| Year |
Citation |
Score |
| 2003 |
Knowles J. Chemistry. Seeing is believing. Science (New York, N.Y.). 299: 2002-3. PMID 12637674 DOI: 10.1126/Science.1084036 |
0.361 |
|
| 1996 |
KNOWLES JR. THE ROLE OF METHIONINE IN ALPHA-CHYMOTRYPSIN-CATALYSED REACTIONS. The Biochemical Journal. 95: 180-90. PMID 14333555 DOI: 10.1042/BJ0950180 |
0.336 |
|
| 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 |
0.316 |
|
| 1994 |
Zhang Z, Sugio S, Komives EA, Liu KD, Knowles JR, Petsko GA, Ringe D. Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution. Biochemistry. 33: 2830-7. PMID 8130195 DOI: 10.1021/Bi00176A012 |
0.548 |
|
| 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 |
0.616 |
|
| 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 |
0.535 |
|
| 1994 |
Anderson SR, Anderson VE, Knowles JR. Primary and secondary kinetic isotope effects as probes of the mechanism of yeast enolase. Biochemistry. 33: 10545-55. PMID 8068695 DOI: 10.1021/Bi00200A041 |
0.343 |
|
| 1994 |
Gray JV, Knowles JR. Monofunctional chorismate mutase from Bacillus subtilis: FTIR studies and the mechanism of action of the enzyme. Biochemistry. 33: 9953-9. PMID 8061004 DOI: 10.1021/Bi00199A018 |
0.372 |
|
| 1993 |
Lodi PJ, Knowles JR. Direct evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomerase. Biochemistry. 32: 4338-43. PMID 8476863 DOI: 10.1021/Bi00067A024 |
0.388 |
|
| 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 |
0.389 |
|
| 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 |
0.755 |
|
| 1993 |
Gallo KA, Tanner ME, Knowles JR. Mechanism of the reaction catalyzed by glutamate racemase. Biochemistry. 32: 3991-7. PMID 8097109 DOI: 10.1021/Bi00066A020 |
0.678 |
|
| 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 |
0.413 |
|
| 1993 |
Mueller EG, Crowder MW, Averill BA, Knowles JR. Purple acid phosphatase: a diiron enzyme that catalyzes a direct phospho group transfer to water Journal of the American Chemical Society. 115: 2974-2975. DOI: 10.1021/Ja00060A055 |
0.749 |
|
| 1993 |
Mueller EG, Crowder MW, Averill BA, Knowles JR. Purple acid phosphatase catalyzes the direct transfer of a phospho group from substrate to water. Journal of Inorganic Biochemistry. 51: 106. DOI: 10.1016/0162-0134(93)85142-U |
0.714 |
|
| 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 |
0.572 |
|
| 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 |
0.765 |
|
| 1992 |
Seidel HM, Pompliano DL, Knowles JR. Exons as microgenes? Science (New York, N.Y.). 257: 1489-90. PMID 1523407 |
0.711 |
|
| 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 |
0.673 |
|
| 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 |
0.669 |
|
| 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 |
0.807 |
|
| 1991 |
Lodi PJ, Knowles JR. Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications. Biochemistry. 30: 6948-56. PMID 2069953 DOI: 10.1021/Bi00242A020 |
0.395 |
|
| 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 |
0.623 |
|
| 1991 |
Knowles JR. Enzyme catalysis: not different, just better. Nature. 350: 121-4. PMID 2005961 DOI: 10.1038/350121A0 |
0.432 |
|
| 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 |
0.531 |
|
| 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 |
0.605 |
|
| 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 |
0.518 |
|
| 1991 |
Knowles JR. To build an enzyme.... Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 332: 115-21. PMID 1678530 DOI: 10.1098/Rstb.1991.0039 |
0.441 |
|
| 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 |
0.525 |
|
| 1991 |
Pansegrau PD, Anderson KS, Widlanski T, Ream JE, Sammons RD, Sikorski JA, Knowles JR. Synthesis and evaluation of two new inhibitors of EPSP synthase Tetrahedron Letters. 32: 2589-2592. DOI: 10.1016/S0040-4039(00)78792-2 |
0.696 |
|
| 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 |
0.637 |
|
| 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 |
0.809 |
|
| 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 |
0.428 |
|
| 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 |
0.752 |
|
| 1990 |
Gray JV, Golinelli-Pimpaneau B, Knowles JR. Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli. Biochemistry. 29: 376-83. PMID 2105742 DOI: 10.1021/Bi00454A011 |
0.395 |
|
| 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 |
0.649 |
|
| 1990 |
KNOWLES JR. ChemInform Abstract: Mechanistic Ingenuity in Enzyme Catalysis: Dehydroquinate Synthase Cheminform. 21. DOI: 10.1002/CHIN.199030338 |
0.323 |
|
| 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 |
0.554 |
|
| 1989 |
Knowles JR. The mechanism of biotin-dependent enzymes. Annual Review of Biochemistry. 58: 195-221. PMID 2673009 DOI: 10.1146/Annurev.Bi.58.070189.001211 |
0.367 |
|
| 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 |
0.79 |
|
| 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 |
0.81 |
|
| 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 |
0.374 |
|
| 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 |
0.428 |
|
| 1989 |
Baasov T, Knowles JR. Is the first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tyrosine sensitive), a copper metalloenzyme? Journal of Bacteriology. 171: 6155-60. PMID 2572582 |
0.578 |
|
| 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 |
0.374 |
|
| 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 |
0.623 |
|
| 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 |
0.593 |
|
| 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 |
0.788 |
|
| 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 |
0.698 |
|
| 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 |
0.355 |
|
| 1988 |
Nickbarg EB, Knowles JR. Triosephosphate isomerase: energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli. Biochemistry. 27: 5939-47. PMID 3056516 DOI: 10.1021/Bi00416A018 |
0.428 |
|
| 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 |
0.39 |
|
| 1988 |
Ogita T, Knowles JR. On the intermediacy of carboxyphosphate in biotin-dependent carboxylations. Biochemistry. 27: 8028-33. PMID 2976600 DOI: 10.1021/Bi00421A009 |
0.335 |
|
| 1988 |
Clark JD, O'Keefe SJ, Knowles JR. Malate synthase: proof of a stepwise Claisen condensation using the double-isotope fractionation test. Biochemistry. 27: 5961-71. PMID 2847778 DOI: 10.1021/Bi00416A020 |
0.346 |
|
| 1988 |
Nickbarg EB, Davenport RC, Petsko GA, Knowles JR. Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism. Biochemistry. 27: 5948-60. PMID 2847777 DOI: 10.1021/Bi00416A019 |
0.477 |
|
| 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 |
0.399 |
|
| 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 |
0.391 |
|
| 1987 |
Plückthun A, Knowles JR. The consequences of stepwise deletions from the signal-processing site of beta-lactamase. The Journal of Biological Chemistry. 262: 3951-7. PMID 3549721 |
0.415 |
|
| 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 |
0.604 |
|
| 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 |
0.619 |
|
| 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 |
0.704 |
|
| 1987 |
Copley SD, Knowles JR. The conformational equilibrium of chorismate in solution: Implications for the mechanism of the non-enzymic and the enzyme-catalyzed rearrangement of chorismate to prephenate Journal of the American Chemical Society. 109: 5008-5013. DOI: 10.1021/Ja00250A040 |
0.412 |
|
| 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 |
0.674 |
|
| 1986 |
O'Keefe SJ, Knowles JR. Biotin-dependent carboxylation catalyzed by transcarboxylase is a stepwise process. Biochemistry. 25: 6077-84. PMID 3790507 DOI: 10.1021/Bi00368A036 |
0.38 |
|
| 1986 |
Albery WJ, Knowles JR. Energetics and mechanism of proline racemase. Biochemistry. 25: 2572-2577. PMID 3718964 DOI: 10.1021/Bi00357A043 |
0.448 |
|
| 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 |
0.472 |
|
| 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 |
0.42 |
|
| 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 |
0.403 |
|
| 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 |
0.312 |
|
| 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 |
0.461 |
|
| 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 |
0.342 |
|
| 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 |
0.507 |
|
| 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 |
0.557 |
|
| 1985 |
Kadonaga JT, Plückthun A, Knowles JR. Signal sequence mutants of beta-lactamase. The Journal of Biological Chemistry. 260: 16192-9. PMID 3905810 |
0.605 |
|
| 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 |
0.535 |
|
| 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 |
0.607 |
|
| 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 |
0.355 |
|
| 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 |
0.423 |
|
| 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 |
0.774 |
|
| 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 |
0.679 |
|
| 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 |
0.529 |
|
| 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 |
0.37 |
|
| 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 |
0.349 |
|
| 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 |
0.473 |
|
| 1984 |
Knowles JR. Enzyme catalysis: lessons from stereochemistry Pure and Applied Chemistry. 56: 1005-1010. DOI: 10.1351/pac198456081005 |
0.318 |
|
| 1984 |
BUCHWALD SL, FRIEDMAN JM, KNOWLES JR. ChemInform Abstract: STEREOCHEMISTRY OF NUCLEOPHILIC DISPLACEMENT ON TWO PHOSPHORIC MONOESTERS AND A PHOSPHOGUANIDINE: THE ROLE OF METAPHOSPHATE Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198449255 |
0.341 |
|
| 1984 |
Buchwald SL, Friedman JM, Knowles JR. Stereochemistry of nucleophilic displacement on two phosphoric monoesters and a phosphoguanidine: the role of metaphosphate Journal of the American Chemical Society. 106: 4911-4916. DOI: 10.1002/Chin.198449255 |
0.423 |
|
| 1984 |
Buchwald SL, Pliura DH, Knowles JR. Stereochemical evidence for pseudorotation in the reaction of a phosphoric monoester Journal of the American Chemical Society. 106: 4916-4922. DOI: 10.1002/Chin.198449251 |
0.46 |
|
| 1984 |
BUCHWALD SL, PLIURA DH, KNOWLES JR. ChemInform Abstract: STEREOCHEMICAL EVIDENCE FOR PSEUDOROTATION IN THE REACTION OF A PHOSPHORIC MONOESTER Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198449251 |
0.385 |
|
| 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. DOI: 10.1002/Chin.198433100 |
0.635 |
|
| 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. |
0.592 |
|
| 1983 |
Addadi L, Jaffe EK, Knowles JR. Secondary tritium isotope effects as probes of the enzymic and nonenzymic conversion of chorismate to prephenate. Biochemistry. 22: 4494-501. PMID 6354259 DOI: 10.1021/Bi00288A022 |
0.384 |
|
| 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 |
0.611 |
|
| 1983 |
Belasco JG, Knowles JR. Polarization of substrate carbonyl groups by yeast aldolase: investigation by Fourier transform infrared spectroscopy. Biochemistry. 22: 122-9. PMID 6338912 DOI: 10.1021/Bi00270A018 |
0.375 |
|
| 1983 |
Belasco JG, Albery WJ, Knowles JR. Double isotope fractionation: test for concertedness and for transition-state dominance Journal of the American Chemical Society. 105: 2475-2477. DOI: 10.1021/Ja00346A062 |
0.301 |
|
| 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 |
0.359 |
|
| 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 |
0.351 |
|
| 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 |
0.606 |
|
| 1982 |
Sue JM, Knowles JR. Ribulose-1,5-bisphosphate carboxylase: primary deuterium kinetic isotope effect using [3-2H]ribulose 1,5-bisphosphate. Biochemistry. 21: 5410-4. PMID 6816275 DOI: 10.1021/Bi00265A005 |
0.369 |
|
| 1982 |
Sue JM, Knowles JR. Ribulose-1,5-bisphosphate carboxylase: fate of the tritium label in [3]3H]ribulose 1,5-bisphosphate during the enzyme-catalyzed reaction. Biochemistry. 21: 5404-10. PMID 6816274 DOI: 10.1021/Bi00265A004 |
0.403 |
|
| 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 |
0.364 |
|
| 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 |
0.466 |
|
| 1982 |
Saver BG, Knowles JR. Ribulose-1,5-bisphosphate carboxylase: enzyme-catalyzed appearance of solvent tritium at carbon 3 of ribulose 1,5-bisphosphate reisolated after partial reaction. Biochemistry. 21: 5398-403. PMID 6293539 DOI: 10.1021/Bi00265A003 |
0.391 |
|
| 1982 |
Buchwald SL, Knowles JR. Nucleophilic displacements on phosphoric monoesters: stereochemical evidence Journal of the American Chemical Society. 104: 1438-1440. DOI: 10.1021/Ja00369A055 |
0.426 |
|
| 1982 |
Buchwald SL, Pliura DH, Knowles JR. Stereochemistry and mechanism of an acid-catalyzed 1,2-phospho group migration: evidence for pseudorotation in the reaction of a phosphoric monoester Journal of the American Chemical Society. 104: 845-847. DOI: 10.1021/Ja00367A033 |
0.487 |
|
| 1982 |
BUCHWALD SL, KNOWLES JR. ChemInform Abstract: NUCLEOPHILIC DISPLACEMENTS ON PHOSPHORIC MONOESTERS: STEREOCHEMICAL EVIDENCE Chemischer Informationsdienst. 13. DOI: 10.1002/chin.198226229 |
0.342 |
|
| 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 |
0.47 |
|
| 1981 |
Charnas RL, Knowles JR. Inactivation of RTEM beta-lactamase from Escherichia coli by clavulanic acid and 9-deoxyclavulanic acid. Biochemistry. 20: 3214-9. PMID 7018570 DOI: 10.1021/Bi00514A035 |
0.303 |
|
| 1981 |
Charnas RL, Knowles JR. Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid. Biochemistry. 20: 2732-7. PMID 7018565 |
0.306 |
|
| 1981 |
Fisher J, Charnas RL, Bradley SM, Knowles JR. Inactivation of the RTEM beta-lactamase from Escherichia coli. Interaction of penam sulfones with enzyme. Biochemistry. 20: 2726-31. PMID 7018564 DOI: 10.1021/Bi00513A004 |
0.372 |
|
| 1981 |
Kemal C, Knowles JR. Penicillanic acid sulfone: interaction with RTEM beta-lactamase from Escherichia coli at different pH values. Biochemistry. 20: 3688-95. PMID 6268141 DOI: 10.1021/Bi00516A004 |
0.404 |
|
| 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 |
0.383 |
|
| 1981 |
Charmas R, Knowles J. Corrections - Inhibition of the RTEM β-Lactamase from Escherichia coli. Interaction of Enzyme with Derivatives of Olivanic Acid Biochemistry. 20: 7328-7328. DOI: 10.1021/Bi00528A602 |
0.354 |
|
| 1981 |
BUCHWALD SL, KNOWLES JR. ChemInform Abstract: DETERMINATION OF THE ABSOLUTE CONFIGURATION OF (16O,17O,18O)PHOSPHATE MONOESTERS BY USING PHOSPHORUS-31 NMR Chemischer Informationsdienst. 12. DOI: 10.1002/chin.198103071 |
0.332 |
|
| 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 |
0.481 |
|
| 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 |
0.356 |
|
| 1980 |
Belasco JG, Knowles JR. Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy. Biochemistry. 19: 472-7. PMID 7356939 DOI: 10.1021/Bi00544A012 |
0.374 |
|
| 1980 |
Fisher J, Belasco JG, Khosla S, Knowles JR. beta-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin. Biochemistry. 19: 2895-901. PMID 6994800 DOI: 10.1021/Bi00554A012 |
0.465 |
|
| 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 |
0.462 |
|
| 1980 |
Knowles JR. Enzyme-catalyzed phosphoryl transfer reactions. Annual Review of Biochemistry. 49: 877-919. PMID 6250450 DOI: 10.1146/annurev.bi.49.070180.004305 |
0.318 |
|
| 1980 |
Blättler WA, Knowles JR. Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ. Biochemistry. 19: 738-43. PMID 6243955 |
0.345 |
|
| 1980 |
Fisher J, Belasco JG, Charnas RL, Khosla S, Knowles JR. Beta-lactamase inactivation by mechanism-based reagents. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 289: 309-19. PMID 6109326 DOI: 10.1098/Rstb.1980.0048 |
0.442 |
|
| 1980 |
Buchwald SL, Knowles JR. Determination of the absolute configuration of [16O,17O,18O]phosphate monoesters by using phosphorus-31 NMR Journal of the American Chemical Society. 102: 6601-6602. DOI: 10.1021/Ja00541A056 |
0.414 |
|
| 1979 |
Blättler WA, Knowles JR. Stereochemical course of phosphokinases. The use of adenosine [gamma-(S)-16O,17O,18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase. Biochemistry. 18: 3927-33. PMID 226119 DOI: 10.1021/Bi00585A013 |
0.332 |
|
| 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 |
0.527 |
|
| 1979 |
Boger J, Brenner DG, Knowles JR. Symmetrical triamino-per-O-methyl-.alpha.-cyclodextrin: preparation and characterization of primary trisubstituted .alpha.-cyclodextrins Journal of the American Chemical Society. 101: 7630-7631. DOI: 10.1021/Ja00519A035 |
0.51 |
|
| 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. |
0.473 |
|
| 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 |
0.491 |
|
| 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 |
0.484 |
|
| 1978 |
Jones SR, Kindman LA, Knowles JR. Stereochemistry of phosphoryl group transfer using a chiral [16O, 17O, 18O] stereochemical course of alkaline phosphatase. Nature. 275: 564-5. PMID 357996 DOI: 10.1038/275564A0 |
0.356 |
|
| 1978 |
Staros JV, Knowles JR. Photoaffinity inhibition of dipeptide transport in Escherichia coli. Biochemistry. 17: 3321-5. PMID 356877 DOI: 10.1021/Bi00609A023 |
0.624 |
|
| 1978 |
Charnas RL, Fisher J, Knowles JR. Chemical studies on the inactivation of Escherichia coli RTEM beta-lactamase by clavulanic acid. Biochemistry. 17: 2185-9. PMID 352395 |
0.322 |
|
| 1978 |
Fisher J, Charnas RL, Knowles JR. Kinetic studies on the inactivation of Escherichia coli RTEM beta-lactamase by clavulanic acid. Biochemistry. 17: 2180-4. PMID 352394 DOI: 10.1021/Bi00604A024 |
0.435 |
|
| 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 |
0.603 |
|
| 1978 |
Sue JM, Knowles JR. Retention of the oxygens at C-2 and C-3 of D-ribulose 1,5-bisphosphate in the reaction catalyzed by ribulose-1,5-bisphosphate carboxylase. Biochemistry. 17: 4041-4. PMID 101236 DOI: 10.1021/Bi00612A026 |
0.329 |
|
| 1978 |
Belasco JG, Herlihy JM, Knowles JR. Critical ionization states in the reaction catalyzed by triosephosphate isomerase. Biochemistry. 17: 2971-8. PMID 29659 DOI: 10.1021/Bi00608A005 |
0.398 |
|
| 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 |
0.709 |
|
| 1978 |
Bayley H, Standring DN, Knowles JR. Propane-1,3-dithiol: A selective reagent for the efficient reduction of alkyl and aryl azides to amines Tetrahedron Letters. 19: 3633-3634. DOI: 10.1016/S0040-4039(01)95015-4 |
0.491 |
|
| 1977 |
Bayley H, Knowles JR. Photoaffinity labeling. Methods in Enzymology. 46: 69-114. PMID 909454 DOI: 10.1016/S0076-6879(77)46012-9 |
0.504 |
|
| 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 |
0.371 |
|
| 1977 |
Boger J, Knowles JR. To stabilize a transition state. Ciba Foundation Symposium. 225-42. PMID 252453 |
0.551 |
|
| 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 |
0.389 |
|
| 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 |
0.551 |
|
| 1977 |
Albery WJ, Knowles JR. The determination of the rate-limiting step in a proton transfer reaction from the breakdown of the Swain-Schaad relation Journal of the American Chemical Society. 99: 637-638. DOI: 10.1021/Ja00444A068 |
0.307 |
|
| 1977 |
Albery J, Knowles J. Corrections - Deuterium and Tritium Exchange in Enzyme Kinetics Biochemistry. 16: 2580-2580. DOI: 10.1021/Bi00630A600 |
0.422 |
|
| 1977 |
Knowles JR, Albery WJ. Perfection in enzyme catalysis: the energetics of triosephosphate isomerase Accounts of Chemical Research. 10: 105-111. DOI: 10.1021/Ar50112A001 |
0.428 |
|
| 1976 |
Knowles JR. Whither enzyme mechanisms? Febs Letters. 62: E53-61. PMID 1253971 DOI: 10.1016/0014-5793(76)80854-X |
0.403 |
|
| 1976 |
Hall A, Knowles JR. The uncatalyzed rates of enolization of dihydroxyacetone phoshate and of glyceraldehyde 3-phosphate in neutral aqueous solution. The quantitative assessment of the effectiveness of an enzyme catalyst. Biochemistry. 14: 4348-53. PMID 1182103 DOI: 10.1021/Bi00690A032 |
0.429 |
|
| 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 |
0.422 |
|
| 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 |
0.603 |
|
| 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 |
0.442 |
|
| 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 |
0.428 |
|
| 1976 |
Albery WJ, Knowles JR. Deuterium and tritium exchange in enzyme kinetics. Biochemistry. 15: 5588-600. PMID 999832 DOI: 10.1021/Bi00670A025 |
0.409 |
|
| 1976 |
Hall A, Knowles JR. Directed selective pressure on a beta-lactamase to analyse molecular changes involved in development of enzyme function. Nature. 264: 803-4. PMID 796732 DOI: 10.1038/264803A0 |
0.312 |
|
| 1976 |
Johnson PE, Abbott SJ, Knowles JR. The "phosphoryl-enzyme" from phosphoglycerate kinase. Biochemistry. 15: 2893-8. PMID 779834 |
0.331 |
|
| 1976 |
Johnson P, Abbott S, Orr G, Semeriva M, Knowles J. Correction- The "Phosphoryl-Enzyme" from Phosphoglycerate Kinase Biochemistry. 15: 3902-3902. DOI: 10.1021/Bi00662A605 |
0.576 |
|
| 1975 |
Webb MR, Knowles JR. The existence of an electrophilic component in the reaction catalysed by triose phosphate isomerase. The Biochemical Journal. 141: 589-92. PMID 4375983 DOI: 10.1042/BJ1410589 |
0.325 |
|
| 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 |
0.606 |
|
| 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 |
0.391 |
|
| 1975 |
Newmark AK, Knowles JR. Acyl- and amino-transfer routes in pepsin-catalyzed reactions Journal of the American Chemical Society. 97: 3557-3559. DOI: 10.1021/Ja00845A068 |
0.36 |
|
| 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 |
0.561 |
|
| 1973 |
Paterson AK, Knowles JR. The number of catalytically essential carboxyl groups in pepsin. Modification of the enzyme by trimethyloxonium fluoroborate. European Journal of Biochemistry. 31: 510-7. PMID 4569455 DOI: 10.1111/J.1432-1033.1972.Tb02559.X |
0.358 |
|
| 1972 |
De la Mare S, Coulson AF, Knowles JR, Priddle JD, Offord RE. Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine. The Biochemical Journal. 129: 321-31. PMID 4643320 DOI: 10.1042/BJ1290321 |
0.319 |
|
| 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 |
0.439 |
|
| 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 |
0.447 |
|
| 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 |
0.589 |
|
| 1969 |
Cornish-Bowden AJ, Knowles JR. The pH-dependence of pepsin-catalysed reactions. The Biochemical Journal. 113: 353-62. PMID 4897198 |
0.509 |
|
| 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 |
0.434 |
|
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