A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p

Science

Volumn 272, Issue 5260, 1996, Pages 408-411

  Taunton, Jack ^a   Hassig, Christian A ^a   Schreiber, Stuart L ^a  

^a HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE;

ARTICLE; CELL CYCLE; DEACETYLATION; ENZYME ACTIVE SITE; LEUKEMIA CELL LINE; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; T LYMPHOCYTE; TRANSCRIPTION REGULATION; YEAST;

EID: 0029932598     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.272.5260.408     Document Type: Article

References (27)

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8. J Taunton, C. A. Hassig, S L. Schreiber, unpublished results.
9. 3H]trapoxin indicated that the radiolabel is released into solution after protein denaturation with SDS or guanidinium hydrochloride. Thus, trapoxin binding proteins were expected to elute from the affinity matrix with SDS (J Taunton, C. A. Hassig, S. L Schreiber, unpublished observations)
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27. 3H]trapoxin; W. S Lane and colleagues for unparalleled expertise in peptide microsequencing; J. A. Simon for help with molecular biology; K. L Morrison and L. F. Snow for help with polyclonal antibodies; and Y.-W. Qian and E. Y.-H. Lee for the RbAp48 monoclonal antibody. J.T. extends his gratitude to NSF and Eli Lilly and Co. for predoctoral fellowships. C.A.H. is supported by an NIH predoctoral training grant S L.S. is an investigator at the Howard Hughes Medical Institute