Year |
Citation |
Score |
2021 |
Branch J, Rajagopal BS, Paradisi A, Yates N, Lindley PJ, Smith J, Hollingsworth K, Turnbull B, Henrissat B, Parkin A, Berry A, Hemsworth GR. C-type cytochrome-initiated reduction of bacterial lytic polysaccharide monooxygenases. The Biochemical Journal. PMID 34240737 DOI: 10.1042/BCJ20210376 |
0.32 |
|
2019 |
Drulyte I, Obajdin J, Trinh CH, Kalverda AP, van der Kamp MW, Hemsworth GR, Berry A. Crystal structure of the putative cyclase IdmH from the indanomycin nonribosomal peptide synthase/polyketide synthase. Iucrj. 6: 1120-1133. PMID 31709067 DOI: 10.1107/S2052252519012399 |
0.316 |
|
2017 |
Windle CL, Simmons KJ, Ault JR, Trinh CH, Nelson A, Pearson AR, Berry A. Extending enzyme molecular recognition with an expanded amino acid alphabet. Proceedings of the National Academy of Sciences of the United States of America. PMID 28196894 DOI: 10.1073/Pnas.1616816114 |
0.442 |
|
2014 |
Windle CL, Müller M, Nelson A, Berry A. Engineering aldolases as biocatalysts. Current Opinion in Chemical Biology. 19: 25-33. PMID 24780276 DOI: 10.1016/J.Cbpa.2013.12.010 |
0.35 |
|
2014 |
Daniels AD, Campeotto I, van der Kamp MW, Bolt AH, Trinh CH, Phillips SE, Pearson AR, Nelson A, Mulholland AJ, Berry A. Reaction mechanism of N-acetylneuraminic acid lyase revealed by a combination of crystallography, QM/MM simulation, and mutagenesis. Acs Chemical Biology. 9: 1025-32. PMID 24521460 DOI: 10.1021/Cb500067Z |
0.446 |
|
2013 |
Timms N, Windle CL, Polyakova A, Ault JR, Trinh CH, Pearson AR, Nelson A, Berry A. Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with γ-thialysine by using a chemical mutagenesis strategy. Chembiochem : a European Journal of Chemical Biology. 14: 474-81. PMID 23418011 DOI: 10.1002/Cbic.201200714 |
0.448 |
|
2010 |
Campeotto I, Bolt AH, Harman TA, Dennis C, Trinh CH, Phillips SE, Nelson A, Pearson AR, Berry A. Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution. Journal of Molecular Biology. 404: 56-69. PMID 20826162 DOI: 10.1016/J.Jmb.2010.08.008 |
0.332 |
|
2010 |
Horsfall LE, Nelson A, Berry A. Identification and characterization of important residues in the catalytic mechanism of CMP-Neu5Ac synthetase from Neisseria meningitidis. The Febs Journal. 277: 2779-90. PMID 20491913 DOI: 10.1111/J.1742-4658.2010.07696.X |
0.446 |
|
2009 |
Campeotto I, Carr SB, Trinh CH, Nelson AS, Berry A, Phillips SE, Pearson AR. Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 1088-90. PMID 19923724 DOI: 10.1107/S1744309109037403 |
0.327 |
|
2007 |
Nelson A, Williams G, Woodhall T, Farnsworth L, Berry A. Stereochemically Complementary Biocatalysts Created by Directed Evolution Synfacts. 2007: 0208-0208. DOI: 10.1055/S-2006-955791 |
0.469 |
|
2006 |
Williams GJ, Woodhall T, Farnsworth LM, Nelson A, Berry A. Creation of a pair of stereochemically complementary biocatalysts. Journal of the American Chemical Society. 128: 16238-47. PMID 17165777 DOI: 10.1021/ja065233q |
0.539 |
|
2005 |
Williams GJ, Woodhall T, Nelson A, Berry A. Structure-guided saturation mutagenesis of N-acetylneuraminic acid lyase for the synthesis of sialic acid mimetics. Protein Engineering, Design & Selection : Peds. 18: 239-46. PMID 15897188 DOI: 10.1093/Protein/Gzi027 |
0.568 |
|
2005 |
Woodhall T, Williams G, Berry A, Nelson A. Synthesis of screening substrates for the directed evolution of sialic acid aldolase: towards tailored enzymes for the preparation of influenza A sialidase inhibitor analogues. Organic & Biomolecular Chemistry. 3: 1795-800. PMID 15858666 DOI: 10.1039/B501503K |
0.475 |
|
2005 |
Woodhall T, Williams G, Berry A, Nelson A. Creation of a tailored aldolase for the parallel synthesis of sialic acid mimetics. Angewandte Chemie (International Ed. in English). 44: 2109-12. PMID 15742315 DOI: 10.1002/Anie.200462733 |
0.471 |
|
2005 |
Williams GJ, Nelson AS, Berry A. Directed evolution of enzymes for biocatalysis and the life sciences. Cellular and Molecular Life Sciences : Cmls. 61: 3034-46. PMID 15583865 DOI: 10.1007/s00018-004-4234-5 |
0.349 |
|
2003 |
Williams GJ, Domann S, Nelson A, Berry A. Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution. Proceedings of the National Academy of Sciences of the United States of America. 100: 3143-8. PMID 12626743 DOI: 10.1073/Pnas.0635924100 |
0.55 |
|
2003 |
Suryanti V, Nelson A, Berry A. Cloning, over-expression, purification, and characterisation of N-acetylneuraminate synthase from Streptococcus agalactiae Protein Expression and Purification. 27: 346-356. PMID 12597896 DOI: 10.1016/S1046-5928(02)00633-2 |
0.418 |
|
2003 |
Williams GJ, Berry A. Directed evolution: Creating new enzymes The Biochemist. 25: 13-15. DOI: 10.1042/bio02504013 |
0.608 |
|
2002 |
Hümbelin M, Thomas A, Lin J, Li J, Jore J, Berry A. Genetics of isoprenoid biosynthesis in Paracoccus zeaxanthinifaciens. Gene. 297: 129-39. PMID 12384294 DOI: 10.1016/s0378-1119(02)00877-6 |
0.367 |
|
2002 |
Hall DR, Bond CS, Leonard GA, Watt CI, Berry A, Hunter WN. Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolases. The Journal of Biological Chemistry. 277: 22018-24. PMID 11940603 DOI: 10.1074/jbc.M202464200 |
0.4 |
|
2002 |
Zgiby S, Plater AR, Bates MA, Thomson GJ, Berry A. A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli. Journal of Molecular Biology. 315: 131-40. PMID 11779234 DOI: 10.1006/jmbi.2001.5237 |
0.499 |
|
2000 |
Zgiby SM, Thomson GJ, Qamar S, Berry A. Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases. European Journal of Biochemistry. 267: 1858-68. PMID 10712619 DOI: 10.1046/J.1432-1327.2000.01191.X |
0.483 |
|
2000 |
Williams G, Nelson A, Berry A. Engineering the Mechanisms of C-C Bond Forming Enzymes Biochemical Society Transactions. 28: A70-A70. DOI: 10.1042/Bst028A070 |
0.541 |
|
1999 |
Plater AR, Zgiby SM, Thomson GJ, Qamar S, Wharton CW, Berry A. Conserved residues in the mechanism of the E. coli Class II FBP-aldolase. Journal of Molecular Biology. 285: 843-55. PMID 9878448 DOI: 10.1006/JMBI.1998.2376 |
0.436 |
|
1998 |
Thomson GJ, Howlett GJ, Ashcroft AE, Berry A. The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase. The Biochemical Journal. 437-45. PMID 9531482 DOI: 10.1042/BJ3310437 |
0.328 |
|
1996 |
Cooper SJ, Leonard GA, McSweeney SM, Thompson AW, Naismith JH, Qamar S, Plater A, Berry A, Hunter WN. The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold. Structure (London, England : 1993). 4: 1303-15. PMID 8939754 DOI: 10.1016/S0969-2126(96)00138-4 |
0.306 |
|
1996 |
Qamar S, Marsh K, Berry A. Identification of arginine 331 as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. Protein Science : a Publication of the Protein Society. 5: 154-61. PMID 8771208 DOI: 10.1002/PRO.5560050119 |
0.47 |
|
1996 |
Bashir A, Arscott LD, Perham RN, Williams CH, Berry A. The oxidative and reductive half reactions of subunit interface mutants of Escherichia coli glutathione reductase. Biochemical Society Transactions. 24: 9S. PMID 8674773 DOI: 10.1042/Bst024009S |
0.664 |
|
1995 |
Bashir A, Perham RN, Scrutton NS, Berry A. Altering kinetic mechanism and enzyme stability by mutagenesis of the dimer interface of glutathione reductase. The Biochemical Journal. 312: 527-33. PMID 8526866 |
0.695 |
|
1994 |
Mittl PR, Berry A, Scrutton NS, Perham RN, Schultz GE. A designed mutant of the enzyme glutathione reductase shortens the crystallization time by a factor of forty. Acta Crystallographica. Section D, Biological Crystallography. 50: 228-31. PMID 15299464 DOI: 10.1107/S090744499300993X |
0.595 |
|
1994 |
Rietveld P, Arscott LD, Berry A, Scrutton NS, Deonarain MP, Perham RN, Williams CH. Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli. Biochemistry. 33: 13888-95. PMID 7947797 DOI: 10.1021/Bi00250A043 |
0.626 |
|
1994 |
Mittl PR, Berry A, Scrutton NS, Perham RN, Schulz GE. Anatomy of an engineered NAD-binding site. Protein Science : a Publication of the Protein Society. 3: 1504-14. PMID 7833810 DOI: 10.1002/pro.5560030916 |
0.687 |
|
1993 |
Mittl PR, Berry A, Scrutton NS, Perham RN, Schulz GE. Structural differences between wild-type NADP-dependent glutathione reductase from Escherichia coli and a redesigned NAD-dependent mutant. Journal of Molecular Biology. 231: 191-5. PMID 8510142 DOI: 10.1006/jmbi.1993.1274 |
0.695 |
|
1993 |
Berry A, Marshall KE. Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. Febs Letters. 318: 11-6. PMID 8436219 DOI: 10.1016/0014-5793(93)81317-S |
0.373 |
|
1992 |
Scrutton NS, Deonarain MP, Berry A, Perham RN. Cooperativity induced by a single mutation at the subunit interface of a dimeric enzyme: glutathione reductase. Science (New York, N.Y.). 258: 1140-3. PMID 1439821 |
0.694 |
|
1991 |
Henderson GB, Murgolo NJ, Kuriyan J, Osapay K, Kominos D, Berry A, Scrutton NS, Hinchliffe NW, Perham RN, Cerami A. Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction. Proceedings of the National Academy of Sciences of the United States of America. 88: 8769-73. PMID 1924337 DOI: 10.1073/Pnas.88.19.8769 |
0.705 |
|
1991 |
Perham RN, Scrutton NS, Berry A. New enzymes for old: redesigning the coenzyme and substrate specificities of glutathione reductase. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 13: 515-25. PMID 1755827 DOI: 10.1002/bies.950131005 |
0.703 |
|
1990 |
Scrutton NS, Berry A, Perham RN. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature. 343: 38-43. PMID 2296288 DOI: 10.1038/343038a0 |
0.675 |
|
1990 |
Scrutton NS, Berry A, Deonarain MP, Perham RN. Active site complementation in engineered heterodimers of Escherichia coli glutathione reductase created in vivo. Proceedings. Biological Sciences / the Royal Society. 242: 217-24. PMID 1983037 DOI: 10.1098/rspb.1990.0127 |
0.702 |
|
1990 |
Deonarain MP, Scrutton NS, Berry A, Perham RN. Directed mutagenesis of the redox-active disulphide bridge in glutathione reductase from Escherichia coli. Proceedings. Biological Sciences / the Royal Society. 241: 179-86. PMID 1979442 DOI: 10.1098/rspb.1990.0083 |
0.699 |
|
1989 |
Deonarain MP, Berry A, Scrutton NS, Perham RN. Alternative proton donors/acceptors in the catalytic mechanism of the glutathione reductase of Escherichia coli: the role of histidine-439 and tyrosine-99. Biochemistry. 28: 9602-7. PMID 2558727 DOI: 10.1021/bi00451a008 |
0.697 |
|
1989 |
Berry A, Scrutton NS, Perham RN. Switching kinetic mechanism and putative proton donor by directed mutagenesis of glutathione reductase. Biochemistry. 28: 1264-9. PMID 2540822 |
0.719 |
|
1988 |
Perham RN, Berry A, Scrutton NS. Flavoprotein disulphide oxidoreductases: protein engineering of glutathione reductase from Escherichia coli. Biochemical Society Transactions. 16: 84-7. PMID 3286318 |
0.606 |
|
1988 |
Scrutton NS, Berry A, Perham RN. Engineering of an intersubunit disulphide bridge in glutathione reductase from Escherichia coli. Febs Letters. 241: 46-50. PMID 3058515 DOI: 10.1016/0014-5793(88)81028-7 |
0.717 |
|
1987 |
Scrutton NS, Berry A, Perham RN. Purification and characterization of glutathione reductase encoded by a cloned and over-expressed gene in Escherichia coli. The Biochemical Journal. 245: 875-80. PMID 3311037 |
0.655 |
|
1987 |
Berry A, Bhatnagar RK, Jensen RA. Enzymic basis for leakiness of auxotrophs for phenylalanine in Pseudomonas aeruginosa Journal of General Microbiology. 133. PMID 3128639 |
0.399 |
|
1986 |
Scrutton NS, Berry A, Perham RN. Protein engineering of glutathione reductase: Over-expression of the gene from Escherichia coli Biochemical Society Transactions. 14: 1229-1230. |
0.593 |
|
1985 |
Byng GS, Berry A, Jensen RA. Evolutionary implications of features of aromatic amino acid biosynthesis in the genus Acinetobacter Archives of Microbiology. 143: 122-129. PMID 4074072 DOI: 10.1007/BF00411034 |
0.337 |
|
1982 |
Jordan PM, Berry A. Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides. The Biochemical Journal. 195: 177-81. PMID 6975621 DOI: 10.1042/BJ1950177 |
0.354 |
|
1981 |
BERRY A, JORDAN PM. Porphobilinogen Deaminase: Involvement of stable covalent enzyme intermediate complexes in the enzyme from Rhodopseudomonas spheroides Biochemical Society Transactions. 9: 231-232. DOI: 10.1042/BST0090231 |
0.378 |
|
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