about
Identification of three novel members of the calcium-dependent chloride channel (CaCC) family predominantly expressed in the digestive tract and tracheaMETH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activityADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS familyHuman TRH-degrading ectoenzyme cDNA cloning, functional expression, genomic structure and chromosomal assignmentMultiple viral ligands naturally presented by different class I molecules in transporter antigen processing-deficient vaccinia virus-infected cellsN-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidaseMolecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell typesDipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expressionThe genome of Melanoplus sanguinipes entomopoxvirusCloning of a novel membrane-linked metalloproteinase from human myeloma cellsGene expression of the dibasic-pair cleaving enzyme NRD convertase (N-arginine dibasic convertase) is differentially regulated in the GH3 pituitary and Mat-Lu prostate cell linesMolecular and biotechnological aspects of microbial proteasesADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanismBorrelia burgdorferi, host-derived proteases, and the blood-brain barrierA proteolytic pathway that controls the cholesterol content of membranes, cells, and bloodA family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factorsSegmentally variable genes: a new perspective on adaptationADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis.Proteolytic processing of von Willebrand factor by adamts13 and leukocyte proteasesCarnosinases, their substrates and diseasesEnteric bacterial proteases in inflammatory bowel disease- pathophysiology and clinical implicationsRNA-seq-based metatranscriptomic and microscopic investigation reveals novel metalloproteases of Neobodo sp. as potential virulence factors for soft tunic syndrome in Halocynthia roretziStructure of neurolysin reveals a deep channel that limits substrate accessYeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidasesACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysisSwapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidaseCrystal structure of aminopeptidase N from human pathogen Neisseria meningitidisStructural basis for substrate recognition and hydrolysis by mouse carnosinase CN2Crystal Structure of the Protealysin Precursor: INSIGHTS INTO PROPEPTIDE FUNCTIONThe Exquisite Structure and Reaction Mechanism of Bacterial Pz-peptidase A toward Collagenous Peptides: X-RAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS OF PZ-PEPTIDASE A REVEALS DIFFERENCES FROM MAMMALIAN THIMET OLIGOPEPTIDASEStructure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase familyStructure of theArabidopsis thalianaTOP2 oligopeptidasePromotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon.Identification of yeast aspartyl aminopeptidase gene by purifying and characterizing its product from yeast cells.The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae.The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities.ADAMTS-1 is an active metalloproteinase associated with the extracellular matrixCharacterization of human aspartoacylase: the brain enzyme responsible for Canavan diseaseCrystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization
P2860
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P2860
description
1995 nî lūn-bûn
@nan
1995 թուականին հրատարակուած գիտական յօդուած
@hyw
1995 թվականին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Evolutionary families of metallopeptidases
@ast
Evolutionary families of metallopeptidases
@en
Evolutionary families of metallopeptidases
@nl
type
label
Evolutionary families of metallopeptidases
@ast
Evolutionary families of metallopeptidases
@en
Evolutionary families of metallopeptidases
@nl
prefLabel
Evolutionary families of metallopeptidases
@ast
Evolutionary families of metallopeptidases
@en
Evolutionary families of metallopeptidases
@nl
P3181
P1476
Evolutionary families of metallopeptidases
@en
P2093
A J Barrett
P304
P3181
P356
10.1016/0076-6879(95)48015-3
P407
P577
1995-01-01T00:00:00Z