Methotrexate analogs. 15. A methotrexate analogue designed for active-site-directed irreversible inactivation of dihydrofolate reductase

A. Rosowsky; J. E. Wright; C. Ginty; J. Uren

doi:10.1021/jm00350a015

Methotrexate analogs. 15. A methotrexate analogue designed for active-site-directed irreversible inactivation of dihydrofolate reductase

Journal of Medicinal Chemistry ◽

10.1021/jm00350a015 ◽

1982 ◽

Vol 25 (8) ◽

pp. 960-964 ◽

Cited By ~ 12

Author(s):

A. Rosowsky ◽

J. E. Wright ◽

C. Ginty ◽

J. Uren

Keyword(s):

Dihydrofolate Reductase ◽

Active Site

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Crystallographic analysis reveals a novel second binding site for trimethoprim in active site double mutants of human dihydrofolate reductase

Journal of Structural Biology ◽

10.1016/j.jsb.2011.06.001 ◽

2011 ◽

Vol 176 (1) ◽

pp. 52-59 ◽

Cited By ~ 10

Author(s):

Vivian Cody ◽

Jim Pace ◽

Jennifer Piraino ◽

Sherry F. Queener

Keyword(s):

Binding Site ◽

Dihydrofolate Reductase ◽

Active Site ◽

Crystallographic Analysis ◽

Human Dihydrofolate Reductase

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Ireversible enzyme inhibitors. CLXXIX. Active-site-directed irreversible enzyme inhibitors of dihydrofolate reductase from 1-(3-chlorophenyl)-4,6-diamino-1,2-dihydro-2,2-dimethyl-s-triazine with oxyamide bridges to a terminal sulfonyl fluoride

Journal of Medicinal Chemistry ◽

10.1021/jm00300a032 ◽

1970 ◽

Vol 13 (6) ◽

pp. 1165-1170 ◽

Cited By ~ 3

Author(s):

Bernard Randall Baker ◽

Wallace T. Ashton

Keyword(s):

Dihydrofolate Reductase ◽

Active Site ◽

Enzyme Inhibitors ◽

Sulfonyl Fluoride

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High-resolution structure of a plasmid-encoded dihydrofolate reductase: pentagonal network of water molecules in theD2-symmetric active site

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444906014764 ◽

2006 ◽

Vol 62 (7) ◽

pp. 695-706 ◽

Cited By ~ 6

Author(s):

Narendra Narayana

Keyword(s):

High Resolution ◽

Dihydrofolate Reductase ◽

Active Site ◽

Water Molecules ◽

High Resolution Structure ◽

Resolution Structure

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Correlations of Inhibitor Kinetics forPneumocystis jiroveciiand Human Dihydrofolate Reductase with Structural Data for Human Active Site Mutant Enzyme Complexes†‡

Biochemistry ◽

10.1021/bi801960h ◽

2009 ◽

Vol 48 (8) ◽

pp. 1702-1711 ◽

Cited By ~ 12

Author(s):

Vivian Cody ◽

Jim Pace ◽

Jennifer Makin ◽

Jennifer Piraino ◽

Sherry F. Queener ◽

...

Keyword(s):

Dihydrofolate Reductase ◽

Active Site ◽

Structural Data ◽

Mutant Enzyme ◽

Human Dihydrofolate Reductase ◽

Enzyme Complexes ◽

Inhibitor Kinetics

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Role of the Active-Site Carboxylate in Dihydrofolate Reductase: Kinetic and Spectroscopic Studies of the Aspartate 26 .fwdarw. Asparagine Mutant of the Lactobacillus casei Enzyme

Biochemistry ◽

10.1021/bi00009a018 ◽

1995 ◽

Vol 34 (9) ◽

pp. 2872-2882 ◽

Cited By ~ 14

Author(s):

J. Basran ◽

M. G. Casarotto ◽

I. L. Barsukov ◽

G. C. K. Roberts

Keyword(s):

Dihydrofolate Reductase ◽

Active Site ◽

Lactobacillus Casei ◽

Spectroscopic Studies

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ACTIVE-SITE DIRECTED IRREVERSIBLE INHIBITORS OF DIHYDROFOLATE REDUCTASE

Annals of the New York Academy of Sciences ◽

10.1111/j.1749-6632.1971.tb31146.x ◽

1971 ◽

Vol 186 (1 Folate Antago) ◽

pp. 214-226 ◽

Cited By ~ 31

Author(s):

B. R. Baker

Keyword(s):

Dihydrofolate Reductase ◽

Active Site ◽

Irreversible Inhibitors

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A glutamine 67--> histidine mutation in homotetrameric R67 dihydrofolate reductase results in four mutations per single active site pore and causes substantial substrate and cofactor inhibition

Protein Engineering Design and Selection ◽

10.1093/protein/10.12.1415 ◽

1997 ◽

Vol 10 (12) ◽

pp. 1415-1424 ◽

Cited By ~ 18

Author(s):

H. Park ◽

T. D. Bradrick ◽

E. E. Howell

Keyword(s):

Dihydrofolate Reductase ◽

Active Site ◽

R67 Dihydrofolate Reductase

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Free Energy Simulations of Active-Site Mutants of Dihydrofolate Reductase

The Journal of Physical Chemistry B ◽

10.1021/jp5059963 ◽

2014 ◽

Vol 119 (3) ◽

pp. 906-916 ◽

Cited By ~ 14

Author(s):

Dvir Doron ◽

Vanja Stojković ◽

Lokesh Gakhar ◽

Alexandra Vardi-Kilshtain ◽

Amnon Kohen ◽

...

Keyword(s):

Free Energy ◽

Dihydrofolate Reductase ◽

Active Site ◽

Energy Simulations ◽

Active Site Mutants

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Solvent environments significantly affect the enzymatic function of Escherichia coli dihydrofolate reductase: Comparison of wild-type protein and active-site mutant D27E

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ◽

10.1016/j.bbapap.2013.09.024 ◽

2013 ◽

Vol 1834 (12) ◽

pp. 2782-2794 ◽

Cited By ~ 15

Author(s):

Eiji Ohmae ◽

Yurina Miyashita ◽

Shin-ichi Tate ◽

Kunihiko Gekko ◽

Soichiro Kitazawa ◽

...

Keyword(s):

Escherichia Coli ◽

Dihydrofolate Reductase ◽

Active Site ◽

Wild Type ◽

Enzymatic Function ◽

Type Protein ◽

Wild Type Protein

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Atomic Scale Determination of Enzyme Flexibility and Active Site Stability through Static Modes: Case of Dihydrofolate Reductase

The Journal of Physical Chemistry B ◽

10.1021/jp109874z ◽

2011 ◽

Vol 115 (7) ◽

pp. 1616-1622 ◽

Cited By ~ 5

Author(s):

Marie Brut ◽

Alain Estève ◽

Georges Landa ◽

Guillaume Renvez ◽

Mehdi Djafari Rouhani ◽

...

Keyword(s):

Dihydrofolate Reductase ◽

Active Site ◽

Atomic Scale

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