The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.

The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.

We investigated whether the affinity of tissue inhibitor of metalloproteinases (TIMP)-3 for adamalysins with thrombospondin motifs (ADAMTS)-4 and ADAMTS-5 is affected by the non-catalytic ancillary domains of the enzymes. For this purpose, we first established a novel method of purifying recombinant...

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Bibliographic Details
Main Authors:	Troeberg, L, Fushimi, K, Scilabra, S, Nakamura, H, Dive, V, Thøgersen, I, Enghild, J, Nagase, H
Format:	Journal article
Language:	English
Published:	2009

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