Literature DB >> 24449612

Mind the methyl: methyllysine binding proteins in epigenetic regulation.

Tobias Wagner1, Dina Robaa, Wolfgang Sippl, Manfred Jung.   

Abstract

Epigenetics is defined as the phenomenon of heritable phenotypic traits that are not governed by alteration of the genetic code. Major epigenetic control mechanisms include DNA methylation and post-translational modifications of histones, such as reversible histone acetylation and methylation of lysine residues. Methyllysine binding proteins recognize various levels of lysine methylation and mediate the signaling events that are induced by histone methylation. Therefore, they are also referred to as readers of the epigenetic code. In this article we review the current literature on the structure and biology of methyllysine binding proteins, especially with regard to their potential as drug targets. We also present the available inhibitors that block the interaction of methylated histones with their binding proteins.
© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

Keywords:  X-ray crystallography; epigenetics; histone readers; methyllysine; virtual screening

Mesh:

Substances:

Year:  2014        PMID: 24449612     DOI: 10.1002/cmdc.201300422

Source DB:  PubMed          Journal:  ChemMedChem        ISSN: 1860-7179            Impact factor:   3.466


  18 in total

Review 1.  The upstreams and downstreams of H3K79 methylation by DOT1L.

Authors:  Hanneke Vlaming; Fred van Leeuwen
Journal:  Chromosoma       Date:  2016-01-04       Impact factor: 4.316

Review 2.  Epigenetic regulation of epithelial-mesenchymal transition.

Authors:  Lidong Sun; Jia Fang
Journal:  Cell Mol Life Sci       Date:  2016-07-08       Impact factor: 9.261

Review 3.  Cellular analysis of the action of epigenetic drugs and probes.

Authors:  Mirjam Hau; Fides Zenk; A Ganesan; Nicola Iovino; Manfred Jung
Journal:  Epigenetics       Date:  2017-01-10       Impact factor: 4.528

4.  TIRR regulates 53BP1 by masking its histone methyl-lysine binding function.

Authors:  Pascal Drané; Marie-Eve Brault; Gaofeng Cui; Khyati Meghani; Shweta Chaubey; Alexandre Detappe; Nishita Parnandi; Yizhou He; Xiao-Feng Zheng; Maria Victoria Botuyan; Alkmini Kalousi; William T Yewdell; Christian Münch; J Wade Harper; Jayanta Chaudhuri; Evi Soutoglou; Georges Mer; Dipanjan Chowdhury
Journal:  Nature       Date:  2017-02-27       Impact factor: 49.962

5.  Regulation of Methyllysine Readers through Phosphorylation.

Authors:  Forest H Andrews; Jovylyn Gatchalian; Krzysztof Krajewski; Brian D Strahl; Tatiana G Kutateladze
Journal:  ACS Chem Biol       Date:  2016-01-06       Impact factor: 5.100

6.  Identification of a small-molecule ligand of the epigenetic reader protein Spindlin1 via a versatile screening platform.

Authors:  Tobias Wagner; Holger Greschik; Teresa Burgahn; Karin Schmidtkunz; Anne-Kathrin Schott; Joel McMillan; Lina Baranauskienė; Yan Xiong; Oleg Fedorov; Jian Jin; Udo Oppermann; Daumantas Matulis; Roland Schüle; Manfred Jung
Journal:  Nucleic Acids Res       Date:  2016-02-17       Impact factor: 16.971

Review 7.  Towards understanding methyllysine readout.

Authors:  Catherine A Musselman; Sepideh Khorasanizadeh; Tatiana G Kutateladze
Journal:  Biochim Biophys Acta       Date:  2014-04-13

Review 8.  Synthesis of lysine methyltransferase inhibitors.

Authors:  Chunngai Hui; Tao Ye
Journal:  Front Chem       Date:  2015-07-23       Impact factor: 5.221

Review 9.  Targeting histone methyltransferases and demethylases in clinical trials for cancer therapy.

Authors:  Ludovica Morera; Michael Lübbert; Manfred Jung
Journal:  Clin Epigenetics       Date:  2016-05-24       Impact factor: 6.551

10.  Polycomb Paralog Chromodomain Inhibitors Active against Both CBX6 and CBX8*.

Authors:  Natalia Milosevich; Chelsea R Wilson; Tyler M Brown; Aktan Alpsoy; Sijie Wang; Katelyn E Connelly; Kirsten A D Sinclair; Felino R Ponio; Rebecca Hof; Emily C Dykhuizen; Fraser Hof
Journal:  ChemMedChem       Date:  2021-07-23       Impact factor: 3.540

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.