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Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications.

Abstract:

We have reported previously that reactive-site mutants of N-TIMP-3 [N-terminal inhibitory domain of TIMP-3 (tissue inhibitor of metalloproteinases 3)] modified at the N-terminus, selectively inhibited ADAM17 (a disintegrin and metalloproteinase 17) over the MMPs (matrix metalloproteinases). The primary aggrecanases ADAMTS (ADAM with thrombospondin motifs) -4 and -5 are ADAM17-related metalloproteinases which are similarly inhibited by TIMP-3, but are poorly inhibited by other TIMPs. Using a n...

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Publication status:
Published

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Publisher copy:
10.1042/bj20100725

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDORMS
Role:
Author
Journal:
Biochemical journal More from this journal
Volume:
431
Issue:
1
Pages:
113-122
Publication date:
2010-10-01
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
Language:
English
Keywords:
Pubs id:
pubs:226814
UUID:
uuid:e6ed1b13-6478-4d51-8bf9-8de85d377c10
Local pid:
pubs:226814
Source identifiers:
226814
Deposit date:
2012-12-19

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