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Grover Waldrop - Publications

Affiliations: 
Louisiana State University, Baton Rouge, LA, United States 
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36 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Cavuzic MT, Waldrop GL. Kinetic characterization of the N-terminal domain of Malonyl-CoA reductase. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1872: 140986. PMID 38122963 DOI: 10.1016/j.bbapap.2023.140986  0.418
2017 Evans A, Ribble W, Schexnaydre E, Waldrop GL. Acetyl-CoA carboxylase in Escherichia coli exhibits a pronounced hysteresis when inhibited by palmitoyl-acyl carrier protein. Archives of Biochemistry and Biophysics. PMID 29100983 DOI: 10.1016/j.abb.2017.10.016  0.348
2015 Broussard TC, Pakhomova S, Neau DB, Bonnot R, Waldrop GL. Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase. Biochemistry. 54: 3860-70. PMID 26020841 DOI: 10.1021/Acs.Biochem.5B00340  0.406
2014 Brylinski M, Waldrop GL. Computational redesign of bacterial biotin carboxylase inhibitors using structure-based virtual screening of combinatorial libraries Molecules. 19: 4021-4045. PMID 24699146 DOI: 10.3390/molecules19044021  0.338
2014 Malina A, Bryant SK, Chang SH, Waldrop GL, Gilman SD. Capillary electrophoresis-based assay of phosphofructokinase-1. Analytical Biochemistry. 447: 1-5. PMID 24444856 DOI: 10.1016/j.ab.2013.10.028  0.34
2013 Broussard TC, Price AE, Laborde SM, Waldrop GL. Complex formation and regulation of escherichia coli acetyl-CoA carboxylase Biochemistry. 52: 3346-3357. PMID 23594205 DOI: 10.1021/bi4000707  0.44
2013 Broussard TC, Kobe MJ, Pakhomova S, Neau DB, Price AE, Champion TS, Waldrop GL. The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase Structure. 21: 650-657. PMID 23499019 DOI: 10.1016/J.Str.2013.02.001  0.409
2012 Waldrop GL, Holden HM, Maurice MS. The enzymes of biotin dependent CO2 metabolism: What structures reveal about their reaction mechanisms Protein Science. 21: 1597-1619. PMID 22969052 DOI: 10.1002/Pro.2156  0.373
2011 Novak BR, Moldovan D, Waldrop GL, De Queiroz MS. Behavior of the ATP grasp domain of biotin carboxylase monomers and dimers studied using molecular dynamics simulations Proteins: Structure, Function and Bioinformatics. 79: 622-632. PMID 21120858 DOI: 10.1002/Prot.22910  0.379
2009 Novak BR, Moldovan D, Waldrop GL, de Queiroz MS. Umbrella sampling simulations of biotin carboxylase: is a structure with an open ATP grasp domain stable in solution? The Journal of Physical Chemistry. B. 113: 10097-103. PMID 19585972 DOI: 10.1021/Jp810650Q  0.383
2009 Thalji NK, Crowe WE, Waldrop GL. Kinetic mechanism and structural requirements of the amine-catalyzed decarboxylation of oxaloacetic acid Journal of Organic Chemistry. 74: 144-152. PMID 19035664 DOI: 10.1021/jo8014648  0.355
2009 Bordelon T, Nilsson Lill SO, Waldrop GL. The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase Proteins: Structure, Function and Bioinformatics. 74: 808-819. PMID 18704941 DOI: 10.1002/prot.22190  0.609
2008 Mochalkin I, Miller JR, Evdokimov A, Lightle S, Yan C, Stover CK, Waldrop GL. Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase Protein Science. 17: 1706-1718. PMID 18725455 DOI: 10.1110/ps.035584.108  0.541
2008 Nilsson Lill SO, Gao J, Waldrop GL. Molecular dynamics simulations of biotin carboxylase. The Journal of Physical Chemistry. B. 112: 3149-56. PMID 18271571 DOI: 10.1021/Jp076326C  0.57
2007 de Queiroz MS, Waldrop GL. Modeling and numerical simulation of biotin carboxylase kinetics: Implications for half-sites reactivity Journal of Theoretical Biology. 246: 167-175. PMID 17266990 DOI: 10.1016/j.jtbi.2006.12.025  0.389
2006 Xue QG, Waldrop GL, Schey KL, Itoh N, Ogawa M, Cooper RK, Losso JN, La Peyre JF. A novel slow-tight binding serine protease inhibitor from eastern oyster (Crassostrea virginica) plasma inhibits perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 145: 16-26. PMID 16872855 DOI: 10.1016/J.Cbpb.2006.05.010  0.31
2006 Santoro N, Brtva T, Roest SV, Siegel K, Waldrop GL. A high-throughput screening assay for the carboxyltransferase subunit of acetyl-CoA carboxylase Analytical Biochemistry. 354: 70-77. PMID 16707089 DOI: 10.1016/j.ab.2006.04.006  0.312
2006 Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL. The structure of the carboxyltransferase component of acetyl-CoA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme Biochemistry. 45: 1712-1722. PMID 16460018 DOI: 10.1021/Bi0520479  0.341
2006 Yuan J, Sayegh J, Mendez J, Sward L, Sanchez N, Sanchez S, Waldrop G, Grover S. The regulatory role of residues 226-232 in phosphoenolpyruvate carboxylase from maize. Photosynthesis Research. 88: 73-81. PMID 16453061 DOI: 10.1007/S11120-005-9032-X  0.523
2004 Sloane V, Waldrop GL. Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase Journal of Biological Chemistry. 279: 15772-15778. PMID 14960587 DOI: 10.1074/jbc.M311982200  0.395
2002 Levert KL, Waldrop GL. A bisubstrate analog inhibitor of the carboxyltransferase component of acetyl-CoA carboxylase Biochemical and Biophysical Research Communications. 291: 1213-1217. PMID 11883946 DOI: 10.1006/bbrc.2002.6576  0.304
2001 Janiyani K, Bordelon T, Waldrop GL, Cronan JE. Function of Escherichia coli Biotin Carboxylase Requires Catalytic Activity of Both Subunits of the Homodimer Journal of Biological Chemistry. 276: 29864-29870. PMID 11390406 DOI: 10.1074/Jbc.M104102200  0.44
2001 Sloane V, Blanchard CZ, Guillot F, Waldrop GL. Site-directed mutagenesis of ATP binding residues of biotin carboxylase: Insight into the mechanism of catalysis Journal of Biological Chemistry. 276: 24991-24996. PMID 11346647 DOI: 10.1074/jbc.M101472200  0.579
2000 Thoden JB, Blanchard CZ, Holden HM, Waldrop GL. Movement of the biotin carboxylase B-domain as a result of ATP binding Journal of Biological Chemistry. 275: 16183-16190. PMID 10821865 DOI: 10.1074/Jbc.275.21.16183  0.495
2000 Levert KL, Lloyd RB, Waldrop GL. Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin Biochemistry. 39: 4122-4128. PMID 10747803 DOI: 10.1021/bi992662a  0.47
1999 Blanchard CZ, Amspacher D, Strongin R, Waldrop GL. Inhibition of biotin carboxylase by a reaction intermediate analog: Implications for the kinetic mechanism Biochemical and Biophysical Research Communications. 266: 466-471. PMID 10600526 DOI: 10.1006/Bbrc.1999.1844  0.382
1999 Blanchard CZ, Chapman-Smith A, Wallace JC, Waldrop GL. The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin Journal of Biological Chemistry. 274: 31767-31769. PMID 10542197 DOI: 10.1074/jbc.274.45.31767  0.397
1999 Blanchard CZ, Lee YM, Frantom PA, Waldrop GL. Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin Biochemistry. 38: 3393-3400. PMID 10079084 DOI: 10.1021/Bi982660A  0.454
1998 Blanchard CZ, Waldrop GL. Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase Journal of Biological Chemistry. 273: 19140-19145. PMID 9668099 DOI: 10.1074/jbc.273.30.19140  0.434
1994 Waldrop GL, Braxton BF, Urbauer JL, Cleland WW, Kiick DM. Secondary 18O and primary 13C isotope effects as a probe of transition-state structure for enzymatic decarboxylation of oxalacetate. Biochemistry. 33: 5262-7. PMID 8172901 DOI: 10.1021/Bi00183A032  0.486
1994 Zhou BB, Waldrop GL, Lum L, Schachman HK. A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer Protein Science. 3: 967-974. PMID 8069226 DOI: 10.1002/Pro.5560030612  0.386
1994 Waldrop GL. Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase Biochemistry®. 33: 10249-10256. PMID 7915138 DOI: 10.1021/Bi00200A004  0.354
1992 Waldrop GL, Turnbull JL, Parmentier LE, Lee S, O'Leary MH, Cleland WW, Schachman HK. The contribution of threonine 55 to catalysis in aspartate transcarbamoylase. Biochemistry. 31: 6592-7. PMID 1633171 DOI: 10.1021/Bi00143A032  0.627
1992 Waldrop GL, Turnbull JL, Parmentier LE, O'Leary MH, Cleland WW, Schachman HK. Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine. Biochemistry. 31: 6585-91. PMID 1633170 DOI: 10.1021/Bi00143A031  0.625
1992 Turnbull JL, Waldrop GL, Schachman HK. Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase Biochemistry. 31: 6562-6569. PMID 1633167 DOI: 10.1021/Bi00143A028  0.383
1992 Waldrop GL, Urbauer JL, Cleland WW. Nitrogen-15 isotope effects on nonenzymic and aspartate transcarbamylase catalyzed reactions of carbamyl phosphate Journal of the American Chemical Society. 114: 5941-5945. DOI: 10.1021/Ja00041A006  0.523
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