P. Brown

发表

Microwave absorption in aqueous solutions of DNA

C. Gabriel, E. Grant, R. Tata, 1987, Nature.

Dielectric behavior of aqueous solutions of plasmid DNA at microwave frequencies.

C. Gabriel, E. Grant, R. Tata, 1989, Biophysical journal.

One-step affinity purification of urease from jack beans.

P. Brown, A. Karmali, M. Mendes, 1988, Biochimie.

One-step affinity purification of amidase from mutant strains of Pseudomonas aeruginosa.

P. Brown, A. Karmali, A. Domingos, 1989, Biochimie.

Burkholderia genome analysis reveals new enzymes belonging to the nitrilase superfamily. The amidase of Burkholderia cepacia (hospital isolate).

R. Tata, P. Brown, C. Novo, 2003, International journal of biological macromolecules.

The subunit structure of the aliphatic amidase from Pseudomonas aeruginosa.

P. Brown, P. H. Clarke, M. Rosemeyer, 1973, European journal of biochemistry.

A monoclonal antibody specific for Pseudomonas aeruginosa amidase.

P. Brown, A. Karmali, C. Novo, 2001, Hybridoma.

Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.

R. Tata, P. Brown, S. Farnaud, 2002, The Biochemical journal.

Substitutions of Thr-103-Ile and Trp-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetic properties and enzyme instability

R. Tata, P. Brown, A. Karmali, 2001, Molecular biotechnology.

Substitution of Glu-59 by val in amidase from Pseudomonas aeruginosa results in a catalytically inactive enzyme

R. Tata, P. Brown, A. Karmali, 2000, Molecular biotechnology.

Evidence that cysteine-166 is the active-site nucleophile of Pseudomonas aeruginosa amidase: crystallization and preliminary X-ray diffraction analysis of the enzyme.

R. Tata, P. Brown, B. Sutton, 1999, The Biochemical journal.

Arg-188 and Trp-144 are implicated in the binding of urea and acetamide to the active site of the amidase from Pseudomonas aeruginosa.

R. Tata, P. Brown, P. Marsh, 1994, Biochimica et biophysica acta.

Inhibition of the aliphatic amidase from Pseudomonas aeruginosa by urea and related compounds.

P. Brown, M. Gregoriou, 1979, European journal of biochemistry.

Pseudomonas aeruginosa mutants resistant to urea inhibition of growth on acetanilide

R. Tata, P. Brown, M. Gregoriou, 1977, Journal of bacteriology.

Adaptation to phenylacetamide as a growth substrate by an acetanilide-utilizing mutant of Pseudomonas aeruginosa

P. Brown, M. Gregoriou, 1980, Archives of Microbiology.

Mutations affecting the synthesis of NADP-dependent glutamate dehydrogenase in Pseudomonas aeruginosa.

R. Tata, P. Brown, C. Joannou, 1988, Journal of general microbiology.

Evolution in Action

P. Brown, P. H. Clarke, J. L. Betz, 1974, Nature.

Relationship between mutant amidases of Pseudomonas aeruginosa and hydroxyurea as an inhibitor

R. Tata, P. Brown, M. Gregoriou, 1978, Molecular and General Genetics MGG.

Butyramide-utilizing mutants of Pseudomonas aeruginosa 8602 which produce an amidase with altered substrate specificity.

P. Brown, J. Brown, P. H. Clarke, 1969, Journal of general microbiology.

Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1.

R. Tata, P. Brown, B. Sutton, 2009, Biochimie.

l-Methionine sulfoximine, but not phosphinothricin, is a substrate for an acetyltransferase (gene PA4866) from Pseudomonas aeruginosa: structural and functional studies.

R. Tata, P. Brown, B. Sutton, 2007, Biochemistry.

Dielectric properties of the system bovine albumin: urea: betaine in aqueous solution.

C. Gabriel, E. Grant, P. Brown, 1992, Physics in medicine and biology.

Crystal assembly and phylogenetic evolution in heterococcoliths

Stephen Mann, P. Brown, S. Mann, 1992, Nature.

Pseudomonas aeruginosa aliphatic amidase is related to the nitrilase/cyanide hydratase enzyme family and Cys166 is predicted to be the active site nucleophile of the catalytic mechanism

R. Tata, P. Brown, A. Clemente, 1995, FEBS letters.

Growth of Pseudomonas aeruginosa mutants lacking glutamate synthase activity

R. Tata, P. Brown, 1981, Journal of bacteriology.

Crystal structure of a putative phosphinothricin acetyltransferase (PA4866) from Pseudomonas aeruginosa PAC1

R. Tata, P. Brown, B. Sutton, 2005, Proteins.

Isolation of amidase-negative mutants of Pseudomonas aeruginosa using glycollamide as a selective agent.

R. Tata, P. Brown, 1987, Journal of general microbiology.

Amino acid substitution in an amidase produced by an acetanilide-utilizing mutant of Pseudomonas aeruginosa.

P. Brown, P. H. Clarke, 1972, Journal of general microbiology.