G. Roberts

发表

Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains.

N. Scrutton, A. Gutiérrez, C. Wolf, 2001, Biochemistry.

Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases.

N. Scrutton, A. Gutiérrez, C. Wolf, 2000, Biochemistry.

Engineering of a functional human NADH-dependent cytochrome P450 system.

C. Wolf, G. Roberts, M. Paine, 2001, Proceedings of the National Academy of Sciences of the United States of America.

The role of tyrosine-9 and the C-terminal helix in the catalytic mechanism of Alpha-class glutathione S-transferases.

C. S. Allardyce, P. McDonagh, C. Wolf, 1999, The Biochemical journal.

Histidine residues of Lactobacillus casei dihydrofolate reductase: paramagnetic relaxation and deuterium-exchange studies and partial assignments.

A. Gronenborn, J. Feeney, G. Roberts, 1980, Biochemistry.

Phosphorus-31 nuclear magnetic resonance studies of the binding of oxidized coenzymes to Lactobacillus casei dihydrofolate reductase.

J. Feeney, G. Roberts, A. Burgen, 1980, Biochemistry.

A nuclear magnetic resonance study of nicotinamide adenine dinucleotide phosphate binding to Lactobacillus casei dihydrofolate reductase.

J. L. Way, J. Feeney, G. Roberts, 1975, Biochemistry.

1H nuclear magnetic resonance studies of the tyrosine residues of selectively deuterated Lactobacillus casei dihydrofolate reductase

J. Feeney, G. Roberts, A. Burgen, 1977, Proceedings of the Royal Society of London. Series B. Biological Sciences.

1H nuclear magnetic resonance studies of Lactobacillus casei dihydrofolate reductase: effects of substrate and inhibitor binding on the histidine residues

J. Feeney, G. Roberts, A. Burgen, 1977, Proceedings of the Royal Society of London. Series B. Biological Sciences.

19 Fnuclear magnetic resonance studies of ligand binding to 3-fluorotyrosine-and 6-fluorotryptophan-containing dihydrofolate reductase from Lactobacillus casei.

J. Feeney, G. Roberts, A. Burgen, 1977, Biochemistry.

Proximity of two tryptophan residues in dihydrofolate reductase determined by 19F NMR

B. Sykes, J. Feeney, G. Roberts, 1978, Nature.

Electron Transfer Cofactors

A. Munro, G. Roberts, K. J. McLean, 2012 .

Use of transferred nuclear Overhauser effect measurements to compare binding of coenzyme analogues to dihydrofolate reductase.

J. Feeney, G. Roberts, A. Burgen, 1983, Biochemistry.

Deceptively simple exchange effects in homonuclear Hartmann-Hahn (HOHAHA) spectra of protein-ligand complexes

J. Arnold, M. Carr, T. Frenkiel, 1991 .

The use of saturation transfer NMR experiments to monitor the conformational selection accompanying ligand—protein interactions

J. Feeney, G. Roberts, A. Burgen, 1980, FEBS letters.

Proton nuclear magnetic resonance saturation transfer studies of coenzyme binding to Lactobacillus casei dihydrofolate reductase.

J. Feeney, G. Roberts, A. Burgen, 1980, Biochemistry.

Nuclear magnetic resonance studies of the binding of trimethoprim to dihydrofolate reductase.

E. A. Piper, J. Feeney, G. Roberts, 1979, Biochemistry.

Determinants of specificity for aflatoxin B1-8,9-epoxide in alpha-class glutathione S-transferases.

P. McDonagh, C. Wolf, L. Lian, 1999, The Biochemical journal.

The charge state of trimethoprim bound to Lactobacillus casei dihydrofolate reductase

J. Feeney, G. Roberts, A. Burgen, 1981, FEBS letters.

Effects of coenzyme binding on histidine residues of Lactobacillus casei dihydrofolate reductase.

A. Gronenborn, J. Feeney, G. Roberts, 1981, Biochemistry.

Effects of coenzyme analogues on the binding of p-aminobenzoyl-L-glutamate and 2,4-diaminopyrimidine to Lactobacillus casei dihydrofolate reductase.

G. Roberts, A. Burgen, B. Birdsall, 1980, Biochemistry.

Structural studies on FMN domain of cytochrome P450 reductase.

C. Wolf, L. Lian, G. Roberts, 1995, Biochemical Society transactions.

NMR evidence for the structure of the complex between penicillin and the DD‐carboxypeptidase of streptomyces R61

J. Frère, J. Ghuysen, J. Feeney, 1979, FEBS letters.

Correction for light absorption in fluorescence studies of protein-ligand interactions.

G. Roberts, S. R. Goode, R. B. Dunlap, 1983, Analytical biochemistry.

Structure‐activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin

M. Gasson, G. Roberts, W. Chan, 1996, FEBS letters.

A novel post-translational modification of the peptide antibiotic subtilin: isolation and characterization of a natural variant from Bacillus subtilis A.T.C.C. 6633.

L. Lian, G. Roberts, W. Chan, 1993, The Biochemical journal.

A 31P-nmr study of the intact liver fluke Fasciola hepatica.

J. Feeney, G. Roberts, P. Morris, 1982, Biochimica et biophysica acta.

NMR studies of substrate binding to cytochrome P450 BM3: comparisons to cytochrome P450 cam.

J. M. Boyle, L. Lian, G. Roberts, 1995, Biochemistry.

Solution structures of nisin A and its two major degradation products determined by n.m.r.

L. Lian, G. Roberts, W. Chan, 1992, The Biochemical journal.

31P NMR studies of NADPH and NADP+ binding to L. casei dihydrofolate reductase

J. Feeney, G. Roberts, A. Burgen, 1975, Nature.

Conformational studies of oxytocin and lysine vasopressin in aqueous solution using high resolution NMR spectroscopy.

J. Feeney, G. Roberts, A. Burgen, 1971, Nature: New biology.

Binding of flexible ligands to macromolecules

J. Feeney, G. Roberts, G. Roberts, 1975, Nature.

Unequivocal assignments of NH proton magnetic resonance bands in oxytocin using 2H‐ and 15N‐substituted molecules

J. Feeney, G. Roberts, A. Burgen, 1974, FEBS letters.

Preparation of selectively deuterated aromatic amino acids for use in 1H NMR studies of proteins.

J. Feeney, G. Roberts, A. Burgen, 1976, Biochimica et biophysica acta.

Negative cooperativity between folinic acid and coenzyme in their binding to Lactobacillus casei dihydrofolate reductase.

A S Burgen, J. Feeney, G. Roberts, 1981, Biochemistry.

Binding of coenzyme analogues to Lactobacillus casei dihydrofolate reductase: binary and ternary complexes.

G. Roberts, A. Burgen, B. Birdsall, 1980, Biochemistry.

Cooperativity in ligand binding to dihydrofolate reductase.

G. Roberts, J. F. Rodrigues de Miranda, A. Burgen, 1978, Biochemistry.

Insights into drug metabolism by cytochromes P450 from modelling studies of CYP2D6‐drug interactions

M. Sutcliffe, Jean‐Didier Maréchal, C. Wolf, 2008, British journal of pharmacology.

A kinetic study of wild-type and mutant dihydrofolate reductases from Lactobacillus casei.

S. Benkovic, C. Fierke, J. Feeney, 1989, Biochemistry.

1H‐NMR studies of the histidine residues of human choriogonadotropin and its α‐ and β‐subunits

G. Roberts, F. Frankenne, B. Birdsall, 1983 .

Metabolism of MPTP by cytochrome P4502D6 and the demonstration of 2D6 mRNA in human foetal and adult brain by in situ hybridization.

R. Poulsom, C. Wolf, G. Roberts, 1997, Xenobiotica; the fate of foreign compounds in biological systems.

NMR studies of multiple conformations in complexes of Lactobacillus casei dihydrofolate reductase with analogues of pyrimethamine.

M D Carr, S J Tendler, J. Arnold, 1990, Biochemistry.

A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.

W U Primrose, M. Sutcliffe, C. Wolf, 1996, Biochemistry.

An unusual matrix of stereocomplementarity in the hydroxylation of monohydroxy fatty acids catalysed by cytochrome P-450 from Bacillus megaterium with potential application in biotransformations

Paul M. Cullis, Gck Roberts, Chris L Willis, 1999 .

Functional high level expression of cytochrome P450 CYP2D6 using baculoviral expression systems.

C. Wolf, G. Roberts, M. Paine, 1996, Archives of Biochemistry and Biophysics.

Design and synthesis of some substrate analogue inhibitors of phospholipase A2 and investigations by NMR and molecular modeling into the binding interactions in the enzyme-inhibitor complex.

W U Primrose, G. Roberts, G. Roberts, 1992, Journal of medicinal chemistry.

PROTON FOURIER TRANSFORM NMR STUDIES OF THE UNFOLDING OF RIBONUCLEASE

G. Roberts, F. W. Benz, 1973, Annals of the New York Academy of Sciences.

Role of the conserved phenylalanine 181 of NADPH-cytochrome P450 oxidoreductase in FMN binding and catalytic activity.

C. Wolf, L. Lian, G. Roberts, 2001, Biochemistry.

Identification and properties of pathways for K+ transport in guinea‐pig and rat alveolar epithelial type II cells.

G. Roberts, C. Boyd, P. Kemp, 1994, The Journal of physiology.

The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts.

J. Arnold, M. Carr, T. Frenkiel, 1990, European journal of biochemistry.

NMR studies of differences in the conformations and dynamics of ligand complexes formed with mutant dihydrofolate reductases.

R. Davies, J. Feeney, G. Roberts, 1989, Biochemistry.

Trimethoprim binding to Lactobacillus casei dihydrofolate reductase: a 13C NMR study using selectively 13C-enriched trimethoprim.

J. Feeney, G. Roberts, M. Searle, 1986, Biochemistry.

Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP+ complex.

A. Gronenborn, G. Clore, J. Feeney, 1984, Biochemistry.

Electron transfer in human cytochrome P450 reductase.

N. Scrutton, A. Gutiérrez, A. Munro, 2001, Biochemical Society transactions.

Identification of the 1H resonances of valine and leucine residues in dihydrofolate reductase by using a combination of selective deuteration and two‐dimensional correlation spectroscopy

J. Feeney, G. Roberts, M. Searle, 1986, FEBS letters.

1H and 15N NMR studies of protonation and hydrogen-bonding in the binding of trimethoprim to dihydrofolate reductase

L. Kuyper, J. Feeney, G. Roberts, 2004, European Biophysics Journal.

The solution structure of the complex of Lactobacillus casei dihydrofolate reductase with methotrexate.

T. Frenkiel, J. Feeney, C. Bauer, 1998, Journal of molecular biology.

31P NMR studies of the binding of adenosine‐2′‐phosphate to Lactobacillus casei dihydrofolate reductase

J. Feeney, G. Roberts, A. Burgen, 1977, FEBS letters.

15N and 1H NMR evidence for multiple conformations of the complex of dihydrofolate reductase with its substrate, folate

J. Feeney, G. Roberts, M. Searle, 1987, FEBS letters.

Hydrogen-1 nuclear magnetic resonance study of the complexes of two diastereoisomers of folinic acid with dihydrofolate reductase.

J. Feeney, G. Roberts, P. Charlton, 1981, Biochemistry.

Direct observation by NMR of two coexisting conformations of an enzyme–ligand complex in solution

A. Gronenborn, J. Feeney, G. Roberts, 1981, Nature.

The combined use of selective deuteration and double resonance experiments in assigning the 1H resonances of valine and tyrosine residues of dihydrofolate reductase

J. Feeney, G. Roberts, M. Searle, 1984, FEBS letters.

A single mutation in cytochrome P450 BM3 changes substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation.

W U Primrose, M. Sutcliffe, L. Lian, 1997, Biochemistry.

Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution.

M. Carr, T. Frenkiel, J. McCormick, 1991, Biochemistry.

1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450

C. Wolf, L. Lian, G. Roberts, 1997, Journal of biomolecular NMR.

1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine as a substrate of cytochrome P450 2D6: allosteric effects of NADPH-cytochrome P450 reductase.

W U Primrose, M. Sutcliffe, C. Wolf, 1997, Biochemistry.

Crystallization and preliminary X-ray diffraction studies of human cytochrome P450 reductase.

H P Driessen, L Y Lian, G C Roberts, 1996, Journal of structural biology.

Identification of the C2‐1H histidine NMR resonances in chloramphenicol acetyltransferase by a 13C‐1H heteronuclear multiple quantum coherence method

W. V. Shaw, G. Roberts, L. Lian, 1991, FEBS letters.

Determinants of the substrate specificity of human cytochrome P-450 CYP2D6: design and construction of a mutant with testosterone hydroxylase activity.

M. Sutcliffe, C. Wolf, L. Lian, 1998, The Biochemical journal.

Determination of the structure of an N-substituted protoporphyrin isolated from the livers of griseofulvin-fed mice.

L. Lian, G. Roberts, F. De Matteis, 1995, The Biochemical journal.

NMR and IR Studies of the Effect of Calcium on the Binding of Inhibitors to Phospholipase A2

C. Wharton, G. Roberts, W. U. Primrose, 1993 .

Protein-ligand interactions: exchange processes and determination of ligand conformation and protein-ligand contacts.

M. Sutcliffe, G. Roberts, L. Lian, 1994, Methods in enzymology.

Proceedings: NMR studies of the binding of substrate analogues to L. casei dihydrofolate reductase.

J. Dann, J. Feeney, G. Roberts, 1974, British Journal of Pharmacology.

Structure-activity relationships in the sulphonamide-carbonic anhydrase systemi NMR studies of the binding of substrate analogues to L. casei dihydrofolate reductase

G. Roberts, V. Yuferov, A. Burgen, 2006 .

The conformation of 5‐hydroxytryptamine in solution

G. Roberts, P. Partington, R. R. Ison, 1972, The Journal of pharmacy and pharmacology.

The binding of amide substrate analogues to phospholipase A2. Studies by 13C-nuclear-magnetic-resonance and infrared spectroscopy.

C. Wharton, G. Roberts, W. U. Primrose, 1992, The Biochemical journal.

Dynamics of trimethoprim bound to dihydrofolate reductase.

J. Feeney, G. Roberts, M. Forster, 1988, Proceedings of the National Academy of Sciences of the United States of America.