B W Matthews

发表

Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile.

B. Matthews, L. Weaver, M. Grütter, 1987, Journal of molecular biology.

Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin.

B. Matthews, B. Roques, S. Roderick, 1989, Biochemistry.

Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.

B. Matthews, W. Baase, F. Dahlquist, 1999, Biochemistry.

Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme

B. Matthews, W. Baase, Michael L. Quillin, 2001, Protein science : a publication of the Protein Society.

Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme.

B. Matthews, H. Nicholson, S. Dao-pin, 1991, Biochemistry.

Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking.

B. Matthews, D. Heinz, B W Matthews, 1994, Protein engineering.

Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor.

D E Tronrud, B. Matthews, M. Holmes, 1983, Biochemistry.

A systematic approach to the comparison of protein structures.

S J Remington, B. Matthews, S. Remington, 1980, Journal of molecular biology.

Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues.

H M Holden, D E Tronrud, B. Matthews, 1989, Biochemistry.

The conformation of thermolysin.

B. Matthews, L. Weaver, W. R. Kester, 1974, The Journal of biological chemistry.

Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.

B. Matthews, K. Wilson, L. Shewchuk, 1992, Proceedings of the National Academy of Sciences of the United States of America.

The introduction of strain and its effects on the structure and stability of T4 lysozyme.

B. Matthews, W. Baase, B W Matthews, 1999, Journal of molecular biology.

The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme.

B. Matthews, W. Baase, E. Baldwin, 1994, Science.

The response of T4 lysozyme to large‐to‐small substitutions within the core and its relation to the hydrophobic effect

B. Matthews, W. Baase, J. Xu, 1998, Protein science : a publication of the Protein Society.

A general method to assess similarity of protein structures, with applications to T4 bacteriophage lysozyme.

S J Remington, B. Matthews, S. Remington, 1978, Proceedings of the National Academy of Sciences of the United States of America.

A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substances.

B. Matthews, L. Weaver, W. R. Kester, 1977, Journal of molecular biology.

Comparison of the structures of carboxypeptidase A and thermolysin.

B. Matthews, W. R. Kester, B W Matthews, 1977, The Journal of biological chemistry.

Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme.

D E Tronrud, E Söderlind, B. Matthews, 1990, Journal of molecular biology.

Studies on protein stability with T4 lysozyme.

B. Matthews, B W Matthews, 1995, Advances in protein chemistry.

Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis.

B. Matthews, M. Holmes, B W Matthews, 1982, Biochemistry.

Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme.

I R Vetter, B. Matthews, C. Bustamante, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.

J A Wozniak, B. Matthews, W. Baase, 1991 .

The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis.

H M Holden, B. Matthews, H. Holden, 1989, The Journal of biological chemistry.

Structural and genetic analysis of electrostatic and other interactions in bacteriophage T4 lysozyme.

J A Wozniak, B. Matthews, H. Nicholson, 1991, Ciba Foundation symposium.

Structural analysis of zinc substitutions in the active site of thermolysin

D. R. Holland, B. Matthews, A. Hausrath, 1995, Protein science : a publication of the Protein Society.

Context‐dependent protein stabilization by methionine‐to‐leucine substitution shown in T4 lysozyme

L. A. Lipscomb, W. Baase, N. Gassner, 1998, Protein science : a publication of the Protein Society.

An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides.

B. Matthews, A. Monzingo, D. Hangauer, 1984, Biochemistry.

Structure of a mercaptan-thermolysin complex illustrates mode of inhibition of zinc proteases by substrate-analogue mercaptans.

B. Matthews, A. Monzingo, B W Matthews, 1982, Biochemistry.

Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.

J A Wozniak, E Söderlind, U. Sauer, 1991, Journal of molecular biology.

Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent

B. Matthews, B W Matthews, P Pjura, 1993, Protein science : a publication of the Protein Society.

Three-dimensional structure of human basic fibroblast growth factor.

B. Matthews, A. Eriksson, L. Weaver, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein.

B. Matthews, D. P. Sun, T. Alber, 1987, Biochemistry.

A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme.

B. Matthews, W. Baase, N. Gassner, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin.

D E Tronrud, B. Matthews, D. Tronrud, 1989, European journal of biochemistry.

Stabilization of phage T4 lysozyme by engineered disulfide bonds.

M Levitt, M. Levitt, B. Matthews, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site.

B. Matthews, W. Baase, X. Zhang, 2000, Protein engineering.

Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59.

U. Sauer, B. Matthews, W. Baase, 1992, Biochemistry.

Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid.

B. Matthews, T M Gray, B W Matthews, 1988, The Journal of biological chemistry.

Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A.

B. Matthews, A. Hausrath, B W Matthews, 1994, The Journal of biological chemistry.

Hydrophobic core repacking and aromatic–aromatic interaction in the thermostable mutant of T4 lysozyme ser 117 → phe

D. E. Anderson, B. Matthews, J. Hurley, 1993, Protein science : a publication of the Protein Society.

B. Matthews, W. Baase, A. Eriksson, 1993, Journal of molecular biology.

Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.

B. Matthews, W. Baase, L. Weaver, 1999, Journal of molecular biology.

Kinetic studies on Cro repressor-operator DNA interaction.

B. Matthews, W. Anderson, J. Kim, 1987, Journal of molecular biology.

The structure of thermolysin: an electron density map at 2-3 A resolution.

B. Matthews, P. Colman, J. Jansonius, 1972, Journal of molecular biology.

Structure and thermal stability of phage T4 lysozyme.

B. Matthews, T. Alber, B W Matthews, 1987, Methods in enzymology.

Control of enzyme activity by an engineered disulfide bond.

B. Matthews, M. Matsumura, B W Matthews, 1994, Science.

Conservation of solvent‐binding sites in 10 crystal forms of T4 lysozyme

B. Matthews, X. Zhang, B W Matthews, 1994, Protein science : a publication of the Protein Society.

Multiple alanine replacements within α‐helix 126–134 of T4 lysozyme have independent, additive effects on both structure and stability

B. Matthews, W. Baase, X. Zhang, 1991, Protein science : a publication of the Protein Society.

Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants.

B. Matthews, M. Matsumura, W. Baase, 1989, Proceedings of the National Academy of Sciences of the United States of America.

High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His.

J A Wozniak, B. Matthews, D. E. Anderson, 1989, Biochemistry.

Core-packing constraints, hydrophobicity and protein design.

B. Matthews, E. Baldwin, B W Matthews, 1994, Current opinion in biotechnology.

Atomic coordinates for T4 phage lysozyme.

S J Remington, B. Matthews, S. Remington, 1977, Biochemical and biophysical research communications.

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes.

R A Bradshaw, B. Matthews, S. Arfin, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?

B. Matthews, B W Matthews, M M Dixon, 1989, Biochemistry.

Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.

B. Matthews, M. Blaber, D. Heinz, 1993, Biochemistry.

Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.

J A Wozniak, B. Matthews, D. P. Sun, 1990, Science.

Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.

B. Matthews, H. Nicholson, W. Becktel, 1988, Nature.

Comparison of protein structures.

M G Rossmann, B. Matthews, M. Rossmann, 1985, Methods in enzymology.

Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.

B. Matthews, K. Wilson, B. Malcolm, 1993, The Journal of biological chemistry.

Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme.

B. Matthews, J. Hurley, W. Baase, 1993, Journal of molecular biology.

Structure and X-ray amino acid sequence of a bacteriochlorophyll A protein from Prosthecochloris aestuarii refined at 1.9 A resolution.

M F Schmid, D E Tronrud, B. Matthews, 1986, Journal of molecular biology.

A relationship between protein stability and protein function.

B K Shoichet, B. Matthews, B. Shoichet, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Three-dimensional structure of tosyl-alpha-chymotrypsin.

R Henderson, P B Sigler, D M Blow, 1967, Nature.

Structural basis of amino acid alpha helix propensity.

B. Matthews, M. Blaber, X. Zhang, 1993, Science.

Enhancement of the method of molecular replacement by incorporation of known structural information.

B W Matthews, X J Zhang, Xuejun C. Zhang, 1994, Acta crystallographica. Section D, Biological crystallography.

Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.

B. Matthews, M. He, B W Matthews, 2000, Biochemistry.

Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins.

B. Matthews, T M Gray, B W Matthews, 1984, Journal of molecular biology.

The helix-turn-helix DNA binding motif.

B. Matthews, R. Brennan, B W Matthews, 1989, The Journal of biological chemistry.

Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases.

B. Matthews, A. Monzingo, B W Matthews, 1984, Biochemistry.

Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond.

H M Holden, D E Tronrud, B. Matthews, 1987, Science.

Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3-->Pro.

B. Matthews, H. Nicholson, W. Baase, 1993, Journal of molecular biology.

Nerve growth factor in different crystal forms displays structural flexibility and reveals zinc binding sites.

D. R. Holland, B. Matthews, L. Cousens, 1994, Journal of molecular biology.

Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity.

B. Matthews, A. Morton, B W Matthews, 1995, Biochemistry.

Relation between hen egg white lysozyme and bacteriophage T4 lysozyme: evolutionary implications.

S J Remington, B. Matthews, S. Remington, 1981, Journal of molecular biology.

Three-dimensional structure of thermolysin.

B P Schoenborn, B. Matthews, B. Schoenborn, 1972, Nature: New biology.

Structure of thermolysin refined at 1.6 A resolution.

B. Matthews, M. Holmes, B W Matthews, 1982, Journal of molecular biology.

Genetic and structural analysis of the protein stability problem.

B. Matthews, B W Matthews, Brian W. Matthews, 1987, Biochemistry.

Stabilization of functional proteins by introduction of multiple disulfide bonds.

B. Matthews, M. Matsumura, B W Matthews, 1991, Methods in enzymology.

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.

B. Matthews, H. Nicholson, W. Becktel, 1987, Proceedings of the National Academy of Sciences of the United States of America.

The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue.

B. Matthews, L. Weaver, M. Grütter, 1995, Journal of molecular biology.

Structural and genetic analysis of protein stability.

B. Matthews, B W Matthews, 1993, Annual review of biochemistry.

The structure of a repressor: crystallographic data for the Cro regulatory protein of bacteriophage lambda.

B. Matthews, H. Echols, W. Anderson, 1979, Journal of molecular biology.

Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive.

B K Shoichet, B. Matthews, B. Shoichet, 1995, Protein engineering.

Structure of a stabilizing disulfide bridge mutant that closes the active‐site cleft of T4 lysozyme

B. Matthews, M. Matsumura, H. R. Faber, 1992, Protein science : a publication of the Protein Society.