("droserain ... The names cephalotusin, dionaeasin and droserasin have been proposed for similar aspartic endopeptidases originating from the ...

*Legumain

... clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Lett. 441: 361-365. doi:10.1016/S0014-5793(98)01574- ... Legumain is a cysteine protease from the C13 family of the CD clan of proteases (MEROPS). It uses a catalytic triad of Cysteine ... Hara-Nishimura, I. (1998). "Asparaginyl endopeptidase". In Barrett, A.J.; Rawlings, N.D.; Woessner, J.F. Handbook of ... Legumain (EC 3.4.22.34, asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 gene product or LGMN (Homo ...

*LGMN

... clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Lett. 441 (3): 361-5. doi:10.1016/S0014-5793(98) ... 1999). "An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation". Nature. 396 (6712): 695-9. ... This gene encodes a cysteine protease, legumain, that has a strict specificity for hydrolysis of asparaginyl bonds. This enzyme ... 1998). "Cloning and expression of mouse legumain, a lysosomal endopeptidase". Biochem. J. 335 (Pt 1): 111-7. PMC 1219758 . PMID ...

*DISC1

... is also known to play a role in axon regeneration and has an additional DISC1-modulated function as a cysteine endopeptidase. ...

*Cathepsin L

... (EC 3.4.22.15, Aldrichina grahami cysteine proteinase) is an important lysosomal endopeptidase enzyme which is ... Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and ... Venkatesh K, Prasanth B, Rajesh P, Annie JG, Mukesh P, Jesu A (2014). "A murrel cysteine protease, cathepsin L: bioinformatics ... Barrett, A.J.; Buttle, D.J.; Mason, R.W. (1988). "Lysosomal cysteine proteinases". ISI Atlas of Science. Biochemistry. 1: 256- ...

*TEV protease

... (EC 3.4.22.44, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine ... Bazan JF, Fletterick RJ (November 1988). "Viral cysteine proteases are homologous to the trypsin-like family of serine ... TEV protease uses a cysteine as its catalytic nucleophile (as do many other viral proteases). Covalent catalysis is performed ...

*Ficain

It is of a family of proteases known as the cysteine endopeptidases, a group that also includes papain derived from papaya ... doi:10.1016/0076-6879(70)19020-3. Brocklehurst, K.; Willenbrock, F.; Salih, E. (1987). "Cysteine proteinases". In Neuberger, A ...

*List of MeSH codes (D08)

... cysteine endopeptidases MeSH D08.811.277.656.300.215.096 --- bromelains MeSH D08.811.277.656.300.215.120 --- calpain MeSH ... endopeptidase clp MeSH D08.811.277.656.149.500 --- protease la MeSH D08.811.277.656.300 --- endopeptidases MeSH D08.811.277.656 ... endopeptidase clp MeSH D08.811.277.656.300.760.247 --- endopeptidase k MeSH D08.811.277.656.300.760.284 --- enteropeptidase ... aspartic endopeptidases MeSH D08.811.277.656.300.066.180 --- cathepsin d MeSH D08.811.277.656.300.066.185 --- cathepsin e MeSH ...

*Coeliac disease

... prolyl endopeptidase and a barley glutamine-specific cysteine endopeptidase (EP-B2)) that degrade the putative 33-mer peptide ...

*Kexin

... paired-basic endopeptidase, yeast cysteine proteinase F, paired-basic endopeptidase, andrenorphin-Gly-generating enzyme, ... Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (1988). "Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin- ... Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (1989). "Characterization of KEX2-encoded endopeptidase from yeast ... "Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast ...

*Adenain

This cysteine endopeptidase is coded by adenoviruses. Webster, A.; Hay, R.T.; Kemp, G. (1993). "The adenovirus protease is ...

*Cysteine protease

The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases Cysteine endopeptidases at the US National ... In fact, dozens of latices of different plant families are known to contain cysteine proteases. Cysteine proteases are used as ... Within each superfamily, families are designated by their catalytic nucleophile (C = cysteine proteases). Families of Cysteine ... Plant cysteine proteases isolated from these plants have been found to have high proteolytic activities that are known to ...

*Glutamyl endopeptidase GluV8

Glutamyl endopeptidase proteolytically activates the zymogen of the cysteine protease staphopain B (staphopain A is activated ... Glutamyl endopeptidase is in S. aureus expressed from the gene sspA within the operon ssp. Downstream of sspA, the operon also ... Glutamyl endopeptidase is expressed as a zymogen that, in order to become fully active, has been modified both through ... Glutamyl endopeptidase can inhibit the activation of targets within the complement system. It is indicated to cause inhibition ...

*Glycyl endopeptidase

"Affinity purification of the novel cysteine proteinase papaya proteinase IV and papain from papaya latex". Biochem. J. 261: 469 ... Glycyl endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Glycyl endopeptidase (EC 3.4.22.25, papaya peptidase B, papaya proteinase IV, glycine-specific proteinase, chymopapain, Papaya ...

*CHAP domain

Cysteine peptidases belonging to MEROPS peptidase family C51 (D-alanyl-glycyl endopeptidase, clan CA). Rigden DJ, Jedrzejas MJ ... The CHAP domain contains two invariant residues, a cysteine and a histidine. These residues form part of the putative active ... It has been suggested that CHAP domain containing proteins utilise a catalytic cysteine residue in a nucleophilic-attack ... The domain is named after the acronym cysteine, histidine-dependent amidohydrolases/peptidases. Many of these proteins are ...

*Cysteine protease

Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases. *Cysteine+endopeptidases at the US ... Cysteine Peptidase. Crystal structure of the cysteine peptidase papain in complex with its covalent inhibitor E-64. Rendered ... In fact, dozens of latices of different plant families are known to contain cysteine proteases.[1] Cysteine proteases are used ...

*Aureolysin

An immunization survey of human serum samples suggests that exposure to S. aureus glutamyl endopeptidase is common, although a ... a cysteine protease. Aureolysin cleaves different proteins among inflammatory regulators and immune components. Aureolysin can ... it proteolytically activates the zymogen of the serine protease glutamyl endopeptidase, which in turn is the activator of ...

*Cathepsin W

cysteine-type endopeptidase activity. • cysteine-type peptidase activity. • hydrolase activity. Cellular component. • lysosome ... The protein encoded by this gene, a member of the peptidase C1 family, is a cysteine proteinase that may have a specific ... 1998). "Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase". Leukemia. 12 (11): 1771-81. doi: ... Linnevers C, Smeekens SP, Bromme D (May 1997). "Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ ...

*Cathepsin D

serine-type endopeptidase activity. • cysteine-type endopeptidase activity. • aspartic-type endopeptidase activity. ... Lenarcic B, Kos J, Dolenc I, Lucovnik P, Krizaj I, Turk V (July 1988). "Cathepsin D inactivates cysteine proteinase inhibitors ...

*Caspase 8

cysteine-type endopeptidase activity involved in apoptotic process. • tumor necrosis factor receptor binding. • cysteine-type ... cysteine-type peptidase activity. • cysteine-type endopeptidase activity involved in apoptotic signaling pathway. • protein ... cysteine-type endopeptidase activity involved in execution phase of apoptosis. Cellular component. • cell body. • cytosol. • ... activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway. • response to antibiotic. • ...

*MALT1

cysteine-type endopeptidase activity. • hydrolase activity. • identical protein binding. Cellular component. • cytoplasm. • ... Cysteine 464 and histidine 414 are crucial for this activity. Like metacaspases, the paracaspase cleaves substrates after an ...

*NAIP - Википедия

cysteine-type endopeptidase inhibitor activity. • связывание с ионом металла. • ubiquitin-protein transferase activity. • ... negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • response to amino acid. • negative ... inhibition of cysteine-type endopeptidase activity involved in apoptotic process. • негативная регуляция апоптоза. ...

*Cathepsin Z

... a cysteine protease with the proregion covalently linked to the active site cysteine". Journal of Molecular Biology. 295 (4): ... It is an exopeptidase with strict carboxypeptidase activity, while most other cathepsins are endopeptidases. Cathepsin Z has an ... "Entrez Gene: CTSZ cathepsin Z". Turk V, Stoka V, Vasiljeva O, Renko M, Sun T, Turk B, Turk D (January 2012). "Cysteine ... It is a member of the cysteine cathepsin protease family, which has 11 members. As one of the 11 cathepsins, cathepsin Z ...

*Proteasome

This is then transferred to E1's active-site cysteine residue in concert with the adenylylation of a second ubiquitin.[48] This ... Wilk S, Orlowski M (November 1980). "Cation-sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary ... Wilk S, Orlowski M (March 1983). "Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease ... adenylylated ubiquitin is then transferred to a cysteine of a second enzyme, ubiquitin-conjugating enzyme (E2). In the last ...

*Vasopressin

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • regulation of blood vessel size. • ... cysteine-type endopeptidase inhibitor activity involved in apoptotic process. • neurohypophyseal hormone activity. • receptor ... with the cysteine residues forming a disulfide bond and the C-terminus of the sequence converted to a primary amide.[27] Lysine ...
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2. Leu and Gln were most favoured at P2 and P1 positions, respectively. Substrate preferences at P5 to P3 positions were important in enhancing the main protease activity. Super-reactive substrate sequences were engineered, with more than a 2-fold increase in activity, by combining the best residue choices at P5 to P3 positions ...
Cell growth and viability are dependent on the function of the multicatalytic proteinase complex (proteasome), a multisubunit particle that affects progression through the mitotic cycle by degradation of cyclins. Exposure of rodent fibroblasts and human lymphoblasts in culture to benzyloxycarbonyl-leucyl-leucyl-phenylalaninal (Z-LLF-CHO), a cell-permeable peptidyl aldehyde inhibitor of the chymotrypsin-like activity of the proteasome, resulted in the induction of apoptosis in a rapid, dose-dependent fashion. Fibroblasts transformed with ras and myc, lymphoblasts transformed by c-myc alone, and a Burkitts lymphoma (BL) cell line that overexpresses c-Myc were up to 40-fold more susceptible to apoptosis than were either primary rodent fibroblasts or immortalized nontransformed human lymphoblasts, respectively. To determine whether such preferential apoptosis could impact upon tumor growth in vivo, toxicological studies were performed in mice with severe combined immunodeficiency and showed that ...
The SCOP classification for the CNF1/YfiH-like putative cysteine hydrolases superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
The SCOP classification for the CNF1/YfiH-like putative cysteine hydrolases superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
The beta coronavirus genome encodes several structural proteins, including the glycosylated spike(S) protein that functions as a major inducer of host immune responses. This S protein mediate shost cell invasion by SARS-CoV-2 via binding to a receptor protein called angiotensin-convertingenzyme 2 (ACE2) located on the surface membrane of host cells. A recent study also revealed that this invasion process requires S protein priming which is facilitated by the host cell-produced serine protease TMPRSS211. In addition, the viral genome also encodes several nonstructural proteins including RNA-dependent RNA polymerase (RdRp), coronavirus main protease (3CLpro), and papain-like protease (PLpro). Upon entrance to the host cells, the viral genome is released as a single-stranded positive RNA. Subsequently, it is translated into viral polyproteins using host cell proteintranslation machinery, which are then cleaved into effector proteins by viral proteinases 3CLpro and PLpro. PLpro also behaves as a ...
The AP-1 (activator protein-1) complex, which consists of proteins of the Fos and Jun families, is thought to play an important role in the balance between cell proliferation and apoptosis, the response to genotoxic stress ...
Proteases are one of the largest and best-characterized families of enzymes in the human proteome. Unfortunately, the understanding of protease function in the context of complex proteolytic cascades remains in its infancy. One major reason for this gap in understanding is the lack of technologies t …
The picornaviral 3C protease mediates viral polyprotein maturation and multiple cleavages of host proteins to modulate viral translation and transcription. The 3C protease has been regarded as a valid target due to its structural similarity among different picornaviruses and minimal sequence similarity with host proteins; therefore, the development of potent inhibitors against the 3C protease as an antiviral drug is ongoing. Duck hepatitis A virus (DHAV) belongs to the Picornavidea family and is a major threat to the poultry industry. To date, little is known about the roles of the DHAV 3C protease plays during infection. In this study, we compared the full-length DHAV 3C protein sequence with other 3C sequences to obtain an alignment for the construction of a phylogenetic tree. Then, we expressed and purified recombinant DHAV 3C protease in the BL21 expression system using nickel-NTA affinity chromatography. The optimization of the cleavage assay conditions and the kinetic analysis for DHAV 3C protease
TY - JOUR. T1 - Characterization of legumain. AU - Schwarz, Gerold. AU - Brandenburg, Jens. AU - Reich, Michael. AU - Burster, Timo. AU - Driessen, Christoph. AU - Kalbacher, Hubert. PY - 2002/11. Y1 - 2002/11. N2 - The mammalian legumain, also called asparaginyl endopeptidase (AEP), is critically involved in the processing of bacterial antigens for MHC class II presentation. In order to investigate the substrate specificity of AEP in the P1 position, we created a peptide library and digested it with purified pig kidney AEP. Digestion was less efficient only when proline was in the P1 position. Maximum AEP activity was found in lysosomal fractions of different types of antigen presenting cells (APC). When the multiple sclerosis-associated autoantigen myelin basic protein (MBP) was digested with AEP, the immunodominant epitope 83-99 was destroyed. Myoglobin as an alternative substrate was AEP resistant. These results suggest an important, but not necessarily critical role for AEP in lysosomal ...
Streptococcal pyrogenic exotoxin B (SPE B), a conserved extracellular cysteine protease expressed by the human pathogenic bacterium Streptococcus pyogenes, was purified and shown to cleave inactive human interleukin 1 beta precursor (pIL-1 beta) to produce biologically active IL-1 beta. SPE B cleaves pIL-1 beta one residue amino-terminal to the site where a recently characterized endogenous human cysteine protease acts. IL-1 beta resulting from cleavage of pIL-1 beta by SPE B induced nitric oxide synthase activity in vascular smooth muscle cells and killed of the human melanoma A375 line. Two additional naturally occurring SPE B variants cleaved pIL-1 beta in a similar fashion. By demonstrating that SPE B catalyzes the formation of biologically active IL-1 beta from inactive pIL-1 beta, our data add a further dimension to an emerging theme in microbial pathogenesis that bacterial and viral virulence factors act directly on host cytokine pathways. The data also contribute to an enlarging ...
The parasitic protozoon Leishmania mexicana possesses an abundance of developmentally regulated cathepsin L-like cysteine proteinases expressed at highest levels in amastigotes. We recently characterised lmcpa, a single-copy gene encoding one such proteinase, LmCPa, which differs from other homologues by possessing a 3-amino-acid insertion at the amino terminal of the predicted mature proteinase. To investigate the role of LmCPa in L. mexicana, we used gene-targeting of promastigotes with hygromycin- and phleomycin-resistance markers to generate null mutants by disrupting sequentially both alleles of lmcpa. The promastigote null mutants did not differ significantly from wild-type L. mexicana in growth rate or morphology and could differentiate to metacyclics and the amastigote-like form, both of which could infect the J774G8 macrophage-like cell line. The null mutant amastigote-like form obtained from the J774G8 cells could also establish rump lesions in CBA mice. By these criteria, therefore, ...
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the gamma subunit of the 11S regulator. Six ...
Papain-like cysteine proteases are important for the survival of the flagellated protozoa Trypanosoma cruzi, the causative agent of Chagas Disease. the lysosomal cysteine protease designated as cruzipain or cruzain, is the archetype of a multigene family of related isoforms. We investigated the substrate specificity of the cruzipain 2 isoform using internally quenched fluorogenic substrates. We found that cruzipain 2 and cruzain differ substantially regarding the specificity in the S-2, S-1() and S-2() pockets. Our study indicates that cruzipain 2 has a more restricted specificity than cruzain, suggesting that these isoforms might act on distinct natural substrates ...
Proteasome activator complex subunit 3 is a protein that in humans is encoded by the PSME3 gene. The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S ...
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a non-ATPase subunit of the 19S regulator base that functions as a chaperone protein during 26S proteasome assembly. [provided by RefSeq, Jul 2012 ...
Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe. In fact, dozens of latices of different plant families are known to contain cysteine proteases. Cysteine proteases are used as an ingredient in meat tenderizers. The MEROPS protease classification system counts 14 superfamilies plus several currently unassigned families (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. For superfamilies, P = superfamily containing a mixture of nucleophile class families, C = purely cysteine proteases. superfamily. Within each superfamily, ...
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome. Plays a pivotal role in development of CD8-positive T-cells.
2GT8: Crystal structure of SARS coronavirus main peptidase (with an additional Ala at the N-terminus of each protomer) in the space group P43212
Caspase 3 (Apopain or Cysteine Protease CPP32 or Protein Yama or SREBP Cleavage Activity 1 or CASP3 or EC 3.4.22.56) - Pipeline Review, H1 2017 Size and Share Published in 2017-05-30 Available for US$ 3500 at Researchmoz.us
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the association of the SCF(TIR1) E3 ubiquitin ligase complex with the proteasome.
Almost all protease families have been associated with plant development, particularly senescence, which is the final developmental stage of every organ before cell death. Proteolysis remobilizes and recycles nitrogen from senescent organs that is required, for example, seed development. Senescence-associated expression of proteases has recently been characterized using large-scale gene expression analysis seeking to identify and characterize senescence-related genes. Increasing activities of proteolytic enzymes, particularly cysteine proteases, are observed during the senescence of legume nodules, in which a symbiotic relationship between the host plant and bacteria (Rhizobia) facilitate the fixation of atmospheric nitrogen. It is generally considered that cysteine proteases are compartmentalized to prevent uncontrolled proteolysis in nitrogen-fixing nodules. In addition, the activities of cysteine proteases are regulated by endogenous cysteine protease inhibitors called cystatins. These small proteins
The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. Two alternative transcripts encoding different isoforms have been identified. [provided by RefSeq, Jul 2008] ...
Proteasome subunit beta type ; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (245 aa ...
Destruction of cancer cells by cytotoxic T lymphocytes depends on immunogenic tumor peptides generated by proteasomes and presented by human leukocyte antigen (HLA) molecules. Functional differences arising from alleles of immunoproteasome subunits have not been recognized so far. We analyzed the genetic polymorphism of the immunoproteasome subunits LMP2 and LMP7 and of the transporters associated with antigen processing (TAP1 and TAP2) in two independently collected panels of colorectal carcinoma patients (N1 = 112, N2 = 62; controls, N = 165). High risk of colon cancer was associated with the LMP7-K/Q genotype (OR = 8.10, P = 1.10 × 10−11) and low risk with the LMP7-Q/Q genotype (OR = 0.10, P = 5.97 × 10−13). The basis for these distinct associations of LMP7 genotypes was functionally assessed by IFN-γ stimulation of colon carcinoma cell lines (N = 10), followed by analyses of mRNA expression of HLA class I, TAP1, TAP2, and LMP7, with real-time PCR. Whereas induction of HLA-B, TAP1, and ...
The Ubiquitin-proteasome system is responsible for the regulated protein degradation in eucaryotic cells. The 20S proteasome is as a multicatalytic protease the central complex of these system. This study has shown that it is possible to separate 20S proteasome subtypes from HeLa cells by chromatography. 20s proteasome subtypes differ in structure and proteolytic activity. The subtype-pattern and the activity are significantly changed after an induction of the cells with gamma-Interferon (gamma-IFN) under formation of immuno proteasomes. After gamma-IFN induction mainly mixed complexes have been formed with both constitutive and immuno subunits. Further it has been shown that in cell compartements cytoplasm, microsomes and nucleus of HeLaS3 cells different 20S proteasome subtypes are located. Among other things glycosylation of some subunits is responsible for that phenomenon. With regard to new strategies in diagnostic and therapy of human diseases the exactly knowledge of structure and ...
TY - JOUR. T1 - Base-CP proteasome can serve as a platform for stepwise lid formation. AU - Yu,Zanlin. AU - Livnat-Levanon,Nurit. AU - Kleifeld,Oded. AU - Mansour,Wissam. AU - Nakasone,Mark A.. AU - Castaneda,Carlos A.. AU - Dixon,Emma K.. AU - Fushman,David. AU - Reis,Noa. AU - Pick,Elah. AU - Glickman,Michael H.. PY - 2015. Y1 - 2015. N2 - 26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S RP is divisible into base and lid sub-complexes. Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rpn8, Rpn9 and Rpn11), which interacts with both CP and base sub-complexes and module 2 (Rpn3, Rpn7, Rpn12 and Rpn15) that is attached mainly to module 1. We now show that suppression of RPN11 expression halted lid assembly yet enabled the base and 20S CP to pre-assemble and form a base-CP. A key role for Regulatory particle non-ATPase 11 (Rpn11) in bridging lid ...
PA700 proteasome activator: high MW, ATP-dependent activator of 20 S proteasome; MW 700 kDa; composed of 16 peptides ranging in MW from 20-100 kDa
Relationship of the surface export of SDH and SpeB secretion. (A) Determination of the relative cysteine protease activities of SpeB present in the culture supe
4EKF: Regulation of a Viral Proteinase by a Peptide and DNA in One-dimensional Space: III. ATOMIC RESOLUTION STRUCTURE OF THE NASCENT FORM OF THE ADENOVIRUS PROTEINASE.
The 26S proteasome is a multicatalytic proteise complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator.The…
the constitute families differ by insertion into and circular permutation of the common catalytic core made of one alpha-helix and 3-strands of beta- ...
SiliaBond® Cysteine (Si-Cys) is the silica bound equivalent of the amino acid Cysteine. By attaching the molecule to the backbone via the amino group, the thiol group remains free and accessible for higher metal scavenging efficiency.
[80 Pages Report] Check for Discount on Global L- Cysteine Market Data Survey Report 2025 report by HeyReport. Summary Cysteine (abbreviated as Cys or C) is an a-...
Sera from patients with systemic lupus erythematosus contain specific autoantibodies directed against different polypeptide components of the multicatalytic proteinase (also known as proteasome or prosome). These human autoantibodies, in contrast to polyclonal antibodies obtained in rabbits against the purified enzyme, recognize highly conserved epitopes of the multicatalytic proteinase polypeptides from yeast to human. ...
l-Asparaginase is a key therapeutic agent for treatment of childhood acute lymphoblastic leukemia (ALL). There is wide individual variation in pharmacokinetics, and little is known about its metabolism. The mechanisms of therapeutic failure with l-asparaginase remain speculative. Here, we now report that 2 lysosomal cysteine proteases present in lymphoblasts are able to degrade l-asparaginase. Cathepsin B (CTSB), which is produced constitutively by normal and leukemic cells, degraded asparaginase produced by Escherichia coli (ASNase) and Erwinia chrysanthemi. Asparaginyl endopeptidase (AEP), which is overexpressed predominantly in high-risk subsets of ALL, specifically degraded ASNase. AEP thereby destroys ASNase activity and may also potentiate antigen processing, leading to allergic reactions. Using AEP-mediated cleavage sequences, we modeled the effects of the protease on ASNase and created a number of recombinant ASNase products. The N24 residue on the flexible active loop was identified as ...
26S Proteasome regulatory subunit p55, 50 µg. The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator.
THE Fas/APO-1 receptor is one of the major regulators of apoptosis(1-7). We report here that Fas/APO-1-mediated apoptosis requires the activation of a new class of cysteine proteases, including interleukin-1 beta-converting enzyme (ICE)(8-10) which are homologous to the product of the Caenorhabditis elegans cell-death gene ced-3 (refs 11, 12). Triggering of Fas/APO-1 rapidly stimulated the proteolytic activity of ICE. Overexpression of ICE, achieved by electroporation and microinjection, strongly potentiated Fas/APO-1-mediated cell death. In addition, inhibition of ICE activity by protease inhibitors, as well as by transient expression of the pox virus-derived serpin inhibitor CrmA or an antisense ICE construct, substantially suppressed Fas/APO-1-triggered cell death. We conclude that activation of ICE or an ICE-related protease is a critical event in Fas/APO-1-mediated cell death.. ...
C.1 Purification and Proteomic Mapping of Murine Liver 19S Proteasome Complexes D. Wang, M.-C. Koag, C. Zong, X. Li, A. Gomes, and P. Ping Department of Physiology and Medicine, Division of Cardiology, University of California, Los Angeles, CA Proteasome complexes play an indispensable role in maintaining cell homeostasis. 19S proteasome complexes, also known as the regulatory particles, are critical components of the 26S proteasome system by governing substrates entry and tuning the catalytic activities of the 20S proteasomes. Multiple studies on proteasome functions reported accumulatively a total of 22 mammalian 19S subunits forming two sub-complexes, the base and the lid. Unfortunately, a comprehensive proteomic blueprint of mammalian 19S complexes remains scarce; which has made it difficult to advance our understanding of the dynamics of proteasome function and substrate specificity. A key limitation is the technology challenges encountered in order to obtain purified 19S proteasome ...
Rpt6-1 is a thermosensitive yeast mutant with a deletion of a gene encoding a regulatory subunit of the 26S proteasome, RPT6, which is able to grow at 25°C but not at 37°C. In this study, peptidase activities, activation profiles, and the subunit composition of the 20S proteasome purified from the rpt6-1 mutant was characterized. The 20S proteasome purified from rpt6-1 exhibited low levels of peptidase activities in the absence of activators, but nearly same activated activities in the presence of activators, suggesting a gating defect in the proteasome channel. Detailed analyses of the composition of the 20S proteasome through separation of all subunits by two-dimensional gel electrophoresis followed by identification of each subunit using MALDI-TOF-MS revealed that two subunits, α1 and α7, differed from those of wild-type cells in both electrophoretic mobility and pI values. The changes in these two α-subunits were apparent at the permissive temperature, but disappeared during stress response at
Characterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesin-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes
There are no specific protocols for Recombinant human Cathepsin L protein (ab81780). Please download our general protocols booklet
Two plant cysteine proteases have been shown to have immunosuppressive and immunostimulant effects, respectively in mammalian systems. These molecules therefore have therapeutic potential in a variety of diseases, but their mechanism of action is presently not characterised. We will characterise the molecular mechanism by which these proteases interact with their substrate molecules and then apply the information learned to discerning their substrates on a vital component of the immune system, the T-cell. The information will therefore significantly advance the development of these molecules as therapeutic agents by uncovering their mechanism of action ...
The proteasome is a 700-kD multisubunit enzyme complex with several proteolytically active sites. The enzyme complex is involved in both ubiquitin-dependent and -independent protein degradation and may contribute to the processing of antigens presented by major histocompatibility complex (MHC) class I molecules. Here we demonstrate that treatment of mouse fibroblast cells with 20 U interferon gamma (IFN-gamma) for 3 d induces a change in the proteasome subunit composition and that the beta-type subunit LMP2, which is encoded in the MHC class II region, is incorporated into the enzyme complex. This is paralleled by reduction of the homologous delta-subunit. IFN-gamma stimulation results in a downregulation of the chymotrypsin-like Suc-LLVY-MCA peptide hydrolyzing activity of 20S proteasomes whereas the trypsin-like activity remains unaffected. When tested as a substrate a synthetic 25-mer polypeptide whose sequence covers the antigenic nonapeptide YPHFMPTNL of the MCMV pp89, 20S proteasomes of ...
TY - JOUR. T1 - An interstitial peptide is readily processed from within seed proteins. AU - Pouvreau, Benjamin. AU - Fenske, Ricarda. AU - Ivanova, Aneta. AU - Murcha, Monika W.. AU - Mylne, Joshua S.. PY - 2019/8/1. Y1 - 2019/8/1. N2 - The importance of de novo protein evolution is apparent, but most examples are de novo coding transcripts evolving from silent or non-coding DNA. The peptide macrocycle SunFlower Trypsin Inhibitor 1 (SFTI-1) evolved over 45 million years from genetic expansion within the N-terminal discarded region of an ancestral seed albumin precursor. SFTI-1 and its adjacent albumin are both processed into separate, mature forms by asparaginyl endopeptidase (AEP). Here to determine whether the evolution of SFTI-1 in a latent region of its precursor was critical, we used a transgene approach in A. thaliana analysed by peptide mass spectrometry and RT-qPCR. SFTI could emerge from alternative locations within preproalbumin as well as emerge with precision from unrelated seed ...
Members of the cathepsin family of cysteine proteases are gaining interest as potential imaging biomarkers and drug targets due to their multifunctional roles in a range of diseases such as cancer, asthma and arthritis ...
Active Caspase-1, rat recombinant protein , Interleukin-1 beta convertase, Interleukin-1 beta-converting enzyme, IL-1BC, p45. validated in (PBV11136r-25), Abgent
The proteasome is a protein-destroying apparatus involved in many essential cellular functions, such as regulation of cell cycle, cell differentiation, signal transduction pathways, antigen processing for appropriate immune responses, stress signaling, inflammatory responses, and apoptosis. It is capable of degrading a variety of cellular proteins in a rapid and timely fashion and most substrate proteins are modified by ubiquitin before their degradation by the proteasome. The proteasome is a large protein complex consisting of a proteolytic core called the 20S particle and ancillary factors that regulate its activity in various ways. The most common form is the 26S proteasome containing one 20S core particle and two 19S regulatory particles that enable the proteasome to degrade ubiquitinated proteins by an ATP-dependent mechanism. Another form is the immunoproteasome containing two 11S regulatory particles, PA28 alpha and PA28 beta, which are induced by interferon gamma under the conditions of ...
The proteasome is a protein-destroying apparatus involved in many essential cellular functions, such as regulation of cell cycle, cell differentiation, signal transduction pathways, antigen processing for appropriate immune responses, stress signaling, inflammatory responses, and apoptosis. It is capable of degrading a variety of cellular proteins in a rapid and timely fashion and most substrate proteins are modified by ubiquitin before their degradation by the proteasome. The proteasome is a large protein complex consisting of a proteolytic core called the 20S particle and ancillary factors that regulate its activity in various ways. The most common form is the 26S proteasome containing one 20S core particle and two 19S regulatory particles that enable the proteasome to degrade ubiquitinated proteins by an ATP-dependent mechanism. Another form is the immunoproteasome containing two 11S regulatory particles, PA28 alpha and PA28 beta, which are induced by interferon gamma under the conditions of ...
Summary Global Markets Directs, 20s Proteasome - Pipeline Review, H2 2016, provides in depth analysis on 20s Proteasome targeted pipeline therapeutics. The report provides comprehensive information on the 20s Proteasome , targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type. The
Cao W, Baniecki ML, McGrath WJ, Bao C, Deming CB, Rade JJ, Lowenstein CJ, Mangel WF. Nitric oxide inhibits the adenovirus proteinase in vitro and viral infectivity in vivo. FASEB J. 2003 Dec; 17(15):2345-6 ...
MG-115 is a potent, reversible proteasome inhibitor with Ki of 21 nM for 20S proteasome and 35 nM for 26S proteasome. The inhibition of proteasome was through specific inhibition of chymotrypsin-like activity of the proteasome. Also shown to induce apopto
Cysteine proteases recognized by the active site-directed probe DCG-04 in macrophage cell lysates. (A) Schematic overview of the approach designed to examine
Allen339, member , July 11th, 2019 CASP14 caspase 14, apoptosis-related cysteine peptidase BackgroundCaspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis.1 The precursor form of all.... view details ...
A peptide derived from the C-terminal part of a plant cysteine protease folds into a stack of two beta-hairpins, a scaffold present in the emerging family of granulin-like growth factors ...
Public Release: 22-Jun-2015 Purdue University Caption A kinetic model outlines the behavior of MERS 3C-like protease in the presence and absence of molecules to bind to a target site. A Purdue University-led team found that at low concentrations an inhibitor activated the protease, but at higher concentrations it successfully blocked the activity of this essential…
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The main benefits of cysteine include the prevention of cancer growths in some of the bodys tissues, the treatment of poisoning...
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Taenia solium metacestode, a larval pork tapeworm, is a causative agent of neurocysticercosis, one of the most common parasitic diseases in the human central nervous system. In this study, we identified a cDNA encoding for a cathepsin L-like cysteine protease from the T solium metacestode (TsCL-1) and characterized the biochemical properties of the recombinant enzyme. The cloned cDNA of 1216 bp encoded 339 amino acids with an approximate molecular weight of 37.6 kDa which containing a typical signal peptide sequence (17 amino acids), a pro-domain (106 amino acids), and a mature domain (216 amino acids). Sequence alignments of TsCL-1 showed low sequence similarity of 27.3-44.6 to cathepsin L-like cysteine proteases from other helminth parasites, but the similarity was increased to 35.9-55.0 when compared to mature domains. The bacterially expressed recombinant protein (rTsCL-1) did not show enzyme activity; however, the rTsCL-1 expressed in Pichia pastoris showed typical biochemical ...
TY - JOUR. T1 - Cloning and sequencing of the gene encoding a novel lysine-specific cysteine proteinase (Lys-Gingipain) in porphyromonas gingivalis. T2 - Structural relationship with the arginine-specific cysteine proteinase (Arg-Gingipain). AU - Okamoto, Kuniaki. AU - Kadowaki, Tomoko. AU - Nakayama, Koji. AU - Yamamoto, Kenji. PY - 1996. Y1 - 1996. N2 - Lys-gingipain (KGP), so termed due to its peptide cleavage specificity for lysine residues, is a cysteine proteinase produced by the Gram-negative anaerobic bacterium Porphyromonas gingivalis. Mixed oligonucleotide primers designed from the NH2-terminal sequence of the purified enzyme were used to clone the KGP-encoding gene (kgp) from the organism. The nucleotide sequence of kgp had a 5,169-bp open reading frame encoding 1,723 amino acids with a calculated molecular mass of 218 kDa. As the extracellular mature enzyme had an apparent molecular mass of 51 kDa in gels, the precursor of KGP was found to comprise at least four domains, the signal ...
The report generally describes clasto-lactacystin beta-lactone, examines its uses, production methods, patents. CLASTO-LACTACYSTIN BETA-LACTONE market
Bacteroides fragilis is a Gram-negative member of the normal human gut microbiota. The Bacteroidetes constitutes one of the major bacterial phyla in the healthy human gut [1]. However, B. fragilis is also an important opportunistic pathogen, and it is the most frequently isolated anaerobic bacterium in clinical specimens, including abdominal abscesses and bloodstream infections [2]. Indeed, while B. fragilis accounts for only 4 to 13% of the normal human fecal microbiota, it is responsible for 63 to 80% of Bacteroides infections [3]. Only a few virulence factors have been described for B. fragilis, with the best characterized being the polysaccharide (PS) capsule [4] and a secreted metalloprotease, fragilysin [5]. The capsule, which displays antigenic variation, promotes the formation of abscesses [4], and the reduction of pro-inflammatory responses to B. fragilis[4, 6]. The metalloprotease fragilysin, which has been linked to diarrheal disease [5], has activity against the zonula junctions ...
Complexes of gold( I) have long been used to treat rheumatoid arthritis although the precise biological targets of gold are not well understood. One intriguing therapeutic target of Au( I) is the cathepsin family of lysosomal cysteine proteases. Here, we present the inhibition of cathepsin B by a known Au( I)-based drug and a series of derivatives. The complexes investigated were reversible, competitive inhibitors with IC50 values ranging from 0.3 to 250 mu M, depending on the substituents around the Au( I). ...
Lactacystin is a Streptomyces metabolite that inhibits cell cycle progression and induces neurite outgrowth in a murine neuroblastoma cell line. Tritium-labeled lactacystin was used to identify the 20S proteasome as its specific cellular target. Three distinct peptidase activities of this enzyme complex (trypsin-like, chymotrypsin-like, and peptidylglutamyl-peptide hydrolyzing activities) were inhibited by lactacystin, the first two irreversibly and all at different rates. None of five other proteases were inhibited, and the ability of lactacystin analogs to inhibit cell cycle progression and induce neurite outgrowth correlated with their ability to inhibit the proteasome. Lactacystin appears to modify covalently the highly conserved amino-terminal threonine of the mammalian proteasome subunit X (also called MB1), a close homolog of the LMP7 proteasome subunit encoded by the major histocompatibility complex. This threonine residue may therefore have a catalytic role, and subunit X/MB1 may be a ...
Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues only and by resistance to inhibition by members of the cystatin family of cysteine proteinase inhibitors. Glycyl endopeptidase has been crystallized from high salt with a substrate-like inhibitor covalently bound to the catalytic Cys 25. The structure has been solved by molecular replacement with the structure of papain and refined at 2.1 A to an R factor of 0.196 (Rfree = 0.258) with good geometry. The structure of the S1 substrate binding site of glycyl endopeptidase differs from that of papain by the substitution of glycines at residues 23 and 65 in papain, with glutamic acid and arginine, respectively, in glycyl endopeptidase. The side chains of these residues form a barrier across the binding pocket, effectively excluding substrate residues with large side chains from the S1 subsite. The constriction of this subsite in glycyl endopeptidase explains ...
Increased human cathepsin L activity is linked to invasive and metastatic cancers where it promotes degradation of the extracellular matrix. This major cysteine protease found in cell lysosomes and secreted from tissues ...
CIECHANOVER, Aaron. Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Medicina (B. Aires) [online]. 2010, vol.70, n.2, pp. 105-119. ISSN 0025-7680.. Between the 1950s and 1980s, scientists were focusing mostly on how the genetic code is transcribed to RNA and translated to proteins, but how proteins are degraded has remained a neglected research area. With the discovery of the lysosome by Christian de Duve it was assumed that cellular proteins are degraded within this organelle. Yet, several independent lines of experimental evidence strongly suggested that intracellular proteolysis is largely non-lysosomal, but the mechanisms involved remained obscure. The discovery of the ubiquitin-proteasome system resolved the enigma. We now recognize that degradation of intracellular proteins is involved in regulation of a broad array of cellular processes, such as cell cycle and division, regulation of ...
TY - JOUR. T1 - Effects of the combination of a proteasome inhibitor (PSI) and an inhibitor of ubiquitin-ligases (Leu-Ala) on the ultrastructure of human leukemic U937 cells. AU - Biały, P.. AU - Ziemba, H.. AU - Pleban, E.. AU - Wójcik, Cezary. PY - 2002/1/1. Y1 - 2002/1/1. N2 - We have used the dipeptide Leu-Ala in an attempt to prevent the formation of ubiquitin-protein conjugates in U937 cells by inhibition of cellular E3 enzymes (ubiquitin ligases). Proteasome inhibitors induce the formation of perinuclear aggregates for ubiquitinated proteins and proteasomes (aggresomes) in the area of the proteolytic center of the cell. Leu-Ala did not prevent the formation of those aggregates under the action of PSI (peptidyl aldehyde, selective inhibitor of the chymotrypsin-like activity of the proteasome), however it induced an accumulation of lipid droplets in treated cells, suggesting a previously unknown involvement of Leu-Ala in lipid metabolism. We conclude, that either Leu-Ala is not able to ...
Apoptosis is a major form of cell death, characterized initially by a series of stereotypic morphological changes. In the nematode Caenorhabditis elegans, the gene ced-3 encodes a protein required for developmental cell death. Since the recognition that CED-3 has sequence identity with the mammalian cysteine protease interleukin-1β-converting enzyme (ICE), a family of at least 10 related cysteine proteases has been identified. These proteins are characterized by almost absolute specificity for aspartic acid in the P1 position. All the caspases (ICE-like proteases) contain a conserved QACXG (where X is R, Q or G) pentapeptide active-site motif. Caspases are synthesized as inactive proenzymes comprising an N-terminal peptide (prodomain) together with one large and one small subunit. The crystal structures of both caspase-1 and caspase-3 show that the active enzyme is a heterotetramer, containing two small and two large subunits. Activation of caspases during apoptosis results in the cleavage of ...
The 26S Proteasome Is A Multisubunit Protease Responsible For Regulated Proteolysis In Eukaryotic Cells. It Is Composed Of One Catalytic 20S Proteasome And Two 19S Regulatory Particles Attached On Both Ends Of 20S Proteasomes. Here, We Describe The
Our study shows that liver proteasome activity is reduced by ~30-40% in genetic and dietary models of obesity and diabetes with coordinate upregulation of genes involved in the ubiquitin-proteasome pathway. In concert with our findings, recent systematic analyses of liver tissue in obese mice also revealed increased proteasome components (36,37), which may compensate for impaired proteasome function. To test a hypothesis that proteasome dysfunction may be a primary event that links obesity and insulin resistance in the liver, we established a mouse model of impaired proteasome function by deleting PA28 genes. The livers of PA28 KO mice showed impaired proteasome function similar to that observed in mouse models of obesity and type 2 diabetes, accumulation of ubiquitinated proteins and damaged organelles, ER stress, JNK activation, and insulin resistance (Supplementary Fig. 2). A chemical chaperone PBA administration almost completely alleviated proteasome dysfunction-mediated insulin resistance, ...
Angewandte Chemie Total Synthesis An Efficient Synthesis of Lactacystin b-Lactone** Timothy J. Donohoe,* Herman O. Sintim, Leena Sisangia, and John D. Harling Proteasomes are proteins within cells that are responsible for protein degradation. The 20 S proteasome, a 700-kDa protein that consists of 14 distinct subunits, is implicated in the ubiquitin proteasome pathway (UPP).[1] UPP, present in all eukaryotic cells, is essential for the normal turnover of cellular proteins and for the removal of damaged or misfolded [*] Dr. T. J. Donohoe, Dr. H. O. Sintim, L. Sisangia Department of Chemistry, Chemistry Research Laboratory University of Oxford Mansfield Road, Oxford, OX1 3TA (UK) Fax: (+ 44) 1865?275?708 E-mail: [email protected] Dr. J. D. Harling GlaxoSmithKline, Medicines Research Centre Gunnels Wood Road, Stevenage, SG1 2NY (UK) [**] We thank the EPSRC and GlaxoSmithKline for funding this project. AstraZeneca, Pfizer, and Novartis are thanked for generous unrestricted funding. ...
Fluorogenic Proteasome Substrate (Z-VKM-AMC) is used to measure the peptidase activity of the 20S proteasome.Also used as a fluorogenic substrate for Alzheimers Disease
Cells have multiple protein complexes to keep the genome intact and functional. Based on the current studies, the relationship among the components of the complexes may well differ between cells with and without the Blm10-20S proteasome activator. Loss of the activator downregulated numerous genes crucial for maintaining genomic stability, heightened DNA damage, and selectively sensitized cells to agents with different mechanisms of action. Although the exact or direct cause of the elevated DNA damage in Blm10 cells was not investigated for the current studies, the simultaneous downregulated expression appears important and suggests ways that Blm10 loss predisposes cells to lethal effects of agents with diverse mechanisms of action. We propose that modulated chromatin structure could compromise DNA integrity in blm10Δ/blm10Δ mutant cells, and conclude that the hypersusceptibilities establish Blm10 as a guardian against cellular stresses.. Even without external stimuli, cells were stressed ...
As highlighted by the similarity of their fold and the superimposition of their active site, we have shown that NsPCS belongs to the papain superfamily of cysteine proteases. 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. By analogy with such a mechanism, Cys-70, His-183, and Asp-201 (equivalent to Cys-56, His-162, and Asp-180 in AtPCS1) correspond to the catalytic triad in NsPCS. Moreover, it is also highly probable that Cys-70 and His-183 form a thiolate-imidazolium ion pair, stabilized by Asp-201, and that the nucleophilic attack of Cys-70 on the Cys-Gly peptide bond is favored by the oxyanion hole, made up of Cys-70 and Gln-64. In a second step, the water molecule W153, whose nucleophilicity is enhanced by the proximity of His-183 and Asp-201, is then ideally placed to attack the thioester bond and liberate the γ-glutamylcysteine. We could trap the ...
MG-115 (Z-Leu-Leu-Nva-H) is a potent, reversible peptide aldehyde inhibitor of proteasome chymotrypsin-like and caspase-like activities. It induces p53 dependent apoptosis. Blockade of proteasomal degradation by MG115 can activate autophagy. Treatment wi
Plpro/papain-like protease research reagents are researched and produced in house with premium quality at affordable price. Bulk in stock.
These are the general reagents used for all ligation reactions. Discussion of the specific reagents will be in each individual protocol. Sortase: A Sortase A construct with the N-terminal membrane targeting sequence removed is readily purified in N-terminally His-tagged form. The pETMCSIII based vector pLLC064 is available for expression of this construct. The protein is easily overexpresed and purified using standard nickel affinity chromatography conditions. It should be noted that the protein migrates anomalously on SDS-PAGE gels and appears to run as a protein of ~26 kDa molecular weight (###). We have confirmed the correct molecular weight of Sortase A expressed from pLLC064 by MS. The protein is very stable. We find it convenient to store the protein in Sortase buffer (50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, pH 7.5). The protein appears stable to multiple freeze-thaw cycles. We have not as yet investigated the potential to freeze dry Sortase for storage although we hope to carry out this ...
cysteine proteinase I: cleaves peptides primarily from the C-terminal region of thyroglobulin making thyroid hormone-containing sites accessible to cleavage by other endopeptidases
This review focuses on recent insights into the mechanisms and the biological functions of the proteasome. This large ATP-dependent proteolytic complex is the main site for protein degradation in mammalian cells and catalyses the rapid degradation of ubiquitinated proteins, and is the source of most antigenic peptides used by the immune system to screen for viruses and cancer. ATP is required to unfold globular proteins to open the gated channel into the 20S proteasome and to facilitate protein translation into it. Inhibitors of its proteolytic activity are widely used as research tools and have proven effective in cancer therapy. ...
in Phytochemistry (2017), (138), 29-51. Crude pineapple proteases extract (aka stem bromelain; EC 3.4.22.4) is an important proteolytic mixture that contains enzymes belonging to the cysteine proteases of the papain family. Numerous studies ... [more ▼]. Crude pineapple proteases extract (aka stem bromelain; EC 3.4.22.4) is an important proteolytic mixture that contains enzymes belonging to the cysteine proteases of the papain family. Numerous studies have been reported aiming at the fractionation and characterization of the many molecular species present in the extract, but more efforts are still required to obtain sufficient quantities of the various purified protease forms for detailed physicochemical, enzymatic and structural characterization. In this work, we describe an efficient strategy towards the purification of at least eight enzymatic forms. Thus, following rapid fractionation on a SP-Sepharose FF column, two sub-populations with proteolytic activity were obtained: the unbound ...
ROZMAN PUNGERČAR, Jerica, KOPITAR-JERALA, Nataša, BOGYO, M., TURK, Dušan, VASILJEVA, Olga, KLEMENČIČ, Ivica, VANDENABEELE, P., BR MME, D., PUIZDAR, Vida, FONOVIĆ, Marko, TRSTENJAK-PREBANDA, Mojca, DOLENC, Iztok, TURK, Vito, TURK, Boris. Inhibition of papain-like cysteine proteases and legumain by caspase-specific inhibitors : when reaction mechanism is more important than specificity. Cell Death Differ, 2003, vol. 10, str. 881-888 ...
Recent animal studies have suggested that TA has a cancer-preventative activity (3 , 5, 6, 7) . Cell culture studies also indicate that TA can induce either growth arrest (8) or apoptosis (9 , 10) . However, the involved molecular target(s) have not been identified. In the current study, we demonstrated that TA was a potent inhibitor of the proteasomal chymotrypsin-like activity both in vitro and in vivo. Inhibition of the proteasome activity by TA in intact Jurkat T cells resulted in accumulation of p27 and Bax, associated with G1 arrest and apoptosis. This finding is consistent with previous reports that show inhibition of the chymotrypsin-like, but not trypsin-like, activity of the proteasome by a specific inhibitor was sufficient to induce either tumor cell growth arrest or apoptosis (15 , 16) .. It has been shown that the ester bond carbon of β-lactone is responsible for potently and specifically inhibiting the proteasome (29) . Our results suggest that ester bonds present in TA are also ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Reaktivität: Hund, Wüstenrennmaus, Human and more. 94 verschiedene CASP14 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Sigma-Aldrich offers abstracts and full-text articles by [G Fenteany, R F Standaert, W S Lane, S Choi, E J Corey, S L Schreiber].
This gene encodes a component of the 26S proteasome. The 26S proteasome is a large multiprotein complex that catalyzes the degradation of ubiquitinated intracellular proteins. The encoded protein is a component of the 19S regulatory cap complex of the 26S proteasome and mediates substrate deubiquitination. A pseudogene of this gene is also located on the long arm of chromosome 2 ...
References for Abcams Proteasome 20S LMP2 peptide (ab4944). Please let us know if you have used this product in your publication
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Hoeller D, Dikic I. Targeting the ubiquitin system in cancer therapy.Nature. 2009 Mar 26;458(7237):438-44 [http://www.nature.com/nature/journal/v458/n7237/pdf/nature07960.pdf ...
It has been demonstrated that the Porphyromonas gingivalis cysteine proteinases (gingipains) activate and/or degrade a broad range of host proteins. Inactivation of gingipains R prior to infection of mice results in a decrease in the virulence of P. gingivalis. Analysis of mouse, rabbit, and chicken antisera raised to gingipain R1 demonstrated that the hemagglutinin domains of gingipains are very immunogenic; however, immunization of mice with a peptide derived from the hemagglutinin domain did not protect mice from P. gingivalis infection. Our recent studies indicate that immunization of mice with a peptide corresponding to the N-terminus of the catalytic domain of gingipains R results in the generation of an immune response that affords protection of mice from P. gingivalis infection. It is postulated that the protection observed results from the inactivation of the enzymatic activity of gingipains R as a result of antibody recognition of a processing site on the gingipain R precursor.. ...
Porphyromonas gingivalis, the major etiologic agent of chronic periodontitis, produces a broad spectrum of virulence factors, including Arg- and Lys-gingipain cysteine proteinases. In this study, we investigated the capacity of P. gingivalis gingipains to trigger a proinflammatory response in human monocyte-derived macrophages. Both Arg- and Lys-gingipain preparations induced the secretion of TNF-α and IL-8 by macrophages. Stimulation of macrophages with Arg-gingipain A/B preparation at the highest concentration was associated with lower amounts of cytokines detected, a phenomenon likely related to proteolytic degradation. The inflammatory response induced by gingipains was not dependent of their catalytic activity since heat-inactivated preparations were still effective. Stimulating macrophages with gingipain preparations was associated with increased levels of phosphorylated p38α MAPK suggesting its involvement in cell activation. In conclusion, our study brought clear evidence that P. gingivalis
TY - JOUR. T1 - Differential expression of SUMO-specific protease 7 variants regulates epithelial-mesenchymal transition. AU - Bawa-Khalfe, Tasneem. AU - Lu, Long-Sheng. AU - Zuo, Yong. AU - Huang, Chao. AU - Dere, Ruhee. AU - Lin, Feng Ming. AU - Yeh, Edward. PY - 2012/10/23. Y1 - 2012/10/23. N2 - Two Sentrin/small ubiquitin-like modifier (SUMO)-specific protease 7 (SENP7) variants are naturally expressed in breast epithelia. Breast cancer (BCa) onset down-regulates the short SENP7 splice variant (SENP7S) and enhances the long transcript (SENP7L). Here, we show that SENP7L induction promotes gene expression profiles that favor aberrant proliferation and initiate epithelial-mesenchymal transition (EMT). SENP7L exhibits an interaction domain for the epigenetic remodeler heterochromatin protein 1 α (HP1α) and isopeptidase activity against SUMO-modified HP1α. Loss of this interaction domain, as observed with SENP7S, favors HP1α SUMOylation. SUMOylated HP1α is enriched at E2F-responsive and ...
Protein breakdown by the ubiquitin‐proteasome system ensures cell survival and proliferation. The 20S proteasome core particle (CP) constitutes the heart of this non‐lysosomal protein degradation pathway. In mammals, three different CP types are known: the constitutive proteasome (cCP), the immunoproteasome (iCP), and the thymoproteasome (tCP) (Murata et al, 2007; Groettrup et al, 2010). All of them are built of seven different α‐ and seven different β‐subunits that are stacked in four heptameric rings around a central pore. Each type of CP incorporates a distinct set of catalytically active β1, β2 and β5 subunits (cCP: β1c, β2c and β5c; iCP: β1i, β2i and β5i; tCP: β1i, β2i and β5t) (Groll et al, 1997; Unno et al, 2002; Murata et al, 2007; Huber et al, 2012; Harshbarger et al, 2015). These subunits employ the same mechanism of peptide bond hydrolysis (Huber et al, 2012, 2016), but display different substrate specificities. Because of its pivotal biological role, the ...
Purpose : We have previously demonstrated that an accumulation of advanced glycation end-products (AGEs) in the Bruchs membrane (BrM) can alter retinal pigment epithelium (RPE) lysosomal activity by changing expression of key effectors and inhibitors. Altered activity of lysosomal cysteine proteases, the cathepsins, can in turn impact signalling via the NF-kB pathway. The aim of this study therefore was to analyse the effects of AGEs on specific lysosomal cathepsins, and the endogenous levels of effectors of the NF-kB signalling pathway in RPE. Methods : ARPE-19 cells were cultured on AGE-containing BrM mimics in vitro for 7-14 days. Intracellular processing of the cysteine proteases cathepsins B, L and S were assessed by qPCR and immunoblotting, while their intracellular activity was assessed using fluorescence-based cleavage assays. Expression of NF-kB (p65) and its main regulatory protein, IκBα, was assessed by qPCR and immunoblotting. Statistical analysis was performed using the ...
T-cell-mediated immune responses to defined antigens of Trypanosoma congolense were measured in cattle undergoing primary infection. The antigens used were the variable surface glycoprotein and two invariant antigens, a 33-kDa cysteine protease (congopain) and a recombinant form of a 69-kDa heat-shock protein. Proliferative responses were highest during the second week postinfection and were detected in cells obtained from the lymph node draining the site of infection but not in peripheral blood mononuclear cells. Production of IL-2 and IFN- was measured in supernatants from antigen-stimulated lymph node cell cultures. Expression of IL-2, IL-4, and IFN- mRNA was detected in antigen-stimulated lymph node cells by reverse transcription-polymerase chain amplification ...
TY - JOUR. T1 - Cysteine protease secreted by Paragonimus westermani attenuates effector functions of human eosinophils stimulated with immunoglobulin G. AU - Myeong Heon Shin, Heon Shin. AU - Kita, H.. AU - Hae Young Park, Young Park. AU - Ju Young Seoh, Young Seoh. PY - 2001/3/14. Y1 - 2001/3/14. N2 - An immunoglobulin G (IgG)-coated surface, such as that found on helminth parasites, is one of the most effective physiologic stimuli for eosinophil activation. The cysteine proteases secreted by tissue-invasive helminth larvae play an important role in evasion of the immune response by degrading the host immunoglobulins. In this study, we investigated whether cysteine proteases in the excretory-secretory product (ESP) produced by Paragonimus westermani newly existed metacercariae (PwNEM), which cause pulmonary or extrapulmonary paragonimiasis in human beings, could modify effector functions of human eosinophils stimulated with IgG. We coated 96-well plates with human IgG in the absence or ...

Systemic elastin degradation in chronic obstructive pulmonary disease | ThoraxSystemic elastin degradation in chronic obstructive pulmonary disease | Thorax

46 as have cysteine proteases (eg, cathepsin K) in animal models.47 ,48 Thus, these other proteases may be involved in systemic ... are zinc-dependent endopeptidases with similar structures and therefore may be potential targets for treatment.39 Indeed, ...
more infohttp://thorax.bmj.com/content/67/7/606

cathepsin H Inhibitors | SCBT - Santa Cruz Biotechnologycathepsin H Inhibitors | SCBT - Santa Cruz Biotechnology

A broad spectrum cysteine proteinase and calpain activation inhibitor. 66701-25-5. sc-201276. sc-201276A. sc-201276B. 5 mg. 25 ... can act both as an aminopeptidase and as an endopeptidase. Elevated levels of cathepsin H correlates with malignant progression ...
more infohttps://www.scbt.com/browse/cathepsin-h-Inhibitors/_/N-1uam9m9

calcium-dependent cysteine-type endopeptidase activity Gene Ontology Term (GO:0004198)calcium-dependent cysteine-type endopeptidase activity Gene Ontology Term (GO:0004198)

The Gene Ontology (GO) project is a collaborative effort to address the need for consistent descriptions of gene products across databases. You can use this browser to view terms, definitions, and term relationships in a hierarchical display. Links to summary annotated gene data at MGI are provided in Term Detail reports.
more infohttp://www.informatics.jax.org/vocab/gene_ontology/GO:0004198

NAVER Academic | Legumains - a family of asparagine-specific cysteine endopeptidases involved in propolypeptide processing and...NAVER Academic | Legumains - a family of asparagine-specific cysteine endopeptidases involved in propolypeptide processing and...

Legumains are a recently discovered family of plant and animal cysteine endopeptidases with a cleavage specificity for Asn in ... Legumains are a recently discovered family of plant and animal cysteine endopeptidases with a cleavage specificity for Asn in ... asparagine-specific cysteine endopeptidases, biosynthesis, evolution, legumain, propolypeptide processing, protein degradation ... Legumains - a family of asparagine-specific cysteine endopeptidases involved in propolypeptide processing and protein breakdown ...
more infohttps://academic.naver.com/article.naver?doc_id=65292764

MEROPS - the Peptidase DatabaseMEROPS - the Peptidase Database

Subclass 3.4 (Peptidases) ,, Sub-subclass 3.4.22 (Cysteine endopeptidases) ,, Peptidase 3.4.22.27. ...
more infohttps://www.ebi.ac.uk/merops/cgi-bin/pepsum?id=C01.034

Delta9-tetrahydrocannabinol induces apoptosis in macrophages and lymphocytes: involvement of Bcl-2 and caspase-1.Delta9-tetrahydrocannabinol induces apoptosis in macrophages and lymphocytes: involvement of Bcl-2 and caspase-1.

Cysteine Endopeptidases / physiology*. DNA / biosynthesis, isolation & purification. DNA Fragmentation. Electrophoresis, ... 0/Hallucinogens; 0/Proto-Oncogene Proteins c-bcl-2; 1972-08-3/Tetrahydrocannabinol; 9007-49-2/DNA; EC 3.4.22.-/Cysteine ...
more infohttp://www.biomedsearch.com/nih/Delta9-tetrahydrocannabinol-induces-apoptosis-in/9694974.html

Lymphocyte apoptosis in the inflammatory reaction around Taenia solium metacestodes in porcine cysticercosis.Lymphocyte apoptosis in the inflammatory reaction around Taenia solium metacestodes in porcine cysticercosis.

Two events, high metacestode viability (100%) and high cysteine protease activity were found to be ... Cysteine Endopeptidases / metabolism. Cysticercosis / immunology, parasitology, veterinary*. DNA Fragmentation. Flow Cytometry ... 0/Annexin A5; 0/Culture Media; 0/Fluorescent Dyes; EC 3.4.22.-/Cysteine Endopeptidases ... Two events, high metacestode viability (100%) and high cysteine protease activity were found to be closely related to a high ...
more infohttp://www.biomedsearch.com/nih/Lymphocyte-apoptosis-in-inflammatory-reaction/16621283.html

MEDLINE - Resultado p gina 1
	MEDLINE - Resultado p gina 1

Cysteine Endopeptidases); EC 3.4.22.37 (argingipain, Porphyromonas gingivalis). ... Ciste na Endopeptidases/qu mica. C lulas Epiteliais/microbiologia. Flavonoides/isolamento & purifica o. cido G lico/qu mica. ...
more infohttp://bases.bireme.br/cgi-bin/wxislind.exe/iah/online/?IsisScript=iah/iah.xis&nextAction=lnk&base=MEDLINE&lang=p&format=detailed.pft&indexSearch=EX&exprSearch=B01.650.940.800.575.912.250.198.500.937

KEGG ENZYME: 3.4.22.38KEGG ENZYME: 3.4.22.38

Cysteine endopeptidases. Reaction(IUBMB). Broad proteolytic activity. With small-molecule substrates and inhibitors, the major ... Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin ... Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone. ...
more infohttps://www.genome.jp/dbget-bin/www_bget?ec:3.4.22.38

KEGG ENZYME: 3.4.22.58KEGG ENZYME: 3.4.22.58

Cysteine endopeptidases. Reaction(IUBMB). Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence ... Identification of a cysteine protease closely related to interleukin-1 beta-converting enzyme. ... Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine proteases, are CrmA-inhibitable proteases. ...
more infohttps://www.genome.jp/dbget-bin/www_bget?enzyme+3.4.22.58

MEDLINE - Resultado p gina 1
	MEDLINE - Resultado p gina 1

Cysteine Endopeptidases); EC 3.4.22.28 (3C proteases); EC 3.5.4.1 (Cytosine Deaminase). ... Ciste na Endopeptidases/gen tica. Ciste na Endopeptidases/metabolismo. Citosina Desaminase/gen tica. Citosina Desaminase/ ... Ciste na Endopeptidases/bioss ntese. Citosina Desaminase/bioss ntese. Flucitosina/farmacologia. Terapia Gen tica/m todos. V rus ...
more infohttp://bases.bireme.br/cgi-bin/wxislind.exe/iah/online/?IsisScript=iah/iah.xis&nextAction=lnk&base=MEDLINE&lang=p&format=detailed.pft&indexSearch=EX&exprSearch=G05.360.340.024.340.825.500

Related Articles by Review for PubMed (Select 12838346) - PubMed - NCBIRelated Articles by Review for PubMed (Select 12838346) - PubMed - NCBI

Toward computer-based cleavage site prediction of cysteine endopeptidases.. Lohmüller T, Wenzler D, Hagemann S, Kiess W, Peters ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed?linkname=pubmed_pubmed_reviews&from_uid=12838346

Caspase-3 (P42574) | InterPro | EMBL-EBICaspase-3 (P42574) | InterPro | EMBL-EBI

GO:0004197 cysteine-type endopeptidase activity GO:0008234 cysteine-type peptidase activity ...
more infohttp://www.ebi.ac.uk/interpro/protein/P42574

CAPN5 calpain 5 [Homo sapiens (human)] - Gene - NCBICAPN5 calpain 5 [Homo sapiens (human)] - Gene - NCBI

calcium-dependent cysteine-type endopeptidase activity IBA Inferred from Biological aspect of Ancestor. more info ... Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. A ... Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell ... Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell ...
more infohttps://www.ncbi.nlm.nih.gov/gene/726

Identification of biomarkers for amyotrophic lateral sclerosis by comprehensive analysis of exosomal mRNAs in human...Identification of biomarkers for amyotrophic lateral sclerosis by comprehensive analysis of exosomal mRNAs in human...

negative regulation of cysteine-type endopeptidase activity. down. 2.80E-06. Enrichment of Gene Ontology (GO) in DEGs was ...
more infohttps://link.springer.com/article/10.1186%2Fs12920-019-0473-z

HOGENOM: RHOPS 1 PE1007HOGENOM: RHOPS 1 PE1007

DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR ...
more infohttp://pbil.univ-lyon1.fr/cgi-bin/acnuc-search-id?query=RHOPS_1_PE1007&db=HOGENOM&ident=SCRATCH

Cysteine protease - WikipediaCysteine protease - Wikipedia

Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases. *Cysteine+endopeptidases at the US ... Cysteine Peptidase. Crystal structure of the cysteine peptidase papain in complex with its covalent inhibitor E-64. Rendered ... In fact, dozens of latices of different plant families are known to contain cysteine proteases.[1] Cysteine proteases are used ...
more infohttps://en.m.wikipedia.org/wiki/Cysteine_endopeptidase

P3N-PIPO polyprotein - Bean common mosaic necrosis virus (strain NL-3) (BCMNV)P3N-PIPO polyprotein - Bean common mosaic necrosis virus (strain NL-3) (BCMNV)

cysteine-type endopeptidase activity Source: InterPro. *serine-type peptidase activity Source: UniProtKB-KW ...
more infohttps://www.uniprot.org/uniprot/P0CJ94

Ctsk - Cathepsin K precursor - Mus musculus (Mouse) - Ctsk gene & proteinCtsk - Cathepsin K precursor - Mus musculus (Mouse) - Ctsk gene & protein

cysteine-type endopeptidase activity Source: MGI. *cysteine-type peptidase activity Source: MGIInferred from sequence orthology ... p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues ...
more infohttps://www.uniprot.org/uniprot/P55097

Usp7 - Ubiquitin carboxyl-terminal hydrolase 7 - Mus musculus (Mouse) - Usp7 gene & proteinUsp7 - Ubiquitin carboxyl-terminal hydrolase 7 - Mus musculus (Mouse) - Usp7 gene & protein

cysteine-type endopeptidase activity Source: UniProtKB ,p>Inferred from Mutant Phenotype,/p> ,p>Describes annotations that are ...
more infohttps://www.uniprot.org/uniprot/Q6A4J8

CTSS Gene - GeneCards | CATS Protein | CATS AntibodyCTSS Gene - GeneCards | CATS Protein | CATS Antibody

cysteine-type endopeptidase activity. IDA,TAS. --. GO:0004252. serine-type endopeptidase activity. TAS. --. ... cathepsin S,lysosomal cysteine proteinase,expressed in spleen,heart and lung,papain superfamily,specifically involved in MHCII- ... The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may participate ... GO annotations related to this gene include peptidase activity and cysteine-type peptidase activity. An important paralog of ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=CTSS

CFLAR Gene - GeneCards | CFLAR Protein | CFLAR AntibodyCFLAR Gene - GeneCards | CFLAR Protein | CFLAR Antibody

activation of cysteine-type endopeptidase activity involved in apoptotic process. IBA. --. GO:0007519. skeletal muscle tissue ... Gene Ontology (GO) annotations related to this gene include cysteine-type peptidase activity. ...
more infohttps://www.genecards.org/cgi-bin/carddisp.pl?gene=CFLAR

Activity-based Probes That Target Diverse Cysteine Protease Families - PubMedActivity-based Probes That Target Diverse Cysteine Protease Families - PubMed

Cysteine Endopeptidases / chemistry *. Actions. * Search in PubMed * Search in MeSH * Add to Search ... Activity-based Probes That Target Diverse Cysteine Protease Families Daisuke Kato 1 , Kelly M Boatright, Alicia B Berger, Tamim ... Activity-based Probes That Target Diverse Cysteine Protease Families Daisuke Kato et al. Nat Chem Biol. Jun 2005 ... Novel aza peptide inhibitors and active-site probes of papain-family cysteine proteases. Verhelst SH, Witte MD, Arastu-Kapur S ...
more infohttps://pubmed.ncbi.nlm.nih.gov/16407991/

Discrete Cleavage Motifs of Constitutive and Immunoproteasomes Revealed by Quantitative Analysis of Cleavage Products - PubMedDiscrete Cleavage Motifs of Constitutive and Immunoproteasomes Revealed by Quantitative Analysis of Cleavage Products - PubMed

Cysteine Endopeptidases / chemistry Actions. * Search in PubMed * Search in MeSH * Add to Search ... and multicatalytic endopeptidase complex--like (MECL)-1 leads to the formation of immunoproteasomes which have been associated ...
more infohttps://pubmed.ncbi.nlm.nih.gov/11435468/
  • 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)
  • These reagents selectively form covalent bonds with the active-site thiol of a cysteine protease, allowing direct biochemical profiling of protease activities in complex proteomes. (nih.gov)
  • Further expression analysis revealed that the induction of genes encoding alcohol dehydrogenase 3, metalloprotease FtsH, cysteine protease 1 precursor, phytepsin precursor (aspartic protease), and a 26S proteasome regulatory subunit was associated with the androgenic potential of microspores, whereas the induction of transcripts involved in signaling and cytoprotection was associated with stress responses. (tudelft.nl)
  • endopeptidases (serine, aspartic, cysteine and metalloproteinases) cleave the peptide distal to the terminus. (thermofisher.com)
  • Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). (abcam.com)
  • Cysteine protease inhibitors block schistosome hemoglobin degradation in vitro and decrease worm burden and egg production in vivo (1996) Wasilewski Margaret M et al. (naver.com)