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Volumn 291, Issue 6-7, 2001, Pages 523-529

The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases

Author keywords

ADP ribosylation; ADP ribosyltransferase; ARTT motif; Catalytic mechanism; NAD

Indexed keywords

PSEUDOMONAS;

EID: 0036196923     PISSN: 14384221     EISSN: None     Source Type: Journal    
DOI: 10.1078/1438-4221-00162     Document Type: Article
Times cited : (80)

References (29)
  • 5
    • 0029746051 scopus 로고    scopus 로고
    • Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacterial and T-even bacteriophages
    • (1996) Mol. Microbiol. , vol.21 , pp. 667-674
    • Domenighini, M.1    Rappuoli, R.2
  • 16
    • 0018140316 scopus 로고
    • Activation of adenylate cyclase by heat-labile Escherichia coli enterotoxin. Evidence for ADP-ribosyltransferase activity similar to that of choleragen
    • (1978) J. Clin. Invest. , vol.62 , pp. 281-285
    • Moss, J.1    Richardson, S.H.2
  • 25
    • 0003085965 scopus 로고
    • Pertussis toxin as a valuable probe for G-protein involvement in signal transduction
    • (Moss, J., Vaughan, M., eds.). American Society for Microbiology, Washington, D.C.
    • (1990) ADP-ribosylating toxins and G proteins , pp. 45-77
    • Ui, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.