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Volumn 276, Issue 32, 2001, Pages 29651-29656

The Plasmodium falciparum Bifunctional Ornithine Decarboxylase, S-Adenosyl-L-methionine Decarboxylase, Enables a Well Balanced Polyamine Synthesis without Domain-Domain Interaction

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; CHEMICAL ACTIVATION; ENZYME KINETICS; MALARIA CONTROL; MUTAGENESIS; PROTEINS;

EID: 0035839493     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M100578200     Document Type: Article
Times cited : (51)

References (48)
  • 5
    • 0039524295 scopus 로고
    • (Palfreyman, M. G., McCann, P. P., Lovenberg, W., Temple, J. G., Jr., and Sjoerdsma, A., eds), Academic Press, San Diego, CA
    • Pegg, A. E., McCann, P. P., and Sjoerdsma, A. (1989) in Enzymes as Targets for Drug Design (Palfreyman, M. G., McCann, P. P., Lovenberg, W., Temple, J. G., Jr., and Sjoerdsma, A., eds) pp. 157-183, Academic Press, San Diego, CA
    • (1989) Enzymes as Targets for Drug Design , pp. 157-183
    • Pegg, A.E.1    McCann, P.P.2    Sjoerdsma, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.