Disulfide engineering of human Kunitz-type serine protease inhibitors enhances proteolytic stability and target affinity toward mesotrypsin-Reference-Cited by-同舟云学术

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Disulfide engineering of human Kunitz-type serine protease inhibitors enhances proteolytic stability and target affinity toward mesotrypsin

Published:2019-03 Issue:13 Volume:294 Page:5105-5120
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cohen Itay,Coban Matt,Shahar Anat,Sankaran Banumathi,Hockla Alexandra,Lacham Shiran,Caulfield Thomas R.,Radisky Evette S.^ORCID,Papo Niv^ORCID

Funder

European Research Council

Prostate Cancer Foundation

Israel Science Foundation

DKFZ-MOST

National Institutes of Health

United States-Israel Binational Science Foundation

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference69 articles.

1. Disulphide bridges in globular proteins;Thornton;J. Mol. Biol,1981

2. Disulfide bond formation and its impact on the biological activity and stability of recombinant therapeutic proteins produced by Escherichia coli expression system;Zhang;Biotechnol. Adv,2011

3. Protein folding guides disulfide bond formation;Qin;Proc. Natl. Acad. Sci. U.S.A,2015

4. Protein degradation and protection against misfolded or damaged proteins;Goldberg;Nature,2003

5. Protein disulfide engineering;Dombkowski;FEBS Lett,2014

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