ADAMTS proteins in human disorders

TJ Mead, SS Apte - Matrix Biology, 2018 - Elsevier
ADAMTS proteins are a superfamily of 26 secreted molecules comprising two related, but
distinct families. ADAMTS proteases are zinc metalloendopeptidases, most of whose …

[HTML][HTML] Insights on ADAMTS proteases and ADAMTS-like proteins from mammalian genetics

J Dubail, SS Apte - Matrix Biology, 2015 - Elsevier
The mammalian ADAMTS superfamily comprises 19 secreted metalloproteinases and 7
ADAMTS-like proteins, each the product of a distinct gene. Thus far, all appear to be relevant …

The ADAMTS (L) family and human genetic disorders

C Le Goff, V Cormier-Daire - Human molecular genetics, 2011 - academic.oup.com
ADAMTS designates a family of 19 secreted enzymes, whose the first member ADAMTS1
was described in 1997. The ADAMTS family has a role in extracellular matrix degradation …

Functional evolution of ADAMTS genes: evidence from analyses of phylogeny and gene organization

AC Nicholson, SB Malik, JM Logsdon… - BMC evolutionary …, 2005 - Springer
Abstract Background The ADAMTS (A Disintegrin-like and Metalloprotease with
Thrombospondin motifs) proteins are a family of metalloproteases with sequence similarity …

Double‐knockout of ADAMTS‐4 and ADAMTS‐5 in mice results in physiologically normal animals and prevents the progression of osteoarthritis

MK Majumdar, R Askew, S Schelling… - … : Official Journal of …, 2007 - Wiley Online Library
Objective To phenotypically characterize ADAMTS‐4–and ADAMTS‐5–double‐knockout
mice, and to determine the effect of deletion of ADAMTS‐4 and ADAMTS‐5 on the …

Evolutionary divergence and functions of the ADAM and ADAMTSgene families

CN Brocker, V Vasiliou, DW Nebert - Human genomics, 2009 - Springer
The'A-disintegrin and metalloproteinase'(ADAM) and'A-disintegrin and metalloproteinase
with thrombospondin motifs'(ADAMTS) genes make up two similar, yet distinct, gene …

The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family

GP Kaushal, SV Shah - The Journal of clinical investigation, 2000 - Am Soc Clin Investig
Comparison of domain structures of ADAMTSs, ADAMs and SVMPs. The first three boxes of
each bar represent, respectively, the common prodomain and the metalloprotease and …

Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation

RPT Somerville, KA Jungers, SS Apte - Journal of Biological Chemistry, 2004 - ASBMB
We describe the discovery and characterization of ADAMTS10, a novel metalloprotease
encoded by a locus on human chromosome 19 and mouse chromosome 17. ADAMTS10 …

Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains

S Gerhardt, G Hassall, P Hawtin, E McCall… - Journal of molecular …, 2007 - Elsevier
The ADAMTS (a disintegrin-like and metalloproteinase domain with thrombospondin type I
motifs) family of proteases plays a role in pathological conditions including arthritis, cancer …

The ADAMTS metalloproteinases

S Porter, IM Clark, L Kevorkian… - Biochemical …, 2005 - portlandpress.com
The ADAMTSs (ad isintegrin a nd m etalloproteinase with t hrombo s pondin motifs) are a
group of proteases that are found both in mammals and invertebrates. Since the prototype …