| Year |
Citation |
Score |
| 2023 |
Daudu OI, Meeks KR, Zhang L, Seravalli J, Tanner JJ, Becker DF. Functional Impact of a Cancer-Related Variant in Human Δ-Pyrroline-5-Carboxylate Reductase 1. Acs Omega. 8: 3509-3519. PMID 36713721 DOI: 10.1021/acsomega.2c07788 |
0.634 |
|
| 2021 |
Patel SM, Seravalli J, Stiers KM, Tanner JJ, Becker DF. Kinetics of human pyrroline-5-carboxylate reductase in L-thioproline metabolism. Amino Acids. 53: 1863-1874. PMID 34792644 DOI: 10.1007/s00726-021-03095-4 |
0.602 |
|
| 2021 |
Mao Y, Seravalli J, Smith TG, Morton M, Tanner JJ, Becker DF. Evidence for Proline Catabolic Enzymes in the Metabolism of Thiazolidine Carboxylates. Biochemistry. 60: 3610-3620. PMID 34752700 DOI: 10.1021/acs.biochem.1c00625 |
0.663 |
|
| 2021 |
Patel SM, Seravalli J, Liang X, Tanner JJ, Becker DF. Disease variants of human Δ-pyrroline-5-carboxylate reductase 2 (PYCR2). Archives of Biochemistry and Biophysics. 108852. PMID 33771508 DOI: 10.1016/j.abb.2021.108852 |
0.639 |
|
| 2020 |
Patel S, Smith T, Morton MD, Stiers K, Seravalli J, Mayclin S, Edwards T, Tanner JJ, Becker DF. Cautionary tale of using tris(alkyl)phosphine reducing agents with NAD-dependent enzymes. Biochemistry. PMID 32841567 DOI: 10.1021/Acs.Biochem.0C00490 |
0.679 |
|
| 2020 |
Campbell AC, Becker DF, Gates KS, Tanner JJ. Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate. Acs Chemical Biology. PMID 32159324 DOI: 10.1021/Acschembio.9B00935 |
0.433 |
|
| 2019 |
Christgen SL, Becker SM, Becker DF. Methods for determining the reduction potentials of flavin enzymes. Methods in Enzymology. 620: 1-25. PMID 31072483 DOI: 10.1016/Bs.Mie.2019.03.004 |
0.328 |
|
| 2019 |
Kochert BA, Fleischhacker AS, Wales TE, Becker DF, Engen JR, Ragsdale SW. Dynamic and structural differences between heme oxygenase-1 and -2 are due to differences in their C-terminal regions. The Journal of Biological Chemistry. PMID 30944174 DOI: 10.1074/Jbc.Ra119.008592 |
0.582 |
|
| 2018 |
Korasick DA, Campbell AC, Christgen SL, Chakravarthy S, White TA, Becker DF, Tanner JJ. Redox Modulation of Oligomeric State in Proline Utilization A. Biophysical Journal. 114: 2833-2843. PMID 29925020 DOI: 10.1016/J.Bpj.2018.04.046 |
0.413 |
|
| 2018 |
Tanner JJ, Fendt SM, Becker DF. The proline cycle as a potential cancer therapy target. Biochemistry. PMID 29648801 DOI: 10.1021/Acs.Biochem.8B00215 |
0.379 |
|
| 2017 |
Korasick DA, Pemberton TA, Arentson BW, Becker DF, Tanner JJ. Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline. Molecules (Basel, Switzerland). 23. PMID 29295473 DOI: 10.3390/molecules23010032 |
0.313 |
|
| 2017 |
Christgen S, Zhu W, Sanyal N, Bibi BM, Tanner JJ, Becker DF. Discovery of the Membrane Binding Domain in Trifunctional Proline Utilization A. Biochemistry. PMID 29090935 DOI: 10.1021/Acs.Biochem.7B01008 |
0.389 |
|
| 2017 |
Liu LK, Becker DF, Tanner JJ. Structure, function, and mechanism of proline utilization A (PutA). Archives of Biochemistry and Biophysics. PMID 28712849 DOI: 10.1016/J.Abb.2017.07.005 |
0.45 |
|
| 2017 |
Moxley MA, Zhang L, Christgen S, Tanner JJ, Becker DF. Identification of a Conserved Histidine as Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein. Biochemistry. PMID 28558236 DOI: 10.1021/Acs.Biochem.7B00046 |
0.458 |
|
| 2017 |
Korasick D, Gamage TT, Christgen S, Stiers KM, Beamer LJ, Henzl MT, Becker DF, Tanner JJ. Structure and characterization of a class 3B proline utilization A: ligand-induced dimerization and importance of the C-terminal domain for catalysis. The Journal of Biological Chemistry. PMID 28420730 DOI: 10.1074/Jbc.M117.786855 |
0.432 |
|
| 2017 |
Christensen EM, Patel SM, Korasick DA, Campbell AC, Krause KL, Becker DF, Tanner JJ. Resolving the Cofactor Binding Site in the Proline Biosynthetic Enzyme Human Pyrroline-5-Carboxylate Reductase 1. The Journal of Biological Chemistry. PMID 28258219 DOI: 10.1074/Jbc.M117.780288 |
0.453 |
|
| 2016 |
Natarajan SK, Muthukrishnan E, Khalimonchuk O, Mott JL, Becker DF. Evidence for Pipecolate Oxidase in Mediating Protection Against Hydrogen Peroxide Stress. Journal of Cellular Biochemistry. PMID 27922192 DOI: 10.1002/Jcb.25825 |
0.337 |
|
| 2016 |
Arentson BW, Hayes EL, Zhu W, Singh H, Tanner JJ, Becker DF. Engineering a Trifunctional Proline Utilization A Chimera By Fusing a DNA-Binding Domain to a Bifunctional PutA. Bioscience Reports. PMID 27742866 DOI: 10.1042/Bsr20160435 |
0.37 |
|
| 2016 |
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ. Structures of Proline Utilization A Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. The Journal of Biological Chemistry. PMID 27679491 DOI: 10.1074/Jbc.M116.756965 |
0.434 |
|
| 2015 |
Inoguchi N, Chaiseeda K, Yamanishi M, Kim MK, Jang Y, Bajaj M, Chia CP, Becker DF, Moriyama H. Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation. Bmc Research Notes. 8: 784. PMID 26666293 DOI: 10.1186/S13104-015-1760-1 |
0.431 |
|
| 2015 |
Zhao H, Ghirlando R, Alfonso C, Arisaka F, Attali I, Bain DL, Bakhtina MM, Becker DF, Bedwell GJ, Bekdemir A, Besong TM, Birck C, Brautigam CA, Brennerman W, Byron O, et al. A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation. Plos One. 10: e0126420. PMID 25997164 DOI: 10.1371/Journal.Pone.0126420 |
0.587 |
|
| 2015 |
Sanyal N, Arentson BW, Luo M, Tanner JJ, Becker DF. First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions. The Journal of Biological Chemistry. 290: 2225-34. PMID 25492892 DOI: 10.1074/Jbc.M114.625483 |
0.42 |
|
| 2015 |
Zhang L, Alfano JR, Becker DF. Proline metabolism increases katG expression and oxidative stress resistance in Escherichia coli. Journal of Bacteriology. 197: 431-40. PMID 25384482 DOI: 10.1128/Jb.02282-14 |
0.357 |
|
| 2014 |
Spencer AL, Bagai I, Becker DF, Zuiderweg ER, Ragsdale SW. Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase. The Journal of Biological Chemistry. 289: 29836-58. PMID 25196843 DOI: 10.1074/Jbc.M114.582783 |
0.766 |
|
| 2014 |
Kang M, Duncan GA, Kuszynski C, Oyler G, Zheng J, Becker DF, Van Etten JL. Chlorovirus PBCV-1 encodes an active copper-zinc superoxide dismutase. Journal of Virology. 88: 12541-50. PMID 25142578 DOI: 10.1128/Jvi.02031-14 |
0.32 |
|
| 2014 |
Luo M, Christgen S, Sanyal N, Arentson BW, Becker DF, Tanner JJ. Evidence that the C-terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channeling. Biochemistry. 53: 5661-73. PMID 25137435 DOI: 10.1021/Bi500693A |
0.391 |
|
| 2014 |
Liang X, Dickman MB, Becker DF. Proline biosynthesis is required for endoplasmic reticulum stress tolerance in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 289: 27794-806. PMID 25112878 DOI: 10.1074/Jbc.M114.562827 |
0.317 |
|
| 2014 |
Arentson BW, Luo M, Pemberton TA, Tanner JJ, Becker DF. Kinetic and structural characterization of tunnel-perturbing mutants in Bradyrhizobium japonicum proline utilization A. Biochemistry. 53: 5150-61. PMID 25046425 DOI: 10.1021/Bi5007404 |
0.319 |
|
| 2014 |
Singh H, Arentson BW, Becker DF, Tanner JJ. Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proceedings of the National Academy of Sciences of the United States of America. 111: 3389-94. PMID 24550478 DOI: 10.1073/Pnas.1321621111 |
0.435 |
|
| 2014 |
Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ. Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. Biochemistry. 53: 1350-9. PMID 24502590 DOI: 10.1021/Bi500048B |
0.466 |
|
| 2014 |
Moxley MA, Sanyal N, Krishnan N, Tanner JJ, Becker DF. Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA). The Journal of Biological Chemistry. 289: 3639-51. PMID 24352662 DOI: 10.1074/Jbc.M113.523704 |
0.433 |
|
| 2013 |
Zhu W, Haile AM, Singh RK, Larson JD, Smithen D, Chan JY, Tanner JJ, Becker DF. Involvement of the β3-α3 loop of the proline dehydrogenase domain in allosteric regulation of membrane association of proline utilization A. Biochemistry. 52: 4482-91. PMID 23713611 DOI: 10.1021/Bi400396G |
0.387 |
|
| 2012 |
Luo M, Arentson BW, Srivastava D, Becker DF, Tanner JJ. Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release. Biochemistry. 51: 10099-108. PMID 23151026 DOI: 10.1021/Bi301312F |
0.433 |
|
| 2012 |
Natarajan SK, Zhu W, Liang X, Zhang L, Demers AJ, Zimmerman MC, Simpson MA, Becker DF. Proline dehydrogenase is essential for proline protection against hydrogen peroxide-induced cell death. Free Radical Biology & Medicine. 53: 1181-91. PMID 22796327 DOI: 10.1016/J.Freeradbiomed.2012.07.002 |
0.357 |
|
| 2012 |
Srivastava D, Singh RK, Moxley MA, Henzl MT, Becker DF, Tanner JJ. The three-dimensional structural basis of type II hyperprolinemia. Journal of Molecular Biology. 420: 176-89. PMID 22516612 DOI: 10.1016/J.Jmb.2012.04.010 |
0.409 |
|
| 2012 |
Arentson BW, Sanyal N, Becker DF. Substrate channeling in proline metabolism. Frontiers in Bioscience (Landmark Edition). 17: 375-88. PMID 22201749 DOI: 10.2741/3932 |
0.33 |
|
| 2012 |
Moxley MA, Becker DF. Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein. Biochemistry. 51: 511-20. PMID 22148640 DOI: 10.1021/Bi201603F |
0.386 |
|
| 2011 |
Moxley MA, Tanner JJ, Becker DF. Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Archives of Biochemistry and Biophysics. 516: 113-20. PMID 22040654 DOI: 10.1016/J.Abb.2011.10.011 |
0.447 |
|
| 2011 |
Singh RK, Larson JD, Zhu W, Rambo RP, Hura GL, Becker DF, Tanner JJ. Small-angle X-ray scattering studies of the oligomeric state and quaternary structure of the trifunctional proline utilization A (PutA) flavoprotein from Escherichia coli. The Journal of Biological Chemistry. 286: 43144-53. PMID 22013066 DOI: 10.1074/Jbc.M111.292474 |
0.369 |
|
| 2011 |
Becker DF, Zhu W, Moxley MA. Flavin redox switching of protein functions. Antioxidants & Redox Signaling. 14: 1079-91. PMID 21028987 DOI: 10.1089/Ars.2010.3417 |
0.336 |
|
| 2010 |
Pierce E, Becker DF, Ragsdale SW. Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate. The Journal of Biological Chemistry. 285: 40515-24. PMID 20956531 DOI: 10.1074/Jbc.M110.155739 |
0.707 |
|
| 2010 |
Wanduragala S, Sanyal N, Liang X, Becker DF. Purification and characterization of Put1p from Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics. 498: 136-42. PMID 20450881 DOI: 10.1016/J.Abb.2010.04.020 |
0.359 |
|
| 2010 |
Srivastava D, Schuermann JP, White TA, Krishnan N, Sanyal N, Hura GL, Tan A, Henzl MT, Becker DF, Tanner JJ. Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum. Proceedings of the National Academy of Sciences of the United States of America. 107: 2878-83. PMID 20133651 DOI: 10.1073/Pnas.0906101107 |
0.385 |
|
| 2010 |
Srivastava D, Zhu W, Johnson WH, Whitman CP, Becker DF, Tanner JJ. The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction. Biochemistry. 49: 560-9. PMID 19994913 DOI: 10.1021/Bi901717S |
0.424 |
|
| 2010 |
Natarajan SK, Becker DF. Importance of Proline Dehydrogenase in Proline Protection against Oxidative Stress Free Radical Biology and Medicine. 49: S191-S192. DOI: 10.1016/J.Freeradbiomed.2010.10.551 |
0.309 |
|
| 2009 |
Singh S, Madzelan P, Stasser J, Weeks CL, Becker D, Spiro TG, Penner-Hahn J, Banerjee R. Modulation of the heme electronic structure and cystathionine β-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation Journal of Inorganic Biochemistry. 103: 689-697. PMID 19232736 DOI: 10.1016/J.Jinorgbio.2009.01.009 |
0.38 |
|
| 2008 |
Zhou Y, Larson JD, Bottoms CA, Arturo EC, Henzl MT, Jenkins JL, Nix JC, Becker DF, Tanner JJ. Structural basis of the transcriptional regulation of the proline utilization regulon by multifunctional PutA. Journal of Molecular Biology. 381: 174-88. PMID 18586269 DOI: 10.1016/J.Jmb.2008.05.084 |
0.338 |
|
| 2008 |
Krishnan N, Doster AR, Duhamel GE, Becker DF. Characterization of a Helicobacter hepaticus putA mutant strain in host colonization and oxidative stress. Infection and Immunity. 76: 3037-44. PMID 18458068 DOI: 10.1128/Iai.01737-07 |
0.315 |
|
| 2008 |
Zhou Y, Zhu W, Bellur PS, Rewinkel D, Becker DF. Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli. Amino Acids. 35: 711-8. PMID 18324349 DOI: 10.1007/S00726-008-0053-6 |
0.378 |
|
| 2008 |
Krishnan N, Dickman MB, Becker DF. Proline modulates the intracellular redox environment and protects mammalian cells against oxidative stress. Free Radical Biology & Medicine. 44: 671-81. PMID 18036351 DOI: 10.1016/J.Freeradbiomed.2007.10.054 |
0.37 |
|
| 2007 |
White TA, Krishnan N, Becker DF, Tanner JJ. Structure and kinetics of monofunctional proline dehydrogenase from Thermus thermophilus. The Journal of Biological Chemistry. 282: 14316-27. PMID 17344208 DOI: 10.1074/Jbc.M700912200 |
0.44 |
|
| 2007 |
Zhang W, Zhang M, Zhu W, Zhou Y, Wanduragala S, Rewinkel D, Tanner JJ, Becker DF. Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA--membrane binding. Biochemistry. 46: 483-91. PMID 17209558 DOI: 10.1021/Bi061935G |
0.381 |
|
| 2006 |
Larson JD, Jenkins JL, Schuermann JP, Zhou Y, Becker DF, Tanner JJ. Crystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition. Protein Science : a Publication of the Protein Society. 15: 2630-41. PMID 17001030 DOI: 10.1110/Ps.062425706 |
0.362 |
|
| 2006 |
Chen C, Wanduragala S, Becker DF, Dickman MB. Tomato QM-like protein protects Saccharomyces cerevisiae cells against oxidative stress by regulating intracellular proline levels. Applied and Environmental Microbiology. 72: 4001-6. PMID 16751508 DOI: 10.1128/Aem.02428-05 |
0.355 |
|
| 2006 |
Krishnan N, Becker DF. Oxygen reactivity of PutA from Helicobacter species and proline-linked oxidative stress Journal of Bacteriology. 188: 1227-1235. PMID 16452403 DOI: 10.1128/Jb.188.4.1227-1235.2006 |
0.387 |
|
| 2006 |
Zhang W, Krishnan N, Becker DF. Kinetic and thermodynamic analysis of Bradyrhizobium japonicum PutA-membrane associations Archives of Biochemistry and Biophysics. 445: 174-183. PMID 16310755 DOI: 10.1016/J.Abb.2005.10.022 |
0.342 |
|
| 2005 |
Zhu W, Becker DF. Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy. Biochemistry. 44: 12297-306. PMID 16156643 DOI: 10.1021/Bi051026B |
0.385 |
|
| 2005 |
Krishnan N, Becker DF. Characterization of a bifunctional PutA homologue from Bradyrhizobium japonicum and identification of an active site residue that modulates proline reduction of the flavin adenine dinucleotide cofactor Biochemistry. 44: 9130-9139. PMID 15966737 DOI: 10.1021/Bi050629K |
0.454 |
|
| 2004 |
Zhang W, Zhou Y, Becker DF. Regulation of PutA-membrane associations by flavin adenine dinucleotide reduction. Biochemistry. 43: 13165-74. PMID 15476410 DOI: 10.1021/Bi048596G |
0.35 |
|
| 2004 |
Baban BA, Vinod MP, Tanner JJ, Becker DF. Probing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA. Biochimica Et Biophysica Acta. 1701: 49-59. PMID 15450175 DOI: 10.1016/J.Bbapap.2004.06.001 |
0.368 |
|
| 2004 |
Zhang M, White TA, Schuermann JP, Baban BA, Becker DF, Tanner JJ. Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. Biochemistry. 43: 12539-48. PMID 15449943 DOI: 10.1021/Bi048737E |
0.446 |
|
| 2004 |
Gu D, Zhou Y, Kallhoff V, Baban B, Tanner JJ, Becker DF. Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme. The Journal of Biological Chemistry. 279: 31171-6. PMID 15155740 DOI: 10.1074/Jbc.M403701200 |
0.333 |
|
| 2003 |
Zhu W, Becker DF. Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli. Biochemistry. 42: 5469-77. PMID 12731889 DOI: 10.1021/Bi0272196 |
0.424 |
|
| 2002 |
Zhu W, Gincherman Y, Docherty P, Spilling CD, Becker DF. Effects of proline analog binding on the spectroscopic and redox properties of PutA. Archives of Biochemistry and Biophysics. 408: 131-6. PMID 12485611 DOI: 10.1016/S0003-9861(02)00535-0 |
0.393 |
|
| 2002 |
Vinod MP, Bellur P, Becker DF. Electrochemical and functional characterization of the proline dehydrogenase domain of the PutA flavoprotein from Escherichia coli. Biochemistry. 41: 6525-32. PMID 12009917 DOI: 10.1021/Bi025706F |
0.374 |
|
| 2001 |
Horng YC, Becker DF, Ragsdale SW. Mechanistic studies of methane biogenesis by methyl-coenzyme M reductase: evidence that coenzyme B participates in cleaving the C-S bond of methyl-coenzyme M. Biochemistry. 40: 12875-85. PMID 11669624 DOI: 10.1021/Bi011196Y |
0.744 |
|
| 2001 |
Pellett JD, Becker DF, Saenger AK, Fuchs JA, Stankovich MT. Role of aromatic stacking interactions in the modulation of the two-electron reduction potentials of flavin and substrate/product in Megasphaera elsdenii short-chain acyl-coenzyme A dehydrogenase. Biochemistry. 40: 7720-8. PMID 11412126 DOI: 10.1021/Bi010206S |
0.726 |
|
| 2001 |
Becker DF, Thomas EA. Redox properties of the PutA protein from Escherichia coli and the influence of the flavin redox state on PutA - DNA interactions Biochemistry. 40: 4714-4721. PMID 11294639 DOI: 10.1021/Bi0019491 |
0.345 |
|
| 2000 |
Telser J, Horng YC, Becker DF, Hoffman BM, Ragsdale SW. On the assignment of nickel oxidation states of the Ox1, Ox2 forms of methyl-coenzyme M reductase Journal of the American Chemical Society. 122: 182-183. DOI: 10.1021/Ja992386N |
0.73 |
|
| 1998 |
Ogrünç M, Becker DF, Ragsdale SW, Sancar A. Nucleotide excision repair in the third kingdom. Journal of Bacteriology. 180: 5796-8. PMID 9791138 DOI: 10.1128/Jb.180.21.5796-5798.1998 |
0.433 |
|
| 1998 |
Becker DF, Leartsakulpanich U, Surerus KK, Ferry JG, Ragsdale SW. Electrochemical and spectroscopic properties of the iron-sulfur flavoprotein from Methanosarcina thermophila Journal of Biological Chemistry. 273: 26462-26469. PMID 9756881 DOI: 10.1074/Jbc.273.41.26462 |
0.529 |
|
| 1998 |
Becker DF, Ragsdale SW. Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide Biochemistry. 37: 2639-2647. PMID 9485414 DOI: 10.1021/Bi972145X |
0.572 |
|
| 1996 |
Dakoji S, Shin I, Becker DF, Stankovich MT, Liu HW. Studies of acyl-CoA dehydrogenase catalyzed allylic isomerization: A one-base or two-base mechanism? Journal of the American Chemical Society. 118: 10971-10979. DOI: 10.1021/Ja962532E |
0.674 |
|
| 1994 |
Becker DF, Fuchs JA, Stankovich MT. Product binding modulates the thermodynamic properties of a Megasphaera elsdenii short-chain acyl-CoA dehydrogenase active-site mutant Biochemistry. 33: 7082-7087. PMID 8003473 DOI: 10.1021/Bi00189A010 |
0.688 |
|
| 1994 |
Shin I, Li D, Becker DF, Stankovich MT, Liu H. Cyclobutaneacetyl-CoA: A Janus-faced substrate for acyl-CoA dehydrogenases Journal of the American Chemical Society. 116: 8843-8844. DOI: 10.1021/Ja00098A068 |
0.604 |
|
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