Publication Name	World Journal of Biological Chemistry
Manuscript ID	20410
Country	United States

Received	2015-06-03 17:22
Peer-Review Started	2015-06-04 11:30
First Decision by Editorial Office Director
Return for Revision	2015-07-12 14:58
Revised	2016-02-19 00:00
Publication Fee Transferred
Second Decision by Editor	2016-02-29 09:29
Second Decision by Editor-in-Chief	2016-02-29 09:31
Final Decision by Editorial Office Director	2016-03-14 11:46
Articles in Press	2016-03-14 11:46
Edit the Manuscript by Language Editor
Typeset the Manuscript	2016-05-10 15:18
Publish the Manuscript Online	2016-05-17 17:31

ISSN	1949-8454 (online)
Open Access	This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Copyright	© The Author(s) 2016. Published by Baishideng Publishing Group Inc. All rights reserved.
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Category	Biochemistry & Molecular Biology
Manuscript Type	Review
Article Title	High mobility group protein 1: A collaborator in nucleosome dynamics and estrogen-responsive gene expression
Manuscript Source	Invited Manuscript
All Author List	William M Scovell
Funding Agency and Grant Number	Funding Agency Grant Number National Institutes of Health GM054357-04
Corresponding Author	William M Scovell, Emeritus Professor, Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403, United States. wscovel@bgsu.edu
Key Words	Nucleosome dynamics; Estrogen receptor; High mobility group protein 1; Conformational dynamics; Energy landscape
Core Tip	Response elements or target sites for transcrip-tion factors in DNA are often found veiled within a nucleosome in a chromatin milieu and in many cases are not accessible. Although the nucleosome/chromatin network is generally repressive to transcription, there are now a number of enzymatic strategies that have now been recognized that remodel the nucleosome to facilitate transcription factor access. We recently showed that estrogen receptor does not bind to a canonical nucleosome. However, we have discovered that high mobility group protein 1 (HMGB1) restructures the nucleosome in a nonenzymatic manner to facilitate strong estrogen receptor binding. This review will provide background for this work and outline our findings, characterize the HMGB1-restructured nucleo-somes and propose a working model to account for the HMGB1 restructuring activity.
Publish Date	2016-05-17 17:31
Citation	Scovell WM. High mobility group protein 1: A collaborator in nucleosome dynamics and estrogen-responsive gene expression. World J Biol Chem 2016; 7(2): 206-222
URL	http://www.wjgnet.com/1949-8454/full/v7/i2/206.htm
DOI	http://dx.doi.org/10.4331/wjbc.v7.i2.206

Full Article (PDF)	WJBC-7-206.pdf
Full Article (Word)	WJBC-7-206.doc
Manuscript File	20410-Review.docx
Answering Reviewers	20410-Answering reviewers.pdf
Audio Core Tip	20410-Audio core tip.mp3
Conflict-of-Interest Disclosure Form	20410-Conflict-of-interest statement.pdf
Copyright License Agreement	20410-Copyright assignment.pdf
Peer-review Report	20410-Peer-review(s).pdf
Journal Editor-in-Chief Review Report	20410-Journal editor-in-chief review report.pdf
Scientific Misconduct Check	20410-Scientific misconduct check.pdf
Scientific Editor Work List	20410-Scientific editor work list.pdf