Please use this identifier to cite or link to this item: http://lib.jncasr.ac.in:8080/jspui/handle/10572/2083
Title: Aberrant lysine acetylation in tumorigenesis: Implications in the development of therapeutics
Authors: Kaypee, Stephanie
Sudarshan, Deepthi
Shanmugam, Muthu K.
Mukherjee, Debanjan
Sethi, Gautam
Kundu, Tapas Kumar
Keywords: Pharmacology & Pharmacy
Chromatin
Histones
Post-translational modification
Lysine acetylation
Lysine acetyltransferase
Epigenetic therapeutics
Nf-Kappa-B
Epithelial-Mesenchymal Transition
Acute Myeloid-Leukemia
Small-Molecule Inhibitor
Squamous-Cell Carcinoma
Histone Acetyltransferase Inhibitor
Creb-Binding-Protein
Cancer Stem-Cells
Transcription Factor Complex
P300/Cbp Associated Factor
Issue Date: 2016
Publisher: Pergamon-Elsevier Science Ltd
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
Pharmacology & therapeutics
162
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.
Description: Open Access (Accepted Manuscript)
URI: http://hdl.handle.net/10572/2083
ISSN: 0163-7258
Appears in Collections:Research Papers (Tapas K. Kundu)

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