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Jeremy R. Knowles - Publications

Affiliations: 
Harvard University, Cambridge, MA, United States 
Area:
enzyme catalysis
Website:
http://www.thecrimson.com/article/2008/4/4/jeremy-r-knowles-jeremy-r-knowles/

118 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
1995 Schurig H, Beaucamp N, Ostendorp R, Jaenicke R, Adler E, Knowles JR. Phosphoglycerate kinase and triosephosphate isomerase from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex. The Embo Journal. 14: 442-51. PMID 7859734  1
1995 Bertolaet BL, Seidel HM, Knowles JR. Introns and the origin of protein-coding genes. Science (New York, N.Y.). 268: 1367; author reply 1. PMID 7761859  1
1994 Seidel HM, Knowles JR. Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site. Biochemistry. 33: 5641-6. PMID 8180189 DOI: 10.1021/bi00184a037  0.48
1994 Lodi PJ, Chang LC, Knowles JR, Komives EA. Triosephosphate isomerase requires a positively charged active site: the role of lysine-12. Biochemistry. 33: 2809-14. PMID 8130193 DOI: 10.1021/Bi00176A009  1
1994 Fanuel L, Granier B, Wilkin JM, Bellefroid-Bourguignon C, Joris B, Knowles J, Komives E, Van Beeumen J, Ghuysen JM, Frère JM. The precursor of the Streptomyces R61 DD-peptidase containing a C-terminal extension is inactive. Febs Letters. 351: 49-52. PMID 8076692 DOI: 10.1016/0014-5793(94)00822-1  1
1993 Gallo KA, Knowles JR. Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus. Biochemistry. 32: 3981-90. PMID 8385993 DOI: 10.1021/Bi00066A019  0.52
1993 Tanner ME, Gallo KA, Knowles JR. Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase. Biochemistry. 32: 3998-4006. PMID 8097110 DOI: 10.1021/Bi00066A021  1
1993 Petsko G, Ringe D, Allen K, Lavie A, Gerhart-Mueller E, Clifton J, Hasson M, Fujita S, Sugio S, Xhang X, Davenport R, Lolis E, Neidhart D, Kenyon G, Gerlt J, ... ... Knowles J, et al. The structural enzymology of proton-transfer reactions Protein Engineering, Design and Selection. 6: 37. DOI: 10.1093/Protein/6.Supplement.37-A  1
1992 Sauter NK, Glick GD, Crowther RL, Park SJ, Eisen MB, Skehel JJ, Knowles JR, Wiley DC. Crystallographic detection of a second ligand binding site in influenza virus hemagglutinin. Proceedings of the National Academy of Sciences of the United States of America. 89: 324-8. PMID 1729702 DOI: 10.1073/Pnas.89.1.324  1
1992 Seidel HM, Pompliano DL, Knowles JR. Phosphonate biosynthesis: molecular cloning of the gene for phosphoenolpyruvate mutase from Tetrahymena pyriformis and overexpression of the gene product in Escherichia coli. Biochemistry. 31: 2598-608. PMID 1547241 DOI: 10.1021/Bi00124A021  1
1992 Seidel HM, Pompliano DL, Knowles JR. Exons as microgenes? Science (New York, N.Y.). 257: 1489-90. PMID 1523407  1
1992 Sampson NS, Knowles JR. Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase. Biochemistry. 31: 8488-94. PMID 1390633 DOI: 10.1021/Bi00151A015  1
1992 Sampson NS, Knowles JR. Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase. Biochemistry. 31: 8482-7. PMID 1390632 DOI: 10.1021/Bi00151A014  1
1992 Pollack SJ, Freeman S, Pompliano DL, Knowles JR. Cloning, overexpression and mechanistic studies of carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus. European Journal of Biochemistry / Febs. 209: 735-43. PMID 1330557 DOI: 10.1111/J.1432-1033.1992.Tb17342.X  1
1991 Komives EA, Chang LC, Lolis E, Tilton RF, Petsko GA, Knowles JR. Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95. Biochemistry. 30: 3011-9. PMID 2007138 DOI: 10.1021/Bi00226A005  1
1991 Toogood PL, Galliker PK, Glick GD, Knowles JR. Monovalent sialosides that bind tightly to influenza A virus. Journal of Medicinal Chemistry. 34: 3138-40. PMID 1920363 DOI: 10.1021/Jm00114A025  1
1991 Blacklow SC, Liu KD, Knowles JR. Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase. Biochemistry. 30: 8470-6. PMID 1883832 DOI: 10.1021/Bi00098A026  0.92
1991 Glick GD, Toogood PL, Wiley DC, Skehel JJ, Knowles JR. Ligand recognition by influenza virus. The binding of bivalent sialosides. The Journal of Biological Chemistry. 266: 23660-9. PMID 1748643  1
1991 Glick GD, Knowles JR. Molecular Recognition of Bivalent Sialosides by Influenza Virus Journal of the American Chemical Society. 113: 4701-4703. DOI: 10.1021/Ja00012A060  1
1990 Blacklow SC, Knowles JR. How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases. Biochemistry. 29: 4099-108. PMID 2361134 DOI: 10.1021/Bi00469A012  1
1990 Pompliano DL, Peyman A, Knowles JR. Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry. 29: 3186-94. PMID 2185832 DOI: 10.1021/Bi00465A005  1
1990 Gray JV, Eren D, Knowles JR. Monofunctional chorismate mutase from Bacillus subtilis: kinetic and 13C NMR studies on the interactions of the enzyme with its ligands. Biochemistry. 29: 8872-8. PMID 2125470 DOI: 10.1021/Bi00489A051  1
1990 Mueller EG, Khandekar SS, Knowles JR, Jacobson GR. Stereochemical course of the reactions catalyzed by the bacterial phosphoenolpyruvate:mannitol phosphotransferase system. Biochemistry. 29: 6892-6. PMID 2118803 DOI: 10.1021/Bi00481A019  1
1990 Hermes JD, Blacklow SC, Knowles JR. Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme. Proceedings of the National Academy of Sciences of the United States of America. 87: 696-700. PMID 1967829 DOI: 10.1073/Pnas.87.2.696  1
1990 Seidel HM, Freeman S, Schwalbe CH, Knowles JR. Phosphonate biosynthesis: The stereochemical course of phosphoenolpyruvate mutase Journal of the American Chemical Society. 112: 8149-8155.  0.48
1989 Hermes JD, Parekh SM, Blacklow SC, Köster H, Knowles JR. A reliable method for random mutagenesis: the generation of mutant libraries using spiked oligodeoxyribonucleotide primers. Gene. 84: 143-51. PMID 2691332 DOI: 10.1016/0378-1119(89)90148-0  1
1989 Burbaum JJ, Knowles JR. Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinase. Biochemistry. 28: 9306-17. PMID 2611231 DOI: 10.1021/Bi00450A010  0.36
1989 Burbaum JJ, Raines RT, Albery WJ, Knowles JR. Evolutionary optimization of the catalytic effectiveness of an enzyme. Biochemistry. 28: 9293-305. PMID 2611230 DOI: 10.1021/Bi00450A009  1
1989 Widlanski T, Bender SL, Knowles JR. Dehydroquinate synthase: the use of substrate analogues to probe the late steps of the catalyzed reaction. Biochemistry. 28: 7572-82. PMID 2611201  1
1989 Bender SL, Widlanski T, Knowles JR. Dehydroquinate synthase: the use of substrate analogues to probe the early steps of the catalyzed reaction. Biochemistry. 28: 7560-72. PMID 2611200 DOI: 10.1021/Bi00445A010  1
1989 Bender SL, Mehdi S, Knowles JR. Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry. 28: 7555-60. PMID 2514789 DOI: 10.1021/Bi00445A009  1
1989 Summers RG, Harris CR, Knowles JR. A conservative amino acid substitution, arginine for lysine, abolishes export of a hybrid protein in Escherichia coli. Implications for the mechanism of protein secretion. The Journal of Biological Chemistry. 264: 20082-8. PMID 2511198  1
1989 Freeman S, Seidel HM, Schwalbe CH, Knowles JR. Phosphonate biosynthesis: The stereochemical course of phosphoenolpyruvate phosphomutase Journal of the American Chemical Society. 111: 9233-9234. DOI: 10.1021/Ja00208A018  0.48
1989 Widlanski T, Bender SL, Knowles JR. Dehydroquinate synthase: A sheep in Wolf's clothing? Journal of the American Chemical Society. 111: 2299-2300. DOI: 10.1021/Ja00188A052  1
1989 Burbaum JJ, Knowles JR. The nature of pyruvate bound to pyruvate kinase as determined by 13C NMR spectroscopy Bioorganic Chemistry. 17: 359-371. DOI: 10.1016/0045-2068(89)90037-0  0.36
1988 Blacklow SC, Raines RT, Lim WA, Zamore PD, Knowles JR. Triosephosphate isomerase catalysis is diffusion controlled. Appendix: Analysis of triose phosphate equilibria in aqueous solution by 31P NMR. Biochemistry. 27: 1158-67. PMID 3365378 DOI: 10.1021/Bi00404A013  1
1988 Seidel HM, Freeman S, Seto H, Knowles JR. Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond. Nature. 335: 457-8. PMID 3138545 DOI: 10.1038/335457A0  0.48
1988 Butler-Ransohoff JE, Kendall DA, Freeman S, Knowles JR, Kaiser ET. Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphatase. Biochemistry. 27: 4777-80. PMID 3048390 DOI: 10.1021/Bi00413A029  1
1988 Kountz PD, Freeman S, Cook AG, el-Maghrabi MR, Knowles JR, Pilkis SJ. The stereochemical course of phospho group transfer catalyzed by rat liver 6-phosphofructo-2-kinase. The Journal of Biological Chemistry. 263: 16069-72. PMID 2972703  1
1988 Ho MF, Bramson HN, Hansen DE, Knowles JR, Kaiser ET. Stereochemical course of the phospho group transfer catalyzed by cAMP-dependent protein kinase Journal of the American Chemical Society. 110: 2680-2681. DOI: 10.1021/Ja00216A068  1
1987 Albery WJ, Knowles JR. Energetics of enzyme catalysis. II. Oversaturation, case diagrams, reversible and irreversible behaviour. Journal of Theoretical Biology. 124: 173-89. PMID 3657192 DOI: 10.1016/S0022-5193(87)80260-6  1
1987 Albery WJ, Knowles JR. Energetics of enzyme catalysis. I. Isotopic experiments, enzyme interconversion, and oversaturation. Journal of Theoretical Biology. 124: 137-71. PMID 3657191 DOI: 10.1016/S0022-5193(87)80259-X  1
1987 Hermes JD, Blacklow SC, Knowles JR. The development of enzyme catalytic efficiency: an experimental approach. Cold Spring Harbor Symposia On Quantitative Biology. 52: 597-602. PMID 3454280 DOI: 10.1101/Sqb.1987.052.01.068  1
1987 Raines RT, Knowles JR. Enzyme relaxation in the reaction catalyzed by triosephosphate isomerase: detection and kinetic characterization of two unliganded forms of the enzyme. Biochemistry. 26: 7014-20. PMID 3427057 DOI: 10.1021/Bi00396A024  1
1987 Mehdi S, Frost JW, Knowles JR. Dehydroquinate synthase from Escherichia coli, and its substrate 3-deoxy-D-arabino-heptulosonic acid 7-phosphate. Methods in Enzymology. 142: 306-14. PMID 3037261 DOI: 10.1016/S0076-6879(87)42041-7  1
1987 Widlanski TS, Bender SL, Knowles JR. Stereochemical course of the cryptic elimination and cyclization steps in the reaction catalyzed by dehydroquinate synthase Journal of the American Chemical Society. 109: 1873-1875. DOI: 10.1021/Ja00240A054  1
1986 Fisher LM, Albery WJ, Knowles JR. Energetics of proline racemase: racemization of unlabeled proline in the unsaturated, saturated, and oversaturated regimes. Biochemistry. 25: 2529-37. PMID 3755058  0.4
1986 Albery WJ, Knowles JR. Energetics and mechanism of proline racemase. Biochemistry. 25: 2572-2577. PMID 3718964 DOI: 10.1021/Bi00357A043  0.4
1986 Belasco JG, Bruice TW, Fisher LM, Albery WJ, Knowles JR. Energetics of proline racemase: rates, fractionation factors, and buffer catalysis in the oversaturated region. Nature of the interconversion of the two forms of free enzyme. Biochemistry. 25: 2564-71. PMID 3718963 DOI: 10.1021/Bi00357A042  0.4
1986 Belasco JG, Bruice TW, Albery WJ, Knowles JR. Energetics of proline racemase: fractionation factors for the essential catalytic groups in the enzyme-substrate complexes. Biochemistry. 25: 2558-64. PMID 3718962 DOI: 10.1021/Bi00357A041  0.4
1986 Belasco JG, Albery WJ, Knowles JR. Energetics of proline racemase: double fractionation experiment, a test for concertedness and for transition-state dominance. Biochemistry. 25: 2552-8. PMID 3521739 DOI: 10.1021/Bi00357A040  0.4
1986 Fisher LM, Belasco JG, Bruice TW, Albery WJ, Knowles JR. Energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic steps. Biochemistry. 25: 2543-51. PMID 3521738 DOI: 10.1021/Bi00357A039  0.4
1986 Fisher LM, Albery WJ, Knowles JR. Energetics of proline racemase: tracer perturbation experiments using [14C]proline that measure the interconversion rate of the two forms of free enzyme. Biochemistry. 25: 2538-42. PMID 3521737 DOI: 10.1021/Bi00357A038  0.4
1986 Minsky A, Summers RG, Knowles JR. Secretion of beta-lactamase into the periplasm of Escherichia coli: evidence for a distinct release step associated with a conformational change. Proceedings of the National Academy of Sciences of the United States of America. 83: 4180-4. PMID 3520569 DOI: 10.1073/Pnas.83.12.4180  1
1986 Raines RT, Knowles JR. The mechanistic pathway of a mutant triosephosphate isomerase. Annals of the New York Academy of Sciences. 471: 266-71. PMID 3460499 DOI: 10.1111/J.1749-6632.1986.Tb48042.X  1
1986 Raines RT, Sutton EL, Straus DR, Gilbert W, Knowles JR. Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate. Biochemistry. 25: 7142-54. PMID 2879556 DOI: 10.1021/Bi00370A057  1
1985 Kadonaga JT, Plückthun A, Knowles JR. Signal sequence mutants of beta-lactamase. The Journal of Biological Chemistry. 260: 16192-9. PMID 3905810  1
1985 Kadonaga JT, Knowles JR. A simple and efficient method for chemical mutagenesis of DNA. Nucleic Acids Research. 13: 1733-45. PMID 3889841 DOI: 10.1093/Nar/13.5.1733  1
1985 Straus D, Raines R, Kawashima E, Knowles JR, Gilbert W. Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme. Proceedings of the National Academy of Sciences of the United States of America. 82: 2272-6. PMID 3887397 DOI: 10.1073/Pnas.82.8.2272  0.52
1985 Cook AG, Knowles JR. Phosphoenolpyruvate synthetase and pyruvate, orthophosphate dikinase: stereochemical consequences at both the beta-phospho and gamma-phospho groups of ATP. Biochemistry. 24: 51-8. PMID 2986676 DOI: 10.1021/Bi00322A009  1
1985 Hansen DE, Knowles JR. N-carboxybiotin formation by pyruvate carboxylase: The stereochemical consequence at phosphorus Journal of the American Chemical Society. 107: 8304-8305. DOI: 10.1021/Ja00312A105  0.52
1984 Buchwald SL, Saini MS, Knowles JR, Van Etten RL. Stereochemical course of phospho group transfer by human prostatic acid phosphatase. The Journal of Biological Chemistry. 259: 2208-13. PMID 6698963  1
1984 Frost JW, Bender JL, Kadonaga JT, Knowles JR. Dehydroquinate synthase from Escherichia coli: purification, cloning, and construction of overproducers of the enzyme. Biochemistry. 23: 4470-5. PMID 6386050 DOI: 10.1021/Bi00314A036  1
1984 Frost JW, Knowles JR. 3-Deoxy-D-arabino-heptulosonic acid 7-phosphate: chemical synthesis and isolation from Escherichia coli auxotrophs. Biochemistry. 23: 4465-9. PMID 6386049 DOI: 10.1021/Bi00314A035  1
1984 Kadonaga JT, Gautier AE, Straus DR, Charles AD, Edge MD, Knowles JR. The role of the beta-lactamase signal sequence in the secretion of proteins by Escherichia coli. The Journal of Biological Chemistry. 259: 2149-54. PMID 6365904  1
1984 Brenner DG, Knowles JR. 6-(Methoxymethylene)penicillanic acid: inactivator of RTEM beta-lactamase from Escherichia coli. Biochemistry. 23: 5839-46. PMID 6098300 DOI: 10.1021/Bi00319A025  1
1984 Brenner DG, Knowles JR. Penicillanic acid sulfone: nature of irreversible inactivation of RTEM beta-lactamase from Escherichia coli. Biochemistry. 23: 5833-9. PMID 6098299 DOI: 10.1021/Bi00319A024  1
1984 Easton CJ, Knowles JR. Correlation of the effect of beta-lactamase inhibitors on the beta-lactamase in growing cultures of gram-negative bacteria with their effect on the isolated beta-lactamase. Antimicrobial Agents and Chemotherapy. 26: 358-63. PMID 6095753  0.96
1984 Sogo SG, Widlanski TS, Hoare JH, Grimshaw CE, Berchtold GA, Knowles JR. Stereochemistry of the rearrangement of chorismate to prephenate: Chorismate mutase involves a chair transition state Journal of the American Chemical Society. 106: 2701-2703.  1
1983 Kadonaga JT, Knowles JR. Role of mono- and divalent metal cations in the catalysis by yeast aldolase. Biochemistry. 22: 130-6. PMID 6338913 DOI: 10.1021/Bi00270A019  1
1982 Hansen DE, Knowles JR. The stereochemical course at phosphorus of the reaction catalyzed by phosphoenolpyruvate carboxylase. The Journal of Biological Chemistry. 257: 14795-8. PMID 7174666  0.52
1982 Hassett A, Blättler W, Knowles JR. Pyruvate kinase: is the mechanism of phospho transfer associative or dissociative? Biochemistry. 21: 6335-40. PMID 7150563 DOI: 10.1021/Bi00268A002  0.52
1982 Wong CH, Pollak A, McCurry SD, Sue JM, Knowles JR, Whitesides GM. Synthesis of ribulose 1,5-bisphosphate: routes from glucose 6-phosphate (via 6-phosphogluconate) and from adenosine monophosphate (via ribose 5-phosphate). Methods in Enzymology. 89: 108-21. PMID 7144568 DOI: 10.1016/S0076-6879(82)89020-4  1
1982 Easton CJ, Knowles JR. Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acid. Biochemistry. 21: 2857-62. PMID 7049231 DOI: 10.1021/Bi00541A008  0.96
1982 Grimshaw CE, Sogo SG, Knowles JR. The fate of the hydrogens of phosphoenolpyruvate in the reaction catalyzed by 5-enolpyruvylshikimate-3-phosphate synthase. Isotope effects and isotope exchange. The Journal of Biological Chemistry. 257: 596-8. PMID 7033217  0.32
1982 Begley GS, Hansen DE, Jacobson GR, Knowles JR. Stereochemical course of the reactions catalyzed by the bacterial phosphoenolpyruvate:glucose phosphotransferase system. Biochemistry. 21: 5552-6. PMID 6756472 DOI: 10.1021/bi00265a026  0.52
1982 Buchwald SL, Hansen DE, Hassett A, Knowles JR. Chiral [16O, 17O, 18O]phosphoric monoesters as stereochemical probes of phosphotransferases. Methods in Enzymology. 87: 279-301. PMID 6294451 DOI: 10.1016/S0076-6879(82)87018-3  0.52
1982 Charles AD, Gautier AE, Edge MD, Knowles JR. Targeted point mutation that creates a unique Eco RI site within the signal codons of the beta-lactamase gene without altering enzyme secretion or processing. The Journal of Biological Chemistry. 257: 7930-2. PMID 6282862  1
1981 Saini MS, Buchwald SL, Van Etten RL, Knowles JR. Stereochemistry of phospho transfer catalyzed by bovine liver acid phosphatase. The Journal of Biological Chemistry. 256: 10453-5. PMID 7287718  1
1981 Hansen DE, Knowles JR. The stereochemical course of the reaction catalyzed by creatine kinase. The Journal of Biological Chemistry. 256: 5967-9. PMID 7240185  0.52
1981 Brenner DG, Knowles JR. Penicillanic acid sulfone: an unexpected isotope effect in the interaction of 6 alpha- and 6 beta-monodeuterio and of 6,6-dideuterio derivatives with RTEM beta-lactamase from Escherichia coli. Biochemistry. 20: 3680-7. PMID 6268140 DOI: 10.1021/Bi00516A003  1
1980 Bayley H, Knowles JR. Photogenerated reagents for membranes: selective labeling of intrinsic membrane proteins in the human erythrocyte membrane. Biochemistry. 19: 3883-92. PMID 7407075 DOI: 10.1021/Bi00558A001  0.72
1980 Standring DN, Knowles JR. Photoaffinity labeling of lactate dehydrogenase by the carbene derived from the 3-diazirino analogue of nicotinamide adenine dinucleotide. Biochemistry. 19: 2811-6. PMID 7397106 DOI: 10.1021/Bi00553A042  0.72
1980 Bayley H, Knowles JR. Photogenerated, hydrophobic reagents for intrinsic membrane proteins. Annals of the New York Academy of Sciences. 346: 45-58. PMID 6930191 DOI: 10.1111/J.1749-6632.1980.Tb22090.X  0.72
1979 Boger J, Knowles JR. Symmetrical triamino-per-O-methyl-.alpha.-cyclodextrin: a host for phosphate esters exploiting both hydrophobic and electrostatic interactions in aqueous solution Journal of the American Chemical Society. 101: 7631-7633. DOI: 10.1021/Ja00519A036  0.96
1979 Boger J, Knowles JR. Symmetrical triamino-per-O-methyl-α-cyclodextrin: A host for phosphate esters exploiting both hydrophobic and electrostatic interactions in aqueous solution [13] Journal of the American Chemical Society. 101: 7631-7633.  1
1978 Bayley H, Knowles JR. Photogenerated reagents for membrane labeling. 2. Phenylcarbene and adamantylidene formed within the lipid bilayer. Biochemistry. 17: 2420-3. PMID 678520 DOI: 10.1021/Bi00605A026  0.72
1978 Bayley H, Knowles JR. Photogenerated reagents for membrane labeling. 1. Phenylnitrene formed within the lipid bilayer. Biochemistry. 17: 2414-9. PMID 678519 DOI: 10.1021/Bi00605A025  0.72
1978 Staros JV, Knowles JR. Photoaffinity inhibition of dipeptide transport in Escherichia coli. Biochemistry. 17: 3321-5. PMID 356877 DOI: 10.1021/Bi00609A023  1
1978 Orr GA, Simon J, Jones SR, Chin GJ, Knowles JR. Adenosine 5'-O-([gamma-18O]gamma-thio)triphosphate chiral at the gamma-phosphorus: stereochemical consequences of reactions catalyzed by pyruvate kinase, glycerol kinase, and hexokinase. Proceedings of the National Academy of Sciences of the United States of America. 75: 2230-3. PMID 209459 DOI: 10.1073/Pnas.75.5.2230  1
1978 Staros JV, Bayley H, Standring DN, Knowles JR. Reduction of aryl azides by thiols: implications for the use of photoaffinity reagents. Biochemical and Biophysical Research Communications. 80: 568-72. PMID 24446 DOI: 10.1016/0006-291X(78)91606-6  1
1977 Bayley H, Knowles JR. Photoaffinity labeling. Methods in Enzymology. 46: 69-114. PMID 909454 DOI: 10.1016/S0076-6879(77)46012-9  0.72
1977 Webb MR, Standring DN, Knowles JR. Phosphorus-31 nuclear magnetic resonance of dihydroxyacetone phosphate in the presence of triosephosphate isomerase. The question of nonproductive binding of the substrate hydrate. Biochemistry. 16: 2738-41. PMID 889785 DOI: 10.1021/Bi00631A023  0.72
1977 Albery WJ, Knowles JR. Efficiency and evolution of enzyme catalysis. Angewandte Chemie (International Ed. in English). 16: 285-93. PMID 406815 DOI: 10.1002/Anie.197702851  0.4
1977 Boger J, Knowles JR. To stabilize a transition state. Ciba Foundation Symposium. 225-42. PMID 252453  0.76
1977 Breathnach R, Knowles JR. Phosphoglycerate mutase from wheat germ: studies with 18O-labeled substrate, investigations of the phosphatase and phosphoryl transfer activities, and evidence for a phosphoryl-enzyme intermediate. Biochemistry. 16: 3054-60. PMID 196622 DOI: 10.1021/Bi00633A002  0.44
1977 Leadlay PF, Breathnach R, Gatehouse JA, Johnson PE, Knowles JR. Phosphoglycerate mutase from wheat germ: studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular. Appendix: phosphoglycerate mutase from wheat germ: isolation, crystallization, and properties. Biochemistry. 16: 3045-53. PMID 19039 DOI: 10.1021/Bi00633A001  0.44
1976 Albery WJ, Knowles JR. Evolution of enzyme function and the development of catalytic efficiency. Biochemistry. 15: 5631-40. PMID 999839  0.4
1976 Albery WJ, Knowles JR. Free-energy profile of the reaction catalyzed by triosephosphate isomerase. Biochemistry. 15: 5627-31. PMID 999838  0.4
1976 Fisher LM, Albery WJ, Knowles JR. Energetics of triosephosphate isomerase: the nature of the proton transfer between the catalytic base and solvent water. Biochemistry. 15: 5621-6. PMID 999837 DOI: 10.1021/Bi00670A030  1
1976 Leadlay PF, Albery WJ, Knowles JR. Energetics of triosephosphate isomerase: deuterium isotope effects in the enzyme-catalyzed reaction. Biochemistry. 15: 5617-20. PMID 999836 DOI: 10.1021/Bi00670A029  0.44
1976 Fletcher SJ, Herlihy JM, Albery WJ, Knowles JR. Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate glyceraldehyde 3-phosphate and in product. Biochemistry. 15: 5612-7. PMID 999835 DOI: 10.1021/Bi00670A028  1
1976 Maister SG, Pett CP, Albery WJ, Knowles JR. Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product. Biochemistry. 15: 5607-12. PMID 999834 DOI: 10.1021/Bi00670A027  0.4
1976 Herlihy JM, Maister SG, Albery WJ, Knowles JR. Energetics of triosephosphate isomerase: the fate of the 1(R)-3H label of tritiated dihydroxyacetone phsophate in the isomerase reaction. Biochemistry. 15: 5601-7. PMID 999833 DOI: 10.1021/Bi00670A026  1
1976 Albery WJ, Knowles JR. Deuterium and tritium exchange in enzyme kinetics. Biochemistry. 15: 5588-600. PMID 999832 DOI: 10.1021/Bi00670A025  0.4
1976 Johnson PE, Maister SG, Knowles JR. Crystalline 3-phospho-d-glycerate kinase from horse muscle. Biochemistry. 15: 2899-901. PMID 985698  0.44
1976 Johnson PE, Abbott SJ, Knowles JR. The "phosphoryl-enzyme" from phosphoglycerate kinase. Biochemistry. 15: 2893-8. PMID 779834  1
1975 Johnson PE, Abbott SJ, Orr GA, Sémériva M, Knowles JR. On the "phosphoryl-enzyme" of phosphoglycerate kinase. Biochemical and Biophysical Research Communications. 62: 382-9. PMID 234227 DOI: 10.1016/S0006-291X(75)80150-1  1
1975 Fisher LM, Albery WJ, Knowles JR. The nature of the proton transfer from an acid group at the active site of an enzyme, to solvent water. The extent of 2H and 3H transfer in the reaction catalysed by triose phosphate isomerase Faraday Symposia of the Chemical Society. 10: 154-159. DOI: 10.1039/Fs9751000154  1
1974 Joyce CM, Knowles JR. Affinity chromatography of aminoacyl-tRNA synthetases on specific tRNA columns without prior purification of tRNA Biochemical and Biophysical Research Communications. 60: 1278-1285. PMID 4608676 DOI: 10.1016/0006-291X(74)90336-2  1
1974 Orr GA, Knowles JR. The interaction of the phosphonate analogue of 3-phospho-D-glycerate with phosphoglycerate kinase. The Biochemical Journal. 141: 721-3. PMID 4463959  1
1974 Bridges AJ, Knowles JR. An examination of the utility of photogenerated reagents by using α chymotrypsin Biochemical Journal. 143: 663-668. PMID 4462748 DOI: 10.1042/BJ1430663  1
1972 Knowles JR, Leadlay PF, Maister SG. Triosephosphate isomerase: isotope studies on the mechanistic pathway. Cold Spring Harbor Symposia On Quantitative Biology. 36: 157-64. PMID 4508134 DOI: 10.1101/Sqb.1972.036.01.022  0.44
1972 Fleet GW, Knowles JR, Porter RR. The antibody binding site. Labelling of a specific antibody against the photo-precursor of an aryl nitrene. The Biochemical Journal. 128: 499-508. PMID 4117794 DOI: 10.1042/Bj1280499  1
1969 Cornish-Bowden AJ, Greenwell P, Knowles JR. The rate-determining step in pepsin-catalysed reactions, and evidence against an acyl-enzyme intermediate. The Biochemical Journal. 113: 369-75. PMID 4897200  1
1969 Cornish-Bowden AJ, Knowles JR. The pH-dependence of pepsin-catalysed reactions. The Biochemical Journal. 113: 353-62. PMID 4897198  1
1968 Richards FM, Knowles JR. Glutaraldehyde as a protein cross-linking reagent Journal of Molecular Biology. 37: 231-233. PMID 5760492 DOI: 10.1016/0022-2836(68)90086-7  1
1967 Hawkins MJ, Knowles JR, Wilson L, Witcher D. The interaction of alpha-chymotrypsin with isosteric substrates of different charge type. The Biochemical Journal. 104: 762-6. PMID 6049922 DOI: 10.1042/BJ1040762  1
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