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Structure of nucleosome-bound human BAF complex

Authors: Shuang He; Zihan Wu; Yuan Tian; Zishuo Yu; Jiali Yu; Xinxin Wang; Jie Li; +2 Authors

Structure of nucleosome-bound human BAF complex

Abstract

Architecture of human BAF complex The SWI/SNF family chromatin remodelers regulate chromatin and transcription. The protein complexes BAF and PBAF are mammalian SWI/SNF remodelers that play essential functions in diverse developmental and physiological processes. He et al. determined the structure of the human BAF complex, which contains three modules that bind the nucleosome on the top, bottom, and side, making this nucleosome-recognition pattern distinct from other chromatin remodelers. Mutations in BAF that are frequently associated with human cancer cluster into a nucleosome-interacting region. This structure provides a framework for understanding the BAF-mediated chromatin remodeling mechanism and its dysregulation in cancer. Science , this issue p. 875

Related Organizations
Keywords

Adenosine Triphosphatases, Protein Conformation, alpha-Helical, Chromosomal Proteins, Non-Histone, Hydrolysis, Cryoelectron Microscopy, DNA Helicases, Nuclear Proteins, SMARCB1 Protein, Chromatin Assembly and Disassembly, Nucleosomes, DNA-Binding Proteins, Adenosine Triphosphate, Neoplasms, Mutation, Humans, Transcription Factors

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Powered by OpenAIRE graph
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
280
Top 0.1%
Top 10%
Top 0.1%