Molecular dynamics simulations of wild type and mutant of Pin1 peptidyl-prolyl isomerase-Reference-Cited by-同舟云学术

Molecular dynamics simulations of wild type and mutant of Pin1 peptidyl-prolyl isomerase

Published:2016-06-29 Issue:15 Volume:42 Page:1281-1291
ISSN:0892-7022
Container-title:Molecular Simulation
language:en
Short-container-title:Molecular Simulation

Author:

Chang Shan¹,Kong Ren¹,Wang Li-qin²,Shi Hang³,Piao Lian-hua¹

Affiliation:

1. School of Electrical and Information Engineering, Institute of Bioinformatics and Medical Engineering, Jiangsu University of Technology, Changzhou, P.R. China

2. Changzhou College of Information Technology, Changzhou, P.R. China

3. School of Computer Science & Engineering, Jiangsu University of Technology, Changzhou, P.R. China

Funder

National Natural Science Foundation of China

Special Program for Applied Research on Super Computation of the NSFC-Guangdong Joint Fund

Foundation for Outstanding Young Teachers in Higher Education of Guangdong

Publisher

Informa UK Limited

Subject

Condensed Matter Physics,General Materials Science,General Chemical Engineering,Modelling and Simulation,Information Systems,General Chemistry

Link

https://www.tandfonline.com/doi/pdf/10.1080/08927022.2016.1185791

Reference42 articles.

1. The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease

2. Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins

3. Prolyl cis/trans isomerase signalling pathways in cancer

4. Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases

5. Prolyl cis-trans isomerization as a molecular timer

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