Citrullination regulates pluripotency and histone H1 binding to chromatin

Nature

Volumn 507, Issue 7490, 2014, Pages 104-108

  Christophorou, Maria A ^a   Castelo Branco, Gonçalo ^a,b   Halley Stott, Richard P ^a,c   Oliveira, Clara Slade ^a,c,d   Loos, Remco ^e   Radzisheuskaya, Aliaksandra ^c   Mowen, Kerri A ^f   Bertone, Paul ^c,e,g   Silva, José C R ^c   Zernicka Goetz, Magdalena ^a,c   Nielsen, Michael L ^h   Gurdon, John B ^a,c   Kouzarides, Tony ^a,c  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^d EMBRAPA CERRADOS   (Brazil)

^e WELLCOME TRUST SANGER INSTITUTE   (United Kingdom)

^f SCRIPPS RESEARCH INSTITUTE   (United States)

^g EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^h University of Copenhagen   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; DNA; HISTONE H1; PEPTIDYLARGININE DEIMINASE 4; PROTEIN ARGININE DEIMINASE; PROTEIN VARIANT; UNCLASSIFIED DRUG;

AMINO ACID; CANCER; CELL ORGANELLE; CHROMOSOME; EMBRYO; ENZYME ACTIVITY; HYDROGEN; IMMUNE RESPONSE; PHYSIOLOGY; PROTEIN;

ANIMAL CELL; ARTICLE; BINDING SITE; BLASTOCYST; CHROMATIN CONDENSATION; CITRULLINATION; CONTROLLED STUDY; DNA BINDING; EMBRYO; EMBRYO DEVELOPMENT; EMBRYONIC STEM CELL; ENZYME ACTIVITY; FLOW CYTOMETRY; FUNCTIONAL PROTEOMICS; GENE EXPRESSION; GENE ONTOLOGY; GENE REGULATORY NETWORK; GENETIC TRANSCRIPTION; MOUSE; MOUSE EMBRYO; NONHUMAN; NUCLEAR REPROGRAMMING; PLURIPOTENT STEM CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MODIFICATION;

VERTEBRATA;

ANIMALS; ARGININE; BINDING SITES; CHROMATIN; CHROMATIN ASSEMBLY AND DISASSEMBLY; CITRULLINE; DNA; EMBRYO, MAMMALIAN; GENE EXPRESSION REGULATION; HISTONES; HYDROLASES; MICE; NUCLEAR REPROGRAMMING; PLURIPOTENT STEM CELLS; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOMICS; SUBSTRATE SPECIFICITY; TRANSCRIPTION, GENETIC;

EID: 84895875371     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12942     Document Type: Article

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