Protein Disorder Is Positively Correlated with Gene Expression in Escherichia coli-Reference-Cited by-同舟云学术

Protein Disorder Is Positively Correlated with Gene Expression in Escherichia coli

Published:2008-05-09 Issue:6 Volume:7 Page:2234-2245
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Paliy Oleg¹,Gargac Shawn M.¹,Cheng Yugong¹,Uversky Vladimir N.¹,Dunker A. Keith¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, Wright State University, Dayton, Ohio 45435, Center for Computational Biology and Bioinformatics and Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, and Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/pr800055r

Reference124 articles.

1. Intrinsically disordered protein

2. p27 binds cyclin–CDK complexes through a sequential mechanism involving binding-induced protein folding

3. Coupling of Local Folding to Site-Specific Binding of Proteins to DNA

4. Disordered RNA chaperone proteins: from functions to disease

5. The role of structural disorder in the function of RNA and protein chaperones

Cited by 31 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. Proteome-wide landscape of solubility limits in a bacterial cell;Scientific Reports;2022-04-21

2. Proteome-wide landscape of solubility limits in a bacterial cell;2021-10-07

3. Tyrosine phosphorylation-dependent localization of TmaR that controls activity of a major bacterial sugar regulator by polar sequestration;Proceedings of the National Academy of Sciences;2020-12-29

4. Exploring Potential Signals of Selection for Disordered Residues in Prokaryotic and Eukaryotic Proteins;Genomics, Proteomics & Bioinformatics;2020-10

5. Tyrosine phosphorylation-dependent localization of TmaR, a novel E. coli polar protein that controls activity of the major sugar regulator by polar sequestration;2020-08-02