Dimer formation and conformational flexibility ensure cytoplasmic stability and nuclear accumulation of Elk-1

Nucleic Acids Research

Volumn 39, Issue 15, 2011, Pages 6390-6402

  Evans, Emma L ^a   Saxton, Janice ^a   Shelton, Samuel J ^a   Begitt, Andreas ^a   Holliday, Nicholas D ^a   Hipskind, Robert A ^b   Shaw, Peter E ^a  

^a QUEEN S MEDICAL CENTRE   (United Kingdom)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

MONOMER; PROTEASOME; TRANSCRIPTION FACTOR ELK 1; ATP DEPENDENT 26S PROTEASE; DNA;

ARTICLE; CELL NUCLEUS; CELLULAR DISTRIBUTION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOPLASM; DIMERIZATION; ETS DOMAIN; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; SERUM RESPONSE FACTOR INTERACTION DOMAIN; AMINO ACID SEQUENCE; CELL LINE; CHEMISTRY; GENE DELETION; METABOLISM; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; CELL LINE; CELL NUCLEUS; CYTOPLASM; DIMERIZATION; DNA; ETS-DOMAIN PROTEIN ELK-1; HUMANS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION;

EID: 80055076025     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr266     Document Type: Article

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