John C. Shimko, Ph.D.

Affiliations: 
2011 Biochemistry Program, Ohio State Ohio State University, Columbus, Columbus, OH 
Area:
peptide and protein chemistry
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"John Shimko"
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Parents

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Jennifer J. Ottesen grad student 2011 Ohio State
 (Synthetic Tools for the Preparation of Modified Histones.)
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Publications

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Brehove M, Wang T, North J, et al. (2015) Histone Core Phosphorylation Regulates DNA Accessibility. The Journal of Biological Chemistry. 290: 22612-21
Howard CJ, Yu RR, Gardner ML, et al. (2015) Chemical and biological tools for the preparation of modified histone proteins. Topics in Current Chemistry. 363: 193-226
Shimko JC, Howard CJ, Poirier MG, et al. (2013) Preparing semisynthetic and fully synthetic histones h3 and h4 to modify the nucleosome core. Methods in Molecular Biology (Clifton, N.J.). 981: 177-92
North JA, Shimko JC, Javaid S, et al. (2012) Regulation of the nucleosome unwrapping rate controls DNA accessibility. Nucleic Acids Research. 40: 10215-27
Mahto SK, Howard CJ, Shimko JC, et al. (2011) A reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-Acylurea approach. Chembiochem : a European Journal of Chemical Biology. 12: 2488-94
Simon M, North JA, Shimko JC, et al. (2011) Histone fold modifications control nucleosome unwrapping and disassembly. Proceedings of the National Academy of Sciences of the United States of America. 108: 12711-6
Shimko JC, North JA, Bruns AN, et al. (2011) Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes. Journal of Molecular Biology. 408: 187-204
Mahto SK, Howard CJ, Shimko JC, et al. (2011) Corrigendum: A Reversible Protection Strategy To Improve Fmoc-SPPS of Peptide Thioesters by the N-Acylurea Approach Chembiochem. 12: 2386-2386
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