Year |
Citation |
Score |
2023 |
Cornish-Bowden A, Cárdenas ML. Evolution of Henrik Kacser's thought: Early publications on the organization of the whole system. Bio Systems. 104883. PMID 36931555 DOI: 10.1016/j.biosystems.2023.104883 |
0.601 |
|
2021 |
Cornish-Bowden A, Cárdenas ML. The essence of life revisited: how theories can shed light on it. Theory in Biosciences = Theorie in Den Biowissenschaften. PMID 33956294 DOI: 10.1007/s12064-021-00342-w |
0.609 |
|
2019 |
Cornish-Bowden A, Cárdenas ML. Contrasting Theories of Life: Historical Context, Current Theories. In search of an ideal theory. Bio Systems. 104063. PMID 31715221 DOI: 10.1016/J.Biosystems.2019.104063 |
0.646 |
|
2019 |
Mariscal C, Barahona A, Aubert-Kato N, Aydinoglu AU, Bartlett S, Cárdenas ML, Chandru K, Cleland C, Cocanougher BT, Comfort N, Cornish-Bowden A, Deacon T, Froese T, Giovannelli D, Hernlund J, et al. Hidden Concepts in the History and Philosophy of Origins-of-Life Studies: a Workshop Report. Origins of Life and Evolution of the Biosphere : the Journal of the International Society For the Study of the Origin of Life. PMID 31399826 DOI: 10.1007/S11084-019-09580-X |
0.621 |
|
2017 |
Cornish-Bowden A. Enthalpy-entropy compensation and the isokinetic temperature in enzyme catalysis. Journal of Biosciences. 42: 665-670. PMID 29229884 DOI: 10.1007/S12038-017-9719-0 |
0.326 |
|
2017 |
Cornish-Bowden A, Cárdenas ML. Life before LUCA. Journal of Theoretical Biology. 434: 68-74. PMID 28536033 DOI: 10.1016/J.Jtbi.2017.05.023 |
0.629 |
|
2017 |
Cárdenas ML, Benomar S, Cornish-Bowden A. Rosennean complexity and its relevance to ecology Ecological Complexity. 35: 13-24. DOI: 10.1016/J.Ecocom.2017.04.005 |
0.641 |
|
2016 |
Bocedi A, Fabrini R, Lo Bello M, Caccuri AM, Federici G, Mannervik B, Cornish-Bowden A, Ricci G. Evolution of Negative Cooperativity in Glutathione Transferase Enabled Preservation of Enzyme Function. The Journal of Biological Chemistry. 291: 26739-26749. PMID 27815499 DOI: 10.1074/Jbc.M116.749507 |
0.328 |
|
2015 |
Cornish-Bowden A. One hundred years of Michaelis–Menten kinetics☆ Perspectives On Science. 4: 3-9. DOI: 10.1016/J.Pisc.2014.12.002 |
0.327 |
|
2014 |
Cornish-Bowden A, Mazat JP, Nicolas S. Victor Henri: 111 years of his equation. Biochimie. 107: 161-6. PMID 25252213 DOI: 10.1016/J.Biochi.2014.09.018 |
0.35 |
|
2014 |
Cornish-Bowden A, Pereto J, Cardenas ML. Biochemistry and evolutionary biology: two disciplines that need each other? Journal of Biosciences. 39: 13-27. PMID 24499786 DOI: 10.1007/S12038-014-9414-3 |
0.639 |
|
2014 |
Asenjo JL, Ludwig HC, Droppelmann CA, Cárcamo JG, Concha II, Yáñez AJ, Cárdenas ML, Cornish-Bowden A, Slebe JC. Subunit interactions in pig-kidney fructose-1,6-bisphosphatase: binding of substrate induces a second class of site with lowered affinity and catalytic activity. Biochimica Et Biophysica Acta. 1840: 1798-807. PMID 24444799 DOI: 10.1016/J.Bbagen.2013.12.027 |
0.645 |
|
2014 |
Cornish-Bowden A. Introduction: Enzyme catalysis and allostery: a century of advances in molecular understanding. The Febs Journal. 281: 433-4. PMID 24405881 DOI: 10.1111/Febs.12695 |
0.327 |
|
2014 |
Curien G, Cárdenas ML, Cornish-Bowden A. Analytical kinetic modeling: a practical procedure. Methods in Molecular Biology (Clifton, N.J.). 1090: 261-80. PMID 24222421 DOI: 10.1007/978-1-62703-688-7_16 |
0.68 |
|
2014 |
Cornish-Bowden A. Understanding allosteric and cooperative interactions in enzymes. The Febs Journal. 281: 621-32. PMID 23910900 DOI: 10.1111/Febs.12469 |
0.32 |
|
2014 |
Tipton KF, Armstrong RN, Bakker BM, Bairoch A, Cornish-Bowden A, Halling PJ, Hofmeyr J, Leyh TS, Kettner C, Raushel FM, Rohwer J, Schomburg D, Steinbeck C. Standards for Reporting Enzyme Data: The STRENDA Consortium: What it aims to do and why it should be helpful Perspectives in Science. 1: 131-137. DOI: 10.1016/J.Pisc.2014.02.012 |
0.603 |
|
2014 |
Cornish-Bowden A. Analysis and interpretation of enzyme kinetic data Perspectives On Science. 1: 121-125. DOI: 10.1016/J.Pisc.2014.02.010 |
0.314 |
|
2014 |
Cornish-Bowden A. Current IUBMB recommendations on enzyme nomenclature and kinetics Perspectives On Science. 1: 74-87. DOI: 10.1016/J.Pisc.2014.02.006 |
0.332 |
|
2013 |
Cornish-Bowden A. Biochemistry: Curbing the excesses of low demand. Nature. 500: 157-8. PMID 23903659 DOI: 10.1038/Nature12461 |
0.363 |
|
2013 |
Cornish-Bowden A. The origins of enzyme kinetics. Febs Letters. 587: 2725-30. PMID 23791665 DOI: 10.1016/J.Febslet.2013.06.009 |
0.349 |
|
2013 |
Cornish-Bowden A, Piedrafita G, Morán F, Cárdenas ML, Montero FJ. Simulating a model of metabolic closure Biological Theory. 8: 383-390. DOI: 10.1007/S13752-013-0132-0 |
0.665 |
|
2012 |
Piedrafita G, Cornish-Bowden A, Morán F, Montero F. Size matters: influence of stochasticity on the self-maintenance of a simple model of metabolic closure. Journal of Theoretical Biology. 300: 143-51. PMID 22266121 DOI: 10.1016/J.Jtbi.2012.01.013 |
0.328 |
|
2011 |
Letelier JC, Cárdenas ML, Cornish-Bowden A. From L'Homme Machine to metabolic closure: steps towards understanding life. Journal of Theoretical Biology. 286: 100-13. PMID 21763318 DOI: 10.1016/J.Jtbi.2011.06.033 |
0.777 |
|
2011 |
Cárdenas ML, Letelier JC, Gutierrez C, Cornish-Bowden A, Soto-Andrade J. Corrigendum to "Closure to efficient causation, computability and artificial life" [J. Theor. Biol. 263 (2010) 79-92] Journal of Theoretical Biology. 274: 186. DOI: 10.1016/J.Jtbi.2011.01.030 |
0.742 |
|
2010 |
Cornish-Bowden A, Cárdenas ML. Specificity of non-Michaelis-Menten enzymes: necessary information for analyzing metabolic pathways. The Journal of Physical Chemistry. B. 114: 16209-13. PMID 21028874 DOI: 10.1021/Jp106968P |
0.669 |
|
2010 |
Apweiler R, Armstrong R, Bairoch A, Cornish-Bowden A, Halling PJ, Hofmeyr JH, Kettner C, Leyh TS, Rohwer J, Schomburg D, Steinbeck C, Tipton K. A large-scale protein-function database. Nature Chemical Biology. 6: 785. PMID 20956966 DOI: 10.1038/Nchembio.460 |
0.583 |
|
2010 |
Piedrafita G, Montero F, Morán F, Cárdenas ML, Cornish-Bowden A. A simple self-maintaining metabolic system: robustness, autocatalysis, bistability. Plos Computational Biology. 6. PMID 20700491 DOI: 10.1371/Journal.Pcbi.1000872 |
0.628 |
|
2010 |
Cárdenas ML, Letelier JC, Gutierrez C, Cornish-Bowden A, Soto-Andrade J. Closure to efficient causation, computability and artificial life. Journal of Theoretical Biology. 263: 79-92. PMID 19962389 DOI: 10.1016/J.Jtbi.2009.11.010 |
0.766 |
|
2009 |
Meléndez-Hevia E, De Paz-Lugo P, Cornish-Bowden A, Cárdenas ML. A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen synthesis. Journal of Biosciences. 34: 853-72. PMID 20093739 DOI: 10.1007/S12038-009-0100-9 |
0.643 |
|
2009 |
Curien G, Bastien O, Robert-Genthon M, Cornish-Bowden A, Cárdenas ML, Dumas R. Understanding the regulation of aspartate metabolism using a model based on measured kinetic parameters. Molecular Systems Biology. 5: 271. PMID 19455135 DOI: 10.1038/Msb.2009.29 |
0.627 |
|
2008 |
Cornish-Bowden A. Reinhart Heinrich (1946-2006): an annotated bibliography. Journal of Theoretical Biology. 252: 379-87. PMID 18190930 DOI: 10.1016/J.Jtbi.2007.11.011 |
0.316 |
|
2008 |
Cornish-Bowden A, Cárdenas ML. Self-organization at the origin of life. Journal of Theoretical Biology. 252: 411-8. PMID 17889904 DOI: 10.1016/J.Jtbi.2007.07.035 |
0.631 |
|
2007 |
Cornish-Bowden A, Cárdenas ML. The threat from creationism to the rational teaching of biology. Biological Research. 40: 113-22. PMID 18064348 DOI: 10.4067/S0716-97602007000200002 |
0.613 |
|
2007 |
Cornish-Bowden A, Cárdenas ML. Organizational invariance in (M,R)-systems. Chemistry & Biodiversity. 4: 2396-406. PMID 17955465 DOI: 10.1002/Cbdv.200790195 |
0.643 |
|
2007 |
Cornish-Bowden A, Cárdenas ML, Letelier JC, Soto-Andrade J. Beyond reductionism: metabolic circularity as a guiding vision for a real biology of systems. Proteomics. 7: 839-45. PMID 17370262 DOI: 10.1002/Pmic.200600431 |
0.788 |
|
2006 |
Letelier JC, Soto-Andrade J, Guíñez Abarzúa F, Cornish-Bowden A, Luz Cárdenas M. Organizational invariance and metabolic closure: analysis in terms of (M,R) systems. Journal of Theoretical Biology. 238: 949-61. PMID 16122760 DOI: 10.1016/J.Jtbi.2005.07.007 |
0.744 |
|
2005 |
Cornish-Bowden A, Cárdenas ML. Systems biology may work when we learn to understand the parts in terms of the whole. Biochemical Society Transactions. 33: 516-9. PMID 15916554 DOI: 10.1042/Bst0330516 |
0.671 |
|
2005 |
Apweiler R, Cornish-Bowden A, Hofmeyr JH, Kettner C, Leyh TS, Schomburg D, Tipton K. The importance of uniformity in reporting protein-function data. Trends in Biochemical Sciences. 30: 11-2. PMID 15653320 DOI: 10.1016/J.Tibs.2004.11.002 |
0.58 |
|
2004 |
Cornish-Bowden A, Cárdenas ML, Letelier JC, Soto-Andrade J, Abarzúa FG. Understanding the parts in terms of the whole. Biology of the Cell. 96: 713-7. PMID 15567526 DOI: 10.1016/J.Biolcel.2004.06.006 |
0.803 |
|
2003 |
Cornish-Bowden A, Cárdenas ML. Metabolic analysis in drug design. Comptes Rendus Biologies. 326: 509-15. PMID 12886878 DOI: 10.1016/S1631-0691(03)00117-3 |
0.676 |
|
2003 |
Hucka M, Finney A, Sauro HM, Bolouri H, Doyle JC, Kitano H, Arkin AP, Bornstein BJ, Bray D, Cornish-Bowden A, Cuellar AA, Dronov S, Gilles ED, Ginkel M, Gor V, et al. The systems biology markup language (SBML): a medium for representation and exchange of biochemical network models. Bioinformatics (Oxford, England). 19: 524-31. PMID 12611808 DOI: 10.1093/Bioinformatics/Btg015 |
0.592 |
|
2002 |
Cornish-Bowden A, Cárdenas ML. Metabolic balance sheets. Nature. 420: 129-30. PMID 12432369 DOI: 10.1038/420129A |
0.638 |
|
2002 |
María LC, Ortega F, Cascante M, Cornish-Bowden A. Modulation of metabolite concentrations with no net effect on fluxes. Molecular Biology Reports. 29: 17-20. PMID 12241051 DOI: 10.1023/A:1020337831393 |
0.355 |
|
2002 |
Cornish-Bowden A, Hofmeyr JH. The role of stoichiometric analysis in studies of metabolism: an example. Journal of Theoretical Biology. 216: 179-91. PMID 12079370 DOI: 10.1006/Jtbi.2002.2547 |
0.617 |
|
2002 |
Cornish-Bowden A, Hofmeyr JH, Cárdenas ML. Stoicheiometric analysis in studies of metabolism. Biochemical Society Transactions. 30: 43-6. PMID 12023821 DOI: 10.1042/Bst0300043 |
0.737 |
|
2002 |
Cornish-Bowden A, Hofmeyr JS. The role of stoicheiometric analysis in studies of metabolism Biochemical Society Transactions. 30: A6-A6. DOI: 10.1042/Bst030A006C |
0.609 |
|
2001 |
Cornish-Bowden A, Cárdenas ML. Information transfer in metabolic pathways. Effects of irreversible steps in computer models. European Journal of Biochemistry / Febs. 268: 6616-24. PMID 11737216 DOI: 10.1046/J.0014-2956.2001.02616.X |
0.654 |
|
2001 |
Cornish-Bowden A, Cárdenas ML. Complex networks of interactions connect genes to phenotypes. Trends in Biochemical Sciences. 26: 463-5. PMID 11504611 DOI: 10.1016/S0968-0004(01)01920-X |
0.615 |
|
2001 |
Cortés A, Cascante M, Cárdenas ML, Cornish-Bowden A. Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: new ways of analysing data. The Biochemical Journal. 357: 263-8. PMID 11415458 DOI: 10.1042/Bj3570263 |
0.627 |
|
2001 |
Cornish-Bowden A. Detection of errors of interpretation in experiments in enzyme kinetics. Methods (San Diego, Calif.). 24: 181-90. PMID 11384193 DOI: 10.1006/Meth.2001.1179 |
0.333 |
|
2001 |
Cornish-Bowden A, Cárdenas ML. Functional genomics. Silent genes given voice. Nature. 409: 571-2. PMID 11214302 DOI: 10.1038/35054646 |
0.59 |
|
2000 |
Hofmeyr JS, Cornish-Bowden A. Regulating the cellular economy of supply and demand. Febs Letters. 476: 47-51. PMID 10878248 DOI: 10.1016/S0014-5793(00)01668-9 |
0.619 |
|
2000 |
Cárdenas ML, Cornish-Bowden A. Metabolic analysis in drug discovery. Science (New York, N.Y.). 288: 618-9. PMID 10798998 DOI: 10.1126/Science.288.5466.617E |
0.625 |
|
2000 |
Cornish-Bowden A, Cárdenas ML. From genome to cellular phenotype--a role for metabolic flux analysis? Nature Biotechnology. 18: 267-8. PMID 10700136 DOI: 10.1038/73696 |
0.643 |
|
2000 |
Hofmeyr JS, Cornish-Bowden A. Making sense of the cellular economy and its regulation: a framework for biotechnological manipulation Biochemical Society Transactions. 28: A106-A106. DOI: 10.1042/Bst028A106C |
0.569 |
|
2000 |
Cornish-Bowden A. A solid account of enzymes Trends in Biochemical Sciences. 25: 646-647. DOI: 10.1016/S0968-0004(00)01651-0 |
0.32 |
|
1999 |
De Atauri P, Curto R, Puigjaner J, Cornish-Bowden A, Cascante M. Advantages and disadvantages of aggregating fluxes into synthetic and degradative fluxes when modelling metabolic pathways. European Journal of Biochemistry / Febs. 265: 671-9. PMID 10504399 DOI: 10.1046/J.1432-1327.1999.00760.X |
0.365 |
|
1999 |
Cornish-Bowden A. Enzyme kinetics from a metabolic perspective. Biochemical Society Transactions. 27: 281-4. PMID 10093748 DOI: 10.1042/Bst0270281 |
0.394 |
|
1999 |
Cárdenas ML, Cornish-Bowden A, Ureta T. Evolution of Hexokinases Biochemical Society Transactions. 27. DOI: 10.1042/Bst027A056A |
0.601 |
|
1999 |
Cornish-Bowden A. Metabolic complexity has no bearing on genetic determinism Behavioral and Brain Sciences. 22: 889-890. DOI: 10.1017/S0140525X99272202 |
0.316 |
|
1998 |
Cárdenas ML, Cornish-Bowden A, Ureta T. Evolution and regulatory role of the hexokinases. Biochimica Et Biophysica Acta. 1401: 242-64. PMID 9540816 DOI: 10.1016/S0167-4889(97)00150-X |
0.61 |
|
1998 |
Eisenthal R, Cornish-Bowden A. Prospects for antiparasitic drugs. The case of Trypanosoma brucei, the causative agent of African sleeping sickness. The Journal of Biological Chemistry. 273: 5500-5. PMID 9488673 DOI: 10.1074/Jbc.273.10.5500 |
0.345 |
|
1997 |
Giordani R, Buc J, Cornish-Bowden A, Cárdenas ML. Kinetics of membrane-bound nitrate reductase A from Escherichia coli with analogues of physiological electron donors--different reaction sites for menadiol and duroquinol. European Journal of Biochemistry / Febs. 250: 567-77. PMID 9428711 DOI: 10.1111/J.1432-1033.1997.0567A.X |
0.614 |
|
1997 |
Hofmeyr JH, Cornish-Bowden A. The reversible Hill equation: how to incorporate cooperative enzymes into metabolic models. Computer Applications in the Biosciences : Cabios. 13: 377-85. PMID 9283752 DOI: 10.1093/Bioinformatics/13.4.377 |
0.592 |
|
1996 |
Hofmeyr JH, Cornish-Bowden A. Co-response analysis: a new experimental strategy for metabolic control analysis. Journal of Theoretical Biology. 182: 371-80. PMID 8944170 DOI: 10.1006/Jtbi.1996.0176 |
0.632 |
|
1996 |
Giersch C, Cornish-Bowden A. Extending double modulation: combinatorial rules for identifying the modulations necessary for determining elasticities in metabolic pathways. Journal of Theoretical Biology. 182: 361-9. PMID 8944169 DOI: 10.1006/Jtbi.1996.0175 |
0.35 |
|
1995 |
Buc J, Santini CL, Blasco F, Giordani R, Cárdenas ML, Chippaux M, Cornish-Bowden A, Giordano G. Kinetic studies of a soluble alpha beta complex of nitrate reductase A from Escherichia coli. Use of various alpha beta mutants with altered beta subunits. European Journal of Biochemistry / Febs. 234: 766-72. PMID 8575433 DOI: 10.1111/J.1432-1033.1995.766_A.X |
0.569 |
|
1995 |
Cornish-Bowden A, Hofmeyr JHS, Cárdenas ML. Strategies for manipulating metabolic fluxes in biotechnology Bioorganic Chemistry. 23: 439-449. DOI: 10.1006/bioo.1995.1030 |
0.568 |
|
1994 |
Cornish-Bowden A, Hofmeyr JH. Determination of control coefficients in intact metabolic systems. The Biochemical Journal. 298: 367-75. PMID 8135743 DOI: 10.1042/Bj2980367 |
0.606 |
|
1994 |
Cornish-Bowden A. Encyclopaedic enzyme kinetics: Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems by Irwin H. Segel, Wiley, 1993 (reprint of 1975 edition). £39.95 (957 pages) ISBN 0 471 30309 7 Trends in Biochemical Sciences. 19: 142. DOI: 10.1016/0968-0004(94)90211-9 |
0.338 |
|
1993 |
Cárdenas ML, Cornish-Bowden A. Rounding error, an unexpected fault in the output from a recording spectrophotometer: implications for model discrimination. The Biochemical Journal. 292: 37-40. PMID 8503861 DOI: 10.1042/Bj2920037 |
0.595 |
|
1993 |
Cornish-Bowden A, Cárdenas ML. Channelling can affect concentrations of metabolic intermediates at constant net flux: artefact or reality? European Journal of Biochemistry / Febs. 213: 87-92. PMID 8477736 DOI: 10.1111/J.1432-1033.1993.Tb17737.X |
0.663 |
|
1993 |
Hofmeyr JH, Cornish-Bowden A, Rohwer JM. Taking enzyme kinetics out of control; putting control into regulation. European Journal of Biochemistry / Febs. 212: 833-7. PMID 8462553 |
0.554 |
|
1993 |
Chevillard C, Cárdenas ML, Cornish-Bowden A. The competition plot: a simple test of whether two reactions occur at the same active site. The Biochemical Journal. 289: 599-604. PMID 8424801 DOI: 10.1042/Bj2890599 |
0.652 |
|
1992 |
Szedlacsek SE, Cárdenas ML, Cornish-Bowden A. Response coefficients of interconvertible enzyme cascades towards effectors that act on one or both modifier enzymes. European Journal of Biochemistry / Febs. 204: 807-13. PMID 1541294 DOI: 10.1111/J.1432-1033.1992.Tb16699.X |
0.655 |
|
1992 |
Cornish-Bowden A, Cárdenas ML. Cornish-Bowden and Cárdenas reply Trends in Biochemical Sciences. 17: 59. DOI: 10.1016/0968-0004(92)90501-Y |
0.576 |
|
1991 |
Cornish-Bowden A, Hofmeyr JH. MetaModel: a program for modelling and control analysis of metabolic pathways on the IBM PC and compatibles. Computer Applications in the Biosciences : Cabios. 7: 89-93. PMID 2004280 DOI: 10.1093/Bioinformatics/7.1.89 |
0.612 |
|
1991 |
Hofmeyr JH, Cornish-Bowden A. Quantitative assessment of regulation in metabolic systems. European Journal of Biochemistry / Febs. 200: 223-36. PMID 1879427 DOI: 10.1111/J.1432-1033.1991.Tb21071.X |
0.635 |
|
1989 |
Cárdenas ML, Cornish-Bowden A. Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector. The Biochemical Journal. 257: 339-45. PMID 2930453 DOI: 10.1042/Bj2570339 |
0.666 |
|
1989 |
Cornish-Bowden A. Metabolic control therapy and biochemical systems theory: different objectives, different assumptions, different results. Journal of Theoretical Biology. 136: 365-77. PMID 2682007 DOI: 10.1016/S0022-5193(89)80154-7 |
0.307 |
|
1989 |
Cornish-Bowden A. Nonequilibrium isotope exchange methods for investigating enzyme mechanisms. Current Topics in Cellular Regulation. 30: 143-69. PMID 2533544 DOI: 10.1016/B978-0-12-152830-0.50007-4 |
0.339 |
|
1987 |
Pollard-Knight D, Cornish-Bowden A. Kinetics of hexokinase D ('glucokinase') with inosine triphosphate as phosphate donor. Loss of kinetic co-operativity with respect to glucose. The Biochemical Journal. 245: 625-9. PMID 3663182 DOI: 10.1042/Bj2450625 |
0.33 |
|
1987 |
Cornish-Bowden A. Dominance is not inevitable. Journal of Theoretical Biology. 125: 333-8. PMID 3657214 DOI: 10.1016/S0022-5193(87)80065-6 |
0.401 |
|
1987 |
Cornish-Bowden A, Cárdenas ML. Co-operativity in monomeric enzymes. Journal of Theoretical Biology. 124: 1-23. PMID 3309473 DOI: 10.1016/S0022-5193(87)80248-5 |
0.646 |
|
1986 |
Gregoriou M, Trayer IP, Cornish-Bowden A. Allosteric character of the inhibition of rat-muscle hexokinase B by glucose 6-phosphate. European Journal of Biochemistry / Febs. 161: 171-6. PMID 3780733 DOI: 10.1111/J.1432-1033.1986.Tb10138.X |
0.697 |
|
1986 |
Cornish-Bowden A. Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides. Febs Letters. 203: 3-6. PMID 3720956 DOI: 10.1016/0014-5793(86)81424-7 |
0.367 |
|
1986 |
Cornish-Bowden A, Storer AC. Mechanistic origin of the sigmoidal rate behaviour of rat liver hexokinase D ('glucokinase'). The Biochemical Journal. 240: 293-6. PMID 3493769 DOI: 10.1042/Bj2400293 |
0.622 |
|
1986 |
Cornish-Bowden A. Why are enzymes so small? or why do biochemists ask 'why are enzymes so big?' Trends in Biochemical Sciences. 11: 286. DOI: 10.1016/0968-0004(86)90028-9 |
0.322 |
|
1985 |
Burns JA, Cornish-Bowden A, Groen AK, Heinrich R, Kacser H, Porteous JW, Rapoport SM, Rapoport TA, Stucki JW, Tager JM, Wanders RJA, Westerhoff HV. Control analysis of metabolic systems Trends in Biochemical Sciences. 10: 16. DOI: 10.1016/0968-0004(85)90008-8 |
0.308 |
|
1984 |
Cornish-Bowden A. Enzyme specificity: its meaning in the general case. Journal of Theoretical Biology. 108: 451-7. PMID 6748701 DOI: 10.1016/S0022-5193(84)80045-4 |
0.346 |
|
1984 |
Pollard-Knight D, Cornish-Bowden A. Solvent isotope effects on the glucokinase reaction. Negative co-operativity and a large inverse isotope effect in 2H2O. European Journal of Biochemistry / Febs. 141: 157-63. PMID 6327304 DOI: 10.1111/J.1432-1033.1984.Tb08170.X |
0.327 |
|
1984 |
Adams KAH, Storer AC, Cornish-Bowden A. Enzyme kinetics calculations - The direct linear plot procedure Journal of Chemical Education. 61: 527. DOI: 10.1021/Ed061P527.1 |
0.587 |
|
1984 |
Dixon HBF, Cornish-Bowden A. Revision of enzyme nomenclature: Listing enzymes: Nomenclature Committee of the International Union of Biochemistry Archives of Biochemistry and Biophysics. 229: 657. DOI: 10.1016/0003-9861(84)90199-1 |
0.324 |
|
1983 |
Cornish-Bowden A. Metabolic efficiency: is it a useful concept? Biochemical Society Transactions. 11: 44-45. PMID 6825914 DOI: 10.1042/Bst0110044 |
0.312 |
|
1983 |
Gregoriou M, Trayer IP, Cornish-Bowden A. Isotope-exchange evidence that glucose 6-phosphate inhibits rat-muscle hexokinase II at an allosteric site. European Journal of Biochemistry / Febs. 134: 283-8. PMID 6603359 DOI: 10.1111/J.1432-1033.1983.Tb07563.X |
0.675 |
|
1982 |
Pollard-Knight D, Cornish-Bowden A. Mechanism of liver glucokinase. Molecular and Cellular Biochemistry. 44: 71-80. PMID 7048063 DOI: 10.1007/Bf00226892 |
0.349 |
|
1982 |
Jackson RH, Cole JA, Cornish-Bowden A. The steady state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12. The reduction of single-electron acceptors Biochemical Journal. 203: 505-510. PMID 6288003 DOI: 10.1042/Bj2030505 |
0.302 |
|
1981 |
Gregoriou M, Cornish-Bowden A, Trayer IP. Isotope-exchange evidence for allosteric regulation of hexokinase II by glucose 6-phosphate and for an obligatory addition of substrates. Biochemical Society Transactions. 9: 62-3. PMID 7011877 DOI: 10.1042/Bst0090062A |
0.674 |
|
1981 |
Gregoriou M, Trayer IP, Cornish-Bowden A. Isotope-exchange evidence for an ordered mechanism for rat-liver glucokinase, a monomeric cooperative enzyme. Biochemistry. 20: 499-506. PMID 7011363 DOI: 10.1021/Bi00506A009 |
0.697 |
|
1981 |
Jackson RH, Cole JA, Cornish-Bowden A. The steady-state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12. Nitrite and hydroxylamine reduction Biochemical Journal. 199: 171-178. PMID 6279095 DOI: 10.1042/Bj1990171 |
0.355 |
|
1981 |
Gregoriou M, Trayer IP, Cornish-Bowden A. MECHANISTIC STUDIES OF RAT MUSCLE HEXOKINASE II Biochemical Society Transactions. 9: 158P-158P. DOI: 10.1042/Bst009158Pe |
0.63 |
|
1981 |
Cornish-Bowden A, Gregoriou M. Measurement of flux ratios as a probe of enzyme mechanisms Trends in Biochemical Sciences. 6: 149-150. DOI: 10.1016/0968-0004(81)90055-4 |
0.696 |
|
1980 |
Cornish-Bowden A. Number 3 in the Enzymes dynasty Nature. 286: 745-745. DOI: 10.1038/286745A0 |
0.31 |
|
1979 |
Cornish-Bowden A, Connolly BA, Gregoriou M, Holroyde MJ, Storer AC, Trayer IP. Mammalian hexokinases: a system for the study of co-operativity in monomeric enzymes. Archivos De Biologãa Y Medicina Experimentales. 12: 581-5. PMID 552244 |
0.74 |
|
1978 |
Coleman KJ, Cornish-Bowden A, Cole JA. Purification and properties of nitrite reductase from Escherichia coli K12 Biochemical Journal. 175: 483-493. PMID 217342 DOI: 10.1042/Bj1750483 |
0.331 |
|
1977 |
Brocklehurst K, Cornish-Bowden A. The pre-eminence of k(cat) in the manifestation of optimal enzymic activity delineated by using the Briggs-Haldane two-step irreversible kinetic model. The Biochemical Journal. 159: 165-6. PMID 999634 DOI: 10.1042/Bj1590165 |
0.346 |
|
1977 |
Storer AC, Cornish-Bowden A. Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinase. The Biochemical Journal. 165: 61-9. PMID 889576 DOI: 10.1042/Bj1650061 |
0.615 |
|
1976 |
Holroyde MJ, Allen MB, Storer AC, Warsy AS, Chesher JM, Trayer IP, Cornish-Bowden A, Walker DG. The purification in high yield and characterization of rat hepatic glucokinase. The Biochemical Journal. 153: 363-73. PMID 1275894 DOI: 10.1042/Bj1530363 |
0.6 |
|
1976 |
Cornish-Bowden A. The effect of natural selection on enzymic catalysis Journal of Molecular Biology. 101: 1-9. PMID 1255718 DOI: 10.1016/0022-2836(76)90062-0 |
0.356 |
|
1976 |
Storer AC, Cornish-Bowden A. Kinetics of rat liver glucokinase. Co-operative interactions with glucose at physiologically significant concentrations. The Biochemical Journal. 159: 7-14. PMID 999645 DOI: 10.1042/Bj1590007 |
0.579 |
|
1976 |
Storer AC, Cornish-Bowden A. Concentration of MgATP2- and other ions in solution. Calculation of the true concentrations of species present in mixtures of associating ions. The Biochemical Journal. 159: 1-5. PMID 11772 |
0.517 |
|
1976 |
Cornish-Bowden A. Estimation of the dissociation constants of enzyme-substrate complexes from steady-state measurements. Interpretation of pH-independence of Km. Biochemical Journal. 153: 455-461. PMID 6011 DOI: 10.1042/Bj1530455 |
0.314 |
|
1975 |
Storer AC, Darlison MG, Cornish-Bowden A. The nature of experimental error in enzyme kinetic measurments. The Biochemical Journal. 151: 361-7. PMID 1218083 DOI: 10.1042/Bj1510361 |
0.587 |
|
1975 |
Cornish-Bowden A. The use of the direct linear plot for determining initial velocities. The Biochemical Journal. 149: 305-12. PMID 1180900 DOI: 10.1042/Bj1490305 |
0.334 |
|
1975 |
Cornish-Bowden A, Koshland DE. Diagnostic uses of the Hill (logit and Nernst) plots Journal of Molecular Biology. 95: 201-212. PMID 171413 DOI: 10.1016/0022-2836(75)90390-3 |
0.422 |
|
1974 |
Eisenthal R, Cornish-Bowden A. The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. The Biochemical Journal. 139: 715-20. PMID 4854723 DOI: 10.1042/Bj1390715 |
0.323 |
|
1974 |
Storer AC, Cornish-Bowden A. The kinetics of coupled enzyme reactions. Applications to the assay of glucokinase, with glucose 6-phosphate dehydrogenase as coupling enzyme. The Biochemical Journal. 141: 205-9. PMID 4375970 DOI: 10.1042/Bj1410205 |
0.608 |
|
1971 |
Cornish-Bowden AJ, Koshland DE. The quaternary structure of proteins composed of identical subunits Journal of Biological Chemistry. 246: 3092-3102. PMID 5574388 |
0.32 |
|
1970 |
Cornish-Bowden A, Koshland DE. The influence of binding domains on the nature of subunit interactions in oligomeric proteins. Application to unusual kinetic and binding patterns Journal of Biological Chemistry. 245: 6241-6250. PMID 5484808 |
0.329 |
|
1970 |
Cornish-Bowden A, Koshland DE. A general method for the quantitative determination of saturation curves for multisubunit proteins Biochemistry. 9: 3325-3336. PMID 4330854 DOI: 10.1021/Bi00819A006 |
0.33 |
|
1970 |
Cornish-Bowden AJ, Cook RA, Koshland DE. A curve-fitting procedure for the study of the binding of small molecules to multi-subunit proteins Il Farmaco; Edizione Scientifica. 25: 786-798. PMID 4320826 |
0.337 |
|
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 |
0.505 |
|
1969 |
Cornish-Bowden AJ, Knowles JR. The pH-dependence of pepsin-catalysed reactions. The Biochemical Journal. 113: 353-62. PMID 4897198 |
0.45 |
|
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