C. Williams

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Acyl-coenzyme A dehydrogenase from pig kidney. Purification and properties.

R. Matthews, C. Thorpe, C. Williams, 1979, Biochemistry.

Synthesis and Biological Activity of a Novel Class of Purine Nucleoside Phosphorylase Inhibitors

S. P. Walton, J. Montgomery, C. Williams, 2000, Nucleosides, nucleotides & nucleic acids.

Glutathione reductase from yeast. Differential reactivity of the nascent thiols in two-electron reduced enzyme and properties of a monoalkylated derivative.

C. Thorpe, C. Williams, L. Arscott, 1981, Biochemistry.

Crystal Structure of Escherichia coli Thioredoxin Reductase Refined at 2 Å Resolution

J Kuriyan, G Waksman, J. Kuriyan, 1994 .

Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase.

M. Ludwig, C. Williams, C H Williams, 2000, Science.

Evidence for two conformational states of thioredoxin reductase from Escherichia coli: Use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation

C. Williams, S. Mulrooney, C. Williams, 1997, Protein science : a publication of the Protein Society.

Mechanism and structure of thioredoxin reductase from Escherichia coli

C. Williams, C. Williams, 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Overexpression and mutagenesis of the lipoamide dehydrogenase of Escherichia coli.

J. Guest, C. Williams, N. Allison, 1988, The Biochemical journal.

Characterization of two active site mutations of thioredoxin reductase from Escherichia coli.

D. Engelke, A. Prongay, C. Williams, 1989, The Journal of biological chemistry.

Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis.

C. Walsh, S. Miller, D. Ballou, 1991, Biochemistry.

Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase.

M. Moore, C. Walsh, M. Distefano, 1989, Biochemistry.

Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart.

R. Matthews, C. Williams, 1976, The Journal of biological chemistry.

Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase.

G. Schulz, C. Williams, L. Arscott, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Conformational basis of energy transduction in membrane systems VIII. Configurational changes of mitochondria

R. Harris, D. E. Green, E. Valdivia, 1970, Journal of bioenergetics.

Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis.

R. Matthews, K. Wilkinson, C. Thorpe, 1979, Methods in enzymology.

The determination of phosphorus in Kjeldahl digests of plant material by automatic analysis

C. Williams, J. Twine, 1971 .

Reductive half-reaction of thioredoxin reductase from Escherichia coli.

C. Williams, B. Lennon, 1997, Biochemistry.

Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: Evidence that cysteine‐138 functions to initiate dithiol‐disulfide interchange and to accept the reducing equivalent from reduced flavin

P. Wang, C. Williams, S. Mulrooney, 1998, Protein science : a publication of the Protein Society.

The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli.

R. Schirmer, K. Becker, S. Gromer, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism of reduction of quinones by Trypanosoma congolense trypanothione reductase.

J. Blanchard, N. Čėnas, C. Williams, 1994, Biochemistry.

THE ACCUMULATION IN SOIL OF CADMIUM RESIDUES FROM PHOSPHATE FERTILIZERS AND THEIR EFFECT ON THE CADMIUM CONTENT OF PLANTS

C. Williams, D. J. David, 1976 .

Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase.

M. Moore, C. Walsh, M. Distefano, 1990, Biochemistry.

On the reaction mechanism of yeast glutathione reductase.

V. Massey, C. Williams, 1965, The Journal of biological chemistry.

Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis.

C. Williams, B. Lennon, 1996, Biochemistry.

L-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family.

D. Giegel, V. Massey, C. Williams, 1990, The Journal of biological chemistry.

High-performance liquid chromatographic analysis of biogenic amines in biological materials as o-phthalaldehyde derivatives.

H. D. Johnson, K. Kuo, C. Gehrke, 1979, Journal of chromatography.

Teratogenic studies with 2,4,5-T and 2,4-D in the hamster

C. Williams, T. Collins, Clara H. Williams, 1971, Bulletin of environmental contamination and toxicology.

The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence.

M. Galliano, V. Massey, S. Ronchi, 1982, The Journal of biological chemistry.

13C-labelling of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

C. Williams, 1989 .

Site-directed Mutagenesis of Glycine 99 to Alanine in L-Lactate Monooxygenase from Mycobacterium smegmatis*

V. Massey, C. Williams, Weimei Sun, 1996, The Journal of Biological Chemistry.

Electrophilic amination of a single methionine residue located at the active site of D-amino acid oxidase by O-(2,4-dinitrophenyl)hydroxylamine.

V. Massey, C. Williams, C. D'silva, 1986, Biochemistry.

Evaluation of some fluorogenic substrates for continuous assay of aminopeptidase P.

B. Walker, S. Hawthorne, C. Williams, 1997, Analytical biochemistry.

A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization.

P. Wang, C. Williams, S. Ahn, 1996, Biochemistry.

The determination of chromic oxide in faeces samples by atomic absorption spectrophotometry

C. Williams, D. J. David, O. Iismaa, 1962, The Journal of Agricultural Science.

Visual detection of peptidase activity using fluorogenic substrates in a microtiter plate assay.

G. Irvine, C. Williams, M. Ennis, 1990, Analytical biochemistry.

Amyloidosis in Alzheimer's disease.

D. Allsop, C. Williams, 1994, Biochemical Society transactions.

Identification of methionine-110 as the residue covalently modified in the electrophilic inactivation of D-amino-acid oxidase by O-(2,4-dinitrophenyl) hydroxylamine.

V. Massey, C. Williams, C. D'silva, 1987, Biochemistry.

The isolation and characterization of the lamellar body of bovine lung.

R. Harris, D. E. Green, E. Valdivia, 1971, Preparative biochemistry.

The morphology and configurational states of isolated heavy beef heart mitochondria by the freeze fracture technique

W. Vail, C. Williams, R. Riley, 1972, Journal of bioenergetics.

Investigation on the use of a chelating resin for the extraction of sulphur from soil

J. Freney, C. Williams, G. E. Melville, 1969 .

Zebrafish as a platform for in vivo drug discovery

C. Hong, C. Williams, 2012 .

Development of a continuous, fluorometric coupled enzyme assay for thyrotropin-releasing hormone-degrading ectoenzyme.

K. Tipton, C. Williams, J. A. Kelly, 1999, Analytical biochemistry.

The isolation and primary structure of a paptide containing the oxidation-reduction active cystine of Escherichia coli lipoamide dehydrogenase.

B. D. Burleigh, C. Williams, B. Burleigh, 1972, The Journal of biological chemistry.

Studies of the ferredoxin from Thermus thermophilus.

R. Hille, M. Ludwig, J. Fee, 1983, The Journal of biological chemistry.

CHOLESTEROL CONTENT OF SPINAL CORD AND SCIATIC NERVE OF HENS AFTER ORGANOPHOSPHATE AND CARBAMATE ADMINISTRATION

C. Williams, H. Johnson, J. L. Casterline, 1966, Journal of neurochemistry.

Monoamine oxidase. I. Specificity of some substrates and inhibitors.

C. Williams, 1974, Biochemical pharmacology.

A continuous fluorometric assay for leukotriene D4 hydrolase.

N. Hooper, I. White, C. Williams, 1999, Analytical biochemistry.

Potential active-site base of thioredoxin reductase from Escherichia coli: examination of histidine245 and aspartate139 by site-directed mutagenesis.

C. Williams, S. Mulrooney, 1994, Biochemistry.

Biochemical and behavioural studies of monoamine oxidase inhibition

C. Williams, F. Dollie, 1978, Irish journal of medical science.

Reaction of both active site thiols of reduced thioredoxin reductase with N-ethylmaleimide.

C. Williams, M. O'Donnell, 1985, Biochemistry.

Demonstration that bovine erythrocyte cytochrome b5 is the hydrophilic segment of liver microsomal cytochrome b5.

C. Williams, S. R. Slaughter, D. Hultquist, 1982, Biochimica et biophysica acta.

The effect of 28-day pesticide feeding on serum and tissue enzyme activities of rats fed diets of varying casein content.

C. Williams, J. L. Casterline, 1971, Toxicology and applied pharmacology.

Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and thioredoxin.

G. Zanetti, C. Williams, L. Arscott, 1967, The Journal of biological chemistry.

Isolation, characterization and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase.

R. Matthews, C. Williams, L. Arscott, 1974, Biochimica et biophysica acta.

Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis.

J. Kuriyan, G. Waksman, C. Williams, 1994, Journal of molecular biology.

On the stereospecificity of monoamine oxidase

C. Williams, 1982, The Journal of pharmacy and pharmacology.

The effect of pesticide administration on serum and tissue esterases of rats fed diets of varying casein, calcium, and magnesium content.

C. Williams, J. L. Casterline, 1969, Toxicology and applied pharmacology.

Monoamine oxidase. II. Time-dependent inhibition by propargylamines.

C. Williams, J. Lawson, 1974, Biochemical pharmacology.

Thioredoxin reductase two modes of catalysis have evolved.

R. Schirmer, K. Becker, S. Müller, 2000, European journal of biochemistry.

Selective inhibitors of monoamine oxidases A and B.

C. Williams, 1984, Biochemical pharmacology.

A new specific inhibitor of monoamine oxidase A.

C. Williams, 1982, Biochemical pharmacology.

Proton nuclear magnetic resonance investigation of the mechanism of flavin C-4a adduct formation induced by oxidized nicotinamide adenine dinucleotide binding to monoalkylated pig heart lipoamide dehydrogenase.

F. A. Johnson, C. Williams, M. O'Donnell, 1983, Biochemistry.

The evaluation of plant-available sulphur in soils

C. Williams, A. Steinbergs, 1962, Plant and Soil.

Lipoamide dehydrogenase from pig heart. Pyridine nucleotide induced changes in monoalkylated two-electron reduced enzyme.

C. Thorpe, C. Williams, 1981, Biochemistry.

Evaluation of Christmas Island C-grade phosphate as a fertilizer on some soils in southern New South Wales.

C. Williams, J. Lipsett, 1970 .

CARBON, NITROGEN, SULPHUR, AND PHOSPHORUS IN SOME SCOTTISH SOILS

C. Williams, E. G. Williams, N. M. Scott, 1960 .

Soil organic matter fractions as sources of plant-available sulphur

J. Freney, C. Williams, G. E. Melville, 1975 .

Dietary supplement of neosugar alters the fecal flora and decreases activities of some reductive enzymes in human subjects.

R. Buddington, C. Williams, S. C. Chen, 1996, The American journal of clinical nutrition.

Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver.

H. Kamin, C. Williams, 1962, The Journal of biological chemistry.

Dietary shifts affect the gastrointestinal microflora of the giant panda (Ailuropoda melanoleuca).

D. Sparks, W. Holmes, C. Williams, 2013, Journal of animal physiology and animal nutrition.

An anaerobic titration assembly for spectrophotometric use.

B. D. Burleigh, V. Massey, C. Williams, 1969, Analytical biochemistry.

The presence of S degrees-containing impurities in commercial samples of oxidized glutathione and their catalytic effect on the reduction of cytochrome c.

V. Massey, C. Williams, G. Palmer, 1971, Biochemical and biophysical research communications.

The effect of stage of growth on the copper, zinc, manganese, and molybdenum contents of Algerian oats grown of thirteen soils

C. Williams, C. Moore, 1952 .

Two-electron reduced mercuric reductase binds Hg(II) to the active site dithiol but does not catalyze Hg(II) reduction.

C. Walsh, S. Miller, D. Ballou, 1986, The Journal of biological chemistry.

The isolation and primary structure of a peptide containing the oxidation-reduction active cystine of Escherichia coli thioredoxin reductase.

S. Ronchi, C. Williams, 1972, The Journal of biological chemistry.

The Gastrointestinal Bacteria of Mink (Mustela vison L): Influence of Age and Diet

R. Buddington, C. Williams, J. Elnif, 1998, Acta Veterinaria Scandinavica.

High-performance liquid-chromatographic separation and fluorescence measurement of biogenic amines in plasma, urine, and tissue.

H. D. Johnson, K. Kuo, C. Gehrke, 1978, Clinical chemistry.

Reconstitution of Escherichia coli thioredoxin reductase with 1-deazaFAD. Evidence for 1-deazaFAD C-4a adduct formation linked to the ionization of an active site base.

C. Williams, M. O'Donnell, 1984, The Journal of biological chemistry.

Proton stoichiometry in the reduction of the FAD and disulfide of Escherichia coli thioredoxin reductase. Evidence for a base at the active site.

C. Williams, M. O'Donnell, 1983, The Journal of biological chemistry.

D-aspartate oxidase from beef kidney. Purification and properties.

V. Massey, C. Williams, A. Negri, 1987, The Journal of biological chemistry.

beta-Glucuronidase activity in the urine, serum, kidney and bladder of rats fed 2-chloro-4-nitrobenzamide, 3,5-dinitrobenzamide or 3,5-dinitro-o-toluamide.

M. Taylor, C. Williams, W. H. Hansen, 1969, Food and cosmetics toxicology.

Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol.

S. Müller, T. Gilberger, C. Williams, 1999, Biochemistry.

Characterization of the active center of thioredoxin reductase.

G. Zanetti, C. Williams, 1967, The Journal of biological chemistry.

Pre-column derivatization and high-performance liquid chromatography of biogenic amines in blood of normal and malignant hyperthermic pigs.

C. Gehrke, T. Davis, C. Williams, 1982, Journal of chromatography.

The use of lanthanum chloride to prevent interferences in the flame photometric determination of exchangeable calcium in soils

C. Williams, 1960 .

STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME C REDUCTASE.

B. Masters, Q. Gibson, H. Kamin, 1965, The Journal of biological chemistry.

Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase.

C. Thorpe, C. Williams, 1976, The Journal of biological chemistry.

Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266.

V. Massey, U. Müh, C. Williams, 1994, The Journal of biological chemistry.

Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides.

C. Williams, N. Hopkins, 1995, Biochemistry.

The primary structure of D-amino acid oxidase from pig kidney. I. Isolation and sequence of the tryptic peptides.

M. Galliano, V. Massey, S. Ronchi, 1982, Journal of Biological Chemistry.

Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S.

C. Williams, N. Hopkins, C. Williams, 1995, Biochemistry.

Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from Escherichia coli by alteration of a nearby charged residue, K53R.

J. Guest, V. Massey, C. Williams, 1994, Biochemistry.

Identification of the thiol residues involved in modifications of pig heart lipoamide dehydrogenase by cupric ion and by iodoacetamide.

R. Matthews, C. Williams, 1974, Biochimica et biophysica acta.

A method for titrating oxygen-sensitive organic redox systems with reducing agents in solution.

C. Williams, G. P. Foust, B. Burleigh, 1969, Analytical biochemistry.

Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290.

V. Massey, U. Müh, C. Williams, 1994, The Journal of biological chemistry.

Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain.

J. Guest, V. Massey, C. Williams, 1991, Biochemistry.

Lipoamide dehydrogenase from Escherichia coli. Steady-state kinetics of the physiological reaction.

L. Sahlman, C. Williams, 1989, The Journal of biological chemistry.

NADH inhibition and NAD activation of Escherichia coli lipoamide dehydrogenase catalyzing the NADH-lipoamide reaction.

K. Wilkinson, C. Williams, 1981, The Journal of biological chemistry.

Evidence for multiple electronic forms of two-electron-reduced lipoamide dehydrogenase from Escherichia coli.

K. Wilkinson, C. Williams, 1979, The Journal of biological chemistry.

Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase.

C. Thorpe, C. Williams, 1976, The Journal of biological chemistry.

Titration studies on the active sites of pig heart lipoamide dehydrogenase and yeast glutathione reductase as monitored by the charge transfer absorbance.

L. Sahlman, C. Williams, 1989, Journal of Biological Chemistry.

Reactions of pig heart lipoamide dehydrogenase with pyridine nucleotides. Evidence for an effector role for bound oxidized pyridine nucleotide.

R. Matthews, D. Ballou, C. Williams, 1979, The Journal of biological chemistry.

Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli.

N. Scrutton, R. Perham, A. Berry, 1994, Biochemistry.

Ion pair formation in pig heart lipoamide dehydrogenase: rationalization of pH profiles for reactivity of oxidized enzyme with dihydrolipoamide and 2-electron-reduced enzyme with lipoamide and iodoacetamide.

R. Matthews, C. Thorpe, D. Ballou, 1977, The Journal of biological chemistry.

Studies on lipoyl dehydrogenase from Escherichia coli.

C. Williams, 1965, Journal of Biological Chemistry.

Influence of photoirradiation on the oxidation-reduction state of thioredoxin reductase.

G. Zanetti, V. Massey, C. Williams, 1968, The Journal of biological chemistry.

Effects of low concentrations of guanidine hydrochloride on pig heart lipoamide dehydrogenase.

C. Thorpe, C. Williams, 1974, Biochemistry.

Effect of pyridine nucleotide on the oxidative half-reaction of Escherichia coli thioredoxin reductase.

C. Williams, B. Lennon, 1995, Biochemistry.

Inactivation-reactivation of two-electron reduced Escherichia coli glutathione reductase involving a dimer-monomer equilibrium.

C. Williams, L. Arscott, D. M. Drake, 1989, Biochemistry.

Interactions of guanidinium chloride and pyridine nucleotides with oxidized and two-electron-reduced lipoamide dehydrogenase from Escherichia coli.

K. Wilkinson, C. Williams, 1979, The Journal of biological chemistry.

Redox potentials for yeast, Escherichia coli and human glutathione reductase relative to the NAD+/NADH redox couple: enzyme forms active in catalysis.

C. Williams, L. Arscott, D. M. Veine, 1998, Biochemistry.

The sequence of amino acid residues around the oxidation-reduction active disulfide in yeast glutathione reductase.

C. Williams, E. Jones, 1975, The Journal of biological chemistry.

Modification of pig heart lipoamide dehydrogenase by cupric ions.

C. Thorpe, C. Williams, 1975, Biochemistry.

Sequence around the Active Center Cystine of Lipoamide Dehydrogenase from Pig Heart, Comparison with the E. coli Enzyme

C. Williams, L. Arscott, 1972, Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie.

Thioredoxin reductase-thioredoxin fusion enzyme from Mycobacterium leprae: comparison with the separately expressed thioredoxin reductase.

J. Marcinkeviciene, J. Blanchard, C. Williams, 1998, Biochemistry.

Evidence for direct interaction between cysteine 138 and the flavin in thioredoxin reductase. A study using flavin analogs.

A. Prongay, C. Williams, 1990, The Journal of biological chemistry.

The rapid determination of trace elements in soils and plants by x-ray fluorescence analysis.

C. Williams, 1976, Journal of the science of food and agriculture.

Role of a hydrophobic polypeptide in the N-terminal region of NADPH-cytochrome P-450 reductase in complex formation with P-450LM.

M. J. Coon, S. D. Black, C. Williams, 1979, Biochemical and biophysical research communications.

Thioredoxin-thioredoxin reductase--a system that has come of age.

C. Williams, Charles H. Williams, 2000, European journal of biochemistry.

Extraction, chemical nature, and properties of soil organic sulphur

J. Freney, C. Williams, G. E. Melville, 1969 .

Biogeochemical interactions of carbon, nitrogen, sulfur and phosphorus in Australian agroecosystems.

C. Williams, J. S. Russell, 1982 .

An examination of Jeffries's magnesium ribbon – potassium oxalate method for the removal of free iron oxide in soils

C. Williams, 1950 .

Organic sulphur fractions labelled by addition of 35S-sulphate to soil

J. Freney, C. Williams, G. E. Melville, 1971 .

Specific inhibitors of Plasmodium falciparum thioredoxin reductase as potential antimalarial agents.

C. Nickel, G. L. Kenyon, K. Becker, 2006, Bioorganic & medicinal chemistry letters.

Some factors affecting the mineralization of organic sulphur in soils

C. Williams, 1967, Plant and Soil.

'Crystal-like structures' of boiled beef heart mitochondria.

C. Williams, J. Popinigis, Y. Takahashi, 1972, Biochimica et Biophysica Acta.

Role of active site tyrosine residues in catalysis by human glutathione reductase.

R. Schirmer, R. Krauth-Siegel, C. Williams, 1998, Biochemistry.

Some aspects of mitochondrial structure

C. Williams, J. Popinigis, T. Wakabayashi, 1971, FEBS letters.

Effect of pesticide administration upon esterase activities in serum and tissues of rats fed variable casein diets.

C. Williams, J. L. Casterline, 1969, Toxicology and applied pharmacology.

The determination of cadmium in soils, plants and fertilizers by dithizone extraction and atomic absorption spectroscopy

C. Williams, D. J. David, O. Iismaa, 1972 .

THE DETERMINATION OF CARBON BONDED SULFUR IN SOIL

J. Freney, C. Williams, G. E. Melville, 1970 .

Bioassay of dieldrin for possible carcinogenicity.

J. Robens, G. Newell, C. Williams, 1978, National Cancer Institute carcinogenesis technical report series.

Chemical modifications of D-amino acid oxidase. Evidence for active site histidine, tyrosine, and arginine residues.

V. Massey, T. Nishino, C. Williams, 1980, The Journal of biological chemistry.

Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell.

C. Williams, L. Arscott, D. M. Veine, 2000, Biochemistry.

Improved purification, amino acid analysis and molecular weight of homogenous D-amino acid oxidase from pig kidney.

G. Ferri, S. Ronchi, C. Williams, 1973, Biochimica et biophysica acta.

Peptidases, Peptides, and the Mammalian Blood–Brain Barrier

C. Williams, J. Brownlees, 1993, Journal of neurochemistry.

Endopeptidase 24:11 activity in cerebral microvessels.

C. Williams, J. Brownlees, 1990, Biochemical Society transactions.

Beta-glucuronidase activity in the serum and liver of rats administered pesticides and hepatotoxic agents.

C. Williams, 1969, Toxicology and applied pharmacology.

Aspects of tyrosine metabolism in schizophrenia

C. Williams, 1971, Psychological Medicine.

Synthesis of ketomethylene amino pseudopeptide analogues via reductive amination of glyoxals derived from alpha-amino acids.

C. Williams, M. Mckervey, M. Groarke, 2000, Bioorganic & medicinal chemistry letters.

Assay of neuropeptidases using fluorogenic substrates.

C. Williams, 1997, Methods in molecular biology.

The behaviour of leucine aminopeptidase towards thionopeptides.

C. Williams, D. Guthrie, R. Beattie, 1987, The Biochemical journal.

Microestimation of tryptophan in plasma by a fluorometric procedure

C. Williams, D. King, J. Cairns, 1972 .

Endopeptidase 3.4.24.11 converts N-1-(R,S)carboxy-3-phenylpropyl-Ala-Ala-Phe-p-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme.

D. Walsh, T. Yamamoto, D. Allsop, 1993, The Biochemical journal.

Oxidation of 3-amino-1-phenylprop-1-enes by monoamine oxidase and their use in a continuous assay of the enzyme.

C. Williams, F. Backwell, J. Lawson, 1988, The Biochemical journal.

Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride.

V. Massey, C. Williams, R. Swenson, 1983, The Journal of biological chemistry.

Direct expression of active spinach glycolate oxidase in Escherichia coli.

P. Macheroux, V. Massey, C. Williams, 1992, Biochimica et biophysica acta.

Inhibition and inactivation of monoamine oxidase by 3-amino-1-phenyl-prop-1-enes.

C. Williams, F. Backwell, J. Lawson, 1992, Biochimica et Biophysica Acta.

A new time-dependent reversible inhibitor of monoamine oxidase.

C. Williams, J. Lawson, J. D. Brady, 1996, Journal of enzyme inhibition.

Monoamine oxidase-III. Further studies of inhibition by propargylamines.

C. Williams, J. Lawson, 1975, Biochemical Pharmacology.

Gas chromatographic headspace analysis of sevoflurane in blood.

C. Williams, M. T. Watts, M. Escarzaga, 1992, Journal of chromatography.

The detection of cholinesterase inhibition in erythrocytes of rats fed low levels of the carbamate Banol.

C. Williams, J. L. Casterline, 1967, The Journal of laboratory and clinical medicine.

Synthesis of 14C-labeled inhibitors of monoamine oxidase

C. Williams, 1981 .

A comparison of two methods for the measurement of erythrocyte cholinesterase inhibition after carbamate administration to rats.

C. Williams, J. L. Casterline, 1969, Food and cosmetics toxicology.

STUDIES ON THE ASSOCIATION OF P-450 LM2 WITH NADPH-CYTOCHROME P-450 REDUCTASE AND WITH TRYPTIC PEPTIDES DERIVED FROM THE REDUCTASE

M. J. Coon, S. D. Black, C. Williams, 1980 .

Immunochemical characterisation of tachykinin immunoreactivity in the central nervous system of the snail, Helix aspersa

G. Irvine, C. Shaw, C. Williams, 1991, Regulatory Peptides.

Beta-glucuronidase activity in the serum and liver of rats treated with parathion.

C. Williams, 1970, Toxicology and applied pharmacology.

A microsomal TPNH-neotetrazolium diaphorase.

H. Kamin, C. Williams, R. Gibbs, 1959, Biochimica et biophysica acta.

Graphical analysis of interactions between oxidation-reduction sites in two site oxidation-reduction proteins.

C. Williams, M. O'Donnell, 1984, Analytical biochemistry.

Oxidation-reduction properties of Escherichia coli thioredoxin reductase altered at each active site cysteine residue.

A. Prongay, C. Williams, 1992, The Journal of biological chemistry.