TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members

PLoS ONE

Volumn 7, Issue 5, 2012, Pages

  Bell, Jessica L ^a   Malyukova, Alena ^a   Holien, Jessica K ^b   Koach, Jessica ^a   Parker, Michael W ^b,c   Kavallaris, Maria ^a   Marshall, Glenn M ^a,d   Cheung, Belamy B ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b ST VINCENT'S INSTITUTE OF MEDICAL RESEARCH   (Australia)

^c UNIVERSITY OF MELBOURNE   (Australia)

^d SYDNEY CHILDREN'S HOSPITAL   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

HETERODIMER; HOMODIMER; MIDLINE 1 PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; TRIPARTITE MOTIF PROTEIN 16; TRIPARTITE MOTIF PROTEIN 24; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

ARTICLE; DIMERIZATION; EMBRYO; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR MODEL; PROTEIN DOMAIN; PROTEIN FUNCTION; RING FINGER MOTIF; UBIQUITINATION;

CELL LINE; CELLS, CULTURED; DNA-BINDING PROTEINS; HUMANS; MICROTUBULE PROTEINS; MODELS, MOLECULAR; NUCLEAR PROTEINS; PROTEIN STRUCTURE, TERTIARY; TRANSCRIPTION FACTORS; TRANSFECTION; TUMOR SUPPRESSOR PROTEINS; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

EID: 84861323733     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0037470     Document Type: Article

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