A truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 function

Journal of Biological Chemistry

Volumn 284, Issue 45, 2009, Pages 30871-30880

  Woo, Sang Hyeok ^a,b   An, Sungkwan ^c   Lee, Hyung Chahn ^a   Jin, Hyeon Ok ^a   Seo, Sung Keum ^a   Yoo, Doo Hyun ^a   Lee, Kee Ho ^a   Rhee, Chang Hun ^a   Choi, Eui Ju ^b   Hong, Seok Il ^a   Park, In Chul ^a  

^a Korea Institute of Radiation and Medical Science   (South Korea)

^b Korea University   (South Korea)

^c Konkuk University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASES; CATALYTIC SUBUNITS; CHAPERONE PATHWAY; CIS-PLATIN; DOWN-REGULATION; IN-CELL; MUTATION ANALYSIS; OVER-EXPRESSION; SERINE PHOSPHORYLATION; SERINE RESIDUES; TELOMERASE; TELOMERASE ACTIVITY; UNDERLYING MECHANISM;

AMINO ACIDS; CELL DEATH; GROWTH KINETICS; PLATINUM COMPOUNDS;

PROTEINS;

CASPASE; CISPLATIN; HEAT SHOCK PROTEIN 90; MESSENGER RNA; PHOSPHOSERINE; PROTEIN P23; SERINE; TELOMERASE; TELOMERASE REVERSE TRANSCRIPTASE; TRUNCATED PROTEIN P23; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; CONTROLLED STUDY; DOWN REGULATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME STABILITY; GENE OVEREXPRESSION; GROWTH INHIBITION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEPLETION; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; SENSITIZATION;

CELL LINE; DNA-BINDING PROTEINS; DOWN-REGULATION; HSP90 HEAT-SHOCK PROTEINS; HUMANS; PHOSPHORYLATION; PROTEIN STABILITY; TELOMERASE;

EID: 71449083363     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.052720     Document Type: Article

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