| Year |
Citation |
Score |
| 2011 |
Alberty RA, Cornish-Bowden A, Goldberg RN, Hammes GG, Tipton K, Westerhoff HV. Recommendations for terminology and databases for biochemical thermodynamics. Biophysical Chemistry. 155: 89-103. PMID 21501921 DOI: 10.1016/J.Bpc.2011.03.007 |
0.619 |
|
| 2010 |
Alberty RA. Biochemical thermodynamics and rapid-equilibrium enzyme kinetics. The Journal of Physical Chemistry. B. 114: 17003-12. PMID 21090637 DOI: 10.1021/Jp107337G |
0.471 |
|
| 2010 |
Alberty RA. Consumption of hydrogen ions in rapid-equilibrium enzyme kinetics. The Journal of Physical Chemistry. B. 114: 16083-6. PMID 20550143 DOI: 10.1021/Jp911945Q |
0.416 |
|
| 2010 |
Alberty RA. Estimation of kinetic parameters when modifiers are bound in enzyme-catalyzed reactions. The Journal of Physical Chemistry. B. 114: 1684-9. PMID 20055362 DOI: 10.1021/Jp908023U |
0.432 |
|
| 2009 |
Alberty RA. Determination of rapid-equilibrium kinetic parameters of ordered and random enzyme-catalyzed reaction A+B=P+Q. The Journal of Physical Chemistry. B. 113: 10043-8. PMID 19558174 DOI: 10.1021/Jp9021097 |
0.41 |
|
| 2009 |
Alberty RA. Determination of kinetic parameters of enzyme-catalyzed reaction a + B + C --> products with the minimum number of velocity measurements. The Journal of Physical Chemistry. B. 113: 1225-31. PMID 19159341 DOI: 10.1021/Jp8080436 |
0.365 |
|
| 2008 |
Alberty RA. Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements. Journal of Theoretical Biology. 254: 156-63. PMID 18582902 DOI: 10.1016/J.Jtbi.2008.05.022 |
0.382 |
|
| 2008 |
Alberty RA. Rapid-equilibrium rate equations for the enzymatic catalysis of A+B=P+Q over a range of pH. Biophysical Chemistry. 132: 114-26. PMID 18061334 DOI: 10.1016/J.Bpc.2007.10.015 |
0.409 |
|
| 2008 |
Alberty RA. Rapid-equilibrium enzyme kinetics Journal of Chemical Education. 85: 1136-1141. DOI: 10.1021/Ed085P1136 |
0.445 |
|
| 2007 |
Alberty RA. Effects of pH in rapid-equilibrium enzyme kinetics. The Journal of Physical Chemistry. B. 111: 14064-8. PMID 18027926 DOI: 10.1021/Jp076742X |
0.483 |
|
| 2007 |
Alberty RA. Three mechanisms and rapid-equilibrium rate equations for a type of reductase reaction. Biophysical Chemistry. 131: 71-9. PMID 17928131 DOI: 10.1016/J.Bpc.2007.09.005 |
0.435 |
|
| 2007 |
Alberty RA. Two different ways that hydrogen ions are involved in the thermodynamics and rapid-equilibrium kinetics of the enzymatic catalysis of S=P and S+H2O=P. Biophysical Chemistry. 128: 204-9. PMID 17490804 DOI: 10.1016/J.Bpc.2007.04.004 |
0.431 |
|
| 2007 |
Alberty RA. Changes in the standard transformed thermodynamic properties of enzyme-catalyzed reactions with ionic strength. The Journal of Physical Chemistry. B. 111: 3847-52. PMID 17388526 DOI: 10.1021/Jp068883P |
0.426 |
|
| 2007 |
Alberty RA. Thermodynamic properties of enzyme-catalyzed reactions involving cytosine, uracil, thymine, and their nucleosides and nucleotides. Biophysical Chemistry. 127: 91-6. PMID 17240519 DOI: 10.1016/J.Bpc.2006.12.010 |
0.448 |
|
| 2007 |
Alberty RA. Changes in binding of hydrogen ions in enzyme-catalyzed reactions. Biophysical Chemistry. 125: 328-33. PMID 17011697 DOI: 10.1016/J.Bpc.2006.09.007 |
0.435 |
|
| 2006 |
Alberty RA. Thermodynamics and kinetics of the glyoxylate cycle. Biochemistry. 45: 15838-43. PMID 17176106 DOI: 10.1021/Bi061829E |
0.441 |
|
| 2006 |
Alberty RA. Calculation of equilibrium compositions of systems of enzyme-catalyzed reactions. The Journal of Physical Chemistry. B. 110: 24775-9. PMID 17134243 DOI: 10.1021/Jp065609M |
0.39 |
|
| 2006 |
Alberty RA. Biochemical thermodynamics: applications of Mathematica. Methods of Biochemical Analysis. 48: 1-458. PMID 16878778 DOI: 10.1002/047003646X |
0.309 |
|
| 2006 |
Alberty RA. Relations between biochemical thermodynamics and biochemical kinetics. Biophysical Chemistry. 124: 11-7. PMID 16766115 DOI: 10.1016/J.Bpc.2006.05.024 |
0.464 |
|
| 2006 |
Alberty RA. Thermodynamics of the reactions of carbamoyl phosphate. Archives of Biochemistry and Biophysics. 451: 17-22. PMID 16684500 DOI: 10.1016/J.Abb.2006.03.025 |
0.495 |
|
| 2006 |
Alberty RA. Thermodynamics of the purine nucleotide cycle. Biophysical Chemistry. 122: 74-7. PMID 16603306 DOI: 10.1016/J.Bpc.2006.02.011 |
0.445 |
|
| 2006 |
Alberty RA. Thermodynamic properties of weak acids involved in enzyme-catalyzed reactions. The Journal of Physical Chemistry. B. 110: 5012-6. PMID 16526744 DOI: 10.1021/Jp0545086 |
0.417 |
|
| 2006 |
Alberty RA. Thermodynamic properties of enzyme-catalyzed reactions involving guanine, xanthine, and their nucleosides and nucleotides. Biophysical Chemistry. 121: 157-62. PMID 16466672 DOI: 10.1016/J.Bpc.2006.01.004 |
0.444 |
|
| 2006 |
Alberty RA. Standard molar entropies, standard entropies of formation, and standard transformed entropies of formation in the thermodynamics of enzyme-catalyzed reactions Journal of Chemical Thermodynamics. 38: 396-404. DOI: 10.1016/J.Jct.2005.06.006 |
0.414 |
|
| 2005 |
Alberty RA. Calculation of thermodynamic properties of species of biochemical reactants using the inverse Legendre transform. The Journal of Physical Chemistry. B. 109: 9132-9. PMID 16852086 DOI: 10.1021/Jp044162J |
0.381 |
|
| 2005 |
Alberty RA. Components and coupling in enzyme-catalyzed reactions. The Journal of Physical Chemistry. B. 109: 2021-6. PMID 16851187 DOI: 10.1021/Jp045423S |
0.443 |
|
| 2005 |
Alberty RA. Thermodynamics of the mechanism of the nitrogenase reaction. Biophysical Chemistry. 114: 115-20. PMID 15829344 DOI: 10.1016/J.Bpc.2004.11.009 |
0.365 |
|
| 2005 |
Alberty RA. Thermodynamic properties of oxidoreductase, transferase, hydrolase, and ligase reactions. Archives of Biochemistry and Biophysics. 435: 363-8. PMID 15708379 DOI: 10.1016/J.Abb.2004.12.027 |
0.429 |
|
| 2004 |
Alberty RA. Standard apparent reduction potentials of biochemical half reactions and thermodynamic data on the species involved. Biophysical Chemistry. 111: 115-22. PMID 15381309 DOI: 10.1016/J.Bpc.2004.05.003 |
0.462 |
|
| 2004 |
Alberty RA. Thermodynamic properties of nucleotide reductase reactions. Biochemistry. 43: 9840-5. PMID 15274638 DOI: 10.1021/Bi049353R |
0.415 |
|
| 2004 |
Alberty RA. A short history of the thermodynamics of enzyme-catalyzed reactions. The Journal of Biological Chemistry. 279: 27831-6. PMID 15073189 DOI: 10.1074/Jbc.X400003200 |
0.383 |
|
| 2004 |
Alberty RA. Equilibrium concentrations for pyruvate dehydrogenase and the citric acid cycle at specified concentrations of certain coenzymes. Biophysical Chemistry. 109: 73-84. PMID 15059661 DOI: 10.1016/J.Bpc.2003.10.019 |
0.401 |
|
| 2004 |
Alberty RA. Principle of detailed balance in kinetics Journal of Chemical Education. 81: 1206-1209. DOI: 10.1021/Ed081P1206 |
0.419 |
|
| 2004 |
Alberty RA. Use of standard Gibbs free energies and standard enthalpies of adenosine(aq) and adenine(aq) in the thermodynamics of enzyme-catalyzed reactions Journal of Chemical Thermodynamics. 36: 593-601. DOI: 10.1016/J.Jct.2004.03.010 |
0.355 |
|
| 2003 |
Alberty RA. Calculation of thermodynamic properties of species from binding of a ligand by a macromolecule. Biophysical Chemistry. 105: 45-58. PMID 12932578 DOI: 10.1016/S0301-4622(03)00133-9 |
0.371 |
|
| 2003 |
Alberty RA. Fundamental equation of thermodynamics for protein-ligand binding. Biophysical Chemistry. 104: 543-59. PMID 12914902 DOI: 10.1016/S0301-4622(03)00057-7 |
0.354 |
|
| 2003 |
Alberty RA. Standard transformed Gibbs energies of coenzyme A derivatives as functions of pH and ionic strength. Biophysical Chemistry. 104: 327-34. PMID 12834851 DOI: 10.1016/S0301-4622(02)00390-3 |
0.456 |
|
| 2003 |
Alberty RA. The role of water in the thermodynamics of dilute aqueous solutions. Biophysical Chemistry. 100: 183-92. PMID 12646365 DOI: 10.1016/S0301-4622(02)00280-6 |
0.411 |
|
| 2003 |
Alberty RA. Thermodynamics of the hydrolysis of adenosine triphosphate as a function of temperature, pH, pMg, and ionic strength Journal of Physical Chemistry B. 107: 12324-12330. DOI: 10.1021/Jp030576L |
0.38 |
|
| 2003 |
Alberty RA. Effect of temperature on the standard transformed thermodynamic properties of biochemical reactions with emphasis on the maxwell equations Journal of Physical Chemistry B. 107: 3631-3635. DOI: 10.1021/Jp022432X |
0.427 |
|
| 2002 |
Alberty RA. Thermodynamics of systems of biochemical reactions. Journal of Theoretical Biology. 215: 491-501. PMID 12069492 DOI: 10.1006/Jtbi.2001.2516 |
0.43 |
|
| 2002 |
Alberty RA. Inverse legendre transform in biochemical thermodynamics: Illustrated with the last five reactions of glycolysis Journal of Physical Chemistry B. 106: 6594-6599. DOI: 10.1021/Jp020764W |
0.466 |
|
| 2002 |
Alberty RA. Use of legendre transforms in chemical thermodynamics: International Union of Pure and Applied Chemistry, Physical Chemistry Division, Commission on Thermodynamics Journal of Chemical Thermodynamics. 34: 1787-1823. DOI: 10.1016/S0021-9614(02)00170-2 |
0.323 |
|
| 2001 |
Alberty RA. Systems of biochemical reactions from the point of view of a semigrand partition function. Biophysical Chemistry. 93: 1-10. PMID 11604212 DOI: 10.1016/S0301-4622(01)00202-2 |
0.418 |
|
| 2001 |
Alberty RA. Standard apparent reduction potentials for biochemical half reactions as a function of pH and ionic strength. Archives of Biochemistry and Biophysics. 389: 94-109. PMID 11370677 DOI: 10.1006/Abbi.2001.2318 |
0.429 |
|
| 2001 |
Alberty RA. Biochemical reaction equilibria from the point of view of a semigrand partition function Journal of Chemical Physics. 114: 8270-8274. DOI: 10.1063/1.1366638 |
0.444 |
|
| 2001 |
Alberty RA. Effect of temperature on standard transformed Gibbs energies of formation of reactants at specified pH and ionic strength and apparent equilibrium constants of biochemical reactions Journal of Physical Chemistry B. 105: 7865-7870. DOI: 10.1021/Jp011308V |
0.382 |
|
| 2001 |
Alberty RA. Calculation of equilibrium compositions of biochemical reaction systems involving water as a reactant Journal of Physical Chemistry B. 105: 1109-1114. DOI: 10.1021/Jp003515L |
0.341 |
|
| 2000 |
Alberty RA. Calculating apparent equilibrium constants of enzyme-catalyzed reactions at pH 7. Biochemical Education. 28: 12-17. PMID 10717447 DOI: 10.1111/J.1539-3429.2000.Tb00003.X |
0.441 |
|
| 2000 |
Alberty RA. Use of the Matrix Form of the Fundamental Equations for Transformed Gibbs Energies of Biochemical Reaction Systems at Three Levels Journal of Physical Chemistry B. 104: 650-657. DOI: 10.1021/Jp993460R |
0.347 |
|
| 2000 |
Alberty RA. Calculation of Equilibrium Compositions of Large Systems of Biochemical Reactions Journal of Physical Chemistry B. 104: 4807-4814. DOI: 10.1021/Jp000185W |
0.427 |
|
| 1999 |
Alberty RA. Calculation of standard formation properties of species from standard transformed formation properties of reactants in biochemical reactions at specified pH Journal of Physical Chemistry B. 103: 261-265. DOI: 10.1021/Jp983770U |
0.416 |
|
| 1998 |
Alberty RA. Calculation of standard transformed formation properties of biochemical reactants and standard apparent reduction potentials of half reactions. Archives of Biochemistry and Biophysics. 358: 25-39. PMID 9750161 DOI: 10.1006/Abbi.1998.0831 |
0.444 |
|
| 1998 |
Alberty RA. Calculation of standard transformed Gibbs energies and standard transformed enthalpies of biochemical reactants. Archives of Biochemistry and Biophysics. 353: 116-30. PMID 9578607 DOI: 10.1006/Abbi.1998.0638 |
0.416 |
|
| 1998 |
Alberty RA. Change in the binding of hydrogen ions and magnesium ions in the hydrolysis of ATP. Biophysical Chemistry. 70: 109-19. PMID 9540204 DOI: 10.1016/S0301-4622(97)00114-2 |
0.338 |
|
| 1997 |
Alberty RA. Apparent equilibrium constants and standard transformed Gibbs energies of biochemical reactions involving carbon dioxide. Archives of Biochemistry and Biophysics. 348: 116-24. PMID 9390181 DOI: 10.1006/Abbi.1997.0403 |
0.394 |
|
| 1997 |
Alberty RA. Constraints and missing reactions in the urea cycle. Biophysical Journal. 72: 2349-56. PMID 9129838 DOI: 10.1016/S0006-3495(97)78879-9 |
0.395 |
|
| 1997 |
Alberty RA. Determination of the seven apparent equilibrium constants for the binding of oxygen by hemoglobin from measured fractional saturations. Biophysical Chemistry. 63: 119-32. PMID 9108687 DOI: 10.1016/S0301-4622(96)02201-6 |
0.323 |
|
| 1997 |
Alberty RA. Thermodynamics of reactions involving phases at different electric potentials Journal of Physical Chemistry B. 101: 7191-7196. DOI: 10.1021/Jp971583A |
0.327 |
|
| 1997 |
Alberty RA. Legendre transforms in chemical thermodynamics Pure and Applied Chemistry. 69: 2221-2230. DOI: 10.1021/Cr00030A001 |
0.33 |
|
| 1996 |
Alberty RA. Thermodynamics of the binding of ligands by macromolecules. Biophysical Chemistry. 62: 141-59. PMID 8962475 DOI: 10.1016/S0301-4622(96)02200-4 |
0.33 |
|
| 1996 |
Alberty RA. IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (JCBN). Recommendations for nomenclature and tables in biochemical thermodynamics. Recommendations 1994. European Journal of Biochemistry / Febs. 240: 1-14. PMID 8925834 DOI: 10.1111/J.1432-1033.1996.0001H.X |
0.424 |
|
| 1996 |
Alberty RA. Calculation of biochemical net reactions and pathways by using matrix operations. Biophysical Journal. 71: 507-15. PMID 8804633 DOI: 10.1016/S0006-3495(96)79252-4 |
0.393 |
|
| 1995 |
Alberty RA. Components in chemical thermodynamics Journal of Chemical Education. 72: 820. DOI: 10.1021/Ed072P820 |
0.355 |
|
| 1994 |
Alberty RA. Constraints in biochemical reactions Biophysical Chemistry. 49: 251-261. DOI: 10.1016/0301-4622(93)E0075-G |
0.398 |
|
| 1993 |
Alberty RA, Goldberg RN. Calorimetric determination of the standard transformed enthalpy of a biochemical reaction at specified pH and pMg. Biophysical Chemistry. 47: 213-23. PMID 8241417 DOI: 10.1016/0301-4622(93)80046-L |
0.359 |
|
| 1993 |
Alberty RA. Levels of thermodynamic treatment of biochemical reaction systems. Biophysical Journal. 65: 1243-54. PMID 8241405 DOI: 10.1016/S0006-3495(93)81146-9 |
0.41 |
|
| 1993 |
Alberty RA. Thermodynamics of reactions of nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate. Archives of Biochemistry and Biophysics. 307: 8-14. PMID 8239668 DOI: 10.1006/Abbi.1993.1552 |
0.457 |
|
| 1993 |
Alberty RA, Cornish-Bowden A. The pH dependence of the apparent equilibrium constant, K', of a biochemical reaction. Trends in Biochemical Sciences. 18: 288-91. PMID 8236440 DOI: 10.1016/0968-0004(93)90036-M |
0.41 |
|
| 1993 |
Alberty RA. The fundamental equation of thermodynamics for biochemical reaction systems Pure and Applied Chemistry. 65: 883-888. DOI: 10.1351/Pac199365050883 |
0.378 |
|
| 1993 |
Alberty RA, Oppenheim I. New fundamental equations of thermodynamics for systems in chemical equilibrium at a specified partial pressure of a reactant and the standard transformed formation properties of reactants The Journal of Chemical Physics. 98: 8900-8904. DOI: 10.1063/1.464448 |
0.358 |
|
| 1993 |
Alberty RA. Degrees of freedom in a gaseous reaction system at a specified partial pressure of a reactant Journal of Physical Chemistry. 97: 6226-6232. DOI: 10.1021/J100125A023 |
0.34 |
|
| 1993 |
Alberty RA, Oppenheim I. Thermodynamics of a reaction system at a specified partial pressure of a reactant Journal of Chemical Education. 70: 629-635. DOI: 10.1021/Ed070P629 |
0.344 |
|
| 1992 |
Alberty RA. Equilibrium calculations on systems of biochemical reactions at specified pH and pMg. Biophysical Chemistry. 42: 117-31. PMID 1567986 DOI: 10.1016/0301-4622(92)85002-L |
0.434 |
|
| 1992 |
Alberty RA, Goldberg RN. Standard thermodynamic formation properties for the adenosine 5'-triphosphate series. Biochemistry. 31: 10610-5. PMID 1420176 DOI: 10.1021/Bi00158A025 |
0.416 |
|
| 1992 |
Alberty RA, Oppenheim I. Use of the fundamental equation to derive expressions for the transformed Gibbs energy, entropy, and enthalpy of a gaseous reaction system at a specified partial pressure of a reactant The Journal of Chemical Physics. 96: 9050-9054. DOI: 10.1063/1.462212 |
0.358 |
|
| 1992 |
Alberty RA. Degrees of freedom in biochemical reaction systems at specified pH and pMg Journal of Physical Chemistry. 96: 9614-9621. DOI: 10.1021/J100203A012 |
0.422 |
|
| 1992 |
Alberty RA. Conversion of chemical equations to biochemical equations Journal of Chemical Education. 69: 493. DOI: 10.1021/Ed069P493 |
0.319 |
|
| 1992 |
Alberty RA. Calculation of transformed thermodynamic properties of biochemical reactants at specified pH and pMg Biophysical Chemistry. 43: 239-254. DOI: 10.1016/0301-4622(92)85024-X |
0.348 |
|
| 1991 |
Alberty RA, Oppenheim I. Use of semigrand ensembles in chemical equilibrium calculations on complex organic systems The Journal of Chemical Physics. 96: 1824-1828. DOI: 10.1063/1.457087 |
0.363 |
|
| 1991 |
Alberty RA. Relation between the thermodynamics and kinetics of a complex reaction system at constant temperature and pressure Journal of Physical Chemistry. 95: 413-417. DOI: 10.1021/J100154A072 |
0.419 |
|
| 1989 |
Alberty RA. Thermodynamics of the formation of benzene series polycyclic aromatic hydrocarbons in a benzene flame Journal of Physical Chemistry. 93: 3299-3304. DOI: 10.1021/J100345A081 |
0.307 |
|
| 1988 |
Alberty RA, Oppenheim I. Fundamental equation for systems in chemical equilibrium The Journal of Chemical Physics. 89: 3689-3693. DOI: 10.1063/1.454889 |
0.381 |
|
| 1987 |
Alberty RA. Kinetics of the polymerization of alkenes on zeolites The Journal of Chemical Physics. 87: 3660-3667. DOI: 10.1063/1.452963 |
0.367 |
|
| 1986 |
Alberty RA. Thermodynamics of chemical reactions written in terms of homologous series The Journal of Chemical Physics. 86: 2243-2248. DOI: 10.1063/1.452123 |
0.354 |
|
| 1986 |
Alberty RA. Use of an ensemble intermediate between the generalized ensemble and the isothermal-isobaric ensemble to calculate the equilibrium distribution of hydrocarbons in homologous series The Journal of Chemical Physics. 85: 2890-2894. DOI: 10.1063/1.451049 |
0.352 |
|
| 1983 |
Alberty RA. Balancing complex chemical equations using a hand-held calculator Journal of Chemical Education. 60: 102. DOI: 10.1021/Ed060P102 |
0.368 |
|
| 1969 |
Alberty RA. Maxwell relations for thermodynamic quantities of biochemical reactions Journal of the American Chemical Society. 91: 3899-3903. DOI: 10.1021/Ja01042A037 |
0.388 |
|
| 1964 |
Taraszka M, Alberty RA. Extensions of the steady-state rate law for the fumarase reaction Journal of Physical Chemistry. 68: 3368-3373. DOI: 10.1021/J100793A044 |
0.347 |
|
| 1963 |
BLOOMFIELD V, ALBERTY RA. MULTIPLE INTERMEDIATES IN STEADY STATE ENZYME KINETICS. VI. THE MECHANISM INVOLVING A SINGLE SUBSTRATE AND TWO PRODUCTS. The Journal of Biological Chemistry. 238: 2811-6. PMID 14063307 DOI: 10.1021/Ja01531A017 |
0.369 |
|
| 1963 |
ALBERTY RA, BLOOMFIELD V. MULTIPLE INTERMEDIATES IN STEADY STATE ENZYME KINETICS. V. EFFECT OF PH ON THE RATE OF A SIMPLE ENZYMATIC REACTION. The Journal of Biological Chemistry. 238: 2804-10. PMID 14063306 |
0.345 |
|
| 1963 |
Brant DA, Barnett LB, Alberty RA. The temperature dependence of the steady state kinetic parameters of the fumarase reaction Journal of the American Chemical Society. 85: 2204-2209. DOI: 10.1021/Ja00898A003 |
0.647 |
|
| 1962 |
Alberty RA, Bloomfield V, Peller L, King EL. Multiple Intermediates in Steady-state Enzyme Kinetics. IV. The Steady State Kinetics of Isotopic Exchange in Enzyme-catalyzed Reactions Journal of the American Chemical Society. 84: 4381-4384. DOI: 10.1021/Ja00882A003 |
0.612 |
|
| 1962 |
Bloomfield V, Peller L, Alberty RA. Multiple Intermediates in Steady-state Enzyme Kinetics. III. Analysis of the Kinetics of Some Reactions Catalyzed by Dehydrogenases Journal of the American Chemical Society. 84: 4375-4381. DOI: 10.1021/Ja00882A002 |
0.63 |
|
| 1962 |
Bloomfield V, Peller L, Alberty RA. Multiple Intermediates in Steady-state Enzyme Kinetics. II. Systems Involving Two Reactants and Two Products Journal of the American Chemical Society. 84: 4367-4374. DOI: 10.1021/Ja00882A001 |
0.568 |
|
| 1962 |
Fleck GM, Alberty RA. Kinetics of the reaction of pyridoxal and alanine Journal of Physical Chemistry. 66: 1678-1682. DOI: 10.1021/J100815A028 |
0.413 |
|
| 1962 |
Alberty RA, Bloomfield V, Peller L, King EL. Multiple intermediates in steady-state enzyme kinetics. IV. The steady state kinetics of isotopic exchange in enzyme-catalyzed reactions Journal of the American Chemical Society. 84: 4381-4384. |
0.311 |
|
| 1962 |
Bloomfield V, Peller L, Alberty RA. Multiple intermediates in steady-state enzyme kinetics. III. Analysis of the kinetics of some reactions catalyzed by dehydrogenases Journal of the American Chemical Society. 84: 4375-4381. |
0.344 |
|
| 1960 |
Hammes GG, Alberty RA. The Relaxation Spectra of Simple Enzymatic Mechanisms1,2 Journal of the American Chemical Society. 82: 1564-1569. DOI: 10.1021/Ja01492A012 |
0.466 |
|
| 1959 |
Alberty RA. The Chemical Kinetics of Enzyme Action. Journal of the American Chemical Society. 81: 1521-1522. DOI: 10.1021/Ja01515A073 |
0.393 |
|
| 1959 |
Erickson LE, Alberty RA. Kinetics and mechanism of the base-catalyzed hydration of fumarate to malate Journal of Physical Chemistry. 63: 705-709. DOI: 10.1021/J150575A014 |
0.364 |
|
| 1959 |
Hammes GG, Alberty RA. The influence of the net protein charge on the rate of formation of enzyme-substrate complexes Journal of Physical Chemistry. 63: 274-279. DOI: 10.1021/J150572A034 |
0.521 |
|
| 1958 |
Miller WG, Alberty RA. Kinetics of the reversible Michaelis-Menten mechanism and the applicability of the steady-state approximation Journal of the American Chemical Society. 80: 5146-5151. DOI: 10.1021/Ja01552A034 |
0.327 |
|
| 1958 |
Alberty RA, Hammes GG. Application of the theory of diffusion-controlled reactions to enzyme kinetics Journal of Physical Chemistry. 62: 154-159. DOI: 10.1021/J150560A005 |
0.566 |
|
| 1957 |
Alberty RA, Miller WG. Integrated rate equations for isotopic exchange in simple reversible reactions The Journal of Chemical Physics. 26: 1231-1237. DOI: 10.1063/1.1743498 |
0.372 |
|
| 1957 |
Alberty RA, Koerber BM. Studies of the enzyme fumarase. VII. Series solutions of integrated rate equations for irreversible and reversible Michaelis-Menten mechanisms Journal of the American Chemical Society. 79: 6379-6382. DOI: 10.1021/Ja01581A011 |
0.331 |
|
| 1957 |
Alberty RA. Studies of the enzyme fumarase. VI.1 Study of the incorporation of deuterium into l-malate during the reaction in deuterium oxide Journal of the American Chemical Society. 79: 3973-3977. DOI: 10.1021/Ja01572A005 |
0.353 |
|
| 1957 |
Alberty RA, Peirce WH. Studies of the Enzyme Fumarase. V.1 Calculation of Minimum and Maximum Values of Constants for the General Fumarase Mechanism2 Journal of the American Chemical Society. 79: 1526-1530. DOI: 10.1021/Ja01564A002 |
0.352 |
|
| 1957 |
Frieden C, Wolfe RG, Alberty RA. Studies of the enzyme fumarase. IV. The dependence of the kinetic constants at 25° on buffer concentration, composition and pH Journal of the American Chemical Society. 79: 1523-1525. DOI: 10.1021/Ja01564A001 |
0.598 |
|
| 1955 |
FRIEDEN C, ALBERTY RA. The effect of pH on fumarase activity in acetate buffer. The Journal of Biological Chemistry. 212: 859-68. PMID 14353887 |
0.475 |
|
| 1955 |
Fisher HF, Frieden C, McKee JSM, Alberty RA. CONCERNING THE STEREOSPECIFICITY OF THE FUMARASE REACTION AND THE DEMONSTRATION OF A NEW INTERMEDIATE1 Journal of the American Chemical Society. 77: 4436-4436. DOI: 10.1021/Ja01621A091 |
0.559 |
|
| 1954 |
MASSEY V, ALBERTY RA. Ionisation constants of fumarase. Biochimica Et Biophysica Acta. 13: 354-9. PMID 13140347 |
0.464 |
|
| 1954 |
ALBERTY RA, MASSEY V. On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction. Biochimica Et Biophysica Acta. 13: 347-53. PMID 13140346 |
0.559 |
|
| 1954 |
Alberty RA. Some Mechanisms for the Interpretation of the Effects of pH and Buffer Salts on a Simple Enzymatic Reaction Journal of the American Chemical Society. 76: 2494-2498. DOI: 10.1021/Ja01638A054 |
0.404 |
|
| 1954 |
Alberty RA, Massey V, Frieden C, Fuhlbrigge AR. Studies of the Enzyme Fumarase. III.1The Dependence of the Kinetic Constants at 25° upon the Concentration and pH of Phosphate Buffers Journal of the American Chemical Society. 76: 2485-2493. DOI: 10.1021/Ja01638A053 |
0.679 |
|
| 1954 |
Frieden C, Bock RM, Alberty RA. Studies of the Enzyme Fumarase. II.1Isolation and Physical Properties of Crystalline Enzyme Journal of the American Chemical Society. 76: 2482-2484. DOI: 10.1021/Ja01638A052 |
0.668 |
|
| 1953 |
Alberty RA, Bock RM. Alteration of the Kinetic Properties of an Enzyme by the Binding of Buffer, Inhibitor, or Substrate. Proceedings of the National Academy of Sciences of the United States of America. 39: 895-900. PMID 16589350 |
0.572 |
|
| 1953 |
Alberty RA. The Relationship between Michaelis Constants, Maximum Velocities and the Equilibrium Constant for an Enzyme-catalyzed Reaction Journal of the American Chemical Society. 75: 1928-1932. DOI: 10.1021/Ja01104A045 |
0.45 |
|
| 1953 |
Bock RM, Alberty RA. Studies of the Enzyme Fumarase. I. Kinetics and Equilibrium Journal of the American Chemical Society. 75: 1921-1925. DOI: 10.1021/Ja01104A043 |
0.636 |
|
| 1951 |
BOCK RM, ALBERTY RA. Analysis of mixtures of adenosinephosphates by the moving boundary method. The Journal of Biological Chemistry. 193: 435-42. PMID 14907731 |
0.475 |
|
| 1951 |
ALBERTY RA, SMITH RM, BOCK RM. The apparent ionization constants of the adenosinephosphates and related compounds. The Journal of Biological Chemistry. 193: 425-34. PMID 14907730 |
0.498 |
|
| 1951 |
BALDWIN RL, LAUGHTON PM, ALBERTY RA. Homogeneity and the electrophoretic behavior of some proteins. III A general method for the determination of mobility distributions. The Journal of Physical and Colloid Chemistry. 55: 111-25. PMID 14814637 DOI: 10.1021/J150484A013 |
0.371 |
|
| 1946 |
DEUTSCH HF, ALBERTY RA, GOSTING LJ. Biophysical studies of blood plasma proteins; separation and purification of a new globulin from normal human plasma. The Journal of Biological Chemistry. 165: 21-35. PMID 21001181 |
0.447 |
|
| Show low-probability matches. |
