| Year | Citation | Score | |||
|---|---|---|---|---|---|
| 2023 | Plapp BV. Solvent isotope and mutagenesis studies on the proton relay system in yeast alcohol dehydrogenase 1. Chemico-Biological Interactions. 388: 110853. PMID 38151107 DOI: 10.1016/j.cbi.2023.110853 | 0.481 | |||
| 2023 | Plapp BV, Kratzer DA, Souhrada SK, Warth E, Jacobi T. Specific base catalysis by yeast alcohol dehydrogenase I with substitutions of histidine-48 by glutamate or serine residues in the proton relay system. Chemico-Biological Interactions. 382: 110558. PMID 37247811 DOI: 10.1016/j.cbi.2023.110558 | 0.545 | |||
| 2022 | Plapp BV, Gakhar L, Subramanian R. Dependence of crystallographic atomic displacement parameters on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenase. Acta Crystallographica. Section D, Structural Biology. 78: 1221-1234. PMID 36189742 DOI: 10.1107/S2059798322008361 | 0.476 | |||
| 2021 | Pal S, Plapp BV. The Thr45Gly substitution in yeast alcohol dehydrogenase substantially decreases catalysis, alters pH dependencies, and disrupts the proton relay system. Chemico-Biological Interactions. 349: 109650. PMID 34529977 DOI: 10.1016/j.cbi.2021.109650 | 0.588 | |||
| 2021 | Plapp BV, Subramanian R. Alternative binding modes in abortive NADH-alcohol complexes of horse liver alcohol dehydrogenase. Archives of Biochemistry and Biophysics. 701: 108825. PMID 33675814 DOI: 10.1016/j.abb.2021.108825 | 0.569 | |||
| 2021 | Guntupalli SR, Li Z, Chang L, Plapp BV, Subramanian R. Cryo-Electron Microscopy Structures of Yeast Alcohol Dehydrogenase. Biochemistry. PMID 33620215 DOI: 10.1021/acs.biochem.0c00921 | 0.46 | |||
| 2020 | Kim K, Plapp BV. Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen Transfer. Biochemistry. PMID 31994873 DOI: 10.1021/Acs.Biochem.9B01074 | 0.695 | |||
| 2019 | Kim K, Plapp BV. Substitution of cysteine-153 ligated to the catalytic zinc in yeast alcohol dehydrogenase with aspartic acid and analysis of mechanisms of related medium chain dehydrogenases. Chemico-Biological Interactions. PMID 30721696 DOI: 10.1016/J.Cbi.2019.01.040 | 0.643 | |||
| 2018 | Kim YH, Gogerty DS, Plapp BV. Substitutions of a buried glutamate residue hinder the conformational change in horse liver alcohol dehydrogenase and yield a surprising complex with endogenous 3'-Dephosphocoenzyme A. Archives of Biochemistry and Biophysics. 653: 97-106. PMID 30018019 DOI: 10.1016/J.Abb.2018.07.003 | 0.655 | |||
| 2017 | Shanmuganatham KK, Wallace RS, Lee AT, Plapp BV. Contribution of Buried Distal Amino Acid Residues in Horse Liver Alcohol Dehydrogenase to Structure and Catalysis. Protein Science : a Publication of the Protein Society. PMID 29271062 DOI: 10.1002/Pro.3370 | 0.624 | |||
| 2017 | Plapp BV, Savarimuthu BR, Ferraro DJ, Rubach JK, Brown EN, Ramaswamy S. Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis. Biochemistry. PMID 28640600 DOI: 10.1021/Acs.Biochem.7B00446 | 0.778 | |||
| 2016 | Kim K, Plapp BV. Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93. Chemico-Biological Interactions. PMID 28025168 DOI: 10.1016/J.Cbi.2016.12.016 | 0.678 | |||
| 2015 | Plapp BV, Charlier HA, Ramaswamy S. Mechanistic Implications from Structures of Yeast Alcohol Dehydrogenase Complexed with Coenzyme and an Alcohol. Archives of Biochemistry and Biophysics. PMID 26743849 DOI: 10.1016/J.Abb.2015.12.009 | 0.611 | |||
| 2015 | Plapp BV, Leidal KG, Murch BP, Green DW. Contribution of liver alcohol dehydrogenase to metabolism of alcohols in rats. Chemico-Biological Interactions. 234: 85-95. PMID 25641189 DOI: 10.1016/J.Cbi.2014.12.040 | 0.575 | |||
| 2014 | Raj SB, Ramaswamy S, Plapp BV. Yeast alcohol dehydrogenase structure and catalysis. Biochemistry. 53: 5791-803. PMID 25157460 DOI: 10.1021/Bi5006442 | 0.568 | |||
| 2014 | Yahashiri A, Rubach JK, Plapp BV. Effects of cavities at the nicotinamide binding site of liver alcohol dehydrogenase on structure, dynamics and catalysis. Biochemistry. 53: 881-94. PMID 24437493 DOI: 10.1021/Bi401583F | 0.811 | |||
| 2013 | Plapp BV, Lee AT, Khanna A, Pryor JM. Bradykinetic alcohol dehydrogenases make yeast fitter for growth in the presence of allyl alcohol. Chemico-Biological Interactions. 202: 104-10. PMID 23200945 DOI: 10.1016/J.Cbi.2012.11.010 | 0.589 | |||
| 2012 | Plapp BV, Ramaswamy S. Atomic-resolution structures of horse liver alcohol dehydrogenase with NAD(+) and fluoroalcohols define strained Michaelis complexes. Biochemistry. 51: 4035-48. PMID 22531044 DOI: 10.1021/Bi300378N | 0.603 | |||
| 2011 | Herdendorf TJ, Plapp BV. Origins of the high catalytic activity of human alcohol dehydrogenase 4 studied with horse liver A317C alcohol dehydrogenase. Chemico-Biological Interactions. 191: 42-7. PMID 21184752 DOI: 10.1016/J.Cbi.2010.12.015 | 0.688 | |||
| 2010 | Plapp BV. Conformational changes and catalysis by alcohol dehydrogenase. Archives of Biochemistry and Biophysics. 493: 3-12. PMID 19583966 DOI: 10.1016/J.Abb.2009.07.001 | 0.656 | |||
| 2009 | Pal S, Park DH, Plapp BV. Activity of yeast alcohol dehydrogenases on benzyl alcohols and benzaldehydes: characterization of ADH1 from Saccharomyces carlsbergensis and transition state analysis. Chemico-Biological Interactions. 178: 16-23. PMID 19022233 DOI: 10.1016/J.Cbi.2008.10.037 | 0.625 | |||
| 2007 | Plapp BV, Gogerty DS, Kim YH. Mutating the buried glutamate‐267 in horse liver alcohol dehydrogenase activates the enzyme and locks it in the open conformation The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A646 | 0.588 | |||
| 2005 | Kovaleva EG, Plapp BV. Deprotonation of the horse liver alcohol dehydrogenase-NAD+ complex controls formation of the ternary complexes. Biochemistry. 44: 12797-808. PMID 16171395 DOI: 10.1021/Bi050865V | 0.75 | |||
| 2005 | Collins XH, Harmon SD, Kaduce TL, Berst KB, Fang X, Moore SA, Raju TV, Falck JR, Weintraub NL, Duester G, Plapp BV, Spector AA. Omega-oxidation of 20-hydroxyeicosatetraenoic acid (20-HETE) in cerebral microvascular smooth muscle and endothelium by alcohol dehydrogenase 4. The Journal of Biological Chemistry. 280: 33157-64. PMID 16081420 DOI: 10.1074/Jbc.M504055200 | 0.375 | |||
| 2004 | LeBrun LA, Park DH, Ramaswamy S, Plapp BV. Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase. Biochemistry. 43: 3014-26. PMID 15023053 DOI: 10.1021/Bi036103M | 0.689 | |||
| 2004 | Strömberg P, Svensson S, Berst KB, Plapp BV, Höög JO. Enzymatic mechanism of low-activity mouse alcohol dehydrogenase 2. Biochemistry. 43: 1323-8. PMID 14756569 DOI: 10.1021/Bi0354482 | 0.661 | |||
| 2003 | Venkataramaiah TH, Plapp BV. Formamides mimic aldehydes and inhibit liver alcohol dehydrogenases and ethanol metabolism. The Journal of Biological Chemistry. 278: 36699-706. PMID 12855684 DOI: 10.1074/Jbc.M305419200 | 0.614 | |||
| 2003 | Rubach JK, Plapp BV. Amino acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase. Biochemistry. 42: 2907-15. PMID 12627956 DOI: 10.1021/Bi0272656 | 0.813 | |||
| 2003 | Plapp BV, Berst KB. Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the uncompetitive inhibition of ethanol metabolism. Chemico-Biological Interactions. 143: 183-93. PMID 12604203 DOI: 10.1016/S0009-2797(02)00202-8 | 0.34 | |||
| 2002 | Rubach JK, Plapp BV. Mobility of fluorobenzyl alcohols bound to liver alcohol dehydrogenases as determined by NMR and X-ray crystallographic studies. Biochemistry. 41: 15770-9. PMID 12501206 DOI: 10.1021/Bi026581H | 0.798 | |||
| 2001 | Rubach JK, Ramaswamy S, Plapp BV. Contributions of valine-292 in the nicotinamide binding site of liver alcohol dehydrogenase and dynamics to catalysis. Biochemistry. 40: 12686-94. PMID 11601993 DOI: 10.1021/Bi011540R | 0.796 | |||
| 2001 | Plapp BV, Mitchell JL, Berst KB. Mouse alcohol dehydrogenase 4: Kinetic mechanism, substrate specificity and simulation of effects of ethanol on retinoid metabolism Chemico-Biological Interactions. 130: 445-456. PMID 11306066 DOI: 10.1016/S0009-2797(00)00284-2 | 0.435 | |||
| 2000 | Charlier HA, Plapp BV. Kinetic cooperativity of human liver alcohol dehydrogenase γ2 Journal of Biological Chemistry. 275: 11569-11575. PMID 10766771 DOI: 10.1074/Jbc.275.16.11569 | 0.628 | |||
| 1999 | Ramaswamy S, Park DH, Plapp BV. Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer Biochemistry. 38: 13951-13959. PMID 10529241 DOI: 10.1021/Bi991731I | 0.667 | |||
| 1999 | LeBrun LA, Plapp BV. Control of coenzyme binding to horse liver alcohol dehydrogenase Biochemistry. 38: 12387-12393. PMID 10493806 DOI: 10.1021/Bi991306P | 0.537 | |||
| 1999 | Duester G, Farrés J, Felder MR, Holmes RS, Höög JO, Parés X, Plapp BV, Yin SJ, Jörnvally H. Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family Biochemical Pharmacology. 58: 389-395. PMID 10424757 DOI: 10.1016/S0006-2952(99)00065-9 | 0.395 | |||
| 1999 | Fan F, Plapp BV. Probing the affinity and specificity of yeast alcohol dehydrogenase I for coenzymes Archives of Biochemistry and Biophysics. 367: 240-249. PMID 10395740 DOI: 10.1006/Abbi.1999.1242 | 0.603 | |||
| 1999 | Plapp BV, Chadha VK, Leidal KG, Cho H, Scholze M, Schindler JF, Berst KB, Ramaswamy S. Uncompetitive inhibitors of alcohol dehydrogenases Advances in Experimental Medicine and Biology. 463: 295-303. PMID 10352698 DOI: 10.1007/978-1-4615-4735-8_36 | 0.578 | |||
| 1998 | Strasser F, Dey J, Eftink MR, Plapp BV. Activation of horse liver alcohol dehydrogenase upon substitution of tryptophan 314 at the dimer interface Archives of Biochemistry and Biophysics. 358: 369-376. PMID 9784252 DOI: 10.1006/Abbi.1998.0882 | 0.585 | |||
| 1998 | Deng H, Schindler JF, Berst KB, Plapp BV, Callender R. A Raman spectroscopic characterization of bonding in the complex of horse liver alcohol dehydrogenase with NADH and N-cyclohexylformamide. Biochemistry. 37: 14267-78. PMID 9760265 DOI: 10.1021/Bi981477E | 0.397 | |||
| 1998 | Schindler JF, Berst KB, Plapp BV. Inhibition of human alcohol dehydrogenases by formamides Journal of Medicinal Chemistry. 41: 1696-1701. PMID 9572895 DOI: 10.1021/Jm9707380 | 0.549 | |||
| 1998 | Cho H, Plapp BV. Specificity of alcohol dehydrogenases for sulfoxides Biochemistry. 37: 4482-4489. PMID 9521768 DOI: 10.1021/Bi9727040 | 0.564 | |||
| 1997 | Ramaswamy S, Scholze M, Plapp BV. Binding of formamides to liver alcohol dehydrogenase Biochemistry. 36: 3522-3527. PMID 9132002 DOI: 10.1021/Bi962491Z | 0.586 | |||
| 1997 | Strasser F, Huyng MN, Plapp BV. Activity of liver alcohol dehydrogenases on steroids Advances in Experimental Medicine and Biology. 414: 313-320. PMID 9059635 DOI: 10.1007/978-1-4615-5871-2_36 | 0.474 | |||
| 1997 | Cho H, Ramaswamy S, Plapp BV. Flexibility of liver alcohol dehydrogenase in stereoselective binding of 3-butylthiolane 1-oxides Biochemistry. 36: 382-389. PMID 9003191 DOI: 10.1021/Bi9624604 | 0.524 | |||
| 1996 | Ramaswamy S, El Ahmed M, Jörnvall H, Plapp BV, Eklund H. Alcohol dehydrogenase: more structures – implications to specificity and function Acta Crystallographica Section a Foundations of Crystallography. 52: C98-C98. DOI: 10.1107/S0108767396095177 | 0.419 | |||
| 1995 | Plapp BV. Site-directed mutagenesis: A tool for studying enzyme catalysis Methods in Enzymology. 249: 91-122. PMID 7791629 DOI: 10.1016/0076-6879(95)49032-9 | 0.509 | |||
| 1995 | Fan F, Plapp BV. Substitutions of isoleucine residues at the adenine binding site activate horse liver alcohol dehydrogenase Biochemistry. 34: 4709-4713. PMID 7718576 DOI: 10.1021/Bi00014A027 | 0.605 | |||
| 1994 | Ramaswamy S, Kratzer DA, Hershey AD, Rogers PH, Arnone A, Eklund H, Plapp BV. Crystallization and preliminary crystallographic studies of Saccharomyces cerevisiae alcohol dehydrogenase I. Journal of Molecular Biology. 235: 777-9. PMID 8289298 DOI: 10.1006/Jmbi.1994.1031 | 0.448 | |||
| 1994 | Ramaswamy S, Eklund H, Plapp BV. Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols Biochemistry. 33: 5230-5237. PMID 8172897 DOI: 10.1021/bi00183a028 | 0.584 | |||
| 1994 | Plapp BV. Control of alcohol metabolism Exs. 71: 311-322. PMID 8032162 | 0.435 | |||
| 1994 | Eklund H, Ramaswamy S, Plapp BV, el-Ahmad M, Danielsson O, Höög JO, Jörnvall H. Crystallographic investigations of alcohol dehydrogenases Exs. 71: 269-277. PMID 8032158 | 0.548 | |||
| 1993 | Bahnson BJ, Park DH, Kim K, Plapp BV, Klinman JP. Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis. Biochemistry. 32: 5503-7. PMID 8504071 DOI: 10.1021/Bi00072A003 | 0.64 | |||
| 1993 | Plapp BV, Green DW, Sun HW, Park DH, Kim K. Substrate specificity of alcohol dehydrogenases Advances in Experimental Medicine and Biology. 328: 391-400. PMID 8493917 DOI: 10.1007/978-1-4615-2904-0_41 | 0.596 | |||
| 1993 | Green DW, Sun HW, Plapp BV. Inversion of the substrate specificity of yeast alcohol dehydrogenase Journal of Biological Chemistry. 268: 7792-7798. PMID 8463307 | 0.574 | |||
| 1993 | Shearer GL, Kim K, Lee KM, Wang CK, Plapp BV. Alternative pathways and reactions of benzyl alcohol and benzaldehyde with horse liver alcohol dehydrogenase. Biochemistry. 32: 11186-94. PMID 8218182 DOI: 10.1021/Bi00092A031 | 0.584 | |||
| 1993 | Ramaswamy S, Plapp BV, Eklund H. Structural studies on alcohol dehydrogenases and inhibitor complexes Acta Crystallographica Section a Foundations of Crystallography. 49: c88-c88. DOI: 10.1107/S0108767378097482 | 0.467 | |||
| 1992 | Light DR, Dennis MS, Forsythe IJ, Liu CC, Green DW, Kratzer DA, Plapp BV. α-isoenzyme of alcohol dehydrogenase from monkey liver: Cloning, expression, mechanism, coenzyme, and substrate specificity Journal of Biological Chemistry. 267: 12592-12599. PMID 1618764 | 0.573 | |||
| 1992 | Sun HW, Plapp BV. Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family Journal of Molecular Evolution. 34: 522-535. PMID 1593644 DOI: 10.1007/Bf00160465 | 0.483 | |||
| 1992 | Park DH, Plapp BV. Interconversion of E and S isoenzymes of horse liver alcohol dehydrogenase. Several residues contribute indirectly to catalysis Journal of Biological Chemistry. 267: 5527-5533. PMID 1544927 | 0.508 | |||
| 1991 | Plapp BV. An aspartate residue in yeast alcohol dehydrogenase i determines the specificity for coenzyme Biochemistry. 30: 6397-6401. PMID 2054345 DOI: 10.1021/Bi00240A008 | 0.67 | |||
| 1991 | Plapp BV, Ganzhorn AJ, Gould RM, Green DW, Jacobi T, Warth E, Kratzer DA. Catalysis by yeast alcohol dehydrogenase. Advances in Experimental Medicine and Biology. 284: 241-51. PMID 2053479 DOI: 10.1007/978-1-4684-5901-2_26 | 0.505 | |||
| 1991 | Park DH, Plapp BV. Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids: cDNA cloning, expression, and comparison of active sites Journal of Biological Chemistry. 266: 13296-13302. PMID 1712777 | 0.358 | |||
| 1990 | Gould RM, Plapp BV. Substitution of arginine for histidine-47 in the coenzyme binding site of yeast alcohol dehydrogenase I. Biochemistry. 29: 5463-8. PMID 2201405 DOI: 10.1021/Bi00475A009 | 0.615 | |||
| 1990 | Sekhar VC, Plapp BV. Rate constants for a mechanism including intermediates in the interconversion of ternary complexes by horse liver alcohol dehydrogenase. Biochemistry. 29: 4289-95. PMID 2161681 | 0.397 | |||
| 1988 | Lee KM, Dahlhauser KF, Plapp BV. Reactivity of horse liver alcohol dehydrogenase with 3-methylcyclohexanols Biochemistry. 27: 3528-3532. PMID 3390450 DOI: 10.1021/Bi00409A060 | 0.543 | |||
| 1988 | Ganzhorn AJ, Plapp BV. Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase Journal of Biological Chemistry. 263: 5446-5454. PMID 3281940 | 0.493 | |||
| 1988 | Sekhar VC, Plapp BV. Mechanism of binding of horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide. Biochemistry. 27: 5082-8. PMID 3167032 DOI: 10.1021/Bi00414A020 | 0.577 | |||
| 1987 | Plapp BV, Parsons M, Leidal KG, Baggenstoss BA, Ferm JR, Wear SS. Characterization of alcohol dehydrogenase from cultured rat hepatoma (HTC) cells Progress in Clinical and Biological Research. 232: 203-215. PMID 3615421 | 0.496 | |||
| 1987 | Ganzhorn AJ, Green DW, Hershey AD, Gould RM, Plapp BV. Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity Journal of Biological Chemistry. 262: 3754-3761. PMID 3546317 | 0.631 | |||
| 1987 | Plapp BV, Ganzhorn AJ, Gould RM, Green DW, Hershey AD. Structure and function in yeast alcohol dehydrogenases Progress in Clinical and Biological Research. 232: 227-236. PMID 3303037 | 0.556 | |||
| 1986 | Plapp BV, Sogin DC, Dworschack RT, Bohlken DP, Woenckhaus C, Jeck R. Kinetics of native and modified liver alcohol dehydrogenase with coenzyme analogues: Isomerization of enzyme-nicotinamide adenine dinucleotide complex Biochemistry. 25: 5396-5402. PMID 3778867 DOI: 10.1021/Bi00367A008 | 0.556 | |||
| 1985 | Chadha VK, Leidal KG, Plapp BV. Inhibition of liver alcohol dehydrogenase and ethanol metabolism by 3-substituted thiolane 1-oxides Journal of Medicinal Chemistry. 28: 36-40. PMID 3155552 DOI: 10.1002/Chin.198521163 | 0.542 | |||
| 1984 | Plapp BV, Leidal KG, Smith RK, Murch BP. Kinetics of inhibition of ethanol metabolism in rats and the rate-limiting role of alcohol dehydrogenase Archives of Biochemistry and Biophysics. 230: 30-38. PMID 6370140 DOI: 10.1016/0003-9861(84)90083-3 | 0.536 | |||
| 1984 | Chadha VK, Plapp BV. Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with 3-bromopropionic acid Biochemistry. 23: 216-221. PMID 6365161 DOI: 10.1021/Bi00297A007 | 0.58 | |||
| 1984 | Plapp BV, Leidal KG, Murch BP. Role of alcohol dehydrogenase in metabolism of alcohols in rats Federation Proceedings. 43. | 0.422 | |||
| 1983 | Hennecke M, Plapp BV. Involvement of histidine residues in the activity of horse liver alcohol dehydrogenase Biochemistry. 22: 3721-3728. PMID 6351909 DOI: 10.1021/Bi00285A001 | 0.629 | |||
| 1983 | Fries RW, Bohlken DP, Murch BP, Leidal KG, Plapp BV. ω-Haloalkyl esters of 5′-adenosine monophosphate as potential active-site-directed reagents for dehydrogenases Archives of Biochemistry and Biophysics. 225: 110-115. PMID 6351750 DOI: 10.1016/0003-9861(83)90012-7 | 0.54 | |||
| 1983 | Chadha VK, Leidal KG, Plapp BV. Inhibition by carboxamides and s ulfoxides of liver alcohol dehydrogenase and ethanol metabolism Journal of Medicinal Chemistry. 26: 916-922. PMID 6343601 DOI: 10.1002/Chin.198409353 | 0.474 | |||
| 1983 | Plapp BV, Eklund H, Jones TA, Brändén CI. Three-dimensional structure of isonicotinimidylated liver alcohol dehydrogenase Journal of Biological Chemistry. 258: 5537-5547. PMID 6343388 DOI: 10.2210/Pdb7Adh/Pdb | 0.529 | |||
| 1982 | Eklund H, Plapp BV, Samama JP, Brändén CI. Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase Journal of Biological Chemistry. 257: 14349-14358. PMID 6754727 | 0.546 | |||
| 1982 | Plapp BV. [25] Application of affinity labeling for studying structure and function of enzymes Methods in Enzymology. 87: 469-499. DOI: 10.1016/S0076-6879(82)87027-4 | 0.458 | |||
| 1981 | Plapp BV, Chen WS. [46] Affinity labeling with ω-bromoacetamido fatty acids and analogs Methods in Enzymology. 72: 587-591. PMID 7031428 DOI: 10.1016/S0076-6879(81)72048-2 | 0.512 | |||
| 1981 | Mundill PHC, Fries RW, Woenckhaus C, Plapp BV. Sulfonate analogues of adenosine nucleotides as inhibitors of nucleotide-binding enzymes Journal of Medicinal Chemistry. 24: 474-477. PMID 7021832 DOI: 10.1002/Chin.198135334 | 0.478 | |||
| 1981 | Chen WS, Bohlken DP, Plapp BV. Inactivation of liver alcohol dehydrogenases and inhibition of ethanol metabolism by ambivalent active-site-directed reagents Journal of Medicinal Chemistry. 24: 190-193. PMID 7009869 DOI: 10.1002/Chin.198128195 | 0.512 | |||
| 1980 | Chen WS, Plapp BV. Kinetics and control of alcohol oxidation in rats Advances in Experimental Medicine and Biology. 132: 543-549. PMID 6999875 DOI: 10.1007/978-1-4757-1419-7_56 | 0.524 | |||
| 1980 | Chen WS, Bohlken DP, Plapp BV. In vivo evaluation of ambivalent active-site-directed inactivators of liver alcohol dehydrogenase Advances in Experimental Medicine and Biology. 132: 129-135. PMID 6999868 DOI: 10.1007/978-1-4757-1419-7_14 | 0.609 | |||
| 1979 | Chen WS, Plapp BV. Ambivalent active-site-directed inactivators of liver alcohol dehydrogenase. Biochemistry. 17: 4916-22. PMID 718865 DOI: 10.1021/Bi00616A009 | 0.551 | |||
| 1979 | Plapp BV. Transition-state analysis of the facilitated alkylation of ribonuclease a by bromoacetate Biochemistry. 18: 3938-3946. PMID 573623 | 0.341 | |||
| 1979 | Fries RW, Bohlken DP, Plapp BV. 3-Substituted pyrazole derivatives as inhibitors and inactivators of liver alcohol dehydrogenase Journal of Medicinal Chemistry. 22: 356-359. PMID 219196 DOI: 10.1002/Chin.197933202 | 0.622 | |||
| 1978 | Plapp BV, Zeppezauer E, Brändém CI. Crystallization of liver alcohol dehydrogenase activated by the modification of amino groups. Journal of Molecular Biology. 119: 451-3. PMID 641997 DOI: 10.1016/0022-2836(78)90225-5 | 0.491 | |||
| 1978 | Plapp BV, Eklund H, Brändén CI. Crystallography of liver alcohol dehydrogenase complexed with substrates Journal of Molecular Biology. 122: 23-32. PMID 209195 DOI: 10.1016/0022-2836(78)90105-5 | 0.535 | |||
| 1978 | Parker DM, Hardman MJ, Plapp BV, Holbrook JJ, Shore JD. pH-dependent changes of intrinsic fluorescence of chemically modified liver alcohol dehydrogenases. The Biochemical Journal. 173: 269-75. PMID 28733 | 0.572 | |||
| 1977 | Dworschack RT, Plapp BV. Kinetics of native and activated isozymes of horse liver alcohol dehydrogenase Biochemistry. 16: 111-116. PMID 831772 DOI: 10.1021/Bi00620A018 | 0.61 | |||
| 1977 | Dworschack RT, Plapp BV. pH, isotope, and substituent effects on the interconversion of aromatic substrates catalyzed by hydroxybutyrimidylated liver alcohol dehydrogenase Biochemistry. 16: 2716-2725. PMID 19037 DOI: 10.1021/Bi00631A020 | 0.656 | |||
| 1977 | Dubied A, Von Wartburg JP, Bohlken DP, Plapp BV. Characterization and kinetics of native and chemically activated human liver alcohol dehydrogenases Journal of Biological Chemistry. 252: 1464-1470. PMID 14152 | 0.512 | |||
| 1976 | Sogin DC, Plapp BV. Inactivation of horse liver alcohol dehydrogenase by modification of cysteine residue 174 with diazonium-1H-tetrazole Biochemistry. 15: 1087-1093. PMID 1252428 DOI: 10.1021/Bi00650A021 | 0.604 | |||
| 1975 | Sogin DC, Plapp BV. Activation and inactivation of horse liver alcohol dehydrogenase with pyridoxal compounds Journal of Biological Chemistry. 250: 205-210. PMID 1170167 | 0.584 | |||
| 1975 | Dworschack R, Tarr G, Plapp BV. Identification of the lysine residue modified during the activation by acetimidylation of horse liver alcohol dehydrogenase Biochemistry. 14: 200-203. PMID 1168062 DOI: 10.1021/Bi00673A002 | 0.543 | |||
| 1975 | Fries RW, Bohlken DP, Blakley RT, Plapp BV. Activation of liver alcohol dehydrogenases by imidoesters generated in solution Biochemistry. 14: 5233-5238. PMID 172120 DOI: 10.1021/Bi00694A034 | 0.619 | |||
| 1975 | Plapp BV. Rate-limiting steps in ethanol metabolism and approaches to changing these rates biochemically Advances in Experimental Medicine and Biology. 56: 77-109. PMID 167557 DOI: 10.1007/978-1-4684-7529-6_4 | 0.46 | |||
| 1975 | Sogin DC, Plapp BV. Inactivation of liver alcohol dehydrogenase by diazonium 1 H tetrazole Federation Proceedings. 34. | 0.42 | |||
| 1974 | Zoltobrocki M, Kim JC, Plapp BV. Activity of liver alcohol dehydrogenase with various substituents on the amino groups Biochemistry. 13: 899-903. PMID 4360354 DOI: 10.1021/Bi00702A011 | 0.6 | |||
| 1973 | Plapp BV. On calculation of rate and dissociation constants from kinetic constants for the Ordered Bi Bi mechanism of liver alcohol dehydrogenase Archives of Biochemistry and Biophysics. 156: 112-114. PMID 4730466 DOI: 10.1016/0003-9861(73)90347-0 | 0.517 | |||
| 1973 | Plapp BV, Brooks RL, Shore JD. Horse liver alcohol dehydrogenase. Amino groups and rate-limiting steps in catalysis Journal of Biological Chemistry. 248: 3470-3475. PMID 4349865 | 0.464 | |||
| 1968 | Plapp BV, Woenckhaus C, Pfleiderer G. Evaluation of N1-(ω-bromoacetamidoalkyl)nicotinamides as inhibitors of dehydrogenases Archives of Biochemistry and Biophysics. 128: 360-368. PMID 4301572 | 0.498 | |||
| 1966 | Plapp BV, Cole RD. Purification and characterization of bovine liver β-glucuronidase Archives of Biochemistry and Biophysics. 116: 193-206. PMID 6006802 DOI: 10.1016/0003-9861(66)90027-0 | 0.331 | |||
| Low-probability matches (unlikely to be authored by this person) | |||||
| 1984 | Hennecke M, Plapp BV. Quantitative analysis of lysine analogs and derivatives Analytical Biochemistry. 136: 110-118. PMID 6424499 DOI: 10.1016/0003-2697(84)90312-9 | 0.277 | |||
| 1974 | Plapp BV, Kim JC. Determination of ε-acetimidyllysine in proteins Analytical Biochemistry. 62: 291-294. PMID 4433048 DOI: 10.1016/0003-2697(74)90390-X | 0.266 | |||
| 1967 | Plapp BV, Cole RD. Demonstration and partial characterization of multiple forms of bovine liver β-glucuronidase Biochemistry. 6: 3676-3681. PMID 5624598 | 0.256 | |||
| 2013 | Plapp BV, Kedishvili NY, Rižner TL, Maser E, O'Brien PJ. Chemico-Biological Interactions. Enzymology and molecular biology of carbonyl metabolism 16. Introduction. Chemico-Biological Interactions. 202: 1. PMID 23497822 DOI: 10.1016/J.Cbi.2013.02.004 | 0.232 | |||
| 2011 | Flynn TG, Kedishvili N, Maser E, O'Brien PJ, Plapp BV. Enzymology and Molecular Biology of Carbonyl Metabolism, 15th International Meeting on Enzymology and Molecular Biology of Carbonyl Metabolism. Introduction. Chemico-Biological Interactions. 191: 1. PMID 21402059 DOI: 10.1016/J.Cbi.2011.03.002 | 0.231 | |||
| 1979 | Plapp BV. Kinetics of carboxymethylation of histidine hydantoin Biochemistry. 18: 3933-3938. PMID 39589 | 0.192 | |||
| 1971 | Plapp BV, Moore S, Stein WH. Activity of bovine pancreatic deoxyribonuclease A with modified amino groups. The Journal of Biological Chemistry. 246: 939-45. PMID 5101176 | 0.115 | |||
| 1963 | PLAPP BV, HOPKINS TR, COLE RD. ZONE ELECTROPHORESIS OF BOVINE LIVER BETA-GLUCURONIDASE The Journal of Biological Chemistry. 238: 3315-3317. PMID 14085378 | 0.109 | |||
| 2009 | Weiner H, Duester G, Maser E, Plapp B. Enzymology and molecular biology of carbonyl metabolism. Introduction. Chemico-Biological Interactions. 178: 1. PMID 19056364 DOI: 10.1016/j.cbi.2008.11.003 | 0.083 | |||
| 1973 | Plapp BV. Mechanisms of carboxymethylation of bovine pancreatic nucleases by haloacetates and tosylglycolate Journal of Biological Chemistry. 248: 4896-4900. PMID 4736883 | 0.077 | |||
| 1967 | Plapp BV, Raftery MA, Cole RD. The tryptic digestion of S-aminoethylated ribonuclease. The Journal of Biological Chemistry. 242: 265-70. PMID 6016611 | 0.062 | |||
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