Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition. [electronic resource]
Producer: 20200225Description: 9476-9488 p. digitalISSN:- 1083-351X
- Amino Acid Sequence
- Binding Sites
- Catalytic Domain
- Crystallography, X-Ray
- Directed Molecular Evolution
- Humans
- Matrix Metalloproteinase 3 -- chemistry
- Matrix Metalloproteinase Inhibitors -- chemistry
- Mutation
- Protein Binding
- Protein Conformation
- Protein Domains
- Tissue Inhibitor of Metalloproteinase-1 -- chemistry
- Two-Hybrid System Techniques
No physical items for this record
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
There are no comments on this title.
Log in to your account to post a comment.