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1
Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate
Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate
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Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate

Hammes, Gordon G ; Porter, Robert W ; Stark, George R

Biochemistry (Easton), 1971-03, Vol.10 (6), p.1046-1050 [Periódico revisado por pares]

United States: American Chemical Society

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2
Comparative studies of the pigeon liver fatty acid synthetase complex and its subunits. Kinetics of partial reactions and the number of binding sites for acetyl and malonyl groups
Comparative studies of the pigeon liver fatty acid synthetase complex and its subunits. Kinetics of partial reactions and the number of binding sites for acetyl and malonyl groups
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Comparative studies of the pigeon liver fatty acid synthetase complex and its subunits. Kinetics of partial reactions and the number of binding sites for acetyl and malonyl groups

Kumar, S ; Dorsey, J A ; Muesing, R A ; Porter, J W

The Journal of biological chemistry, 1970-09, Vol.245 (18), p.4732-4744 [Periódico revisado por pares]

United States

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3
Mutational Analysis of the Ras Converting Enzyme Reveals a Requirement for Glutamate and Histidine Residues
Mutational Analysis of the Ras Converting Enzyme Reveals a Requirement for Glutamate and Histidine Residues
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Mutational Analysis of the Ras Converting Enzyme Reveals a Requirement for Glutamate and Histidine Residues

Plummer, Lisa J. ; Hildebrandt, Emily R. ; Porter, Stephen B. ; Rogers, Victoria A. ; McCracken, Jay ; Schmidt, Walter K.

The Journal of biological chemistry, 2006-02, Vol.281 (8), p.4596-4605 [Periódico revisado por pares]

United States: Elsevier Inc

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4
Aspartate transcarbamylase. Kinetic studies of the catalytic subunit
Aspartate transcarbamylase. Kinetic studies of the catalytic subunit
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Aspartate transcarbamylase. Kinetic studies of the catalytic subunit

Porter, R W ; Modebe, M O ; Stark, G R

The Journal of biological chemistry, 1969-04, Vol.244 (7), p.1846-1859 [Periódico revisado por pares]

United States

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5
Kinetic Analysis of the Effects of Mutagenesis of W501 and V432 of the Hepatitis C Virus NS3 Helicase Domain on ATPase and Strand-Separating Activity
Kinetic Analysis of the Effects of Mutagenesis of W501 and V432 of the Hepatitis C Virus NS3 Helicase Domain on ATPase and Strand-Separating Activity
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Kinetic Analysis of the Effects of Mutagenesis of W501 and V432 of the Hepatitis C Virus NS3 Helicase Domain on ATPase and Strand-Separating Activity

Preugschat, Frank ; Danger, Dana P ; Carter, Luke H ; Davis, Roderick G ; Porter, David J. T

Biochemistry (Easton), 2000-05, Vol.39 (17), p.5174-5183 [Periódico revisado por pares]

United States: American Chemical Society

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6
Kinetic analysis of the individual reductive steps catalyzed by β-hydroxy-β-methylglutaryl-coenzyme A reductase obtained from yeast
Kinetic analysis of the individual reductive steps catalyzed by β-hydroxy-β-methylglutaryl-coenzyme A reductase obtained from yeast
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Kinetic analysis of the individual reductive steps catalyzed by β-hydroxy-β-methylglutaryl-coenzyme A reductase obtained from yeast

Qureshi, Nilofer ; Dugan, Richard E ; Cleland, W. W ; Porter, John W

Biochemistry (Easton), 1976-09, Vol.15 (19), p.4191-4197 [Periódico revisado por pares]

United States: American Chemical Society

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7
Transcriptional Activation Domain of the Herpesvirus Protein VP16 Becomes Conformationally Constrained upon Interaction with Basal Transcription Factors
Transcriptional Activation Domain of the Herpesvirus Protein VP16 Becomes Conformationally Constrained upon Interaction with Basal Transcription Factors
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Transcriptional Activation Domain of the Herpesvirus Protein VP16 Becomes Conformationally Constrained upon Interaction with Basal Transcription Factors

Shen, F ; Triezenberg, S J ; Hensley, P ; Porter, D ; Knutson, J R

The Journal of biological chemistry, 1996-03, Vol.271 (9), p.4827-4837 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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8
Active site amino acids that participate in the catalytic mechanism of nucleoside 2'-deoxyribosyltransferase
Active site amino acids that participate in the catalytic mechanism of nucleoside 2'-deoxyribosyltransferase
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Active site amino acids that participate in the catalytic mechanism of nucleoside 2'-deoxyribosyltransferase

Short, S A ; Armstrong, S R ; Ealick, S E ; Porter, D J

The Journal of biological chemistry, 1996-03, Vol.271 (9), p.4978-4987 [Periódico revisado por pares]

United States

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9
Pyridinyl Imidazole Inhibitors of p38 Mitogen-activated Protein Kinase Bind in the ATP Site
Pyridinyl Imidazole Inhibitors of p38 Mitogen-activated Protein Kinase Bind in the ATP Site
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Pyridinyl Imidazole Inhibitors of p38 Mitogen-activated Protein Kinase Bind in the ATP Site

Young, P R ; McLaughlin, M M ; Kumar, S ; Kassis, S ; Doyle, M L ; McNulty, D ; Gallagher, T F ; Fisher, S ; McDonnell, P C ; Carr, S A ; Huddleston, M J ; Seibel, G ; Porter, T G ; Livi, G P ; Adams, J L ; Lee, J C

The Journal of biological chemistry, 1997-05, Vol.272 (18), p.12116-12121 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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