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Aberrant lysine acetylation in tumorigenesis: Implications in the development of therapeutics

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dc.contributor.author Kaypee, Stephanie
dc.contributor.author Sudarshan, Deepthi
dc.contributor.author Shanmugam, Muthu K.
dc.contributor.author Mukherjee, Debanjan
dc.contributor.author Sethi, Gautam
dc.contributor.author Kundu, Tapas Kumar
dc.date.accessioned 2017-01-24T06:20:41Z
dc.date.available 2017-01-24T06:20:41Z
dc.date.issued 2016
dc.identifier.citation Kaypee, S.; Sudarshan, D.; Shanmugam, M. K.; Mukherjee, D.; Sethi, G.; Kundu, T. K., Aberrant lysine acetylation in tumorigenesis: Implications in the development of therapeutics. Pharmacology & Therapeutics 2016, 162, 98-119 http://dx.doi.org/10.1016/j.pharmthera.2016.01.011 en_US
dc.identifier.citation Pharmacology & therapeutics en_US
dc.identifier.citation 162 en_US
dc.identifier.issn 0163-7258
dc.identifier.uri https://libjncir.jncasr.ac.in/xmlui/10572/2083
dc.description Open Access (Accepted Manuscript) en_US
dc.description.abstract The 'language' of covalent histone modifications translates environmental and cellular cues into gene expression. This vast array of post-translational modifications on histones are more than just covalent moieties added onto a protein, as they also form a platform on which crucial cellular signals are relayed. The reversible lysine acetylation has emerged as an important post-translational modification of both histone and non-histone proteins, dictating numerous epigenetic programs within a cell. Thus, understanding the complex biology of lysine acetylation and its regulators is essential for the development of epigenetic therapeutics. In this review, we will attempt to address the complexities of lysine acetylation in the context of tumorigenesis, their role in cancer progression and emphasize on the modalities developed to target lysine acetyltransferases towards cancer treatment. (C) 2016 Elsevier Inc. All rights reserved. en_US
dc.description.uri http://dx.doi.org/10.1016/j.pharmthera.2016.01.011 en_US
dc.language.iso English en_US
dc.publisher Pergamon-Elsevier Science Ltd en_US
dc.rights @Pergamon-Elsevier Science Ltd, 2016 en_US
dc.subject Pharmacology & Pharmacy en_US
dc.subject Chromatin en_US
dc.subject Histones en_US
dc.subject Post-translational modification en_US
dc.subject Lysine acetylation en_US
dc.subject Lysine acetyltransferase en_US
dc.subject Epigenetic therapeutics en_US
dc.subject Nf-Kappa-B en_US
dc.subject Epithelial-Mesenchymal Transition en_US
dc.subject Acute Myeloid-Leukemia en_US
dc.subject Small-Molecule Inhibitor en_US
dc.subject Squamous-Cell Carcinoma en_US
dc.subject Histone Acetyltransferase Inhibitor en_US
dc.subject Creb-Binding-Protein en_US
dc.subject Cancer Stem-Cells en_US
dc.subject Transcription Factor Complex en_US
dc.subject P300/Cbp Associated Factor en_US
dc.title Aberrant lysine acetylation in tumorigenesis: Implications in the development of therapeutics en_US
dc.type Review en_US


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