It takes a PHD to read the histone code. by Mellor, J

“…The pattern of histone modifications, called the histone code, influences transitions between chromatin states and the regulation of transcriptional activity. …”

Cracking the histone code: Developing inhibitors of bromodomain-acetyl-lysine interactions by Conway, S

Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase. by Yue, W, Hassler, M, Roe, S, Thompson-Vale, V, Pearl, L

“…Together with the absence of specificity subsites in the structure, this suggests an electrostatic sensing mechanism for communicating the modification status of vicinal residues as part of the syntax of the 'histone code.'…”

Bromodomain-peptide displacement assays for interactome mapping and inhibitor discovery. by Philpott, M, Yang, J, Tumber, T, Fedorov, O, Uttarkar, S, Filippakopoulos, P, Picaud, S, Keates, T, Felletar, I, Ciulli, A, Knapp, S, Heightman, T

“…Bromodomains, found in histone acetyl transferases and other chromatin-associated proteins, bind selectively to acetylated lysines, acting as "readers" of the histone code, and have recently been shown to contain a druggable binding pocket. …”

Bromodomain-peptide displacement assays for interactome mapping and inhibitor discovery. by Philpott, M, Yang, J, Tumber, T, Fedorov, O, Uttarkar, S, Filippakopoulos, P, Picaud, S, Keates, T, Felletar, I, Ciulli, A, Knapp, S, Heightman, T

“…Bromodomains, found in histone acetyl transferases and other chromatin-associated proteins, bind selectively to acetylated lysines, acting as "readers" of the histone code, and have recently been shown to contain a druggable binding pocket. …”

Dynamic nucleosomes and gene transcription. by Mellor, J

“…Here, new concepts such as dynamic nucleosomes and a dynamic histone code in gene transcription are explored.…”

Introduction by Mellor, J

“…There are three main components to the epigenetic code: (i) methylated cytosine residues in DNA1; (ii) the range of post-translational modifications to the core histone proteins within the nucleosomes (referred to as the histone code)2,3; and (iii) RNA molecules, often non-coding RNA4. © 2010 The Biochemical Society.…”

Role of hypoxia-inducible factors in epigenetic regulation via histone demethylases. by Yang, J, Ledaki, I, Turley, H, Gatter, K, Montero, J, Li, J, Harris, A

“…These various covalent modifications have been proposed to constitute a "histone code," playing important roles in the establishment of global chromatin environments, transcription, DNA repair, and DNA replication. …”

ChromoHub: a data hub for navigators of chromatin-mediated signalling. by Liu, L, Zhen, X, Denton, E, Marsden, B, Schapira, M

“…UNLABELLED: The rapidly increasing research activity focused on chromatin-mediated regulation of epigenetic mechanisms is generating waves of data on writers, readers and erasers of the histone code, such as protein methyltransferases, bromodomains or histone deacetylases. …”

Interplay of histone marks with serine ADP-ribosylation by Bartlett, E, Bonfiglio, J, Prokhorova, E, Colby, T, Zobel, F, Ahel, I, Matic, I

“…Our findings implicate Ser-ADPr as a dynamic addition to the complex interplay of modifications that shape the histone code.…”

Mechanism of biomolecular recognition of trimethyllysine by the fluorinated aromatic cage of KDM5A PHD3 finger by Pieters, BJGE, Wuts, MHM, Poater, J, Kumar, K, White, PB, Kamps, JJAG, Sherman, W, Pruijn, GJM, Paton, RS, Beuming, T, Bickelhaupt, FM, Mecinovic, J

“…The understanding of biomolecular recognition of posttranslationally modified histone proteins is centrally important to the histone code hypothesis. Despite extensive binding and structural studies on the readout of histones, the molecular language by which posttranslational modifications on histone proteins are read remains poorly understood. …”

Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin. by Eustermann, S, Yang, J, Law, M, Amos, R, Chapman, L, Jelinska, C, Garrick, D, Clynes, D, Gibbons, R, Rhodes, D, Higgs, D, Neuhaus, D

“…The cooperation of ATRX ADD domain and HP1 in chromatin recruitment results in a tripartite interaction that may span neighboring nucleosomes and illustrates how the 'histone-code' is interpreted by a combination of multivalent effector-chromatin interactions.…”

Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin by Eustermann, S, Yang, J, Law, M, Amos, R, Chapman, L, Jelinska, C, Garrick, D, Clynes, D, Gibbons, R, Rhodes, D, Higgs, DR, Neuhaus, D

“…The cooperation of ATRX ADD domain and HP1 in chromatin recruitment results in a tripartite interaction that may span neighboring nucleosomes and illustrates how the 'histone-code' is interpreted by a combination of multivalent effector-chromatin interactions. © 2011 Nature America, Inc. …”

Regulation of RCC1 and its roles in apoptosis. by Li, Hoi Yeung.

“…Therefore, we propose that RCC1 reads the histone code created by caspaseactivated Mst1 to initiate apoptosis by reducing the level of RanGTP in the nucleus. …”
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A homogeneous method for investigation of methylation-dependent protein-protein interactions in epigenetics. by Quinn, A, Bedford, M, Espejo, A, Spannhoff, A, Austin, C, Oppermann, U, Simeonov, A

“…The interplay among methylation states and other histone modifications to direct transcriptional outcome is referred to as the histone code. In addition to histone methyltransferases and demethylases which function to modify the methylation state of lysine sidechains, other proteins recognize specific histone methylation marks essentially serving as code readers. …”

A chemical probe for Tudor domain protein spindlin1 to investigate chromatin function by Fagan, V, Johansson, C, Gileadi, C, Monteiro, O, Dunford, J, Nibhani, R, Philpott, M, Malzahn, J, Wells, G, Farham, R, Cribbs, A, Halidi, N, Li, F, Chau, I, Greschik, H, Velupillai, S, Allali-Hassani, A, Bennett, J, Christott, T, Giroud, C, Lewis, A, Huber, K, Athanasou, N, Bountra, C, Jung, M, Schüle, R, Vedadi, M, Arrowsmith, C, Xiong, Y, Jin, J, Fedorov, O, Farnie, G, Brennan, P, Oppermann, U

“…Modifications of histone tails, including lysine/arginine methylation, provide the basis of a “chromatin or histone code”. Proteins that contain “reader” domains can bind to these modifications and form specific effector complexes, which ultimately mediate chromatin function. …”

A homogeneous method for investigation of methylation-dependent protein-protein interactions in epigenetics. by Quinn, A, Bedford, M, Espejo, A, Spannhoff, A, Austin, C, Oppermann, U, Simeonov, A

“…The interplay among methylation states and other histone modifications to direct transcriptional outcome is referred to as the histone code. In addition to histone methyltransferases and demethylases which function to modify the methylation state of lysine sidechains, other proteins recognize specific histone methylation marks essentially serving as code readers. …”

A homogeneous method for investigation of methylation-dependent protein-protein interactions in epigenetics. by Quinn, A, Bedford, M, Espejo, A, Spannhoff, A, Austin, C, Oppermann, U, Simeonov, A

“…The interplay among methylation states and other histone modifications to direct transcriptional outcome is referred to as the histone code. In addition to histone methyltransferases and demethylases which function to modify the methylation state of lysine sidechains, other proteins recognize specific histone methylation marks essentially serving as code readers. …”

Systems modeling and network inference for genetic and epigenetic regulation of gene expression by Chen, Haifen

“…Our results bring new support for the hypothesis of “histone code”, and provide insight into the study of epigenetic regulatory mechanisms of transcription as well as other biological processes. …”
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Developing small molecule ligands for the study of bromodomain-histone interactions by Brand, M

“…<p>Dynamic changes in DNA methylation, and post-translational modifications on histone proteins which DNA wraps around, form the basis of epigenetic transfer of information. The histone code refers to different combinations of epigenetic marks, each mediating transcription in a specific manner. …”