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Volumn 6, Issue 5, 2000, Pages 1195-1205

Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME A; HISTONE ACETYLTRANSFERASE; HISTONE H1;

EID: 0033635283     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)00116-7     Document Type: Article
Times cited : (146)

References (58)
  • 1
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    • Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila
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    • Akhtar, A.1    Becker, P.B.2
  • 20
    • 0033010021 scopus 로고    scopus 로고
    • Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 angstrom resolution suggests a catalytic mechanism
    • (1999) Mol. Cell , vol.3 , pp. 23-32
    • Hickman, A.B.1    Klein, D.C.2    Dyda, F.3
  • 23
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2
  • 40
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • (1994) Proteins , vol.19 , pp. 277-290
    • Rice, L.M.1    Brunger, A.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.