Multivalent engagement of chromatin modifications by linked binding modules

By Alexander J. Ruthenburg, Haitao Li, Dinshaw J. Patel, C. D. Allis. Nature reviews. Molecular cell biology, 2007

1,054 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/43c372a6dc5fc30bd96a1433cbc789a0dde07343

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Citations in the corpus

Enhancer function: new insights into the regulation of tissue-specific gene expression (2011, positive): “Chromatin features of enhancers The distribution of post-translational histone modifications and the presence of specific histone variants influence gene expression by orchestrating the interaction of transcription factors with the chromatin fibr”
Histone Modifications and Cancer. (2016, background): “Although single marks have been generalized as activating (e.g., H3K9ac, H3K4me3) or repressive (H3K9me3, H3K27me3) (Ruthenburg et al. 2007; Zhu et al. 2013), it is clear that certain PTMs can affect the ability of other marks to either be put down or read (more extensively reviewed by Ruthenburg…”
Chromatin Structure and the Inheritance of Epigenetic Information (2010, background): “Moreover, the discovery of protein domains — including chromodomains, bromodomains, plant homeodomains (PHDs), tudor domains and malignant brain tumour (MBT) domains — that specifically recognize a defined histone modification have advanced our understanding of the role of histone PTM”
Lysine acetylation: codified crosstalk with other posttranslational modifications (2008, background): “To understand how acetylation might crosstalk with other PTMs, we consider the protein modification code, a concept similar to the hotly debated ‘‘histone code’’ (Ruthenburg et al., 2007).”
The many roles of histone deacetylases in development and physiology: implications for disease and therapy (2009, background): “Conversely, histone deacetylation favours transcriptional repression by allowing for chromatin compactio”
Interpreting thelanguage of histone and DNA modifications (2014, background): “This offers a diverse and exciting potential for multivalent histone engagement [98] (Fig.”
Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain Family (2012, background): “The presence of multiple reader modules in chromatin modification complexes led to the proposal that distinct epigenetic signatures are interpreted by a multivalent reading process that engages diverse binding modules (Ruthenburg et al., 2007).”
The age of crosstalk: phosphorylation, ubiquitination, and beyond. (2007, background): “A recent structure of the BTPF PHD domain bound to an H3K4me3 peptide demonstrates how the adjacent bromodomain could in principle bind simultaneously to H3K4me3 and H4K16ac in the same nucleosome (Li et al., 2006; Ruthenburg et al., 2007 ).”
Nucleosome-Interacting Proteins Regulated by DNA and Histone Methylation (2010, background): “…three-dimensional organization of chromatin in the nucleus, DNA methylation and histone modifications most likely act in a concerted manner by creating a ‘‘modification landscape’’ that must be interpreted by proteins that are able to recognize large molecular assemblies (Ruthenburg et al., 2007).”
Global Quantitative Modeling of Chromatin Factor Interactions (2014, background): “Many complex interactions cannot be accurately captured by pair-wise interactions, such as cooperative multivalent binding or inhibition of binding between histone mark and reader protein by other marks [3,17].”
Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification (2011, background): “…histone methylation, acetylation, 1016 Cell 146, 1016–1028, September 16, 2011 ª2011 Elsevier Inc. propionylation, butyrylation, formylation, phosphorylation, ubiquitylation, sumoylation, citrullination, proline isomerization, and ADP ribosylation (Martin and Zhang, 2007; Ruthenburg et al., 2007).”