The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3
- 1 October 2009
- journal article
- Published by Elsevier in Matrix Biology
- Vol. 28 (8) , 463-469
Abstract
No abstract availableKeywords
Funding Information
- National Institute of Arthritis and Musculoskeletal and Skin Diseases
- Wellcome Trust (057473, AR40994)
This publication has 52 references indexed in Scilit:
- Three-dimensional domain architecture of the ADAM family proteinasesSeminars in Cell & Developmental Biology, 2009
- Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificityBlood, 2008
- Structural Determinants of the ADAM Inhibition by TIMP-3: Crystal Structure of the TACE-N-TIMP-3 ComplexJournal of Molecular Biology, 2008
- Calcium pentosan polysulfate is a multifaceted exosite inhibitor of aggrecanasesThe FASEB Journal, 2008
- The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibitionBiochemical Journal, 2008
- Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5Protein Science, 2008
- Identification of the Extracellular Matrix (ECM) Binding Motifs of Tissue Inhibitor of Metalloproteinases (TIMP)-3 and Effective Transfer to TIMP-1Journal of Biological Chemistry, 2007
- Crystallization and preliminary X-ray crystallographic analysis of two vascular apoptosis-inducing proteins (VAPs) fromCrotalus atroxvenomActa Crystallographica Section F Structural Biology and Crystallization Communications, 2006
- Domains and Maturation Processes That Regulate the Activity of ADAMTS-2, a Metalloproteinase Cleaving the Aminopropeptide of Fibrillar Procollagens Types I–III and VJournal of Biological Chemistry, 2005
- Full-Length and N-TIMP-3 Display Equal Inhibitory Activities toward TNF-α ConvertaseBiochemical and Biophysical Research Communications, 2001