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Paul F Cook

TitleProfessor Emeritus
InstitutionUniversity of Oklahoma, Norman
DepartmentChemistry/Biochemistry
Addressn/a
620 Parrington Oval
Norman OK 73019
Phone405/325-1683
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    Collapse Research 
    Collapse research activities and funding
    R01GM071417     (COOK, PAUL F)Sep 15, 2004 - Aug 31, 2009
    NIH
    Lysine Biosynthesis in Yeast
    Role: Principal Investigator
    R01GM050872     (COOK, PAUL F)Dec 1, 1994 - Nov 30, 1999
    NIH
    STRUCTURE/MECHANISM OF 6-PHOSPHOGLUCONATE DEHYDROGENASE
    Role: Principal Investigator
    S15HL047703     (COOK, PAUL F)Sep 1, 1991 - Aug 31, 1992
    NIH
    SMALL INSTRUMENTATION GRANT
    Role: Principal Investigator
    S15HL043958     (COOK, PAUL F)Sep 1, 1989 - Aug 31, 1990
    NIH
    SMALL INSTRUMENTATION PROGRAM
    Role: Principal Investigator
    R01GM037057     (COOK, PAUL F)Dec 1, 1985 - Aug 31, 1992
    NIH
    MECHANISM OF CAMP DEPENDENT PROTEIN KINASE 16.
    Role: Principal Investigator
    R01GM036799     (COOK, PAUL F)Sep 19, 1985 - Aug 31, 1999
    NIH
    STRUCTURE AND MECHANISM OF NAD-MALIC ENZYME
    Role: Principal Investigator
    R01GM032052     (COOK, PAUL F)Aug 1, 1984 - Nov 30, 1985
    NIH
    MECHANISM OF CYCLIC AMP DEPENDENT PROTEIN KINASE
    Role: Principal Investigator
    K04AM001155     (COOK, PAUL F)Apr 1, 1983 - Mar 31, 1988
    NIH
    KINETIC AND CHEMICAL MECHANISM OF ENZYMES
    Role: Principal Investigator
    K04DK001155     (COOK, PAUL F)Apr 1, 1983 - Mar 31, 1988
    NIH
    KINETIC AND CHEMICAL MECHANISM OF ENZYMES
    Role: Principal Investigator

    Collapse Bibliographic 
    Collapse selected publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. Terzyan SS, Cook PF, Heroux A, Hanigan MH. Structure of 6-diazo-5-oxo-norleucine-bound human gamma-glutamyl transpeptidase 1, a novel mechanism of inactivation. Protein Sci. 2017 06; 26(6):1196-1205. PMID: 28378915.
      Citations: 7     Fields:    Translation:HumansCells
    2. Vashishtha AK, West AH, Cook PF. Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis. Arch Biochem Biophys. 2015 Oct 15; 584:98-106. PMID: 26342457.
      Citations:    Fields:    Translation:Animals
    3. Hsu C, West AH, Cook PF. Evidence for an induced conformational change in the catalytic mechanism of homoisocitrate dehydrogenase for Saccharomyces cerevisiae: Characterization of the D271N mutant enzyme. Arch Biochem Biophys. 2015 Oct 15; 584:20-7. PMID: 26325079.
      Citations:    Fields:    Translation:AnimalsCells
    4. Spyrakis F, Singh R, Cozzini P, Campanini B, Salsi E, Felici P, Raboni S, Benedetti P, Cruciani G, Kellogg GE, Cook PF, Mozzarelli A. Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target. PLoS One. 2013; 8(10):e77558. PMID: 24167577.
      Citations: 18     Fields:    Translation:HumansAnimalsCells
    5. Nelson JM, Cook PF, Raterink G. The evolution of a doctor of nursing practice capstone process: programmatic revisions to improve the quality of student projects. J Prof Nurs. 2013 Nov-Dec; 29(6):370-80. PMID: 24267931.
      Citations: 2     Fields:    Translation:Humans
    6. Nelson JM, Cook PF, Ingram JC. Utility of the theory of planned behavior to predict nursing staff blood pressure monitoring behaviours. J Clin Nurs. 2014 Feb; 23(3-4):461-70. PMID: 23581520.
      Citations: 4     Fields:    Translation:Humans
    7. Wickham S, Regan N, West MB, Thai J, Cook PF, Terzyan SS, Li PK, Hanigan MH. Inhibition of human ?-glutamyl transpeptidase: development of more potent, physiologically relevant, uncompetitive inhibitors. Biochem J. 2013 Mar 15; 450(3):547-57. PMID: 23301618.
      Citations: 16     Fields:    Translation:HumansAnimalsCells
    8. Spyrakis F, Felici P, Bayden AS, Salsi E, Miggiano R, Kellogg GE, Cozzini P, Cook PF, Mozzarelli A, Campanini B. Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase. Biochim Biophys Acta. 2013 Jan; 1834(1):169-81. PMID: 23000429.
      Citations: 14     Fields:    Translation:Cells
    9. Kumar VP, West AH, Cook PF. Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Arch Biochem Biophys. 2012 Jun 01; 522(1):57-61. PMID: 22521736.
      Citations: 3     Fields:    Translation:AnimalsCells
    10. Kumar VP, Thomas LM, Bobyk KD, Andi B, Cook PF, West AH. Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2012 Jan 31; 51(4):857-66. PMID: 22243403.
      Citations: 6     Fields:    Translation:AnimalsCells
    11. Karsten WE, Reyes ZL, Bobyk KD, Cook PF, Chooback L. Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae. Arch Biochem Biophys. 2011 Dec 01; 516(1):67-74. PMID: 21982920.
      Citations: 7     Fields:    Translation:Animals
    12. Wickham S, Regan N, West MB, Kumar VP, Thai J, Li PK, Cook PF, Hanigan MH. Divergent effects of compounds on the hydrolysis and transpeptidation reactions of ?-glutamyl transpeptidase. J Enzyme Inhib Med Chem. 2012 Aug; 27(4):476-89. PMID: 21864033.
      Citations: 6     Fields:    Translation:HumansCells
    13. Bobyk KD, Kim SG, Kumar VP, Kim SK, West AH, Cook PF. The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH. Arch Biochem Biophys. 2011 Sep 15; 513(2):71-80. PMID: 21798231.
      Citations: 2     Fields:    Translation:AnimalsCells
    14. Ekanayake DK, West AH, Cook PF. Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction. Arch Biochem Biophys. 2011 Oct; 514(1-2):8-15. PMID: 21819960.
      Citations: 2     Fields:    Translation:AnimalsCells
    15. Burke EG, Nelson J, Kwong J, Cook PF. Cardiovascular risk assessment for persons living with HIV. J Assoc Nurses AIDS Care. 2012 Mar-Apr; 23(2):134-45. PMID: 21775164.
      Citations: 4     Fields:    Translation:HumansPHPublic Health
    16. Kumar VP, West AH, Cook PF. Kinetic and chemical mechanisms of homocitrate synthase from Thermus thermophilus. J Biol Chem. 2011 Aug 19; 286(33):29428-29439. PMID: 21733842.
      Citations: 2     Fields:    Translation:Cells
    17. Mozzarelli A, Bettati S, Campanini B, Salsi E, Raboni S, Singh R, Spyrakis F, Kumar VP, Cook PF. The multifaceted pyridoxal 5'-phosphate-dependent O-acetylserine sulfhydrylase. Biochim Biophys Acta. 2011 Nov; 1814(11):1497-510. PMID: 21549222.
      Citations: 20     Fields:    Translation:Cells
    18. Foley JH, Cook PF, Nesheim ME. Kinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sites. J Biol Chem. 2011 Jun 03; 286(22):19280-6. PMID: 21467042.
      Citations: 7     Fields:    Translation:HumansCells
    19. Wickham S, West MB, Cook PF, Hanigan MH. Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes. Anal Biochem. 2011 Jul 15; 414(2):208-14. PMID: 21447318.
      Citations: 47     Fields:    Translation:Humans
    20. Schnackerz KD, Andi B, Cook PF. (31)P NMR spectroscopy senses the microenvironment of the 5'-phosphate group of enzyme-bound pyridoxal 5'-phosphate. Biochim Biophys Acta. 2011 Nov; 1814(11):1447-58. PMID: 21354475.
      Citations: 9     Fields:    Translation:Cells
    21. Koh C, Nelson JM, Cook PF. Evaluation of a patient navigation program. Clin J Oncol Nurs. 2011 Feb; 15(1):41-8. PMID: 21278040.
      Citations: 22     Fields:    Translation:Humans
    22. Tyapochkin E, Kumar VP, Cook PF, Chen G. Reaction product affinity regulates activation of human sulfotransferase 1A1 PAP sulfation. Arch Biochem Biophys. 2011 Feb 15; 506(2):137-41. PMID: 21111704.
      Citations: 5     Fields:    Translation:HumansCells
    23. Salsi E, Guan R, Campanini B, Bettati S, Lin J, Cook PF, Mozzarelli A. Exploring O-acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy. Arch Biochem Biophys. 2011 Jan 15; 505(2):178-85. PMID: 20937239.
      Citations: 4     Fields:    Translation:Cells
    24. Tian H, Guan R, Salsi E, Campanini B, Bettati S, Kumar VP, Karsten WE, Mozzarelli A, Cook PF. Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A. Biochemistry. 2010 Jul 27; 49(29):6093-103. PMID: 20550197.
      Citations: 11     Fields:    Translation:Cells
    25. Ekanayake DK, Andi B, Bobyk KD, West AH, Cook PF. Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts. J Biol Chem. 2010 Jul 02; 285(27):20756-68. PMID: 20427272.
      Citations: 4     Fields:    Translation:AnimalsCells
    26. Kaserer AO, Andi B, Cook PF, West AH. Kinetic studies of the yeast His-Asp phosphorelay signaling pathway. Methods Enzymol. 2010; 471:59-75. PMID: 20946842.
      Citations: 3     Fields:    Translation:AnimalsCells
    27. Salsi E, Campanini B, Bettati S, Raboni S, Roderick SL, Cook PF, Mozzarelli A. A two-step process controls the formation of the bienzyme cysteine synthase complex. J Biol Chem. 2010 Apr 23; 285(17):12813-22. PMID: 20164178.
      Citations: 12     Fields:    Translation:AnimalsCells
    28. Knuckley B, Causey CP, Pellechia PJ, Cook PF, Thompson PR. Haloacetamidine-based inactivators of protein arginine deiminase 4 (PAD4): evidence that general acid catalysis promotes efficient inactivation. Chembiochem. 2010 Jan 25; 11(2):161-5. PMID: 20014086.
      Citations: 33     Fields:    Translation:HumansCells
    29. Salsi E, Bayden AS, Spyrakis F, Amadasi A, Campanini B, Bettati S, Dodatko T, Cozzini P, Kellogg GE, Cook PF, Roderick SL, Mozzarelli A. Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature. J Med Chem. 2010 Jan 14; 53(1):345-56. PMID: 19928859.
      Citations: 25     Fields:    Translation:Cells
    30. Tyapochkin E, Cook PF, Chen G. para-Nitrophenyl sulfate activation of human sulfotransferase 1A1 is consistent with intercepting the E[middle dot]PAP complex and reformation of E[middle dot]PAPS. J Biol Chem. 2009 Oct 23; 284(43):29357-64. PMID: 19706609.
      Citations: 5     Fields:    Translation:HumansCells
    31. Kaserer AO, Andi B, Cook PF, West AH. Effects of osmolytes on the SLN1-YPD1-SSK1 phosphorelay system from Saccharomyces cerevisiae. Biochemistry. 2009 Aug 25; 48(33):8044-50. PMID: 19618914.
      Citations: 13     Fields:    Translation:AnimalsCells
    32. Cook PF, Goto Y, Lottspeich F. Introduction to the special issue. Foreword. Biochim Biophys Acta. 2009 Sep; 1794(9):1277-9. PMID: 19695350.
      Citations:    Fields:    
    33. Lin Y, West AH, Cook PF. Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2009 Aug 04; 48(30):7305-12. PMID: 19530703.
      Citations: 4     Fields:    Translation:AnimalsCells
    34. Vashishtha AK, West AH, Cook PF. Chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae. Biochemistry. 2009 Jun 30; 48(25):5899-907. PMID: 19449898.
      Citations: 5     Fields:    Translation:Animals
    35. Guan R, Nimmo SA, Schnackerz KD, Cook PF. (31)P NMR studies of O-acetylserine sulfhydrylase-B from Salmonella typhimurium. Arch Biochem Biophys. 2009 Jul 15; 487(2):85-90. PMID: 19501038.
      Citations:    Fields:    Translation:Cells
    36. Aktas DF, Cook PF. A lysine-tyrosine pair carries out acid-base chemistry in the metal ion-dependent pyridine dinucleotide-linked beta-hydroxyacid oxidative decarboxylases. Biochemistry. 2009 Apr 28; 48(16):3565-77. PMID: 19281248.
      Citations: 18     Fields:    Translation:HumansAnimalsCells
    37. Karsten WE, Cook PF. Detection of a gem-diamine and a stable quinonoid intermediate in the reaction catalyzed by serine-glyoxylate aminotransferase from Hyphomicrobium methylovorum. Biochim Biophys Acta. 2009 Jun; 1790(6):575-80. PMID: 19264108.
      Citations: 5     Fields:    Translation:Cells
    38. King JB, West MB, Cook PF, Hanigan MH. A novel, species-specific class of uncompetitive inhibitors of gamma-glutamyl transpeptidase. J Biol Chem. 2009 Apr 03; 284(14):9059-65. PMID: 19203993.
      Citations: 29     Fields:    Translation:AnimalsCells
    39. Nelson JM, Cook PF. Evaluation of a career ladder program in an ambulatory care environment. Nurs Econ. 2008 Nov-Dec; 26(6):353-60. PMID: 19330969.
      Citations: 3     Fields:    Translation:Humans
    40. Tyapochkin E, Cook PF, Chen G. Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase. Biochemistry. 2008 Nov 11; 47(45):11894-9. PMID: 18928301.
      Citations: 10     Fields:    Translation:HumansCells
    41. Lin Y, West AH, Cook PF. Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2008 Oct 07; 47(40):10809-15. PMID: 18785753.
      Citations: 10     Fields:    Translation:AnimalsCells
    42. Aktas DF, Cook PF. Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme. Biochim Biophys Acta. 2008 Dec; 1784(12):2059-64. PMID: 18725329.
      Citations:    Fields:    Translation:AnimalsCells
    43. Qian J, Khandogin J, West AH, Cook PF. Evidence for a catalytic dyad in the active site of homocitrate synthase from Saccharomyces cerevisiae. Biochemistry. 2008 Jul 01; 47(26):6851-8. PMID: 18533686.
      Citations: 10     Fields:    Translation:AnimalsCells
    44. Guan R, Roderick SL, Huang B, Cook PF. Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae. Biochemistry. 2008 Jun 17; 47(24):6322-8. PMID: 18498176.
      Citations: 5     Fields:    Translation:Cells
    45. Vashishtha AK, West AH, Cook PF. Overall kinetic mechanism of saccharopine dehydrogenase (L-glutamate forming) from Saccharomyces cerevisiae. Biochemistry. 2008 May 13; 47(19):5417-23. PMID: 18416559.
      Citations: 3     Fields:    Translation:Animals
    46. Valderas MW, Andi B, Barrow WW, Cook PF. Examination of intrinsic sulfonamide resistance in Bacillus anthracis: a novel assay for dihydropteroate synthase. Biochim Biophys Acta. 2008 May; 1780(5):848-53. PMID: 18342015.
      Citations: 5     Fields:    Translation:Cells
    47. Lin Y, Volkman J, Nicholas KM, Yamamoto T, Eguchi T, Nimmo SL, West AH, Cook PF. Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2008 Apr 01; 47(13):4169-80. PMID: 18321070.
      Citations: 9     Fields:    Translation:AnimalsCells
    48. Tai CH, Rabeh WM, Guan R, Schnackerz KD, Cook PF. Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction. Arch Biochem Biophys. 2008 Apr 15; 472(2):115-25. PMID: 18275838.
      Citations:    Fields:    Translation:Cells
    49. Aktas DF, Cook PF. Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction. Biochemistry. 2008 Feb 26; 47(8):2539-46. PMID: 18215074.
      Citations: 1     Fields:    Translation:AnimalsCells
    50. Cervellati C, Li L, Andi B, Guariento A, Dallocchio F, Cook PF. Proper orientation of the nicotinamide ring of NADP is important for the precatalytic conformational change in the 6-phosphogluconate dehydrogenase reaction. Biochemistry. 2008 Feb 19; 47(7):1862-70. PMID: 18205398.
      Citations: 2     Fields:    Translation:Cells
    51. Tai CH, Rabeh WM, Guan R, Schnackerz KD, Cook PF. Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. Biochim Biophys Acta. 2008 Apr; 1784(4):629-37. PMID: 18243146.
      Citations: 2     Fields:    Translation:Cells
    52. Karsten WE, Cook PF. Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum. Biochemistry. 2007 Dec 18; 46(50):14578-88. PMID: 18027982.
      Citations: 1     Fields:    Translation:HumansAnimalsCells
    53. Nelson JM, Dufraux K, Cook PF. The relationship between glycemic control and falls in older adults. J Am Geriatr Soc. 2007 Dec; 55(12):2041-4. PMID: 17971138.
      Citations: 38     Fields:    Translation:Humans
    54. Andi B, Xu H, Cook PF, West AH. Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Nov 06; 46(44):12512-21. PMID: 17939687.
      Citations: 8     Fields:    Translation:AnimalsCells
    55. Raboni S, Mozzarelli A, Cook PF. Control of ionizable residues in the catalytic mechanism of tryptophan synthase from Salmonella typhimurium. Biochemistry. 2007 Nov 13; 46(45):13223-34. PMID: 17927213.
      Citations: 5     Fields:    Translation:Cells
    56. Chattopadhyay A, Meier M, Ivaninskii S, Burkhard P, Speroni F, Campanini B, Bettati S, Mozzarelli A, Rabeh WM, Li L, Cook PF. Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes. Biochemistry. 2007 Jul 17; 46(28):8315-30. PMID: 17583914.
      Citations: 22     Fields:    Translation:Cells
    57. Xu H, West AH, Cook PF. Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Jun 26; 46(25):7625-36. PMID: 17542618.
      Citations:    Fields:    Translation:AnimalsCells
    58. Xu H, Alguindigue SS, West AH, Cook PF. A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Jan 23; 46(3):871-82. PMID: 17223709.
      Citations: 7     Fields:    Translation:Animals
    59. Lin Y, Alguindigue SS, Volkman J, Nicholas KM, West AH, Cook PF. Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Jan 23; 46(3):890-8. PMID: 17223711.
      Citations: 9     Fields:    Translation:Animals
    60. Yu M, Magalhães ML, Cook PF, Blanchard JS. Bisubstrate inhibition: Theory and application to N-acetyltransferases. Biochemistry. 2006 Dec 12; 45(49):14788-94. PMID: 17144672.
      Citations: 28     Fields:    
    61. Li L, Zhang L, Cook PF. Role of the S128, H186, and N187 triad in substrate binding and decarboxylation in the sheep liver 6-phosphogluconate dehydrogenase reaction. Biochemistry. 2006 Oct 24; 45(42):12680-6. PMID: 17042485.
      Citations: 4     Fields:    Translation:AnimalsCells
    62. Qian J, West AH, Cook PF. Acid-base chemical mechanism of homocitrate synthase from Saccharomyces cerevisiae. Biochemistry. 2006 Oct 03; 45(39):12136-43. PMID: 17002313.
      Citations: 5     Fields:    Translation:AnimalsCells
    63. Xu H, West AH, Cook PF. Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2006 Oct 03; 45(39):12156-66. PMID: 17002315.
      Citations: 8     Fields:    Translation:AnimalsCells
    64. Li L, Cook PF. The 2'-phosphate of NADP is responsible for proper orientation of the nicotinamide ring in the oxidative decarboxylation reaction catalyzed by sheep liver 6-phosphogluconate dehydrogenase. J Biol Chem. 2006 Dec 01; 281(48):36803-10. PMID: 16959777.
      Citations: 9     Fields:    Translation:HumansAnimalsCells
    65. Karsten WE, Cook PF. An isothermal titration calorimetry study of the binding of substrates and ligands to the tartrate dehydrogenase from Pseudomonas putida reveals half-of-the-sites reactivity. Biochemistry. 2006 Jul 25; 45(29):9000-6. PMID: 16846243.
      Citations: 3     Fields:    Translation:Cells
    66. Li L, Dworkowski FS, Cook PF. Importance in catalysis of the 6-phosphate-binding site of 6-phosphogluconate in sheep liver 6-phosphogluconate dehydrogenase. J Biol Chem. 2006 Sep 01; 281(35):25568-76. PMID: 16803886.
      Citations: 8     Fields:    Translation:AnimalsCells
    67. Gibson GE, Harris BG, Cook PF. Optimum activity of the phosphofructokinase from Ascaris suum requires more than one metal ion. Biochemistry. 2006 Feb 21; 45(7):2453-60. PMID: 16475835.
      Citations:    Fields:    Translation:AnimalsCells
    68. Rabeh WM, Mather T, Cook PF. A three-dimensional homology model of the O-acetylserine sulfhydrylase-B from Salmonella typhimurium. Protein Pept Lett. 2006; 13(1):7-13. PMID: 16454663.
      Citations:    Fields:    Translation:Cells
    69. Andi B, Cook PF, West AH. Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-A resolution. Cell Biochem Biophys. 2006; 46(1):17-26. PMID: 16943620.
      Citations: 4     Fields:    Translation:Cells
    70. Xu H, Andi B, Qian J, West AH, Cook PF. The alpha-aminoadipate pathway for lysine biosynthesis in fungi. Cell Biochem Biophys. 2006; 46(1):43-64. PMID: 16943623.
      Citations: 64     Fields:    Translation:AnimalsCells
    71. Karsten WE, Ohshiro T, Izumi Y, Cook PF. Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate. Biochemistry. 2005 Dec 06; 44(48):15930-6. PMID: 16313196.
      Citations: 7     Fields:    Translation:Cells
    72. Campanini B, Speroni F, Salsi E, Cook PF, Roderick SL, Huang B, Bettati S, Mozzarelli A. Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy. Protein Sci. 2005 Aug; 14(8):2115-24. PMID: 15987896.
      Citations: 25     Fields:    Translation:Cells
    73. Andi B, Cook PF. Regulatory mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. II. Theory. J Biol Chem. 2005 Sep 09; 280(36):31633-40. PMID: 15897191.
      Citations: 2     Fields:    Translation:AnimalsCells
    74. Andi B, West AH, Cook PF. Regulatory mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. I. Kinetic studies. J Biol Chem. 2005 Sep 09; 280(36):31624-32. PMID: 15897192.
      Citations: 11     Fields:    Translation:AnimalsCells
    75. Rabeh WM, Alguindigue SS, Cook PF. Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction. Biochemistry. 2005 Apr 12; 44(14):5541-50. PMID: 15807548.
      Citations: 7     Fields:    
    76. Karsten WE, Liu D, Rao GS, Harris BG, Cook PF. A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme. Biochemistry. 2005 Mar 08; 44(9):3626-35. PMID: 15736972.
      Citations: 6     Fields:    Translation:AnimalsCells
    77. Cervellati C, Dallocchio F, Bergamini CM, Cook PF. Role of methionine-13 in the catalytic mechanism of 6-phosphogluconate dehydrogenase from sheep liver. Biochemistry. 2005 Feb 22; 44(7):2432-40. PMID: 15709755.
      Citations: 3     Fields:    Translation:AnimalsCells
    78. Janiak-Spens F, Cook PF, West AH. Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast osmoregulatory phosphorelay system. Biochemistry. 2005 Jan 11; 44(1):377-86. PMID: 15628880.
      Citations: 34     Fields:    Translation:AnimalsCells
    79. Waldmann G, Cook PF, Schnackerz KD. Purification and properties of beta-alanine synthase from calf liver. Protein Pept Lett. 2005 Jan; 12(1):69-73. PMID: 15638804.
      Citations: 2     Fields:    Translation:Animals
    80. Johnson CM, Roderick SL, Cook PF. The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol. Arch Biochem Biophys. 2005 Jan 01; 433(1):85-95. PMID: 15581568.
      Citations: 13     Fields:    Translation:Cells
    81. Johnson CM, Huang B, Roderick SL, Cook PF. Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae. Biochemistry. 2004 Dec 14; 43(49):15534-9. PMID: 15581365.
      Citations: 5     Fields:    Translation:Cells
    82. Andi B, West AH, Cook PF. Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. Biochemistry. 2004 Sep 21; 43(37):11790-5. PMID: 15362863.
      Citations: 8     Fields:    Translation:Animals
    83. Johnson CM, Huang B, Roderick SL, Cook PF. Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae. Arch Biochem Biophys. 2004 Sep 15; 429(2):115-22. PMID: 15313214.
      Citations: 17     Fields:    Translation:Cells
    84. Schnackerz KD, Dobritzsch D, Lindqvist Y, Cook PF. Dihydropyrimidine dehydrogenase: a flavoprotein with four iron-sulfur clusters. Biochim Biophys Acta. 2004 Sep 01; 1701(1-2):61-74. PMID: 15450176.
      Citations: 16     Fields:    Translation:HumansAnimalsCells
    85. Staab JF, Bahn YS, Tai CH, Cook PF, Sundstrom P. Expression of transglutaminase substrate activity on Candida albicans germ tubes through a coiled, disulfide-bonded N-terminal domain of Hwp1 requires C-terminal glycosylphosphatidylinositol modification. J Biol Chem. 2004 Sep 24; 279(39):40737-47. PMID: 15262971.
      Citations: 36     Fields:    Translation:AnimalsCells
    86. Rabeh WM, Cook PF. Structure and mechanism of O-acetylserine sulfhydrylase. J Biol Chem. 2004 Jun 25; 279(26):26803-6. PMID: 15073190.
      Citations: 33     Fields:    Translation:Cells
    87. Andi B, West AH, Cook PF. Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. Arch Biochem Biophys. 2004 Jan 15; 421(2):243-54. PMID: 14984204.
      Citations: 10     Fields:    Translation:AnimalsCells
    88. Karsten WE, Pais JE, Rao GS, Harris BG, Cook PF. Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites. Biochemistry. 2003 Aug 19; 42(32):9712-21. PMID: 12911313.
      Citations: 10     Fields:    Translation:HumansAnimalsCells
    89. Rao GS, Coleman DE, Karsten WE, Cook PF, Harris BG. Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site. J Biol Chem. 2003 Sep 26; 278(39):38051-8. PMID: 12853453.
      Citations: 8     Fields:    Translation:AnimalsCells
    90. Campanini B, Raboni S, Vaccari S, Zhang L, Cook PF, Hazlett TL, Mozzarelli A, Bettati S. Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability. J Biol Chem. 2003 Sep 26; 278(39):37511-9. PMID: 12813039.
      Citations: 11     Fields:    Translation:Cells
    91. Cook PF. Alpha,beta-elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required? Biochim Biophys Acta. 2003 Apr 11; 1647(1-2):66-9. PMID: 12686110.
      Citations: 4     Fields:    
    92. Gojkovic Z, Rislund L, Andersen B, Sandrini MP, Cook PF, Schnackerz KD, Piskur J. Dihydropyrimidine amidohydrolases and dihydroorotases share the same origin and several enzymatic properties. Nucleic Acids Res. 2003 Mar 15; 31(6):1683-92. PMID: 12626710.
      Citations: 19     Fields:    Translation:AnimalsCells
    93. Daum S, Tai CH, Cook PF. Characterization of the S272A,D site-directed mutations of O-acetylserine sulfhydrylase: involvement of the pyridine ring in the alpha,beta-elimination reaction. Biochemistry. 2003 Jan 14; 42(1):106-13. PMID: 12515544.
      Citations: 7     Fields:    Translation:Cells
    94. Karsten WE, Tipton PA, Cook PF. Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD. Biochemistry. 2002 Oct 08; 41(40):12193-9. PMID: 12356321.
      Citations: 7     Fields:    Translation:Cells
    95. Liu D, Hwang CC, Cook PF. Alternative substrates for malic enzyme: oxidative decarboxylation of L-aspartate. Biochemistry. 2002 Oct 08; 41(40):12200-3. PMID: 12356322.
      Citations: 3     Fields:    Translation:AnimalsCells
    96. Coleman DE, Rao GS, Goldsmith EJ, Cook PF, Harris BG. Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution. Biochemistry. 2002 Jun 04; 41(22):6928-38. PMID: 12033925.
      Citations: 15     Fields:    Translation:HumansAnimalsCells
    97. Karsten WE, Cook PF. Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase. Methods Enzymol. 2002; 354:223-37. PMID: 12418230.
      Citations: 2     Fields:    Translation:Cells
    98. Tai CH, Burkhard P, Gani D, Jenn T, Johnson C, Cook PF. Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase. Biochemistry. 2001 Jun 26; 40(25):7446-52. PMID: 11412097.
      Citations: 10     Fields:    Translation:Cells
    99. Karsten WE, Ohshiro T, Izumi Y, Cook PF. Initial velocity, spectral, and pH studies of the serine-glyoxylate aminotransferase from Hyphomicrobiuim methylovorum. Arch Biochem Biophys. 2001 Apr 15; 388(2):267-75. PMID: 11368164.
      Citations: 5     Fields:    Translation:Cells
    100. Tai CH, Cook PF. Pyridoxal 5'-phosphate-dependent alpha,beta-elimination reactions: mechanism of O-acetylserine sulfhydrylase. Acc Chem Res. 2001 Jan; 34(1):49-59. PMID: 11170356.
      Citations: 12     Fields:    Translation:Cells
    101. Sakurai M, Cook PF, Haseman CA, Uyeda K. Glutamate 325 is a general acid-base catalyst in the reaction catalyzed by fructose-2,6-bisphosphatase. Biochemistry. 2000 Dec 26; 39(51):16238-43. PMID: 11123954.
      Citations:    Fields:    Translation:AnimalsCells
    102. Burkhard P, Tai CH, Jansonius JN, Cook PF. Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound. J Mol Biol. 2000 Oct 20; 303(2):279-86. PMID: 11023792.
      Citations: 15     Fields:    Translation:Cells
    103. Liu D, Karsten WE, Cook PF. Lysine 199 is the general acid in the NAD-malic enzyme reaction. Biochemistry. 2000 Oct 03; 39(39):11955-60. PMID: 11009609.
      Citations: 4     Fields:    Translation:AnimalsCells
    104. Stanley TM, Johnson WH, Burks EA, Whitman CP, Hwang CC, Cook PF. Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase. Biochemistry. 2000 Feb 01; 39(4):718-26. PMID: 10651637.
      Citations: 6     Fields:    Translation:Cells
    105. Tai CH, Cook PF. O-acetylserine sulfhydrylase. Adv Enzymol Relat Areas Mol Biol. 2000; 74:185-234. PMID: 10800596.
      Citations: 7     Fields:    Translation:AnimalsCells
    106. Schnackerz KD, Tai CH, Pötsch RK, Cook PF. Substitution of pyridoxal 5'-phosphate in D-serine dehydratase from Escherichia coli by cofactor analogues provides information on cofactor binding and catalysis. J Biol Chem. 1999 Dec 24; 274(52):36935-43. PMID: 10601247.
      Citations: 5     Fields:    Translation:Cells
    107. Zhang L, Chooback L, Cook PF. Lysine 183 is the general base in the 6-phosphogluconate dehydrogenase-catalyzed reaction. Biochemistry. 1999 Aug 31; 38(35):11231-8. PMID: 10471272.
      Citations: 13     Fields:    Translation:AnimalsCells
    108. Burkhard P, Tai CH, Ristroph CM, Cook PF, Jansonius JN. Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. J Mol Biol. 1999 Aug 27; 291(4):941-53. PMID: 10452898.
      Citations: 31     Fields:    Translation:Cells
    109. Karsten WE, Chooback L, Liu D, Hwang CC, Lynch C, Cook PF. Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis. Biochemistry. 1999 Aug 10; 38(32):10527-32. PMID: 10441149.
      Citations: 3     Fields:    Translation:AnimalsCells
    110. Jagannatha Rao GS, Cook PF, Harris BG. Kinetic characterization of a T-state of Ascaris suum phosphofructokinase with heterotropic negative cooperativity by ATP eliminated. Arch Biochem Biophys. 1999 May 15; 365(2):335-43. PMID: 10328829.
      Citations:    Fields:    Translation:AnimalsCells
    111. Karsten WE, Hwang CC, Cook PF. Alpha-secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzyme. Biochemistry. 1999 Apr 06; 38(14):4398-402. PMID: 10194359.
      Citations: 7     Fields:    Translation:AnimalsCells
    112. Mizuguchi H, Cook PF, Tai CH, Hasemann CA, Uyeda K. Reaction mechanism of fructose-2,6-bisphosphatase. A mutation of nucleophilic catalyst, histidine 256, induces an alteration in the reaction pathway. J Biol Chem. 1999 Jan 22; 274(4):2166-75. PMID: 9890979.
      Citations: 6     Fields:    Translation:AnimalsCells
    113. Yuen MH, Mizuguchi H, Lee YH, Cook PF, Uyeda K, Hasemann CA. Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities. J Biol Chem. 1999 Jan 22; 274(4):2176-84. PMID: 9890980.
      Citations: 6     Fields:    Translation:AnimalsCells
    114. Benci S, Vaccari S, Mozzarelli A, Cook PF. Time-resolved fluorescence of O-acetylserine sulfhydrylase. Biochim Biophys Acta. 1999 Jan 11; 1429(2):317-30. PMID: 9989217.
      Citations: 6     Fields:    Translation:Cells
    115. Karsten WE, Chooback L, Cook PF. Glutamate 190 is a general acid catalyst in the 6-phosphogluconate-dehydrogenase-catalyzed reaction. Biochemistry. 1998 Nov 10; 37(45):15691-7. PMID: 9843373.
      Citations: 8     Fields:    Translation:AnimalsCells
    116. Hwang CC, Cook PF. Multiple isotope effects as a probe of proton and hydride transfer in the 6-phosphogluconate dehydrogenase reaction. Biochemistry. 1998 Nov 10; 37(45):15698-702. PMID: 9843374.
      Citations: 6     Fields:    Translation:AnimalsCells
    117. Hwang CC, Berdis AJ, Karsten WE, Cleland WW, Cook PF. Oxidative decarboxylation of 6-phosphogluconate by 6-phosphogluconate dehydrogenase proceeds by a stepwise mechanism with NADP and APADP as oxidants. Biochemistry. 1998 Sep 08; 37(36):12596-602. PMID: 9730832.
      Citations: 10     Fields:    Translation:AnimalsCells
    118. Tai CH, Yoon MY, Kim SK, Rege VD, Nalabolu SR, Kredich NM, Schnackerz KD, Cook PF. Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate. Biochemistry. 1998 Jul 28; 37(30):10597-604. PMID: 9692949.
      Citations: 2     Fields:    Translation:Cells
    119. Chooback L, Price NE, Karsten WE, Nelson J, Sundstrom P, Cook PF. Cloning, expression, purification, and characterization of the 6-phosphogluconate dehydrogenase from sheep liver. Protein Expr Purif. 1998 Jul; 13(2):251-8. PMID: 9675070.
      Citations: 1     Fields:    Translation:AnimalsCells
    120. Rosenbaum K, Jahnke K, Schnackerz KD, Cook PF. Secondary tritium and solvent deuterium isotope effects as a probe of the reaction catalyzed by porcine recombinant dihydropyrimidine dehydrogenase. Biochemistry. 1998 Jun 23; 37(25):9156-9. PMID: 9636062.
      Citations:    Fields:    Translation:AnimalsCells
    121. Burkhard P, Rao GS, Hohenester E, Schnackerz KD, Cook PF, Jansonius JN. Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium. J Mol Biol. 1998; 283(1):121-33. PMID: 9761678.
      Citations: 40     Fields:    Translation:Cells
    122. Mozzarelli A, Bettati S, Pucci AM, Burkhard P, Cook PF. Catalytic competence of O-acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry. J Mol Biol. 1998; 283(1):135-46. PMID: 9761679.
      Citations: 3     Fields:    Translation:Cells
    123. Cook PF. Mechanism from isotope effects. Isotopes Environ Health Stud. 1998; 34(1-2):3-17. PMID: 9854842.
      Citations: 4     Fields:    
    124. Benci S, Vaccari S, Mozzarelli A, Cook PF. Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates. Biochemistry. 1997 Dec 09; 36(49):15419-27. PMID: 9398272.
      Citations: 4     Fields:    Translation:Cells
    125. Mizuguchi H, Cook PF, Hasemann CA, Uyeda K. Chemical mechanism of the fructose-6-phosphate,2-kinase reaction from the pH dependence of kinetic parameters of site-directed mutants of active site basic residues. Biochemistry. 1997 Jul 22; 36(29):8775-84. PMID: 9220964.
      Citations: 1     Fields:    Translation:AnimalsCells
    126. Rosenbaum K, Schaffrath B, Hagen WR, Jahnke K, Gonzalez FJ, Cook PF, Schnackerz KD. Purification, characterization, and kinetics of porcine recombinant dihydropyrimidine dehydrogenase. Protein Expr Purif. 1997 Jul; 10(2):185-91. PMID: 9226714.
      Citations: 1     Fields:    Translation:AnimalsCells
    127. Cook PF. Mechanism from isotope effects. Isotopes Environ Health Stud. 1997 Jul; 33(1-2):3-17. PMID: 22087477.
      Citations:    Fields:    
    128. Chooback L, Karsten WE, Kulkarni G, Nalabolu SR, Harris BG, Cook PF. Expression, purification, and characterization of the recombinant NAD-malic enzyme from Ascaris suum. Protein Expr Purif. 1997 Jun; 10(1):51-4. PMID: 9179290.
      Citations:    Fields:    Translation:AnimalsCells
    129. Price NE, Cook PF. Kinetic and chemical mechanisms of the sheep liver 6-phosphogluconate dehydrogenase. Arch Biochem Biophys. 1996 Dec 15; 336(2):215-23. PMID: 8954568.
      Citations: 13     Fields:    Translation:AnimalsCells
    130. Cook PF, Tai CH, Hwang CC, Woehl EU, Dunn MF, Schnackerz KD. Substitution of pyridoxal 5'-phosphate in the O-acetylserine sulfhydrylase from Salmonella typhimurium by cofactor analogs provides a test of the mechanism proposed for formation of the alpha-aminoacrylate intermediate. J Biol Chem. 1996 Oct 18; 271(42):25842-9. PMID: 8824215.
      Citations:    Fields:    Translation:Cells
    131. Rege VD, Kredich NM, Tai CH, Karsten WE, Schnackerz KD, Cook PF. A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst. Biochemistry. 1996 Oct 15; 35(41):13485-93. PMID: 8873618.
      Citations: 6     Fields:    Translation:Cells
    132. Schmitt U, Jahnke K, Rosenbaum K, Cook PF, Schnackerz KD. Purification and characterization of dihydropyrimidine dehydrogenase from Alcaligenes eutrophus. Arch Biochem Biophys. 1996 Aug 01; 332(1):175-82. PMID: 8806723.
      Citations: 1     Fields:    Translation:AnimalsCells
    133. Tipton PA, Quinn TP, Peisach J, Cook PF. Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex. Protein Sci. 1996 Aug; 5(8):1648-54. PMID: 8844853.
      Citations: 1     Fields:    Translation:AnimalsCells
    134. Strambini GB, Cioni P, Cook PF. Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathway. Biochemistry. 1996 Jun 25; 35(25):8392-400. PMID: 8679597.
      Citations: 4     Fields:    Translation:Cells
    135. Hwang CC, Woehl EU, Minter DE, Dunn MF, Cook PF. Kinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 1996 May 21; 35(20):6358-65. PMID: 8639581.
      Citations: 2     Fields:    Translation:Cells
    136. Gibson GE, Harris BG, Cook PF. Isotope partitioning with Ascaris suum phosphofructokinase is consistent with an ordered kinetic mechanism. Biochemistry. 1996 Apr 30; 35(17):5451-7. PMID: 8611535.
      Citations:    Fields:    Translation:AnimalsCells
    137. Woehl EU, Tai CH, Dunn MF, Cook PF. Formation of the alpha-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 1996 Apr 16; 35(15):4776-83. PMID: 8664267.
      Citations: 11     Fields:    Translation:Cells
    138. Treptau T, Piram P, Cook PF, Rodriguez PH, Hoffmann R, Jung S, Thalhofer HP, Harris BG, Hofer HW. Comparison of the substrate specificities of cAMP-dependent protein kinase from bovine heart and Ascaris suum muscle. Biol Chem Hoppe Seyler. 1996 Mar; 377(3):203-9. PMID: 8722322.
      Citations: 2     Fields:    Translation:AnimalsCells
    139. Schnackerz KD, Cook PF. Resolution of pyridoxal 5'-phosphate from O-acetylserine sulfhydrylase from Salmonella typhimurium and reconstitution of apoenzyme with cofactor and cofactor analogues as a probe of the cofactor binding site. Arch Biochem Biophys. 1995 Dec 01; 324(1):71-7. PMID: 7503562.
      Citations: 1     Fields:    Translation:Cells
    140. Lagueux J, Ménard L, Candas B, Brochu G, Potvin F, Verreault A, Cook PF, Poirier GG. Equilibrium model in an in vitro poly(ADP-ribose) turnover system. Biochim Biophys Acta. 1995 Nov 07; 1264(2):201-8. PMID: 7495864.
      Citations: 3     Fields:    Translation:Animals
    141. Rao GS, Schnackerz KD, Harris BG, Cook PF. A pH-dependent allosteric transition in Ascaris suum phosphofructokinase distinct from that observed with fructose 2,6-bisphosphate. Arch Biochem Biophys. 1995 Oct 01; 322(2):410-6. PMID: 7574715.
      Citations:    Fields:    Translation:AnimalsCells
    142. Schnackerz KD, Tai CH, Simmons JW, Jacobson TM, Rao GS, Cook PF. Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction. Biochemistry. 1995 Sep 26; 34(38):12152-60. PMID: 7547955.
      Citations: 12     Fields:    Translation:Cells
    143. Tai CH, Nalabolu SR, Simmons JW, Jacobson TM, Cook PF. Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies. Biochemistry. 1995 Sep 26; 34(38):12311-22. PMID: 7547974.
      Citations: 3     Fields:    Translation:Cells
    144. Yoon MY, Thayer-Cook KA, Berdis AJ, Karsten WE, Schnackerz KD, Cook PF. Acid-base chemical mechanism of aspartase from Hafnia alvei. Arch Biochem Biophys. 1995 Jun 20; 320(1):115-22. PMID: 7793969.
      Citations: 1     Fields:    Translation:Cells
    145. Payne MA, Rao GS, Harris BG, Cook PF. Acid-base catalytic mechanism and pH dependence of fructose 2,6-bisphosphate activation of the Ascaris suum phosphofructokinase. Biochemistry. 1995 Jun 20; 34(24):7781-7. PMID: 7794888.
      Citations:    Fields:    Translation:AnimalsCells
    146. Karsten WE, Gavva SR, Park SH, Cook PF. Metal ion activator effects on intrinsic isotope effects for hydride transfer from decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum. Biochemistry. 1995 Mar 14; 34(10):3253-60. PMID: 7880820.
      Citations: 2     Fields:    Translation:AnimalsCells
    147. Leu LS, Cook PF. Kinetic mechanism of serine transacetylase from Salmonella typhimurium. Biochemistry. 1994 Mar 08; 33(9):2667-71. PMID: 8117730.
      Citations: 9     Fields:    Translation:Cells
    148. Karsten WE, Cook PF. Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation. Biochemistry. 1994 Mar 01; 33(8):2096-103. PMID: 8117666.
      Citations: 2     Fields:    Translation:AnimalsCells
    149. Bertagnolli BL, Cook PF. Lanthanide pyrophosphates as substrates for the pyrophosphate-dependent phosphofructokinases from Propionibacterium freudenreichii and Phaseolus aureus: evidence for a second metal ion required for reaction. Biochemistry. 1994 Feb 22; 33(7):1663-7. PMID: 8110768.
      Citations:    Fields:    Translation:AnimalsCells
    150. McClure GD, Cook PF. Product binding to the alpha-carboxyl subsite results in a conformational change at the active site of O-acetylserine sulfhydrylase-A: evidence from fluorescence spectroscopy. Biochemistry. 1994 Feb 22; 33(7):1674-83. PMID: 8110769.
      Citations: 10     Fields:    Translation:Cells
    151. Berdis AJ, Cook PF. The 2'-phosphate of NADP is critical for optimum productive binding to 6-phosphogluconate dehydrogenase from Candida utilis. Arch Biochem Biophys. 1993 Sep; 305(2):551-8. PMID: 8373193.
      Citations: 1     Fields:    Translation:Animals
    152. Qamar R, Cook PF. pH dependence of the kinetic mechanism of the adenosine 3',5'-monophosphate dependent protein kinase catalytic subunit in the direction of magnesium adenosine 5'-diphosphate phosphorylation. Biochemistry. 1993 Jul 06; 32(26):6802-6. PMID: 8329403.
      Citations: 2     Fields:    Translation:Cells
    153. Tai CH, Nalabolu SR, Jacobson TM, Minter DE, Cook PF. Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants. Biochemistry. 1993 Jun 29; 32(25):6433-42. PMID: 8518286.
      Citations: 26     Fields:    Translation:Cells
    154. Rao GS, Mottonen J, Goldsmith EJ, Cook PF. Crystallization and preliminary X-ray data for the A-isozyme of O-acetylserine sulfhydrylase from Salmonella typhimurium. J Mol Biol. 1993 Jun 20; 231(4):1130-2. PMID: 8515470.
      Citations: 1     Fields:    Translation:Cells
    155. Jahnke K, Podschun B, Schnackerz KD, Kautz J, Cook PF. Acid-base catalytic mechanism of dihydropyrimidinase from pH studies. Biochemistry. 1993 May 18; 32(19):5160-6. PMID: 8494893.
      Citations: 7     Fields:    Translation:AnimalsCells
    156. Rajapaksa R, Abu-Soud H, Raushel FM, Harris BG, Cook PF. Pre-steady-state kinetics reveal a slow isomerization of the enzyme-NAD complex in the NAD-malic enzyme reaction. Biochemistry. 1993 Mar 02; 32(8):1928-34. PMID: 8448150.
      Citations: 2     Fields:    Translation:AnimalsCells
    157. Berdis AJ, Cook PF. Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis. Biochemistry. 1993 Mar 02; 32(8):2036-40. PMID: 8448161.
      Citations: 8     Fields:    Translation:AnimalsCells
    158. Berdis AJ, Cook PF. Chemical mechanism of 6-phosphogluconate dehydrogenase from Candida utilis from pH studies. Biochemistry. 1993 Mar 02; 32(8):2041-6. PMID: 8448162.
      Citations: 4     Fields:    Translation:Animals
    159. Cook PF, Yoon MY, Hara S, McClure GD. Product dependence of deuterium isotope effects in enzyme-catalyzed reactions. Biochemistry. 1993 Feb 23; 32(7):1795-802. PMID: 8439540.
      Citations: 5     Fields:    Translation:AnimalsCells
    160. Podschun B, Jahnke K, Schnackerz KD, Cook PF. Acid base catalytic mechanism of the dihydropyrimidine dehydrogenase from pH studies. J Biol Chem. 1993 Feb 15; 268(5):3407-13. PMID: 8429016.
      Citations: 2     Fields:    Translation:AnimalsCells
    161. Kulkarni G, Cook PF, Harris BG. Cloning and nucleotide sequence of a full-length cDNA encoding Ascaris suum malic enzyme. Arch Biochem Biophys. 1993 Jan; 300(1):231-7. PMID: 8424657.
      Citations: 9     Fields:    Translation:HumansAnimalsCells
    162. Lai CJ, Harris BG, Cook PF. Mechanism of activation of the NAD-malic enzyme from Ascaris suum by fumarate. Arch Biochem Biophys. 1992 Dec; 299(2):214-9. PMID: 1444459.
      Citations: 3     Fields:    Translation:AnimalsCells
    163. Qamar R, Yoon MY, Cook PF. Kinetic mechanism of the adenosine 3',5'-monophosphate dependent protein kinase catalytic subunit in the direction of magnesium adenosine 5'-diphosphate phosphorylation. Biochemistry. 1992 Oct 20; 31(41):9986-92. PMID: 1327136.
      Citations: 8     Fields:    Translation:Cells
    164. Clancy LL, Rao GS, Finzel BC, Muchmore SW, Holland DR, Watenpaugh KD, Krishnamurthy HM, Sweet RM, Cook PF, Harris BG. Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum. J Mol Biol. 1992 Jul 20; 226(2):565-9. PMID: 1640469.
      Citations:    Fields:    Translation:AnimalsCells
    165. Cook PF, Hara S, Nalabolu S, Schnackerz KD. pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine. Biochemistry. 1992 Mar 03; 31(8):2298-303. PMID: 1540585.
      Citations: 6     Fields:    Translation:Cells
    166. Nalabolu SR, Tai CH, Schnackerz KD, Cook PF. Mechanism of O-acetylserine sulfhydrylase fromSalmonella typhimurium LT-2. Amino Acids. 1992 Feb; 2(1-2):119-25. PMID: 24194279.
      Citations: 1     Fields:    
    167. Rao GS, Cook PF, Harris BG. Modification of the ATP inhibitory site of the Ascaris suum phosphofructokinase results in the stabilization of an inactive T state. Biochemistry. 1991 Oct 15; 30(41):9998-10004. PMID: 1832959.
      Citations: 1     Fields:    Translation:AnimalsCells
    168. Weiss PM, Gavva SR, Harris BG, Urbauer JL, Cleland WW, Cook PF. Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction. Biochemistry. 1991 Jun 11; 30(23):5755-63. PMID: 2043615.
      Citations: 2     Fields:    Translation:AnimalsCells
    169. Gavva SR, Harris BG, Weiss PM, Cook PF. Modification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate. Biochemistry. 1991 Jun 11; 30(23):5764-9. PMID: 2043616.
      Citations: 1     Fields:    Translation:AnimalsCells
    170. Rao GS, Cook PF, Harris BG. Effector-induced conformational transitions in Ascaris suum phosphofructokinase. A fluorescence and circular dichroism study. J Biol Chem. 1991 May 15; 266(14):8884-90. PMID: 1827437.
      Citations: 1     Fields:    Translation:AnimalsCells
    171. Payne MA, Rao GS, Harris BG, Cook PF. Fructose 2,6-bisphosphate and AMP increase the affinity of the Ascaris suum phosphofructokinase for fructose 6-phosphate in a process separate from the relief of ATP inhibition. J Biol Chem. 1991 May 15; 266(14):8891-6. PMID: 1827438.
      Citations:    Fields:    Translation:AnimalsCells
    172. Mallick S, Harris BG, Cook PF. Kinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation. J Biol Chem. 1991 Feb 15; 266(5):2732-8. PMID: 1993653.
      Citations: 10     Fields:    Translation:AnimalsCells
    173. Hara S, Payne MA, Schnackerz KD, Cook PF. A rapid purification procedure and computer-assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium. Protein Expr Purif. 1990 Sep; 1(1):70-6. PMID: 2152186.
      Citations: 3     Fields:    Translation:Cells
    174. Podschun B, Cook PF, Schnackerz KD. Kinetic mechanism of dihydropyrimidine dehydrogenase from pig liver. J Biol Chem. 1990 Aug 05; 265(22):12966-72. PMID: 2198281.
      Citations: 5     Fields:    Translation:Animals
    175. Park SH, Harris BG, Cook PF. Substrate activation by malate induced by oxalate in the Ascaris suum NAD-malic enzyme reaction. Biochemistry. 1989 Jul 25; 28(15):6334-40. PMID: 2790001.
      Citations:    Fields:    Translation:AnimalsCells
    176. Cho YK, Cook PF. pH dependence of the kinetic parameters for the pyrophosphate-dependent phosphofructokinase reaction supports a proton-shuttle mechanism. Biochemistry. 1989 May 16; 28(10):4155-60. PMID: 2548569.
      Citations: 1     Fields:    Translation:Cells
    177. Kong CT, Cook PF. Isotope partitioning in the adenosine 3',5'-monophosphate dependent protein kinase reaction indicates a steady-state random kinetic mechanism. Biochemistry. 1988 Jun 28; 27(13):4795-9. PMID: 3048391.
      Citations: 15     Fields:    Translation:Animals
    178. Weiss PM, Chen CY, Cleland WW, Cook PF. Use of primary deuterium and 15N isotope effects to deduce the relative rates of steps in the mechanisms of alanine and glutamate dehydrogenases. Biochemistry. 1988 Jun 28; 27(13):4814-22. PMID: 3139028.
      Citations: 11     Fields:    Translation:AnimalsCells
    179. Cini JK, Cook PF, Gracy RW. Molecular basis for the isozymes of bovine glucose-6-phosphate isomerase. Arch Biochem Biophys. 1988 May 15; 263(1):96-106. PMID: 3369868.
      Citations:    Fields:    Translation:Animals
    180. Cho YK, Matsunaga TO, Kenyon GL, Bertagnolli BL, Cook PF. Isotope exchange as a probe of the kinetic mechanism of pyrophosphate-dependent phosphofructokinase. Biochemistry. 1988 May 03; 27(9):3320-5. PMID: 2839232.
      Citations:    Fields:    Translation:AnimalsCells
    181. Cho YK, Cook PF. Inactivation of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii by pyridoxal 5'-phosphate. Determination of the pH dependence of enzyme-reactant dissociation constants from protection against inactivation. J Biol Chem. 1988 Apr 15; 263(11):5135-40. PMID: 2833495.
      Citations: 2     Fields:    Translation:Cells
    182. Weiss PM, Garcia GA, Kenyon GL, Cleland WW, Cook PF. Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues. Biochemistry. 1988 Mar 22; 27(6):2197-205. PMID: 3378056.
      Citations: 7     Fields:    Translation:Cells
    183. Bhatnagar A, Das B, Gavva SR, Cook PF, Srivastava SK. The kinetic mechanism of human placental aldose reductase and aldehyde reductase II. Arch Biochem Biophys. 1988 Mar; 261(2):264-74. PMID: 3128169.
      Citations: 2     Fields:    Translation:HumansCells
    184. Chen CY, Harris BG, Cook PF. Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism. Biochemistry. 1988 Jan 12; 27(1):212-9. PMID: 3280016.
      Citations: 1     Fields:    Translation:AnimalsCells
    185. Weiss PM, Cook PF, Hermes JD, Cleland WW. Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase. Biochemistry. 1987 Nov 17; 26(23):7378-84. PMID: 3427079.
      Citations: 15     Fields:    Translation:Animals
    186. Cook PF, Rao GS, Hofer HW, Harris BG. Correlation between hysteresis and allosteric properties for phosphofructokinase from Ascaris suum. J Biol Chem. 1987 Oct 15; 262(29):14063-7. PMID: 2958457.
      Citations: 1     Fields:    Translation:AnimalsCells
    187. Rao GS, Wariso BA, Cook PF, Hofer HW, Harris BG. Reaction of Ascaris suum phosphofructokinase with diethylpyrocarbonate. Inactivation and desensitization to allosteric modulation. J Biol Chem. 1987 Oct 15; 262(29):14068-73. PMID: 2958458.
      Citations: 1     Fields:    Translation:AnimalsCells
    188. Rao GS, Harris BG, Cook PF. Kinetic mechanism of Ascaris suum phosphofructokinase desensitized to allosteric modulation by diethylpyrocarbonate modification. J Biol Chem. 1987 Oct 15; 262(29):14074-9. PMID: 2958459.
      Citations:    Fields:    Translation:AnimalsCells
    189. Yoon MY, Cook PF. Chemical mechanism of the adenosine cyclic 3',5'-monophosphate dependent protein kinase from pH studies. Biochemistry. 1987 Jun 30; 26(13):4118-25. PMID: 2820483.
      Citations: 13     Fields:    Translation:Cells
    190. Rao GS, Kong CT, Benjamin RC, Harris BG, Cook PF. Modification of an arginine residue essential for the activity of NAD-malic enzyme from Ascaris suum. Arch Biochem Biophys. 1987 May 15; 255(1):8-13. PMID: 3592670.
      Citations:    Fields:    Translation:AnimalsCells
    191. Bertagnolli BL, Younathan ES, Voll RJ, Pittman CE, Cook PF. Carbohydrate substrate specificity of bacterial and plant pyrophosphate-dependent phosphofructokinases. Biochemistry. 1986 Aug 12; 25(16):4674-81. PMID: 3021198.
      Citations: 2     Fields:    Translation:AnimalsCells
    192. Bertagnolli BL, Younathan ES, Voll RJ, Cook PF. Kinetic studies on the activation of pyrophosphate-dependent phosphofructokinase from mung bean by fructose 2,6-bisphosphate and related compounds. Biochemistry. 1986 Aug 12; 25(16):4682-7. PMID: 3021199.
      Citations: 6     Fields:    Translation:AnimalsCells
    193. Park SH, Harris BG, Cook PF. pH dependence of kinetic parameters for oxalacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme. Biochemistry. 1986 Jul 01; 25(13):3752-9. PMID: 3741834.
      Citations: 7     Fields:    Translation:AnimalsCells
    194. Kiick DM, Harris BG, Cook PF. Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinucleotide-malic enzyme reaction from isotope effects and pH studies. Biochemistry. 1986 Jan 14; 25(1):227-36. PMID: 3513825.
      Citations: 5     Fields:    Translation:AnimalsCells
    195. Rao JG, Harris BG, Cook PF. Diethylpyrocarbonate inactivation of NAD-malic enzyme from Ascaris suum. Arch Biochem Biophys. 1985 Aug 15; 241(1):67-74. PMID: 4026323.
      Citations: 1     Fields:    Translation:AnimalsCells
    196. Nuiry II, Cook PF. The pH dependence of the reductive carboxylation of pyruvate by malic enzyme. Biochim Biophys Acta. 1985 Jun 10; 829(2):295-8. PMID: 3995057.
      Citations: 2     Fields:    Translation:AnimalsCells
    197. Park SH, Kiick DM, Harris BG, Cook PF. Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum. Biochemistry. 1984 Nov 06; 23(23):5446-53. PMID: 6509028.
      Citations: 2     Fields:    Translation:AnimalsCells
    198. Kiick DM, Allen BL, Rao JG, Harris BG, Cook PF. Determination of dissociation constants for enzyme-reactant complexes for NAD-malic enzyme by modulation of the thiol inactivation rate. Biochemistry. 1984 Nov 06; 23(23):5454-9. PMID: 6509029.
      Citations:    Fields:    Translation:Animals
    199. Nuiry II, Hermes JD, Weiss PM, Chen CY, Cook PF. Kinetic mechanism and location of rate-determining steps for aspartase from Hafnia alvei. Biochemistry. 1984 Oct 23; 23(22):5168-75. PMID: 6509019.
      Citations: 3     Fields:    Translation:Cells
    200. Bertagnolli BL, Cook PF. Kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii. Biochemistry. 1984 Aug 28; 23(18):4101-8. PMID: 6091737.
      Citations: 7     Fields:    Translation:AnimalsCells
    201. Taylor KB, Cook PF, Cleland WW. Solvent isotope effects on the reaction catalyzed by yeast hexokinase. Eur J Biochem. 1983 Aug 15; 134(3):571-4. PMID: 6349994.
      Citations:    Fields:    Translation:AnimalsCells
    202. Kiick DM, Cook PF. pH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase. Biochemistry. 1983 Jan 18; 22(2):375-82. PMID: 6402008.
      Citations: 5     Fields:    Translation:Cells
    203. Cook PF, Neville ME, Vrana KE, Hartl FT, Roskoski R. Adenosine cyclic 3',5'-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit. Biochemistry. 1982 Nov 09; 21(23):5794-9. PMID: 6295440.
      Citations: 96     Fields:    Translation:Animals
    204. Cook PF. Kinetic studies to determine the mechanism of regulation of bovine liver glutamate dehydrogenase by nucleotide effectors. Biochemistry. 1982 Jan 05; 21(1):113-6. PMID: 6120719.
      Citations: 4     Fields:    Translation:AnimalsCells
    205. Grimshaw CE, Cook PF, Cleland WW. Use of isotope effects and pH studies to determine the chemical mechanism of Bacillus subtilis L-alanine dehydrogenase. Biochemistry. 1981 Sep 29; 20(20):5655-61. PMID: 6794612.
      Citations: 6     Fields:    Translation:Cells
    206. Cook PF, Cleland WW. Mechanistic deductions from isotope effects in multireactant enzyme mechanisms. Biochemistry. 1981 Mar 31; 20(7):1790-6. PMID: 7013799.
      Citations: 29     Fields:    Translation:AnimalsCells
    207. Cook PF, Cleland WW. pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same. Biochemistry. 1981 Mar 31; 20(7):1797-805. PMID: 7013800.
      Citations: 22     Fields:    Translation:Animals
    208. Cook PF, Cleland WW. pH variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase. Biochemistry. 1981 Mar 31; 20(7):1805-16. PMID: 7013801.
      Citations: 17     Fields:    Translation:AnimalsCells
    209. Cook PF, Oppenheimer NJ, Cleland WW. Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase. Biochemistry. 1981 Mar 31; 20(7):1817-25. PMID: 7013802.
      Citations: 13     Fields:    Translation:Animals
    210. Cook PF, Kenyon GL, Cleland WW. Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase. Biochemistry. 1981 Mar 03; 20(5):1204-10. PMID: 7013788.
      Citations: 13     Fields:    Translation:Animals
    211. Cook PF, Blanchard JS, Cleland WW. Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions. Biochemistry. 1980 Oct 14; 19(21):4853-8. PMID: 7000186.
      Citations: 10     Fields:    
    212. Viola RE, Cook PF, Cleland WW. Stereoselective preparation of deuterated reduced nicotinamide adenine nucleotides and substrates by enzymatic synthesis. Anal Biochem. 1979 Jul 15; 96(2):334-40. PMID: 224725.
      Citations: 15     Fields:    Translation:Cells
    213. Cook PF, Wedding RT. Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers. J Biol Chem. 1978 Nov 10; 253(21):7874-9. PMID: 359557.
      Citations: 10     Fields:    Translation:Cells
    214. Cook PF, Wedding RT. Overall mechanism and rate equation for O-acetylserine sulfhydrylase. J Biol Chem. 1977 May 25; 252(10):3459. PMID: 863890.
      Citations: 6     Fields:    
    215. Cook PF, Wedding RT. salmonella typhimurium/enzymol. Arch Biochem Biophys. 1977 Jan 15; 178(1):293-302. PMID: 319757.
      Citations: 13     Fields:    Translation:Cells
    216. Cook PF, Wedding RT. A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2. J Biol Chem. 1976 Apr 10; 251(7):2023-9. PMID: 773932.
      Citations: 21     Fields:    Translation:Cells
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