The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
about
Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family membersMetalloprotease-disintegrin MDC9: intracellular maturation and catalytic activityCloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS familyInteraction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpuraMeprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell typesMMP13 mutation causes spondyloepimetaphyseal dysplasia, Missouri type (SEMD(MO)Polymerase chain reaction selects a novel disintegrin proteinase from CD40-activated germinal center dendritic cellsCloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial originTargeting migration inducting gene-7 inhibits carcinoma cell invasion, early primary tumor growth, and stimulates monocyte oncolytic activityAn old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprinThe metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidasesMatrix metalloproteinases: old dogs with new tricksMatrix metalloproteinases in exercise and obesityGlycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunitiesProcessing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme InactivationActivity dependent CAM cleavage and neurotransmissionReaching the melting point: Degradative enzymes and protease inhibitors involved in baculovirus infection and disseminationOptimizing dentin bond durability: control of collagen degradation by matrix metalloproteinases and cysteine cathepsinsMatrix metalloproteinases in kidney homeostasis and diseasesSynaptic circuit remodelling by matrix metalloproteinases in health and diseaseThe 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognitionProenzyme Structure and Activation of Astacin MetallopeptidaseThe structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinasesMatrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP ComplexesStructural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)A Disintegrin and Metalloprotease 17 in the Cardiovascular and Central Nervous SystemsBiochemical and spectroscopic characterization of the catalytic domain of MMP16 (cdMMP16)Pro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagenCatalytic activity of human ADAM33Unconventional activation mechanisms of MMP-26, a human matrix metalloproteinase with a unique PHCGXXD cysteine-switch motifActivation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cellsPeptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26Matrix metalloproteinases as therapeutic targets for idiopathic pulmonary fibrosisThe metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesionTIMP-2 is required for efficient activation of proMMP-2 in vivoADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domainIdentification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats and a unique GON domain
P2860
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P2860
The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
description
1990 nî lūn-bûn
@nan
1990 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
The cysteine switch: a princip ...... metalloproteinase gene family
@ast
The cysteine switch: a princip ...... metalloproteinase gene family
@en
The cysteine switch: a princip ...... metalloproteinase gene family
@nl
type
label
The cysteine switch: a princip ...... metalloproteinase gene family
@ast
The cysteine switch: a princip ...... metalloproteinase gene family
@en
The cysteine switch: a princip ...... metalloproteinase gene family
@nl
prefLabel
The cysteine switch: a princip ...... metalloproteinase gene family
@ast
The cysteine switch: a princip ...... metalloproteinase gene family
@en
The cysteine switch: a princip ...... metalloproteinase gene family
@nl
P2860
P3181
P356
P1476
The cysteine switch: a princip ...... metalloproteinase gene family
@en
P2093
H Birkedal-Hansen
H E Van Wart
P2860
P304
P3181
P356
10.1073/PNAS.87.14.5578
P407
P577
1990-07-01T00:00:00Z