Energetically Most Likely Substrate and Active-Site Protonation Sites and Pathways in the Catalytic Mechanism of Dihydrofolate Reductase-Reference-Cited by-同舟云学术

Energetically Most Likely Substrate and Active-Site Protonation Sites and Pathways in the Catalytic Mechanism of Dihydrofolate Reductase

Published:2001-03-23 Issue:15 Volume:123 Page:3418-3428
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Cummins Peter L.¹,Gready Jill E.¹

Affiliation:

1. Contribution from the Computational Molecular Biology and Drug Design Group, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra ACT 2601, Australia

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0038474

Reference58 articles.

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2. Freisheim, J. H.; Matthews, D. A. InAntagonists as Therapeutic Agents; Sirotnak, F. M., Burchall, J. J., Ensminger, W. D., Montgomery, J. A., Eds.; Academic Press: Orlando, 1984; Vol. 1, pp 69−131.

3. The methotrexate story: A paradigm for development of cancer chemotherapeutic agents

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