| Year |
Citation |
Score |
| 2001 |
Mitchell DJ, Nikolic D, Rivera E, Sablin SO, Choi S, van Breemen RB, Singer TP, Silverman RB. Spectrometric evidence for the flavin-1-phenylcyclopropylamine inactivator adduct with monoamine oxidase N. Biochemistry. 40: 5447-56. PMID 11331009 DOI: 10.1021/Bi010388Q |
0.332 |
|
| 1999 |
Schuler F, Yano T, Di Bernardo S, Yagi T, Yankovskaya V, Singer TP, Casida JE. NADH-quinone oxidoreductase: PSST subunit couples electron transfer from iron-sulfur cluster N2 to quinone. Proceedings of the National Academy of Sciences of the United States of America. 96: 4149-53. PMID 10097178 DOI: 10.1073/Pnas.96.7.4149 |
0.406 |
|
| 1998 |
Sablin SO, Yankovskaya V, Bernard S, Cronin CN, Singer TP. Isolation and characterization of an evolutionary precursor of human monoamine oxidases A and B. European Journal of Biochemistry / Febs. 253: 270-9. PMID 9578486 DOI: 10.1046/J.1432-1327.1998.2530270.X |
0.37 |
|
| 1996 |
Sablin SO, Krueger MJ, Yankovskaya VL, Tkachenko SE, Razdolsky AN, Bachurin SO, Ramsay RR, Singer TP. Inhibition of NADH oxidation by 1-methyl-4-phenylpyridinium analogs as the basis for the prediction of the inhibitory potency of novel compounds. Journal of Biochemical Toxicology. 11: 33-43. PMID 8806050 DOI: 10.1002/(SICI)1522-7146(1996)11:1<33::AID-JBT5>3.0.CO;2-W |
0.342 |
|
| 1996 |
Yankovskaya V, Sablin SO, Ramsay RR, Singer TP, Ackrell BA, Cecchini G, Miyoshi H. Inhibitor probes of the quinone binding sites of mammalian complex II and Escherichia coli fumarate reductase. The Journal of Biological Chemistry. 271: 21020-4. PMID 8702865 DOI: 10.1074/jbc.271.35.21020 |
0.404 |
|
| 1995 |
Ramsay RR, Sablin SO, Singer TP. Redox properties of the flavin cofactor of monoamine oxidases A and B and their relationship to the kinetic mechanism. Progress in Brain Research. 106: 33-9. PMID 8584669 DOI: 10.1016/S0079-6123(08)61199-1 |
0.382 |
|
| 1995 |
Singer TP. The colorful past and bright future of monoamine oxidase research. Progress in Brain Research. 106: 1-22. PMID 8584646 DOI: 10.1016/S0079-6123(08)61197-8 |
0.349 |
|
| 1995 |
Murphy MP, Krueger MJ, Sablin SO, Ramsay RR, Singer TP. Inhibition of complex I by hydrophobic analogues of N-methyl-4-phenylpyridinium (MPP+) and the use of an ion-selective electrode to measure their accumulation by mitochondria and electron-transport particles. The Biochemical Journal. 306: 359-65. PMID 7887889 DOI: 10.1042/Bj3060359 |
0.349 |
|
| 1995 |
Krueger MJ, Mazouz F, Ramsay RR, Milcent R, Singer TP. Dramatic species differences in the susceptibility of monoamine oxidase B to a group of powerful inhibitors. Biochemical and Biophysical Research Communications. 206: 556-62. PMID 7826372 DOI: 10.1006/bbrc.1995.1079 |
0.332 |
|
| 1995 |
Singer TP, Ramsay RR, Ackrell BA. Deficiencies of NADH and succinate dehydrogenases in degenerative diseases and myopathies. Biochimica Et Biophysica Acta. 1271: 211-9. PMID 7599211 DOI: 10.1016/0925-4439(95)00030-8 |
0.358 |
|
| 1994 |
Sablin SO, Krueger MJ, Singer TP, Bachurin SO, Khare AB, Efange SM, Tkachenko SE. Interaction of tetrahydrostilbazoles with monoamine oxidase A and B. Journal of Medicinal Chemistry. 37: 151-7. PMID 8289189 DOI: 10.1021/Jm00027A019 |
0.374 |
|
| 1994 |
Sablin SO, Krueger MJ, Bachurin SO, Solyakov LS, Efange SM, Singer TP. Oxidation products arising from the action of monoamine oxidase B on 1-methyl-4-benzyl-1,2,3,6-tetrahydropyridine, a nonneurotoxic analogue of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. Journal of Neurochemistry. 62: 2012-6. PMID 8158148 DOI: 10.1046/j.1471-4159.1994.62052012.x |
0.338 |
|
| 1994 |
Singer TP, Ramsay RR. The reaction sites of rotenone and ubiquinone with mitochondrial NADH dehydrogenase. Biochimica Et Biophysica Acta. 1187: 198-202. PMID 8075112 DOI: 10.1016/0005-2728(94)90110-4 |
0.358 |
|
| 1994 |
Gluck MR, Youngster SK, Ramsay RR, Singer TP, Nicklas WJ. Studies on the characterization of the inhibitory mechanism of 4'-alkylated 1-methyl-4-phenylpyridinium and phenylpyridine analogues in mitochondria and electron transport particles. Journal of Neurochemistry. 63: 655-61. PMID 8035189 DOI: 10.1046/J.1471-4159.1994.63020655.X |
0.345 |
|
| 1993 |
Krueger MJ, Tan AK, Ackrell BA, Singer TP. Is complex II involved in the inhibition of mitochondrial respiration by N-methyl-4-phenylpyridinium cation (MMP+) and N-methyl-beta-carbolines? The Biochemical Journal. 291: 673-6. PMID 8489493 DOI: 10.1042/Bj2910673 |
0.378 |
|
| 1993 |
Efange SM, Michelson RH, Tan AK, Krueger MJ, Singer TP. Molecular size and flexibility as determinants of selectivity in the oxidation of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine analogs by monoamine oxidase A and B. Journal of Medicinal Chemistry. 36: 1278-83. PMID 8487265 DOI: 10.1021/Jm00061A020 |
0.331 |
|
| 1993 |
Krueger MJ, Sablin SO, Ramsay R, Singer TP. Reactivation of NADH dehydrogenase (complex I) inhibited by 1-methyl-4-(4'-alkylphenyl)pyridinium analogues: a clue to the nature of the inhibition site. Journal of Neurochemistry. 61: 1546-8. PMID 8377005 DOI: 10.1111/J.1471-4159.1993.Tb13653.X |
0.358 |
|
| 1993 |
Ramsay RR, Sablin SO, Bachurin SO, Singer TP. Oxidation of tetrahydrostilbazole by monoamine oxidase A demonstrates the effect of alternate pathways in the kinetic mechanism. Biochemistry. 32: 9025-30. PMID 8369275 DOI: 10.1021/bi00086a007 |
0.367 |
|
| 1992 |
Krueger MJ, Efange SM, Michelson RH, Singer TP. Interaction of flexible analogs of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and of N-methyl-4-phenylpyridinium with highly purified monoamine oxidase A and B. Biochemistry. 31: 5611-5. PMID 1610807 DOI: 10.1021/bi00139a026 |
0.359 |
|
| 1992 |
Ramsay RR, Singer TP. Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoreductase by rotenone, piericidin A, and MPP+. Biochemical and Biophysical Research Communications. 189: 47-52. PMID 1333196 DOI: 10.1016/0006-291X(92)91523-S |
0.318 |
|
| 1992 |
Singer TP, Ramsay RR. Chapter 6 NADH-ubiquinone oxidoreductase New Comprehensive Biochemistry. 23: 145-162. DOI: 10.1016/S0167-7306(08)60174-X |
0.422 |
|
| 1991 |
Ramsay RR, Singer TP. The kinetic mechanisms of monoamine oxidases A and B. Biochemical Society Transactions. 19: 219-23. PMID 2037155 DOI: 10.1042/Bst0190219 |
0.394 |
|
| 1991 |
Ramsay RR, Krueger MJ, Youngster SK, Gluck MR, Casida JE, Singer TP. Interaction of 1-methyl-4-phenylpyridinium ion (MPP+) and its analogs with the rotenone/piericidin binding site of NADH dehydrogenase. Journal of Neurochemistry. 56: 1184-90. PMID 2002336 DOI: 10.1111/J.1471-4159.1991.Tb11409.X |
0.357 |
|
| 1991 |
Ramsay RR, Krueger MJ, Youngster SK, Singer TP. Evidence that the inhibition sites of the neurotoxic amine 1-methyl-4-phenylpyridinium (MPP+) and of the respiratory chain inhibitor piericidin A are the same. The Biochemical Journal. 273: 481-4. PMID 1991043 DOI: 10.1042/Bj2730481 |
0.393 |
|
| 1991 |
Tan AK, Weyler W, Salach JI, Singer TP. Differences in substrate specificities of monoamine oxidase A from human liver and placenta. Biochemical and Biophysical Research Communications. 181: 1084-8. PMID 1764060 DOI: 10.1016/0006-291X(91)92048-O |
0.341 |
|
| 1990 |
Krueger MJ, Singer TP, Casida JE, Ramsay RR. Evidence that the blockade of mitochondrial respiration by the neurotoxin 1-methyl-4-phenylpyridinium (MPP+) involves binding at the same site as the respiratory inhibitor, rotenone. Biochemical and Biophysical Research Communications. 169: 123-8. PMID 2350337 DOI: 10.1016/0006-291X(90)91442-U |
0.358 |
|
| 1990 |
Krueger MJ, McKeown K, Ramsay RR, Youngster SK, Singer TP. Mechanism-based inactivation of monoamine oxidases A and B by tetrahydropyridines and dihydropyridines. The Biochemical Journal. 268: 219-24. PMID 2344359 DOI: 10.1042/Bj2680219 |
0.4 |
|
| 1990 |
Singer TP, Ramsay RR. Mechanism of the neurotoxicity of MPTP. An update. Febs Letters. 274: 1-8. PMID 2253761 DOI: 10.1016/0014-5793(90)81315-F |
0.375 |
|
| 1990 |
Jin YZ, Ramsay RR, Youngster SK, Singer TP. A new class of powerful inhibitors of monamine oxidase A. Biochemical and Biophysical Research Communications. 172: 1338-41. PMID 2244915 DOI: 10.1016/0006-291X(90)91596-K |
0.358 |
|
| 1989 |
Booth RG, Trevor A, Singer TP, Castagnoli N. Studies on semirigid tricyclic analogues of the nigrostriatal toxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. Journal of Medicinal Chemistry. 32: 473-7. PMID 2783613 DOI: 10.1021/Jm00122A031 |
0.302 |
|
| 1989 |
Ramsay RR, Youngster SK, Nicklas WJ, McKeown KA, Jin YZ, Heikkila RE, Singer TP. Structural dependence of the inhibition of mitochondrial respiration and of NADH oxidase by 1-methyl-4-phenylpyridinium (MPP+) analogs and their energized accumulation by mitochondria. Proceedings of the National Academy of Sciences of the United States of America. 86: 9168-72. PMID 2594758 DOI: 10.1073/pnas.86.23.9168 |
0.39 |
|
| 1988 |
Trevor AJ, Castagnoli N, Singer TP. The formation of reactive intermediates in the MAO-catalyzed oxidation of the nigrostriatal toxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Toxicology. 49: 513-9. PMID 3287698 DOI: 10.1016/0300-483X(88)90037-6 |
0.355 |
|
| 1988 |
Singer TP, Ramsay RR, McKeown K, Trevor A, Castagnoli NE. Mechanism of the neurotoxicity of 1-methyl-4-phenylpyridinium (MPP+), the toxic bioactivation product of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Toxicology. 49: 17-23. PMID 3287690 DOI: 10.1016/0300-483X(88)90169-2 |
0.345 |
|
| 1987 |
Ramsay RR, Koerber SC, Singer TP. Stopped-flow studies on the mechanism of oxidation of N-methyl-4-phenyltetrahydropyridine by bovine liver monoamine oxidase B. Biochemistry. 26: 3045-50. PMID 3496919 DOI: 10.1021/Bi00385A015 |
0.389 |
|
| 1987 |
Trevor AJ, Castagnoli N, Caldera P, Ramsay RR, Singer TP. Bioactivation of MPTP: reactive metabolites and possible biochemical sequelae. Life Sciences. 40: 713-9. PMID 3492651 DOI: 10.1016/0024-3205(87)90298-0 |
0.396 |
|
| 1987 |
Trevor AJ, Singer TP, Ramsay RR, Castagnoli N. Processing of MPTP by monoamine oxidases: implications for molecular toxicology. Journal of Neural Transmission. Supplementum. 23: 73-89. PMID 3295117 DOI: 10.1007/978-3-7091-8901-6_5 |
0.384 |
|
| 1987 |
Ramsay RR, McKeown KA, Johnson EA, Booth RG, Singer TP. Inhibition of NADH oxidation by pyridine derivatives. Biochemical and Biophysical Research Communications. 146: 53-60. PMID 2886124 DOI: 10.1016/0006-291X(87)90689-9 |
0.389 |
|
| 1987 |
Ramsay RR, Kowal AT, Johnson MK, Salach JI, Singer TP. The inhibition site of MPP+, the neurotoxic bioactivation product of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine is near the Q-binding site of NADH dehydrogenase. Archives of Biochemistry and Biophysics. 259: 645-9. PMID 2827583 DOI: 10.1016/0003-9861(87)90531-5 |
0.381 |
|
| 1987 |
Singer TP, Trevor AJ, Castagnoli N. Biochemistry of the neurotoxic action of MPTP: or how a faulty batch of 'designer drug' led to parkinsonism in drug abusers Trends in Biochemical Sciences. 12: 266-270. DOI: 10.1016/0968-0004(87)90132-0 |
0.303 |
|
| 1986 |
Singer TP, Salach JI, Castagnoli N, Trevor A. Interactions of the neurotoxic amine 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine with monoamine oxidases. The Biochemical Journal. 235: 785-9. PMID 3489461 DOI: 10.1042/bj2350785 |
0.365 |
|
| 1986 |
Ramsay RR, Dadgar J, Trevor A, Singer TP. Energy-driven uptake of N-methyl-4-phenylpyridine by brain mitochondria mediates the neurotoxicity of MPTP. Life Sciences. 39: 581-8. PMID 3488484 DOI: 10.1016/0024-3205(86)90037-8 |
0.332 |
|
| 1986 |
Ramsay RR, Salach JI, Dadgar J, Singer TP. Inhibition of mitochondrial NADH dehydrogenase by pyridine derivatives and its possible relation to experimental and idiopathic parkinsonism. Biochemical and Biophysical Research Communications. 135: 269-75. PMID 3485428 DOI: 10.1016/0006-291X(86)90972-1 |
0.375 |
|
| 1986 |
Shamala N, Lim LW, Mathews FS, McIntire W, Singer TP, Hopper DJ. Structure of an intermolecular electron-transfer complex: p-cresol methylhydroxylase at 6.0-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 83: 4626-30. PMID 3460061 DOI: 10.1073/Pnas.83.13.4626 |
0.325 |
|
| 1986 |
Ramsay RR, Salach JI, Singer TP. Uptake of the neurotoxin 1-methyl-4-phenylpyridine (MPP+) by mitochondria and its relation to the inhibition of the mitochondrial oxidation of NAD+-linked substrates by MPP+. Biochemical and Biophysical Research Communications. 134: 743-8. PMID 2868716 DOI: 10.1016/S0006-291X(86)80483-1 |
0.378 |
|
| 1985 |
Koerber SC, McIntire W, Bohmont C, Singer TP. Resolution of the flavocytochrome p-cresol methylhydroxylase into subunits and reconstitution of the enzyme. Biochemistry. 24: 5276-80. PMID 4074695 DOI: 10.1021/Bi00340A048 |
0.39 |
|
| 1985 |
Koerber SC, Hopper DJ, McIntire WS, Singer TP. Formation and properties of flavoprotein-cytochrome hybrids by recombination of subunits from different species. The Biochemical Journal. 231: 383-7. PMID 4062904 DOI: 10.1042/Bj2310383 |
0.374 |
|
| 1985 |
Singer TP, Salach JI, Crabtree D. Reversible inhibition and mechanism-based irreversible inactivation of monoamine oxidases by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Biochemical and Biophysical Research Communications. 127: 707-12. PMID 3872126 DOI: 10.1016/S0006-291X(85)80219-9 |
0.407 |
|
| 1985 |
Singer TP, Johnson MK. The prosthetic groups of succinate dehydrogenase: 30 years from discovery to identification. Febs Letters. 190: 189-98. PMID 2995133 DOI: 10.1016/0014-5793(85)81282-5 |
0.349 |
|
| 1985 |
McIntire W, Hopper DJ, Singer TP. p-Cresol methylhydroxylase. Assay and general properties. The Biochemical Journal. 228: 325-35. PMID 2990444 DOI: 10.1042/Bj2280325 |
0.405 |
|
| 1984 |
Singer TP, McIntire WS. Covalent attachment of flavin to flavoproteins: occurrence, assay, and synthesis. Methods in Enzymology. 106: 369-78. PMID 6493063 DOI: 10.1016/0076-6879(84)06039-0 |
0.354 |
|
| 1984 |
Salach JI, Singer TP, Castagnoli N, Trevor A. Oxidation of the neurotoxic amine 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) by monoamine oxidases A and B and suicide inactivation of the enzymes by MPTP. Biochemical and Biophysical Research Communications. 125: 831-5. PMID 6335034 DOI: 10.1016/0006-291X(84)90614-4 |
0.38 |
|
| 1984 |
McIntire W, Hopper DJ, Craig JC, Everhart ET, Webster RV, Causer MJ, Singer TP. Stereochemistry of 1-(4'-hydroxyphenyl)ethanol produced by hydroxylation of 4-ethylphenol by p-cresol methylhydroxylase. The Biochemical Journal. 224: 617-21. PMID 6083780 DOI: 10.1042/bj2240617 |
0.349 |
|
| 1982 |
McIntire W, Singer TP. Resolution of p-cresol methylhydroxylase into catalytically active subunits and reconstitution of the flavocytochrome. Febs Letters. 143: 316-8. PMID 7117535 DOI: 10.1016/0014-5793(82)80124-5 |
0.36 |
|
| 1981 |
Ramsay RR, Dreyer JL, Schloss JV, Jackson RH, Coles CJ, Beinert H, Cleland WW, Singer TP. Relationship of the oxidation state of the iron-sulfur cluster of aconitase to activity and substrate binding. Biochemistry. 20: 7476-82. PMID 7326240 DOI: 10.1021/Bi00529A023 |
0.728 |
|
| 1981 |
McIntire W, Edmondson DE, Hopper DJ, Singer TP. 8 alpha-(O-Tyrosyl)flavin adenine dinucleotide, the prosthetic group of bacterial p-cresol methylhydroxylase. Biochemistry. 20: 3068-75. PMID 7248267 DOI: 10.1021/Bi00514A013 |
0.305 |
|
| 1981 |
Ramsay RR, Ackrell BA, Coles CJ, Singer TP, White GA, Thorn GD. Reaction site of carboxanilides and of thenoyltrifluoroacetone in complex II. Proceedings of the National Academy of Sciences of the United States of America. 78: 825-8. PMID 6940149 DOI: 10.1073/pnas.78.2.825 |
0.339 |
|
| 1980 |
Singer TP, Edmondson DE. Structure, properties, and determination of covalently bound flavins. Methods in Enzymology. 66: 253-64. PMID 7374473 DOI: 10.1016/0076-6879(80)66466-0 |
0.307 |
|
| 1980 |
Ghisla S, Kenney WC, Knappe WR, McIntire W, Singer TP. Chemical synthesis and some properties of 6-substituted flavins. Biochemistry. 19: 2537-44. PMID 6249335 DOI: 10.1021/Bi00553A001 |
0.312 |
|
| 1980 |
Oestreicher G, Grossman S, Goldenberg J, Kearny EB, Edmondson DE, Singer TP, Lambooy JP. Succinate dehydrogenease from baker's yeast: Comparative biochemistry and biosynthetic variants containing covalently bound flavin analogues Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 67: 395-402. DOI: 10.1016/0305-0491(80)90327-2 |
0.309 |
|
| 1979 |
Coles CJ, Holm RH, Kurtz DM, Orme-Johnson WH, Rawlings J, Singer TP, Wong GB. Characterization of the iron-sulfur centers in succinate dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 76: 3805-8. PMID 226982 DOI: 10.1073/Pnas.76.8.3805 |
0.3 |
|
| 1979 |
Singer TP. Mitochondrial electron-transport inhibitors. Methods in Enzymology. 55: 454-62. PMID 223000 DOI: 10.1016/0076-6879(79)55059-9 |
0.361 |
|
| 1978 |
Ackrell BA, Kearney EB, Singer TP. Mammalian succinate dehydrogenase. Methods in Enzymology. 53: 466-83. PMID 713851 DOI: 10.1016/S0076-6879(78)53050-4 |
0.425 |
|
| 1978 |
Edmondson DE, Kenney WC, Singer TP. Synthesis and isolation of 8 alpha-substituted flavins and flavin peptides. Methods in Enzymology. 53: 449-65. PMID 713850 DOI: 10.1016/S0076-6879(78)53049-8 |
0.322 |
|
| 1978 |
Singer TP, Edmondson DE. Flavoproteins (overview). Methods in Enzymology. 53: 397-418. PMID 713846 DOI: 10.1016/S0076-6879(78)53045-0 |
0.371 |
|
| 1977 |
Mowery PC, Steenkamp DJ, Ackrell AC, Singer TP, White GA. Inhibition of mammalian succinate dehydrogenase by carboxins. Archives of Biochemistry and Biophysics. 178: 495-506. PMID 319760 DOI: 10.1016/0306-4565(77)90004-3 |
0.424 |
|
| 1977 |
Hill CL, Steenkamp DJ, Holm RH, Singer TP. Identification of the iron-sulfur center in trimethylamine dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 74: 547-51. PMID 265519 DOI: 10.1073/Pnas.74.2.547 |
0.317 |
|
| 1977 |
Beinert H, Ackrell BA, Vinogradov AD, Kearney EB, Singer TP. Interrelations of reconstitution activity, reactions with electron acceptors, and iron-sulfur centers in succinate dehydrogenase. Archives of Biochemistry and Biophysics. 182: 95-106. PMID 196557 DOI: 10.1016/0003-9861(77)90287-9 |
0.408 |
|
| 1977 |
Ackrell BA, Kearney EB, Coles CJ, Singer TP, Beinert H, Wan YP, Folkers K. Kinetics of the reoxidation of succinate dehydrogenase. Archives of Biochemistry and Biophysics. 182: 107-17. PMID 196550 DOI: 10.1016/0003-9861(77)90288-0 |
0.41 |
|
| 1976 |
Steenkamp DJ, Singer TP. On the presence of a novel covalently bound oxidation-reduction cofactor, iron and labile sulfur in trimethylamine dehydrogenase. Biochemical and Biophysical Research Communications. 71: 1289-95. PMID 971314 DOI: 10.1016/0006-291X(76)90794-4 |
0.369 |
|
| 1976 |
Mowery PC, Ackrell BA, Singer TP. Carboxins: powerful selective inhibitors of succinate oxidation in animal tissues. Biochemical and Biophysical Research Communications. 71: 354-61. PMID 962926 DOI: 10.1016/0002-9149(76)90070-9 |
0.354 |
|
| 1976 |
Kenney WC, Edmondson DE, Singer TP, Steenkamp DJ, Schabort JC. Identification and properties of the covalently bound flavin of beta-cyclopiazonate oxidocyclase. Biochemistry. 15: 4931-5. PMID 10963 DOI: 10.1021/Bi00667A028 |
0.351 |
|
| 1976 |
Kenney WC, Edmondson DE, Singer TP. Identification of the covalently bound flavin of L-gulono-gamma-lactone oxidase. Biochemical and Biophysical Research Communications. 71: 1194-200. PMID 9936 DOI: 10.1016/0006-291X(76)90780-4 |
0.336 |
|
| 1976 |
Maycock AL, Abeles RH, Salach JI, Singer TP. The structure of the covalent adduct formed by the interaction of 3-dimethylamino-1-propyne and the flavine of mitochondrial amine oxidase. Biochemistry. 15: 114-25. PMID 2278 DOI: 10.1021/Bi00646A018 |
0.367 |
|
| 1975 |
Beinert H, Ackrell BA, Kearney EB, Singer TP. Iron-sulfur components of succinate dehydrogenase: stoichiometry and kinetic behavior in activated preparations. European Journal of Biochemistry / Febs. 54: 185-94. PMID 168076 DOI: 10.1111/J.1432-1033.1975.Tb04128.X |
0.359 |
|
| 1975 |
Vinogradov AD, Ackrell BA, Singer TP. On the possible interrelations of the reactivity of soluble succinate dehydrogenase with ferricyanide, reconstitution activity, and the Hipip iron sulfur center. Biochemical and Biophysical Research Communications. 67: 803-9. PMID 1026 DOI: 10.1016/0006-291X(75)90884-0 |
0.39 |
|
| 1974 |
Singer TP, Kenney WC. Biochemistry of covalently bound flavins. Vitamins and Hormones. 32: 1-45. PMID 4617395 DOI: 10.1016/S0083-6729(08)60005-9 |
0.396 |
|
| 1974 |
Kenney WC, Edmondson DE, Singer TP. The covalently bound flavin of Chromatium cytochrome c552. 2. Sequence of flavin peptides and flavin-tyrosine interaction. European Journal of Biochemistry / Febs. 48: 449-53. PMID 4448180 DOI: 10.1111/J.1432-1033.1974.Tb03785.X |
0.314 |
|
| 1974 |
Singer TP, Edmondson DE. 8 alpha-substituted flavins of biological importance. Febs Letters. 42: 1-14. PMID 4369457 DOI: 10.1016/0014-5793(74)80266-8 |
0.344 |
|
| 1974 |
Kenney WC, Edmondson DE, Singer TP, Steenkamp DJ, Schabort JC. The covalently bound flavin prosthetic group of beta-cyclopiazonate oxidocyclase. Febs Letters. 41: 111-4. PMID 4369278 DOI: 10.1016/0014-5793(74)80966-X |
0.387 |
|
| 1974 |
Beinert H, Ackrell BAC, Kearney EB, Singer TP. Epr studies on the mechanism of action of succinate dehydrogenase in activated preparations Biochemical and Biophysical Research Communications. 58: 564-572. PMID 4365409 DOI: 10.1016/S0006-291X(74)80457-2 |
0.394 |
|
| 1974 |
Kenney WC, Edmondson DE, Singer TP. A novel form of covalently bound flavin from thiamine dehydrogenase. Biochemical and Biophysical Research Communications. 57: 106-11. PMID 4363999 DOI: 10.1016/S0006-291X(74)80363-3 |
0.336 |
|
| 1974 |
Grossman S, Oestreicher G, Hogue PK, Cobley JG, Singer TP. Microanalytical determination of the activities of phospholipases A, C, and D and of their mixtures. Analytical Biochemistry. 58: 301-9. PMID 4363440 DOI: 10.1016/0003-2697(74)90470-9 |
0.354 |
|
| 1973 |
Oestreicher G, Hogue P, Singer TP. Regulation of Succinate Dehydrogenase in Higher Plants: II. Activation by Substrates, Reduced Coenzyme Q, Nucleotides, and Anions. Plant Physiology. 52: 622-6. PMID 16658618 DOI: 10.1104/Pp.52.6.622 |
0.399 |
|
| 1973 |
Singer TP, Oestreicher G, Hogue P. Regulation of Succinate Dehyrogenase in Higher Plants: I. Some General Characteristics of the Membrane-bound Enzyme. Plant Physiology. 52: 616-21. PMID 16658617 DOI: 10.1104/Pp.52.6.616 |
0.431 |
|
| 1973 |
Grossman S, Cobley J, Hogue PK, Kearney EB, Singer TP. Relation of phospholipase D activity to the decay of succinate dehydrogenase and of covalently bound flavin in yeast cells undergoing glucose repression. Archives of Biochemistry and Biophysics. 158: 744-53. PMID 4592986 DOI: 10.1016/0003-9861(73)90569-9 |
0.357 |
|
| 1973 |
Cobley JG, Grossman S, Beinert H, Singer TP. Catalytic activity and EPR signals of DPNH dehydrogenase in relation to the acquisition and loss of piericidin sensitivity and of coupling site 1. Biochemical and Biophysical Research Communications. 53: 1273-81. PMID 4147886 DOI: 10.1016/0006-291X(73)90603-7 |
0.32 |
|
| 1972 |
Kenney WC, Zakim D, Hogue PK, Singer TP. Multiplicity and origin of isoenzymes of lipoyl dehydrogenase. European Journal of Biochemistry / Febs. 28: 253-60. PMID 4341738 DOI: 10.1111/J.1432-1033.1972.Tb01908.X |
0.3 |
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| 1972 |
Walker WH, Singer TP, Ghisla S, Hemmerich P. Studies on succinate dehydrogenase. 8 -Histidyl-FAD as the active center of succinate dehydrogenase. European Journal of Biochemistry / Febs. 26: 279-89. PMID 4339951 DOI: 10.1111/J.1432-1033.1972.Tb01766.X |
0.33 |
|
| 1972 |
Salach J, Walker WH, Singer TP, Ehrenberg A, Hemmerich P, Ghisla S, Hartmann U. Studies on succinate dehydrogenase. Site of attachment of the covalently-bound flavin to the peptide chain. European Journal of Biochemistry / Febs. 26: 267-78. PMID 4339950 DOI: 10.1111/J.1432-1033.1972.Tb01765.X |
0.302 |
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| 1972 |
Hendriks R, Cronin JR, Walker WH, Singer TP. Properties of the covalently bound flavin of chromatium cytochrome c-552 and its conversion to 8-carboxy-riboflavin. Biochemical and Biophysical Research Communications. 46: 1262-9. PMID 4334973 DOI: 10.1016/S0006-291X(72)80111-6 |
0.358 |
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| 1972 |
Kearney EB, Mayr M, Singer TP. Regulatory properties of succinate dehydrogenase: activation by succinyl CoA, pH, and anions. Biochemical and Biophysical Research Communications. 46: 531-7. PMID 4333420 DOI: 10.1016/S0006-291X(72)80171-2 |
0.328 |
|
| 1971 |
Singer TP, Gutman M, Kearney EB. On the need for regulation of succinate dehydrogenase. Febs Letters. 17: 11-13. PMID 11945983 DOI: 10.1016/0014-5793(71)80550-1 |
0.418 |
|
| 1971 |
Kearney EB, Salach JI, Walker WH, Seng R, Singer TP. Structure of the covalently bound flavin of monoamine oxidase. Biochemical and Biophysical Research Communications. 42: 490-6. PMID 5542899 DOI: 10.1016/0006-291X(71)90397-4 |
0.344 |
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| 1971 |
Walker WH, Kearney EB, Seng R, Singer TP. Sequence and structure of a cysteinyl flavin peptide from monoamine oxidase. Biochemical and Biophysical Research Communications. 44: 287-92. PMID 5159775 DOI: 10.1016/0006-291X(71)90597-3 |
0.311 |
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| 1971 |
Gutman M, Kearney EB, Singer TP. Multiple control mechanisms for succinate dehydrogenase in mitochondria. Biochemical and Biophysical Research Communications. 44: 526-32. PMID 5123196 DOI: 10.1016/S0006-291X(71)80114-6 |
0.364 |
|
| 1971 |
Gutman M, Singer TP. EPR studies on the iron-sulfur centers of DPNH dehydrogenase during the redox cycle of the enzyme. Biochemical and Biophysical Research Communications. 44: 1572-8. PMID 4334336 DOI: 10.1016/S0006-291X(71)80266-8 |
0.339 |
|
| 1971 |
Kearney EB, Salach JI, Walker WH, Seng RL, Kenney W, Zeszotek E, Singer TP. The covalently-bound flavin of hepatic monoamine oxidase. 1. Isolation and sequence of a flavin peptide and evidence for binding at the 8alpha position. European Journal of Biochemistry / Febs. 24: 321-7. PMID 4333601 DOI: 10.1111/J.1432-1033.1971.Tb19689.X |
0.353 |
|
| 1971 |
Gutman M, Kearney EB, Singer TP. Activation of succinate dehydrogenase by electron flux from NADH and its possible regulatory function. Biochemical and Biophysical Research Communications. 42: 1016-23. PMID 4323843 DOI: 10.1016/0006-291X(71)90005-2 |
0.383 |
|
| 1971 |
Singer TP, Salach J, Hemmerich P, Ehrenberg A. [142] Flavin peptides Methods in Enzymology. 18: 416-427. DOI: 10.1016/S0076-6879(71)18099-8 |
0.308 |
|
| 1970 |
Kenney WC, Walker WH, Kearney EB, Zeszotek E, Singer TP. Amino acid sequence at the active center of succinate dehydrogenase. Biochemical and Biophysical Research Communications. 41: 488-91. PMID 5534739 DOI: 10.1016/0006-291X(70)90532-2 |
0.304 |
|
| 1970 |
Gutman M, Mayr M, Oltzik R, Singer TP. Effect of ATP on the redox cycle of respiratory chain-linked DPNH dehydrogenase and the localization of coupling site I. Biochemical and Biophysical Research Communications. 41: 40-4. PMID 4318856 DOI: 10.1016/0006-291X(70)90465-1 |
0.35 |
|
| 1970 |
Gutman M, Mersmann H, Luthy J, Singer TP. Action of sulfhydryl inhibitors on different forms of the respiratory chain-linked reduced nicotinamide-adenine dinucleotide dehydrogenase. Biochemistry. 9: 2678-87. PMID 4317875 DOI: 10.1021/Bi00815A016 |
0.33 |
|
| 1970 |
Gutman M, Singer TP, Beinert H, Casida JE. Reaction sites of rotenone, piericidin A, and amytal in relation to the nonheme iron components of NADH dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 65: 763-70. PMID 4315616 DOI: 10.1073/Pnas.65.3.763 |
0.385 |
|
| 1970 |
Biggs DR, Nakamura H, Kearney EB, Rocca E, Singer TP. Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. XVI. Characteristics of the membrane-bound dehydrogenase in Candida utilis and Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics. 137: 12-29. PMID 4314054 DOI: 10.1016/0003-9861(70)90406-6 |
0.419 |
|
| 1970 |
Kean EA, Gutman M, Singer TP. Rhein, a selective inhibitor of the DPNH-flavin step in mitochondrial electron transport. Biochemical and Biophysical Research Communications. 40: 1507-13. PMID 4104098 DOI: 10.1016/0006-291X(70)90039-2 |
0.432 |
|
| 1969 |
Walker WH, Salach J, Gutman M, Singer TP, Hyde JS, Ehrenberg A. Endor studies on the covalently bound flavin at the active center of succinate dehydrogenase. Febs Letters. 5: 237-240. PMID 11947287 DOI: 10.1016/0014-5793(69)80342-X |
0.363 |
|
| 1968 |
Salach JI, Turini P, Hauber J, Seng R, Tisdale H, Singer TP. Isolation of phospholipase A isoenzymes from Naja naja venom and their action on membrane-bound enzymes. Biochemical and Biophysical Research Communications. 33: 936-41. PMID 5705754 DOI: 10.1016/0006-291X(68)90402-6 |
0.332 |
|
| 1967 |
Hauber J, Singer TP. Studies on succinate dehydrogenase. 14. Intracellular distribution, catalytic properties and regulation of fumarate reductases in yeast. European Journal of Biochemistry / Febs. 3: 107-16. PMID 6079767 DOI: 10.1111/j.1432-1033.1967.tb19503.x |
0.341 |
|
| 1967 |
Salach J, Tisdale HD, Singer TP, Bader P. Inhibitors of NADH-ubiquinone reductase from mitochondria. Biochimica Et Biophysica Acta. 143: 281-4. PMID 4292786 DOI: 10.1016/0005-2728(67)90134-X |
0.333 |
|
| 1967 |
Salach J, Singer TP, Bader P. Conversion of reduced nicotinamide-adenine dinucleotide dehydrogenase into reduced nicotinamide-adenine dinucleotide-ubiquinone reductase. The Biochemical Journal. 104: 22contd-24c. PMID 4292769 DOI: 10.1042/Bj1040022C |
0.367 |
|
| 1966 |
Cremona T, Singer TP. [59] d-α-Hydroxy acid dehydrogenase Methods in Enzymology. 9: 327-332. DOI: 10.1016/0076-6879(66)09066-9 |
0.396 |
|
| 1966 |
Singer TP, Cremona T. [56] d-(-)-Lactate cytochrome c reductase Methods in Enzymology. 9: 302-314. DOI: 10.1016/0076-6879(66)09063-3 |
0.341 |
|
| 1958 |
RENDINA G, SINGER TP. Solubilization and assay of choline dehydrogenase. Biochimica Et Biophysica Acta. 30: 441-2. PMID 13607473 DOI: 10.1016/0006-3002(58)90081-7 |
0.301 |
|
| 1956 |
SINGER TP, MASSEY V, KEARNEY EB. On the reversibility of succinic dehydrogenase. Biochimica Et Biophysica Acta. 19: 200-1. PMID 13304101 DOI: 10.1016/0006-3002(56)90417-6 |
0.368 |
|
| 1956 |
SINGER TP, KEARNEY EB, MASSEY V. Observations on the flavin moiety of succinic dehydrogenase. Archives of Biochemistry and Biophysics. 60: 255-7. PMID 13283607 DOI: 10.1016/0003-9861(56)90415-5 |
0.372 |
|
| 1955 |
Kearney EB, Singer TP, Zastrow N. On the requirement of succinic dehydrogenase for inorganic phosphate Archives of Biochemistry and Biophysics. 55: 579-581. DOI: 10.1016/0003-9861(55)90436-7 |
0.321 |
|
| 1953 |
SINGER TP, KEARNEY B. Studies on coenzyme III. I. L-Cysteinesulfinic dehydrogenase and its prosthetic group. Biochimica Et Biophysica Acta. 11: 290-9. PMID 13081602 DOI: 10.1016/0006-3002(53)90038-9 |
0.364 |
|
| 1953 |
KEARNEY EB, SINGER TP. Enzymic transformations of L-cysteinesulfinic acid. Biochimica Et Biophysica Acta. 11: 276-89. PMID 13081601 DOI: 10.1016/0006-3002(53)90037-7 |
0.367 |
|
| 1953 |
KARNEY E, SINGER TP. The oxidation of cysteinesulfinic and cysteic acids in Proteus vulgaris. Biochimica Et Biophysica Acta. 11: 270-5. PMID 13081600 DOI: 10.1016/0006-3002(53)90036-5 |
0.311 |
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