Unbinding of Kinesin from Microtubule in the Strongly Bound States Enhances under Assisting Forces-Reference-Cited by-同舟云学术

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Unbinding of Kinesin from Microtubule in the Strongly Bound States Enhances under Assisting Forces

Published:2017-11-07 Issue:4 Volume:37 Page:1700092
ISSN:1868-1743
Container-title:Molecular Informatics
language:en
Short-container-title:Mol. Inf.

Author:

Khataee Hamidreza¹,Naseri Solmaz²,Zhong Yongmin³,Liew Alan Wee-Chung¹

Affiliation:

1. School of Information and Communication Technology; Griffith University; 4222 QLD Australia

2. Department of Chemical and Petroleum Engineering; Sharif University of Technology; Tehran 11365-11155 Iran

3. School of Engineering; RMIT University, Bundoora Campus; 3083 VIC Australia

Funder

Griffith University

Publisher

Wiley

Subject

Organic Chemistry,Computer Science Applications,Drug Discovery,Molecular Medicine,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/minf.201700092/fullpdf

Reference46 articles.

1. Movement of microtubules by single kinesin molecules

2. Kinesin Walks Hand-Over-Hand

3. A universal pathway for kinesin stepping

4. Mechanics of the kinesin step

5. Chemomechanical coupling of the forward and backward steps of single kinesin molecules

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Processivity of molecular motors under vectorial loads;Physical Review E;2020-08-18

2. Processivity of molecular motors under vectorial loads;2020-04-14

3. Force Generated by Two Kinesin Motors Depends on the Load Direction and Intermolecular Coupling;Physical Review Letters;2019-05-08

4. Crowding and Pausing Strongly Affect Dynamics of Kinesin-1 Motors along Microtubules;Biophysical Journal;2018-09

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