J. W. Thomas

发表

Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center.

R. Gennis, J. O. Alben, L. Lemieux, 1993, Biochemistry.

Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides.

R. Gennis, S. Ferguson-Miller, J. Shapleigh, 1993, Biochemistry.

Glucocorticoid receptor-mediated induction of glutamine synthetase in skeletal muscle cells in vitro.

C. Banner, L. Vitković, J. W. Thomas, 1987, Endocrinology.

Dexamethasone regulates glutamine synthetase expression in rat skeletal muscles.

C. Banner, K. Mearow, L. Vitković, 1988, The American journal of physiology.

Glutamate-89 in subunit II of cytochrome bo3 from Escherichia coli is required for the function of the heme-copper oxidase.

B. Barquera, R. Gennis, A. Puustinen, 1999, Biochemistry.

Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli.

R. Gennis, P. Rich, J. Rumbley, 1994, Biochimica et biophysica acta.

Possible proton relay pathways in cytochrome c oxidase.

R. Gennis, S. Ferguson-Miller, J. Shapleigh, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity.

R. Gennis, A. Puustinen, M. Wikström, 1993, Biochemistry.

Guanine nucleotide modulation of [3H]TCP binding to the NMDA receptor complex.

J. Monahan, R. Compton, W. Hood, 1990, European journal of pharmacology.

The cytochrome oxidase superfamily of redox-driven proton pumps.

R. Gennis, M. Calhoun, J. W. Thomas, 1994, Trends in biochemical sciences.

Characterization of photoaffinity labeling of benzodiazepine binding sites.

J. Tallman, J. W. Thomas, J. W. Thomas, 1981, The Journal of biological chemistry.

Identification of diazepam binding in intack animals.

J. Tallman, D. Gallager, J. W. Thomas, 1979, Life sciences.

Oxygen reaction and proton uptake in helix VIII mutants of cytochrome bo3.

R. Gennis, T. Nilsson, L. Lemieux, 1995, Biochemistry.

Isolation of a cDNA for rat brain glutaminase.

R. Wenthold, J. Hwang, D. Huie, 1988, Brain research.

Effect of GABAergic drugs on benzodiazepine binding site sensitivity in rat cerebral cortex.

J. Tallman, D. Gallager, J. W. Thomas, 1978, Biochemical pharmacology.

Solubilization of benzodiazepine binding site from rat cortex.

J. Tallman, J. W. Thomas, M. Ayub Khan Yousufi, 1979, Life sciences.

Proteolytic degradation of neuronal benzodiazepine binding sites.

J. Neale, J. Tallman, A. Bocchetta, 1984, Life sciences.

Photoaffinity labeling of benzodiazepine receptors causes altered agonist-antagonist interactions

J. Tallman, J. W. Thomas, J. W. Thomas, 1983, The Journal of neuroscience : the official journal of the Society for Neuroscience.

Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis.

R. Gennis, Jeffrey W. Thomas, L. Lemieux, 1992, The Journal of biological chemistry.

Structural requirements for the specific recognition of an m7G mRNA cap.

M. Hodel, C. Hagedorn, A. Hodel, 2000, Biochemistry.

A loop between transmembrane helices IX and X of subunit I of cytochrome c oxidase caps the heme a-heme a3-CuB center.

R. Gennis, Y. Kim, J. Shapleigh, 1994, Biochemistry.

Glutamic acid decarboxylase mRNA in rat brain: regional distribution and effects of intrastriatal kainic acid.

S. Paul, E. Ginns, A. Tobin, 1987, Brain research.

Developmental induction of glutaminase in primary cultures of cerebellar granule cells.

A. Novelli, R. Henneberry, J. Tao-Cheng, 1989, Brain Research. Molecular Brain Research.

Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli.

R. Gennis, J. O. Alben, L. Lemieux, 1993, Biochemistry.

The highly conserved methionine of subunit I of the heme‐copper oxidases is not at the heme‐copper dinuclear center: Mutagenesis of M110 in subunit I of cytochrome bo 3‐type ubiquinol oxidase from Escherichia coli

R. Gennis, J. O. Alben, L. Lemieux, 1995, FEBS letters.

Site-directed mutagenesis of residues within helix VI in subunit I of the cytochrome bo3 ubiquinol oxidase from Escherichia coli suggests that tyrosine 288 may be a CuB ligand.

R. Gennis, A. Puustinen, M. Wikström, 1994, Biochemistry.

GABA-benzodiazepine interactions: physiological, pharmacological and developmental aspects.

J. Tallman, P. Mallorga, D. Gallager, 1980, Federation proceedings.

Benzodiazepine binding sites: properties and modulation.

J. Tallman, P. Mallorga, D. Gallager, 1981, Advances in biochemical psychopharmacology.

The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type.

R. Gennis, A. Puustinen, M. Wikström, 1992, Biochemistry.

Neural control of glutamine synthetase activity in rat skeletal muscles.

C. Banner, J. W. Thomas, M. Konagaya, 1990, The American journal of physiology.