Functional crosstalk between histone H2B ubiquitylation and H2A modifications and variants

Nature Communications

Volumn 9, Issue 1, 2018, Pages

  Wojcik, Felix ^a   Dann, Geoffrey P ^a,c   Beh, Leslie Y ^a,b   Debelouchina, Galia T ^a,d   Hofmann, Raphael ^a,e   Muir, Tom W ^a  

^a PRINCETON UNIVERSITY   (United States)

^b Columbia University ^*  (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2A; HISTONE H2AZ; HISTONE H2B; HISTONE H2B AT LYSINE RESIDUE 120; UNCLASSIFIED DRUG; HISTONE; ISOPROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

AMINO ACID; CHEMICAL ALTERATION; ENZYME; GENOME; PROTEIN; SUBSTRATE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHROMATIN ASSEMBLY AND DISASSEMBLY; CONTROLLED STUDY; DNA BARCODING; DNA TEMPLATE; GENE EXPRESSION LEVEL; GENE LIBRARY; HISTONE ACETYLATION; HISTONE MODIFICATION; HISTONE UBIQUITINATION; HUMAN; HUMAN CELL; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; TRANSCRIPTION REGULATION; ALPHA HELIX; AMINO ACID SEQUENCE; BETA SHEET; BINDING SITE; CHEMISTRY; ENZYME SPECIFICITY; GENE EXPRESSION; GENETICS; HEK293 CELL LINE; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR MODEL; NUCLEOSOME; PROTEIN DOMAIN; PROTEIN PROCESSING; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; TRANSCRIPTION INITIATION; UBIQUITINATION;

AMINO ACID SEQUENCE; BINDING SITES; CHROMATIN ASSEMBLY AND DISASSEMBLY; CLONING, MOLECULAR; GENE EXPRESSION; HEK293 CELLS; HISTONES; HUMANS; KINETICS; MODELS, MOLECULAR; NUCLEOSOMES; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN ISOFORMS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TRANSCRIPTIONAL ACTIVATION; UBIQUITINATION;

EID: 85045402454     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/s41467-018-03895-5     Document Type: Article

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