Sort   by:  
 Page size 
ProteomicsPost-translational regulation and proteolytic activity of human adamts-8: a comparison with adamts-1, -4, and -5
A Disintegrin-like And Metalloprotease with Thrombospondin type 1 motifs (ADAMTS)-8 is a secreted protease which has been recently implicated in the pathogenesis of pulmonary arterial hypertension (PAH). However, the substrate repertoire of ADAMTS-8 and regulation of its activity are incompletely u...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027724 | Pride
Ecm Opn Protease Pah Adamts 
GenomicsADAMTS-9 is an aggrecan-degrading enzyme in mouse cartilage
ADAMTS-9 is an aggrecan-degrading enzyme in mouse cartilage
PRJNA434470 | ENA
TranscriptomicsADAMTS-9 is an aggrecan-degrading enzyme in mouse cartilage
Although ADAMTS-4 and ADAMTS-5 are the principal aggrecanases in mice and humans, mice lacking both these enzymes (ADAMTS-4/-5Dcat) are healthy, viable, with no overt skeletal phenotype, suggesting the presence of an alternative aggrecanase in these mice. We previously identified a novel aggrecanase...
ORGANISM(S): Mus musculus 
2019-01-28 | GSE110754 | GEO
UnknownADAMTS-9 in Mouse Cartilage Has Aggrecanase Activity That Is Distinct from ADAMTS-4 and ADAMTS-5.
Not available
S-EPMC6387038 | biostudies-literature
ProteomicsECM characterization of aortas from Adamts5+/+ and Adamts5∆cat AngII-treated mice by LC-MS/MS
Objective - Thoracic aortic aneurysm (TAA), a degenerative disease of the aortic wall, is accompanied by changes in the structure and composition of the aortic extracellular matrix (ECM). The ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family has recently been implicated ...
ORGANISM(S): Mus musculus (Mouse) 
2018-05-08 | PXD009410 | Pride
Aneurysm Protease Ascending aorta Extracellular matrix Lc-ms/ms Adamts 
UnknownRegulation of ADAMTS Proteases.
Not available
S-EPMC8275829 | biostudies-literature
TranscriptomicsComparison of 2 ADAMTS metalloproteases in closure of mouse palate - versican proteolysis in regulating palatal mesenchyme proliferation
We identify a role for two evolutionarily related, secreted metalloproteases of the ADAMTS family (A disintegrin-like and metalloprotease domain with thrombospondin type-1 motif), ADAMTS20 and ADAMTS9, in palatogenesis. Adamts20 mutations cause the mouse white spotting mutant belted (bt), whereas Ad...
ORGANISM(S): Mus musculus 
2010-06-30 | E-GEOD-21358 | biostudies-arrayexpress
UnknownFull-length ADAMTS-1 and the ADAMTS-1 fragments display pro- and antimetastatic activity, respectively.
Not available
S-EPMC2759703 | biostudies-literature
UnknownADAMTS proteins in human disorders.
Not available
S-EPMC6146047 | biostudies-literature
UnknownSecreted Metalloproteinase ADAMTS-3 Inactivates Reelin.
Not available
S-EPMC6596773 | biostudies-literature
Sort   by:  
 Page size