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E E Howell

Showing results (11-20 of 40) with videos related to

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Biochemistry|September 3, 1996
Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric proteinT D Bradrick, J M Beechem, E E Howell
Biochemistry|September 18, 1990
Dihydrofolate reductase from Escherichia coli: probing the role of aspartate-27 and phenylalanine-137 in enzyme conformation and the binding of NADPHS M Dunn, T M Lanigan, E E Howell
Journal of Bacteriology|July 1, 1988
Construction of a dihydrofolate reductase-deficient mutant of Escherichia coli by gene replacementE E Howell, P G Foster, L M Foster
The Journal of Biological Chemistry|January 24, 1997
Mechanistic studies of R67 dihydrofolate reductase. Effects of pH and an H62C mutationH Park, P Zhuang, R Nichols, et al.
The Journal of Biological Chemistry|April 5, 1990
Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPHJ R Appleman, E E Howell, J Kraut, et al.
Biochemistry|November 12, 1991
Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of the N-terminus in the proteinL J Reece, R Nichols, R C Ogden, et al.
Nature Structural Biology|November 1, 1995
A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active siteN Narayana, D A Matthews, E E Howell, et al.
Biochemistry|March 29, 2000
Effects of single-tryptophan mutations on R67 dihydrofolate reductaseF W West, H S Seo, T D Bradrick, et al.
Biochemistry|September 18, 1990
A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27----serine Escherichia coli dihydrofolate reductaseE E Howell, C Booth, M Farnum, et al.
The Journal of Biological Chemistry|October 25, 1993
Artificial duplication of the R67 dihydrofolate reductase gene to create protein asymmetry. Effects on protein activity and foldingP Zhuang, M Yin, J C Holland, et al.
Pageof 4

Showing results (11-20 of 40) with videos related to

Sort By:
Pageof 4
Biochemistry|September 3, 1996
Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric proteinT D Bradrick, J M Beechem, E E Howell
Biochemistry|September 18, 1990
Dihydrofolate reductase from Escherichia coli: probing the role of aspartate-27 and phenylalanine-137 in enzyme conformation and the binding of NADPHS M Dunn, T M Lanigan, E E Howell
Journal of Bacteriology|July 1, 1988
Construction of a dihydrofolate reductase-deficient mutant of Escherichia coli by gene replacementE E Howell, P G Foster, L M Foster
The Journal of Biological Chemistry|January 24, 1997
Mechanistic studies of R67 dihydrofolate reductase. Effects of pH and an H62C mutationH Park, P Zhuang, R Nichols, et al.
The Journal of Biological Chemistry|April 5, 1990
Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPHJ R Appleman, E E Howell, J Kraut, et al.
Biochemistry|November 12, 1991
Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of the N-terminus in the proteinL J Reece, R Nichols, R C Ogden, et al.
Nature Structural Biology|November 1, 1995
A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active siteN Narayana, D A Matthews, E E Howell, et al.
Biochemistry|March 29, 2000
Effects of single-tryptophan mutations on R67 dihydrofolate reductaseF W West, H S Seo, T D Bradrick, et al.
Biochemistry|September 18, 1990
A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27----serine Escherichia coli dihydrofolate reductaseE E Howell, C Booth, M Farnum, et al.
The Journal of Biological Chemistry|October 25, 1993
Artificial duplication of the R67 dihydrofolate reductase gene to create protein asymmetry. Effects on protein activity and foldingP Zhuang, M Yin, J C Holland, et al.
Pageof 4