Discovery of Amino Acid Motifs for Thrombin Cleavage and Validation Using a Model Substrate-Reference-Cited by-同舟云学术

Discovery of Amino Acid Motifs for Thrombin Cleavage and Validation Using a Model Substrate

Published:2011-11-11 Issue:48 Volume:50 Page:10499-10507
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ng Natasha M.¹,Pierce James D.²,Webb Geoffrey I.³,Ratnikov Boris I.²,Wijeyewickrema Lakshmi C.¹,Duncan Renee C.¹,Robertson Amy L.¹,Bottomley Stephen P.¹,Boyd Sarah E.⁴,Pike Robert N.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia

2. Sanford-Burnham Medical Research Institute, La Jolla, California 92037-1062, United States

3. Clayton School of Information Technology, Monash University, Clayton, Victoria 3800, Australia

4. School of Mathematical Sciences, Monash University, Clayton, Victoria 3800, Australia

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi201333g

Reference31 articles.

1. A player of many parts: The spotlight falls on thrombin's structure

2. NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation

3. Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C.

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1. High throughput protease profiling comprehensively defines active site specificity for thrombin and ADAMTS13;Scientific Reports;2018-02-12

2. Protein unfolding is essential for cleavage within the α-helix of a model protein substrate by the serine protease, thrombin;Biochimie;2016-03

3. Substrate-Driven Mapping of the Degradome by Comparison of Sequence Logos;PLoS Computational Biology;2013-11-14