Trypanosoma brucei 14-3-3I and II proteins predominantly form a heterodimer structure that acts as a potent cell cycle regulator in vivo

Journal of Biochemistry

Volumn 153, Issue 5, 2013, Pages 431-439

  Inoue, Masahiro ^a   Yasuda, Kouichi ^a   Uemura, Haruki ^b   Yasaka, Natsumi ^a   Schnaufer, Achim ^c   Yano, Mihiro ^d   Kido, Hiroshi ^d   Kohda, Daisuke ^e   Doi, Hirofumi ^f   Fukuma, Toshihide ^a   Tsuji, Akihiko ^d   Horikoshi, Nobuo ^g  

^a KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b NAGASAKI UNIVERSITY   (Japan)

^c UNIVERSITY OF EDINBURGH   (United Kingdom)

^d UNIVERSITY OF TOKUSHIMA   (Japan)

^e KYUSHU UNIVERSITY   (Japan)

^f Celestar Lexico Sciences Inc   (Japan)

^g UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

14 3 3; cell division; cytokinesis; dimerization; Trypanosoma brucei

Indexed keywords

EPITOPE; HETERODIMER; PROTEIN 14 3 3;

AMINO ACID SEQUENCE; ARTICLE; CELL CYCLE REGULATION; CELL PROLIFERATION; CONTROLLED STUDY; CYTOKINESIS; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VIVO STUDY; NATIVE POLYACRYLAMIDE GEL ELECTROPHORESIS; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN PURIFICATION; TRYPANOSOMA BRUCEI; WESTERN BLOTTING;

14-3-3 PROTEINS; CELL CYCLE; CYTOKINESIS; HUMANS; POLYMERASE CHAIN REACTION; PROTOZOAN PROTEINS; TRYPANOSOMA BRUCEI BRUCEI;

EID: 84877278778     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvt016     Document Type: Article

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