| Year |
Citation |
Score |
| 2011 |
Majtan T, Frerman FE, Kraus JP. Effect of cobalt on Escherichia coli metabolism and metalloporphyrin formation. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 24: 335-47. PMID 21184140 DOI: 10.1007/s10534-010-9400-7 |
0.302 |
|
| 2010 |
Watmough NJ, Frerman FE. The electron transfer flavoprotein: ubiquinone oxidoreductases. Biochimica Et Biophysica Acta. 1797: 1910-6. PMID 20937244 DOI: 10.1016/j.bbabio.2010.10.007 |
0.435 |
|
| 2009 |
Swanson MA, Kathirvelu V, Majtan T, Frerman FE, Eaton GR, Eaton SS. DEER distance measurement between a spin label and a native FAD semiquinone in electron transfer flavoprotein. Journal of the American Chemical Society. 131: 15978-9. PMID 19886689 DOI: 10.1021/Ja9059816 |
0.306 |
|
| 2008 |
Swanson MA, Usselman RJ, Frerman FE, Eaton GR, Eaton SS. The iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase is the electron acceptor for electron transfer flavoprotein. Biochemistry. 47: 8894-901. PMID 18672901 DOI: 10.1021/Bi800507P |
0.319 |
|
| 2007 |
Rao KS, Fu Z, Albro M, Narayanan B, Baddam S, Lee HJ, Kim JJ, Frerman FE. The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate. Biochemistry. 46: 14468-77. PMID 18020372 DOI: 10.1021/bi7009597 |
0.326 |
|
| 2006 |
Rao KS, Albro M, Dwyer TM, Frerman FE. Kinetic mechanism of glutaryl-CoA dehydrogenase. Biochemistry. 45: 15853-61. PMID 17176108 DOI: 10.1021/bi0609016 |
0.318 |
|
| 2006 |
Zhang J, Frerman FE, Kim JJ. Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. Proceedings of the National Academy of Sciences of the United States of America. 103: 16212-7. PMID 17050691 DOI: 10.1073/Pnas.0604567103 |
0.338 |
|
| 2005 |
Rao KS, Albro M, Zirrolli JA, Vander Velde D, Jones DN, Frerman FE. Protonation of crotonyl-CoA dienolate by human glutaryl-CoA dehydrogenase occurs by solvent-derived protons. Biochemistry. 44: 13932-40. PMID 16229482 DOI: 10.1021/bi050525+ |
0.323 |
|
| 2004 |
Fu Z, Wang M, Paschke R, Rao KS, Frerman FE, Kim JJ. Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochemistry. 43: 9674-84. PMID 15274622 DOI: 10.1021/Bi049290C |
0.342 |
|
| 2004 |
Simkovic M, Frerman FE. Alternative quinone substrates and inhibitors of human electron-transfer flavoprotein-ubiquinone oxidoreductase. The Biochemical Journal. 378: 633-40. PMID 14640977 DOI: 10.1042/BJ20031272 |
0.391 |
|
| 2003 |
Rao KS, Albro M, Vockley J, Frerman FE. Mechanism-based inactivation of human glutaryl-CoA dehydrogenase by 2-pentynoyl-CoA: rationale for enhanced reactivity. The Journal of Biological Chemistry. 278: 26342-50. PMID 12716879 DOI: 10.1074/Jbc.M210781200 |
0.311 |
|
| 2002 |
Simkovic M, Degala GD, Eaton SS, Frerman FE. Expression of human electron transfer flavoprotein-ubiquinone oxidoreductase from a baculovirus vector: kinetic and spectral characterization of the human protein. The Biochemical Journal. 364: 659-67. PMID 12049629 DOI: 10.1042/Bj20020042 |
0.31 |
|
| 2002 |
Rao KS, Vander Velde D, Dwyer TM, Goodman SI, Frerman FE. Alternate substrates of human glutaryl-CoA dehydrogenase: structure and reactivity of substrates, and identification of a novel 2-enoyl-CoA product. Biochemistry. 41: 1274-84. PMID 11802727 DOI: 10.1021/bi015617n |
0.402 |
|
| 2001 |
Westover JB, Goodman SI, Frerman FE. Binding, hydration, and decarboxylation of the reaction intermediate glutaconyl-coenzyme A by human glutaryl-CoA dehydrogenase. Biochemistry. 40: 14106-14. PMID 11705404 DOI: 10.1021/bi015637p |
0.359 |
|
| 2001 |
Dwyer TM, Rao KS, Westover JB, Kim JJ, Frerman FE. The function of Arg-94 in the oxidation and decarboxylation of glutaryl-CoA by human glutaryl-CoA dehydrogenase. The Journal of Biological Chemistry. 276: 133-8. PMID 11024031 DOI: 10.1074/jbc.M007672200 |
0.324 |
|
| 2000 |
Dwyer TM, Rao KS, Goodman SI, Frerman FE. Proton abstraction reaction, steady-state kinetics, and oxidation-reduction potential of human glutaryl-CoA dehydrogenase. Biochemistry. 39: 11488-99. PMID 10985795 DOI: 10.1021/bi000700g |
0.429 |
|
| 1999 |
Dwyer TM, Zhang L, Muller M, Marrugo F, Frerman F. The functions of the flavin contact residues, αArg249 and βTyr16, in human electron transfer flavoprotein Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1433: 139-152. PMID 10446367 DOI: 10.1016/S0167-4838(99)00139-9 |
0.392 |
|
| 1999 |
Dwyer TM, Mortl S, Kemter K, Bacher A, Fauq A, Frerman FE. The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer. Biochemistry. 38: 9735-45. PMID 10423253 DOI: 10.1021/bi9903906 |
0.332 |
|
| 1997 |
Salazar D, Zhang L, deGala GD, Frerman FE. Expression and characterization of two pathogenic mutations in human electron transfer flavoprotein. The Journal of Biological Chemistry. 272: 26425-33. PMID 9334218 DOI: 10.1074/jbc.272.42.26425 |
0.345 |
|
| 1994 |
Djordjevic S, Dong Y, Paschke R, Frerman FE, Strauss AW, Kim JJ. Identification of the catalytic base in long chain acyl-CoA dehydrogenase. Biochemistry. 33: 4258-64. PMID 8155643 DOI: 10.1021/Bi00180A021 |
0.328 |
|
| 1992 |
Paulsen KE, Orville AM, Frerman FE, Lipscomb JD, Stankovich MT. Redox properties of electron-transfer flavoprotein ubiquinone oxidoreductase as determined by EPR-spectroelectrochemistry. Biochemistry. 31: 11755-61. PMID 1332770 DOI: 10.1021/Bi00162A012 |
0.354 |
|
| 1992 |
Paulsen KE, Orville AM, Frerman FE, Stankovich MT, Lipscomb JD. EPR-spectroelectrochemistry of mammalian electron-transfer flavoprotein-ubiquinone oxidoreductase. Progress in Clinical and Biological Research. 375: 69-73. PMID 1332074 |
0.322 |
|
| 1990 |
Frerman FE, Turnbull D. Interaction of medium chain acyl-CoA dehydrogenase with substrate and electron transfer flavoprotein. Progress in Clinical and Biological Research. 321: 79-89. PMID 2183244 |
0.362 |
|
| 1990 |
Frerman FE. Electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase. Progress in Clinical and Biological Research. 321: 69-77. PMID 2183243 |
0.305 |
|
| 1988 |
Frerman FE. Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase. Biochemical Society Transactions. 16: 416-8. PMID 3053288 |
0.36 |
|
| 1987 |
Frerman FE. Reaction of electron-transfer flavoprotein ubiquinone oxidoreductase with the mitochondrial respiratory chain. Biochimica Et Biophysica Acta. 893: 161-9. PMID 3620453 DOI: 10.1016/0005-2728(87)90035-1 |
0.366 |
|
| 1987 |
Johnson MK, Morningstar JE, Oliver M, Frerman FE. Electron paramagnetic resonance and magnetic circular dichroism studies of electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver. Febs Letters. 226: 129-33. PMID 2826249 DOI: 10.1016/0014-5793(87)80565-3 |
0.33 |
|
| 1986 |
Di Donato S, Frerman FE, Rimoldi M, Rinaldo P, Taroni F, Wiesmann UN. Systemic carnitine deficiency due to lack of electron transfer flavoprotein:ubiquinone oxidoreductase. Neurology. 36: 957-63. PMID 3714057 DOI: 10.1212/Wnl.36.7.957 |
0.319 |
|
| 1985 |
Beckmann JD, Frerman FE. Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties. Biochemistry. 24: 3913-21. PMID 4052375 |
0.7 |
|
| 1985 |
Cuebas D, Beckmann JD, Frerman FE, Schulz H. Mitochondrial metabolism of 3-mercaptopropionic acid. Chemical synthesis of 3-mercaptopropionyl coenzyme A and some of its S-acyl derivatives. The Journal of Biological Chemistry. 260: 7330-6. PMID 3997872 |
0.653 |
|
| 1985 |
Frerman FE, Goodman SI. Fluorometric assay of acyl-CoA dehydrogenases in normal and mutant human fibroblasts. Biochemical Medicine. 33: 38-44. PMID 3994700 DOI: 10.1016/0006-2944(85)90124-3 |
0.323 |
|
| 1985 |
Beckmann JD, Frerman FE. Reaction of electron-transfer flavoprotein with electron-transfer flavoprotein-ubiquinone oxidoreductase. Biochemistry. 24: 3922-5. PMID 2996585 |
0.688 |
|
| 1984 |
Goodman SI, Frerman FE. Glutaric acidaemia type II (multiple acyl-CoA dehydrogenation deficiency). Journal of Inherited Metabolic Disease. 7: 33-7. PMID 6434842 DOI: 10.1007/Bf03047371 |
0.436 |
|
| 1983 |
Schmidt J, Beckmann J, Frerman F, McFarland JT. Resonance Raman studies of ETF dehydrogenase (an iron sulfur flavoprotein) Biochemical and Biophysical Research Communications. 113: 784-790. PMID 6870891 DOI: 10.1016/0006-291X(83)91068-9 |
0.612 |
|
| 1983 |
Beckmann JD, Frerman FE. The effects of pH, ionic strength, and chemical modifications on the reaction of electron transfer flavoprotein with an acyl coenzyme A dehydrogenase. The Journal of Biological Chemistry. 258: 7563-9. PMID 6863254 |
0.67 |
|
| 1983 |
McKean MC, Beckmann JD, Frerman FE. Subunit structure of electron transfer flavoprotein. The Journal of Biological Chemistry. 258: 1866-70. PMID 6822538 |
0.654 |
|
| 1983 |
Coudron PE, Frerman FE, Schowalter DB. Chemical and catalytic properties of the peroxisomal acyl-coenzyme A oxidase from Candida tropicalis. Archives of Biochemistry and Biophysics. 226: 324-36. PMID 6639056 DOI: 10.1016/0003-9861(83)90299-0 |
0.468 |
|
| 1983 |
Frerman FE, Sabran JL, Taylor JL, Grossberg SE. Leucine catabolism during the differentiation of 3T3-L1 cells. Expression of a mitochondrial enzyme system. The Journal of Biological Chemistry. 258: 7087-93. PMID 6304077 |
0.3 |
|
| 1982 |
Coudron P, Frerman F. CHEMICAL AND CATALYTIC PROPERTIES OF AN ACYL-CoA OXIDASE FROM CANDIDA TROPICALIS Annals of the New York Academy of Sciences. 386: 397-400. DOI: 10.1111/J.1749-6632.1982.Tb21432.X |
0.358 |
|
| 1981 |
Beckmann JD, Frerman FE, McKean MC. Inhibition of general acyl CoA dehydrogenase by electron transfer flavoprotein semiquinone. Biochemical and Biophysical Research Communications. 102: 1290-4. PMID 7317051 DOI: 10.1016/S0006-291X(81)80151-9 |
0.69 |
|
| 1980 |
Frerman FE, Miziorko HM, Beckmann JD. Enzyme-activated inhibitors, alternate substrates, and a dead end inhibitor of the general acyl-CoA dehydrogenase. The Journal of Biological Chemistry. 255: 11192-8. PMID 7440536 |
0.661 |
|
| 1980 |
Auer HE, Frerman FE. Circular dichroism studies of acyl-CoA dehydrogenase and electron transfer flavoprotein. The Journal of Biological Chemistry. 255: 8157-63. PMID 7410355 |
0.383 |
|
| 1980 |
Frerman FE, Kim JJ, Huhta K, McKean MC. Properties of the general acyl-CoA dehydrogenase from pig liver. The Journal of Biological Chemistry. 255: 2195-8. PMID 7354088 |
0.321 |
|
| 1980 |
O'Brien WJ, Frerman FE. The effect of temperature and membrane lipid composition on the rate of beta-oxidation by Escherichia coli. Biochimica Et Biophysica Acta. 617: 20-7. PMID 6986174 DOI: 10.1016/0005-2760(80)90220-9 |
0.328 |
|
| 1980 |
Murphy JV, Frerman FE, Hodach A. Characteristics of an acid active thiamine diphosphatase from beef brain. Neurochemical Research. 5: 145-57. PMID 6102742 DOI: 10.1007/Bf00964328 |
0.347 |
|
| 1979 |
Frerman FE, Duncombe GR. Studies on the subunits of Escherichia coli coenzyme A transferase. Reconstitution of an active enzyme. Biochimica Et Biophysica Acta. 580: 289-97. PMID 42442 DOI: 10.1016/0005-2795(79)90141-7 |
0.385 |
|
| 1977 |
O'Brien WJ, Frerman FE. Evidence for a complex of three beta-oxidation enzymes in Escherichia coli: induction and localization. Journal of Bacteriology. 132: 532-40. PMID 334745 |
0.305 |
|
| 1977 |
Sramek SJ, Frerman FE, McCormick DJ, Duncombe GR. Substrate-induced conformational changes and half-the-sites reactivity in the Escherichia coli CoA transferase. Archives of Biochemistry and Biophysics. 181: 525-33. PMID 332081 DOI: 10.1016/0003-9861(77)90259-4 |
0.459 |
|
| 1977 |
Sramek SJ, Frerman FE, Adams MB. Sulfhydryl group reactivity in the Escherichia coli CoA transferase. Archives of Biochemistry and Biophysics. 181: 516-24. PMID 332080 DOI: 10.1016/0003-9861(77)90258-2 |
0.448 |
|
| 1977 |
Frerman FE, Andreone P, Mielke D. Reaction of pyridoxal 5'-phosphate with Escherichia coli CoA transferase: evidence for an essential lysine residue. Archives of Biochemistry and Biophysics. 181: 508-15. PMID 332079 DOI: 10.1016/0003-9861(77)90257-0 |
0.479 |
|
| 1977 |
Sramek SJ, Frerman FE. Steady state kinetic mechanism of the Escherichia coli coenzyme A transferase. Archives of Biochemistry and Biophysics. 181: 178-84. PMID 18103 DOI: 10.1016/0003-9861(77)90496-9 |
0.456 |
|
| 1976 |
Duncombe GR, Frerman FE. Molecular and catalytic properties of the acetoacetyl-coenzyme A thiolase of Escherichia coli. Archives of Biochemistry and Biophysics. 176: 159-70. PMID 9904 DOI: 10.1016/0003-9861(76)90152-1 |
0.47 |
|
| 1975 |
Sramek SJ, Frerman FE. Escherichia coli coenzyme A-transferase: kinetics, catalytic pathway and structure. Archives of Biochemistry and Biophysics. 171: 27-35. PMID 1103741 DOI: 10.1016/0003-9861(75)90003-X |
0.486 |
|
| 1975 |
Sramek SJ, Frerman FE. Purification and properties of Escherichia coli coenzyme A-transferase. Archives of Biochemistry and Biophysics. 171: 14-26. PMID 1103739 DOI: 10.1016/0003-9861(75)90002-8 |
0.468 |
|
| 1973 |
Frerman FE. The role of acetyl coenzyme A: butyrate coenzyme A in the transferase uptake of butyrate by isolated membrane vesicles of Escherichia coli. Archives of Biochemistry and Biophysics. 159: 444-52. PMID 4593815 DOI: 10.1016/0003-9861(73)90472-4 |
0.35 |
|
| 1973 |
Frerman FE, Bennett W. Studies on the uptake of fatty acids by Escherichia coli. Archives of Biochemistry and Biophysics. 159: 434-43. PMID 4593814 DOI: 10.1016/0003-9861(73)90471-2 |
0.375 |
|
| 1973 |
O'Brien WJ, Frerman FE. A mutant of Escherichia coli with altered inducer specificity for the fad regulon. Biochemical and Biophysical Research Communications. 54: 697-703. PMID 4585691 DOI: 10.1016/0006-291X(73)91479-4 |
0.345 |
|
| Show low-probability matches. |