J. Knox

发表

Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution.

C. Walsh, C. Fan, P. Moews, 1994, Science.

On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target.

J. Frère, J. Ghuysen, B. Joris, 1986, Science.

Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure

J. Knox, J R Knox, 1995, Antimicrobial agents and chemotherapy.

Characterization of a new TEM-derived beta-lactamase produced in a Serratia marcescens strain

A. Oratore, G. Rossolini, F. Luzzaro, 1997, Antimicrobial agents and chemotherapy.

Preliminary crystallographic data for Escherichia coli β-lactamase

N. Murthy, J. Knox, P. Zorsky, 1973 .

Biodegradable polymers: Chymotrypsin degradation of a low molecular weight poly(ester‐urea) containing phenylalanine

S. Huang, J. Knox, D. Bansleben, 1979 .

Crystallization and preliminary X-ray data for the exocellular beta-lactamase of Bacillus licheniformis 749/C.

J. Frère, P. Charlier, O. Dideberg, 1985, Journal of molecular biology.

The Photosynthetic Bacterial Reaction Center

J. Knox, S. Taremi, 1988, NATO ASI Series.

Crystallographic data for a penicillin receptor : exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61.

J. Frère, J. Ghuysen, N. Murthy, 1979, Journal of molecular biology.

D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant.

C. Walsh, C. Fan, J. Knox, 1997, Biochemistry.

The Effects of Some Structural Variations on the Biodegradability of Step-Growth Polymers

K. Leong, S. Huang, J. Knox, 1978 .

Tertiary and secondary structure analysis of penicillin-binding proteins.

M. Delucia, P. Moews, J. Knox, 1980, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Interactions between active-site-serine beta-lactamases and compounds bearing a methoxy side chain on the alpha-face of the beta-lactam ring: kinetic and molecular modelling studies.

J. Frère, G. Dive, J. Lamotte‐Brasseur, 1993, The Biochemical journal.

BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C. REFINEMENT AT 2 ANGSTROMS RESOLUTION AND ANALYSIS OF HYDRATION

P. Moews, J. Knox, 1993 .

D-alanine-D-alanine ligase (ADP) from Salmonella typhimurium. Overproduction, purification, crystallization and preliminary X-ray analysis.

C. Walsh, L. Zawadzke, J. Knox, 1989, Journal of molecular biology.

Crystallographic data for the β-lactamase from Enterobacter cloacae P99

J. Frère, P. Charlier, O. Dideberg, 1983 .

The association behavior of β‐lactamases in polyethylene glycol solution

N. Murthy, J. Knox, E. Braswell, 1988 .

Single Crystals of the Photochemical Reaction Center from Rhodobacter sphaeroides Wild Type Strain 2.4.1 Analyzed by Polarized Light

W. Mäntele, H. Frank, J. Knox, 1988 .

Crystallization and preliminary X-ray and optical spectroscopic characterization of the photochemical reaction center from Rhodobacter sphaeroides strain 2.4.1.

H. Frank, J. Knox, S. Taremi, 1987, Journal of molecular biology.

Crystallite orientation in heat shrinkable polytetrafluoroethylene tubing

J. Knox, S. Petrie, 1976 .

Synthesis and Testing of Biodegradable Fiber-Forming Polymers

K. Leong, J. P. Bell, S. Huang, 1977 .

J. Knox, M. Lockett, 1969, The Journal of endocrinology.

The structure of a cysteine complex of molybdenum(V): Na2Mo2O4[SCH2CH(NH2)CO2]2.5H2O

J. Knox, C. Prout, 1969 .

beta-Lactamase mutations far from the active site influence inhibitor binding.

R. Bonomo, J. Knox, D. Shlaes, 1995, Biochimica et biophysica acta.

Structure-activity relationship of 6-methylidene penems bearing tricyclic heterocycles as broad-spectrum beta-lactamase inhibitors: crystallographic structures show unexpected binding of 1,4-thiazepine intermediates.

R. Bonomo, A. Hujer, A. Agarwal, 2004, Journal of medicinal chemistry.

β‐Lactamase of Bacillus licheniformis 749/C at 2 Å resolution

J. Frère, P. Charlier, O. Dideberg, 1990 .

The crystal and molecular structure of bis-π-cyclopentadienyl(2-aminoethanethiolato)molybdenum iodide

J. Knox, C. Prout, 1969 .

Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog.

E. Billings, R. Pratt, J. Rahil, 1994, Biochemistry.

Vancomycin resistance in enterococci: reprogramming of the D-ala-D-Ala ligases in bacterial peptidoglycan biosynthesis.

C. Walsh, D. Roper, J. Knox, 2000, Chemistry & biology.

Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein

R. Pratt, J. Knox, 1990, Antimicrobial Agents and Chemotherapy.

Structure-activity relationship of 6-methylidene penems bearing 6,5 bicyclic heterocycles as broad-spectrum beta-lactamase inhibitors: evidence for 1,4-thiazepine intermediates with C7 R stereochemistry by computational methods.

A. Agarwal, T. Mansour, J. Knox, 2006, Journal of medicinal chemistry.

The crystal structure of a molybdenum(III) hexaisothiocyanate

J. Knox, K. Eriks, 1968 .

The structure of bis‐π‐cyclopentadienyl(toluene‐3,4‐dithiolato)molybdenum

J. Knox, C. K. Prout, 1969 .

The structure of a nitrogeno–molybdenum carbene chelate: π-C5H5(CO)2MoN(H)NC(CO2C2H5)COH

J. Knox, C. Prout, 1969 .

The crystal structure of 1-decyl .alpha.-D-glucopyranoside: a polar bilayer with a hydrocarbon subcell

P. Moews, J. Knox, 1976 .

Mutational Replacement of Leu-293 in the Class C Enterobacter cloacae P99 β-Lactamase Confers Increased MIC of Cefepime

S. Mobashery, S. Vakulenko, S. Lerner, 2002, Antimicrobial Agents and Chemotherapy.

Structure-Function Studies of Ser-289 in the Class C β-Lactamase from Enterobacter cloacae P99

A. Huletsky, F. Sanschagrin, N. Clairoux, 1999, Antimicrobial Agents and Chemotherapy.

Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase.

J. Frère, H. Zhao, P. Moews, 1993, Proceedings of the National Academy of Sciences of the United States of America.

The crystal and molecular structure of γ‐oxobis[bis(diethyldithiophosphato)oxomolybdenum(V)]–1,2‐dichlorobenzene, Mo2O3[S2P(OC2H5)2]4.2C6H4Cl2

J. Knox, C. Prout, 1969 .

Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam.

R. Bonomo, A. Hujer, A. Kuzin, 2001, Biochemistry.

Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme.

R. Bonomo, V. Anderson, J. Knox, 1998, The Biochemical journal.

Complementary roles of mutations at positions 69 and 242 in a class A beta-lactamase.

R. Bonomo, J. Knox, D. Shlaes, 1995, Biochimica et Biophysica Acta.

The enigmatic catalytic mechanism of active-site serine β-lactamases

Alain Dubus, Moreno Galleni, J. Frère, 1995 .

A crystallographic study of alkaline phosphatase at 7.7 Å resolution

H. Wyckoff, J. Knox, 1973 .

2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams.

J M Ghuysen, J. Frère, J. Ghuysen, 1986, The Journal of biological chemistry.

The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A.

A. W. Hanson, F M Richards, D Tsernoglou, 1970, The Journal of biological chemistry.

Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases.

A. Kuzin, J. Knox, J R Knox, 1995, Biochemistry.

Order parameter measurements in polypeptide liquid crystals

E. Samulski, N. Murthy, J. Knox, 1976 .

Ultrahigh resolution structure of a class A beta-lactamase: on the mechanism and specificity of the extended-spectrum SHV-2 enzyme.

Robert A Bonomo, R. Bonomo, A. Hujer, 2003, Journal of molecular biology.

Hydrolysis of third-generation cephalosporins by class C beta-lactamases. Structures of a transition state analog of cefotoxamine in wild-type and extended spectrum enzymes.

Sanjai Kumar, R. Pratt, J. Knox, 2004, The Journal of biological chemistry.

Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion.

T. Sawai, A. Kuzin, J. Knox, 1999, Biochemistry.

The Structures and Catalytic Mechanisms of Active-Site Serine β-Lactamases

Otto Dideberg, Paulette Charlier, J. Frère, 1994 .

Structure of the SHV-1 beta-lactamase.

R. Bonomo, A. Hujer, A. Kuzin, 1999, Biochemistry.

Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins.

N. Silvaggi, R. Pratt, M. McDonough, 2002, Journal of molecular biology.

Hydrolysis of Third-generation Cephalosporins by Class C β-Lactamases

Sanjai Kumar, R. Pratt, J. Knox, 2004, Journal of Biological Chemistry.

A structure-based analysis of the inhibition of class A beta-lactamases by sulbactam.

S. Mobashery, E. Billings, J. Knox, 1994, Biochemistry.

Structure-Function Studies of Ser-289 in the Class C b-Lactamase from Enterobacter cloacae P 99

A. Huletsky, F. Sanschagrin, N. Clairoux, 1998 .

Molecular evolution of bacterial β-lactam resistance

J. Frère, P. Moews, J. Knox, 1996 .

Construction and characterization of an OHIO-1 beta-lactamase bearing Met69Ile and Gly238Ser mutations

R. Bonomo, J. Knox, D. Shlaes, 1997, Antimicrobial agents and chemotherapy.

Inhibition of class A and class C beta-lactamases by penems: crystallographic structures of a novel 1,4-thiazepine intermediate.

R. Bonomo, T. Mansour, J. Knox, 2003, Biochemistry.

Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone.

J. Knox, J. Buynak, G V Crichlow, 2001, Biochemistry.

Predicted secondary structures of four penicillin beta-lactamases and a comparison with two lysozymes.

P. Moews, J. Knox, 2009, International journal of peptide and protein research.

Secondary structure relations between beta-lactamases and penicillin-sensitive D-alanine-carboxypeptidases.

J. Strominger, D. Waxman, P. Moews, 2009, International journal of peptide and protein research.

5.5 Å crystallographic structure of penicillin β-lactamase and radius of gyration in solution☆

N. Murthy, P. Moews, J. Knox, 1976 .

Interactive graphics for rapid indexing of oscillation films from large unit cells

P. Moews, J. Knox, T. Sakamaki, 1986 .

Penicillin target enzyme and the antibiotic binding site.

J M Ghuysen, J. Frère, J. Ghuysen, 1982, Science.

A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli.

C. Walsh, Y. Shi, C. Fan, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Comparison of β‐lactamases of classes A and D: 1.5‐Å crystallographic structure of the class D OXA‐1 oxacillinase

Tao Sun, J. Knox, T. Sun, 2003, Protein science : a publication of the Protein Society.

Crystallization and preliminary X-ray study of OXA-1, a class D β-lactamase

A. Kuzin, J. Knox, T. Sun, 2001 .

Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration.

P. Moews, J. Knox, J R Knox, 1991, Journal of molecular biology.

Hydration of proteins: SAXS study of native and methoxy polyethyleneglycol (mPEG)‐modified L‐asparaginase and bovine serum albumin in mPEG solutions

N. Murthy, J. Knox, 2004, Biopolymers.

Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration.

P. Moews, J. Knox, 1991 .

Modification of the Rigaku-Denki x-ray goniometer with Kratky collimator for weakly scattering solutions.

N. Murthy, J. Knox, 1976, Journal of Physics E Scientific Instruments.

Inhibition of class A beta-lactamases by carbapenems: crystallographic observation of two conformations of meropenem in SHV-1.

R. Bonomo, A. Hujer, V. Anderson, 2008, Journal of the American Chemical Society.

Inactivation of class A β-lactamases by clavulanic acid : the role of arginine-244 in a proposed nonconcerted sequence of events

Eric M. Billings, S. Mobashery, E. Billings, 1993 .

A catalytically-impaired class A beta-lactamase: 2 A crystal structure and kinetics of the Bacillus licheniformis E166A mutant.

A. Fink, P. Moews, J. Knox, 1993, Protein Engineering.

Inhibitor-resistant class A beta-lactamases: consequences of the Ser130-to-Gly mutation seen in Apo and tazobactam structures of the SHV-1 variant.

R. Bonomo, C. Bethel, J. Knox, 2004, Biochemistry.

Molecular evolution of bacterial beta-lactam resistance.

J. Frère, P. Moews, J. Knox, 1996, Chemistry & biology.

Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type beta-lactamases probed by site-directed mutagenesis and three-dimensional modeling.

A. Huletsky, J. Knox, R. Lévesque, 1993, The Journal of biological chemistry.

The enigmatic catalytic mechanism of active-site serine beta-lactamases.

J. Frère, A. Dubus, M. Galleni, 1995, Biochemical pharmacology.

Small-angle X-ray scattering studies of Escherichia colil-asparaginase

N. Murthy, J. Knox, 1976 .

Small-angle x-ray scattering studies of Escherichia coli L-asparaginase.

N. Murthy, J. Knox, 1976, Journal of Molecular Biology.

Site-saturation mutagenesis and three-dimensional modelling of ROB-1 define a substrate binding role of Ser130 in class A beta-lactamases.

E. Billings, J. Knox, R. Lévesque, 1992, Protein engineering.

Enzymes of vancomycin resistance: the structure of D-alanine-D-lactate ligase of naturally resistant Leuconostoc mesenteroides.

C. Walsh, A. Kuzin, J. Knox, 2000, Structure.

Crystallographic mapping of beta-lactams bound to a D-alanyl-D-alanine peptidase target enzyme.

J. Frère, J. Ghuysen, J. Knox, 1989, Journal of molecular biology.

The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.

J M Ghuysen, J. Frère, G. Dive, 1988, The Biochemical journal.

Side‐chain conformation in poly(γ‐phenethyl‐L‐glutamate)

E. Samulski, J. Knox, J. A. Lefelar, 1983 .

On Soulé‐Porod plots of protein X‐ray scattering data

N. Murthy, J. Knox, 1977 .

Studying enzyme-β-lactam interactions using X-ray diffraction*

J. Knox, J. A. Kelly, Haiching Zhao, 1989 .