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11/23/2015 2:56:00 PM | Browse: 582 | Download: 1872
Publication Name World Journal of Biological Chemistry
Manuscript ID 19088
Country United States
Received
2015-04-29 21:53
Peer-Review Started
2015-04-30 22:15
To Make the First Decision
2015-08-16 16:54
Return for Revision
2015-08-20 11:02
Revised
2015-09-01 00:47
Second Decision
2015-09-21 17:06
Accepted by Journal Editor-in-Chief
2015-09-21 20:45
Accepted by Company Editor-in-Chief
2015-09-30 18:16
Articles in Press
2015-09-30 18:16
Publication Fee Transferred
Edit the Manuscript by Language Editor
Typeset the Manuscript
2015-11-04 09:45
Publish the Manuscript Online
2015-11-23 10:19
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) 2015. Published by Baishideng Publishing Group Inc. All rights reserved.
Article Reprints For details, please visit: http://www.wjgnet.com/bpg/gerinfo/247
Permissions For details, please visit: http://www.wjgnet.com/bpg/gerinfo/207
Publisher Baishideng Publishing Group Inc, 7041 Koll Center Parkway, Suite 160, Pleasanton, CA 94566, USA
Website http://www.wjgnet.com
Category Biochemistry & Molecular Biology
Manuscript Type Basic Study
Article Title Disruption of NAD+ binding site in glyceraldehyde 3-phosphate dehydrogenase affects its intranuclear interactions
Manuscript Source Invited Manuscript
All Author List Manali Phadke, Natalia Krynetskaia, Anurag Mishra, Carlos Barrero, Salim Merali, Scott A Gothe and Evgeny Krynetskiy
Funding Agency and Grant Number
Funding Agency Grant Number
National Cancer Institute R01-CA104729
Jayne Haines Center for Pharmacogenomics and Drug Safety of Temple University School of Pharmacy and Temple University Summer Research Award to Evgeny Krynetskiy
Corresponding Author Evgeny Krynetskiy, PhD, DSc, Associate Professor, Temple University School of Pharmacy, 3307 North Broad Street, Philadelphia, PA 19140, United States. ekrynets@temple.edu
Key Words NAD+; Binding site; Fluorescence recovery after photobleaching; Nuclear proteins; Mutation; Glycer¬aldehyde 3-phosphate dehydrogenase; Anticancer agents
Core Tip We detected the phosphorylated amino acid residues Y94, S98, T99 within the NAD+ binding center of glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Substitution of these amino acids with non-phosphorylated alanine residues did not abrogate intranuclear localization of GAPDH. Instead, such mutations altered the molecular dynamics parameters of intranuclear GAPDH probably by hindering its interactions with yet to be identified nuclear biomolecules. Our molecular modeling experiments invoke an important structural feature -T99-E97 H-bond likely involved in stabilization of NAD+ binding center.
Publish Date 2015-11-23 10:19
Citation Phadke M, Krynetskaia N, Mishra A, Barrero C, Merali S, Gothe SA, Krynetskiy E. Disruption of NAD+ binding site in glyceraldehyde 3-phosphate dehydrogenase affects its intranuclear interactions. World J Biol Chem 2015; 6(4): 366-378
URL http://www.wjgnet.com/1949-8454/full/v6/i4/366.htm
DOI http://dx.doi.org/10.4331/wjbc.v6.i4.366
Full Article (PDF) WJBC-6-366.pdf
Full Article (Word) WJBC-6-366.doc
Manuscript File 19088-Review.docx
Answering Reviewers 19088-Answering reviewers.pdf
Audio Core Tip 19088-Audio core tip.mp3
Conflict-of-Interest Disclosure Form 19088-Conflict-of-interest statement.pdf
Copyright License Agreement 19088-Copyright assignment.pdf
Institutional Review Board Approval Form or Document 19088-Institutional review board statement.pdf
Peer-review Report 19088-Peer-review(s).pdf
Journal Editor-in-Chief Review Report 19088-Journal editor-in-chief review report.pdf
Scientific Misconduct Check 19088-Scientific misconduct check.pdf
Scientific Editor Work List 19088-Scientific editor work list.pdf