Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.
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Activation of human prolegumain by cleavage at a C-terminal asparagine residueStructural and Molecular Mechanism for Autoprocessing of MARTX Toxin of Vibrio cholerae at Multiple SitesPorphyromonas gingivalis Virulence Factor Gingipain RgpB Shows a Unique Zymogenic Mechanism for Cysteine PeptidasesStructural analysis of asparaginyl endopeptidase reveals the activation mechanism and a reversible intermediate maturation stageA metacaspase of Trypanosoma brucei causes loss of respiration competence and clonal death in the yeast Saccharomyces cerevisiae.The GPI transamidase complex of Saccharomyces cerevisiae contains Gaa1p, Gpi8p, and Gpi16p.Inhibition of distant caspase homologues by natural caspase inhibitorsMolecular changes in Opisthorchis viverrini (Southeast Asian liver fluke) during the transition from the juvenile to the adult stageInhibition of mammalian legumain by Michael acceptors and AzaAsn-halomethylketones.Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins.Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes.Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain.The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship.Asparaginyl endopeptidase from the carcinogenic liver fluke, Opisthorchis viverrini, and its potential for serodiagnosis.Helper T cell epitope-mapping reveals MHC-peptide binding affinities that correlate with T helper cell responses to pneumococcal surface protein A.Blastocystis legumain is localized on the cell surface, and specific inhibition of its activity implicates a pro-survival role for the enzyme.Evolutionary lines of cysteine peptidases.Cysteine proteases of Porphyromonas gingivalis.De novo transcriptome sequencing analysis and comparison of differentially expressed genes (DEGs) in Macrobrachium rosenbergii in China.Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease.Structure and mechanism of cysteine peptidase gingipain K (Kgp), a major virulence factor of Porphyromonas gingivalis in periodontitis.Temporal activation of anti- and pro-apoptotic factors in human gingival fibroblasts infected with the periodontal pathogen, Porphyromonas gingivalis: potential role of bacterial proteases in host signalling.Asparagine endopeptidase is an innovative therapeutic target for neurodegenerative diseases.Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease.Bacterial protease inhibitors.Propeptide-mediated inhibition of cognate gingipain proteinases.The role of gingipains in the pathogenesis of periodontal disease.Gingipains from Porphyromonas gingivalis W83 synergistically disrupt endothelial cell adhesion and can induce caspase-independent apoptosis.Polyester synthases: natural catalysts for plastics.The protein structures that shape caspase activity, specificity, activation and inhibition.The Amborella vacuolar processing enzyme family.Counter Selection Substrate Library Strategy for Developing Specific Protease Substrates and Probes.Asparaginyl endopeptidase: case history of a class II MHC compartment protease.Expression profile of cathepsins indicates the potential of cathepsins B and D as prognostic factors in breast cancer patients.Recent developments in the molecular, biochemical and functional characterization of GPI8 and the GPI-anchoring mechanism [review].Phylogeny and physiology of candidate phylum 'Atribacteria' (OP9/JS1) inferred from cultivation-independent genomics.The Paracaspase MALT1.Caspase substrates and inhibitorsWhat happened to plant caspases?Selective ablation of tumor-associated macrophages suppresses metastasis and angiogenesis
P2860
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P2860
Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Identification of the active s ...... an of cysteine endopeptidases.
@ast
Identification of the active s ...... an of cysteine endopeptidases.
@en
Identification of the active s ...... an of cysteine endopeptidases.
@nl
type
label
Identification of the active s ...... an of cysteine endopeptidases.
@ast
Identification of the active s ...... an of cysteine endopeptidases.
@en
Identification of the active s ...... an of cysteine endopeptidases.
@nl
prefLabel
Identification of the active s ...... an of cysteine endopeptidases.
@ast
Identification of the active s ...... an of cysteine endopeptidases.
@en
Identification of the active s ...... an of cysteine endopeptidases.
@nl
P2093
P1433
P1476
Identification of the active s ...... an of cysteine endopeptidases.
@en
P2093
P304
P356
10.1016/S0014-5793(98)01574-9
P407
P577
1998-12-01T00:00:00Z