The “readers” of unacetylated p53 represent a new class of acidic domain proteins

Nucleus

Volumn 8, Issue 4, 2017, Pages 360-369

  Wang, Donglai ^a   Kon, Ning ^a   Tavana, Omid ^a   Gu, Wei ^a  

^a Columbia University ^*  (United States)

Author keywords

acetylation; acidic domain; C terminal domain; p53; SET

Indexed keywords

AMINO ACID; ASPARTIC ACID; GLUTAMIC ACID; GST FUSION PROTEIN; HYBRID PROTEIN; LYSINE ACETYLTRANSFERASE; LYSINE DEACETYLASE; PROTEIN MDM2; PROTEIN P53; TRANSACTIVATION DOMAIN; TRANSCRIPTION FACTOR FKHR; UNCLASSIFIED DRUG;

ACIDIC AMINO ACID CONTAINING DOMAIN; AMINO ACID COMPOSITION; BINDING ASSAY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DNA DAMAGE; EPIGENETICS; IN VITRO BINDING ASSAY; MOLECULAR CLONING; NONHUMAN; NOTE; POINT MUTATION; PROTEIN ACETYLATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; REGULATORY SEQUENCE; SITE DIRECTED MUTAGENESIS; WESTERN BLOTTING; ACETYLATION; AMINO ACID SEQUENCE; BIOLOGY; CHEMISTRY; HUMAN; METABOLISM; PROTEIN DOMAIN;

ACETYLATION; AMINO ACID SEQUENCE; AMINO ACIDS, ACIDIC; BLOTTING, WESTERN; COMPUTATIONAL BIOLOGY; HUMANS; PROTEIN DOMAINS; TUMOR SUPPRESSOR PROTEIN P53;

EID: 85018185111     PISSN: 19491034     EISSN: 19491042     Source Type: Journal    
DOI: 10.1080/19491034.2017.1313939     Document Type: Note

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