Inactivation of N-TIMP-1 by N-terminal acetylation when expressed in bacteria-Reference-Cited by-同舟云学术

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Inactivation of N-TIMP-1 by N-terminal acetylation when expressed in bacteria

Published:2008-11 Issue:11 Volume:89 Page:960-968
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Van Doren Steven R.,Wei Shuo,Gao Guanghua,DaGue Beverly B.,Palmier Mark O.,Bahudhanapati Harinath,Brew Keith

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference56 articles.

1. Matrix metalloproteinases: they're not just for matrix anymore!

2. Matrix metalloproteinases at a glance

3. Tissue inhibitors of metalloproteinases: evolution, structure and function

4. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

5. High Resolution Structure of the N-terminal Domain of Tissue Inhibitor of Metalloproteinases-2 and Characterization of Its Interaction Site with Matrix Metalloproteinase-3

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2. N-acetyltransferase and inflammation: Bridging an unexplored niche;Gene;2023-12

3. Unravelling the distinct biological functions and potential therapeutic applications of TIMP2 in cancer;Carcinogenesis;2022-04-18

4. Thermodynamic profiles of the interactions of suramin, chondroitin sulfate, and pentosan polysulfate with the inhibitory domain of TIMP ‐3;FEBS Letters;2019-09-13

5. Proteomic and genomic characterization of a yeast model for Ogden syndrome;Yeast;2016-12-06

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