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Volumn 311, Issue 5, 2001, Pages 951-956

The primase active site is on the outside of the hexameric bacteriophage T7 gene 4 helicase-primase ring

Author keywords

Electron microscopy; Image analysis; Molecular modeling; Protein DNA complexes; Ring proteins

Indexed keywords

DNA POLYMERASE; DNA PRIMASE; DOUBLE STRANDED DNA; HELICASE; OLIGORIBONUCLEOTIDE; PROTEIN; RNA; RNA POLYMERASE; THYMIDINE TRIPHOSPHATE;

EID: 0035979798     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4932     Document Type: Article
Times cited : (28)

References (35)
  • 3
    • 0024288950 scopus 로고
    • Purification of the 56-kDa component of the bacteriophage T7 primase/helicase and characterization of its nucleoside 5′-triphosphatase activity
    • (1988) J. Biol. Chem. , vol.263 , pp. 14891-14899
    • Bernstein, J.A.1    Richardson, C.C.2
  • 8
    • 0031465797 scopus 로고    scopus 로고
    • Asymmetric interactions of hexameric bacteriophage T7 DNA helicase with the 5′- and 3′-tails of the forked DNA substrate
    • (1997) J. Biol. Chem. , vol.272 , pp. 32267-32273
    • Ahnert, P.1    Patel, S.S.2
  • 16
    • 0023039220 scopus 로고
    • Interactions of the DNA polymerase and gene 4 protein of bacteriophage T7. Protein-protein and protein-DNA interactions involved in RNA-primed DNA synthesis
    • (1986) J. Biol. Chem. , vol.261 , pp. 15208-15216
    • Nakai, H.1    Richardson, C.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.