| Year |
Citation |
Score |
| 2010 |
Reed LJ. Availability of Crystalline DL-agr-Lipoic Acid. Science (New York, N.Y.). 120: 854. PMID 17768989 DOI: 10.1126/Science.120.3125.854 |
0.327 |
|
| 2003 |
Gu Y, Zhou ZH, McCarthy DB, Reed LJ, Stoops JK. 3D electron microscopy reveals the variable deposition and protein dynamics of the peripheral pyruvate dehydrogenase component about the core. Proceedings of the National Academy of Sciences of the United States of America. 100: 7015-20. PMID 12756305 DOI: 10.1073/Pnas.0732060100 |
0.316 |
|
| 2001 |
Reed LJ. A trail of research from lipoic acid to alpha-keto acid dehydrogenase complexes. The Journal of Biological Chemistry. 276: 38329-36. PMID 11477096 DOI: 10.1074/Jbc.R100026200 |
0.369 |
|
| 2001 |
Zhou ZH, Liao W, Cheng RH, Lawson JE, McCarthy DB, Reed LJ, Stoops JK. Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The "breathing" core and its functional relationship to protein dynamics. The Journal of Biological Chemistry. 276: 21704-13. PMID 11285267 DOI: 10.1074/Jbc.M101765200 |
0.317 |
|
| 2000 |
Soo Choi W, Yan J, McCarthy DB, Hee Park S, Reed LJ. One-step purification of the recombinant catalytic subunit of pyruvate dehydrogenase phosphatase. Protein Expression and Purification. 20: 128-31. PMID 11035961 DOI: 10.1006/Prep.2000.1294 |
0.339 |
|
| 2000 |
Knapp JE, Carroll D, Lawson JE, Ernst SR, Reed LJ, Hackert ML. Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase. Protein Science : a Publication of the Protein Society. 9: 37-48. PMID 10739245 DOI: 10.1110/Ps.9.1.37 |
0.337 |
|
| 1998 |
DAS ML, KOIKE M, REED LJ. On the role of thiamine pyrophosphate in oxidative decarboxylation of alpha-keto acids. Proceedings of the National Academy of Sciences of the United States of America. 47: 753-9. PMID 13719842 DOI: 10.1073/Pnas.47.6.753 |
0.322 |
|
| 1998 |
Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. Journal of Molecular Biology. 280: 655-68. PMID 9677295 DOI: 10.1006/Jmbi.1998.1924 |
0.341 |
|
| 1998 |
Toyoda T, Suzuki K, Sekiguchi T, Reed LJ, Takenaka A. Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast. Journal of Biochemistry. 123: 668-74. PMID 9538259 DOI: 10.1093/Oxfordjournals.Jbchem.A021989 |
0.361 |
|
| 1998 |
Reed LJ. From lipoic acid to multi-enzyme complexes. Protein Science : a Publication of the Protein Society. 7: 220-4. PMID 9514279 DOI: 10.1002/Pro.5560070125 |
0.395 |
|
| 1997 |
Lawson JE, Park SH, Mattison AR, Yan J, Reed LJ. Cloning, expression, and properties of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase. The Journal of Biological Chemistry. 272: 31625-9. PMID 9395502 DOI: 10.1074/Jbc.272.50.31625 |
0.342 |
|
| 1997 |
Stoops JK, Cheng RH, Yazdi MA, Maeng CY, Schroeter JP, Klueppelberg U, Kolodziej SJ, Baker TS, Reed LJ. On the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complex. The Journal of Biological Chemistry. 272: 5757-64. PMID 9038189 DOI: 10.1017/S1431927600024892 |
0.325 |
|
| 1996 |
REED LJ, FERNANDEZ-MORAN H, KOIKE M, WILLMS CR. ELECTRON MICROSCOPIC AND BIOCHEMICAL STUDIES OF PYRUVATE DEHYDROGENASE COMPLEX OF ESCHERICHIA COLI. Science (New York, N.Y.). 145: 930-2. PMID 14163814 DOI: 10.1126/Science.145.3635.930 |
0.335 |
|
| 1996 |
Yan J, Lawson JE, Reed LJ. Role of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase. Proceedings of the National Academy of Sciences of the United States of America. 93: 4953-6. PMID 8643510 DOI: 10.1073/Pnas.93.10.4953 |
0.311 |
|
| 1996 |
Maeng CY, Yazdi MA, Reed LJ. Stoichiometry of binding of mature and truncated forms of the dihydrolipoamide dehydrogenase-binding protein to the dihydrolipoamide acetyltransferase core of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae. Biochemistry. 35: 5879-82. PMID 8639549 DOI: 10.1021/Bi9600254 |
0.305 |
|
| 1994 |
Maeng CY, Yazdi MA, Niu XD, Lee HY, Reed LJ. Expression, purification, and characterization of the dihydrolipoamide dehydrogenase-binding protein of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae. Biochemistry. 33: 13801-7. PMID 7947791 DOI: 10.1021/Bi00250A034 |
0.331 |
|
| 1993 |
Lawson JE, Niu XD, Browning KS, Trong HL, Yan J, Reed LJ. Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C. Biochemistry. 32: 8987-93. PMID 8396421 DOI: 10.1021/Bi00086A002 |
0.364 |
|
| 1992 |
Reed LJ, Lawson JE, Niu XD, Yazdi MA, Fussey SP. Biochemical and molecular genetic aspects of eukaryotic pyruvate dehydrogenase multienzyme complexes. Journal of Nutritional Science and Vitaminology. 46-51. PMID 1297788 DOI: 10.3177/Jnsv.38.Special_46 |
0.349 |
|
| 1991 |
Lawson JE, Behal RH, Reed LJ. Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex. Biochemistry. 30: 2834-9. PMID 2007123 DOI: 10.1021/Bi00225A015 |
0.345 |
|
| 1991 |
Lawson JE, Niu XD, Reed LJ. Functional analysis of the domains of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Biochemistry. 30: 11249-54. PMID 1958662 DOI: 10.1021/Bi00111A009 |
0.353 |
|
| 1990 |
Niu XD, Stoops JK, Reed LJ. Overexpression and mutagenesis of the catalytic domain of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Biochemistry. 29: 8614-9. PMID 2271545 DOI: 10.1021/Bi00489A017 |
0.301 |
|
| 1989 |
Hackert ML, Xu WX, Oliver RM, Wall JS, Hainfeld JF, Mullinax TR, Reed LJ. Branched-chain alpha-keto acid dehydrogenase complex from bovine kidney: radial distribution of mass determined from dark-field electron micrographs. Biochemistry. 28: 6816-21. PMID 2819036 DOI: 10.1021/Bi00443A006 |
0.344 |
|
| 1989 |
Behal RH, Browning KS, Reed LJ. Nucleotide and deduced amino acid sequence of the alpha subunit of yeast pyruvate dehydrogenase. Biochemical and Biophysical Research Communications. 164: 941-6. PMID 2684159 DOI: 10.1016/0006-291X(89)91549-0 |
0.342 |
|
| 1989 |
Behal RH, Browning KS, Hall TB, Reed LJ. Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America. 86: 8732-6. PMID 2682658 DOI: 10.1073/Pnas.86.22.8732 |
0.309 |
|
| 1988 |
Browning KS, Uhlinger DJ, Reed LJ. Nucleotide sequence for yeast dihydrolipoamide dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 85: 1831-4. PMID 3279419 DOI: 10.1073/Pnas.85.6.1831 |
0.359 |
|
| 1988 |
Pettit FH, Reed LJ. Branched-chain alpha-keto acid dehydrogenase complex from bovine kidney. Methods in Enzymology. 166: 309-12. PMID 3241565 DOI: 10.1016/S0076-6879(88)66042-3 |
0.375 |
|
| 1988 |
Niu XD, Browning KS, Behal RH, Reed LJ. Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America. 85: 7546-50. PMID 3050999 DOI: 10.1073/Pnas.85.20.7546 |
0.34 |
|
| 1988 |
Damuni Z, Reed LJ. Branched-chain alpha-keto acid dehydrogenase phosphatase and its inhibitor protein from bovine kidney. Methods in Enzymology. 166: 321-9. PMID 2853819 DOI: 10.1016/S0076-6879(88)66044-7 |
0.36 |
|
| 1988 |
Damuni Z, Reed LJ. Purification and properties of a protamine kinase and a type II casein kinase from bovine kidney mitochondria. Archives of Biochemistry and Biophysics. 262: 574-84. PMID 2835010 DOI: 10.1016/0003-9861(88)90408-0 |
0.379 |
|
| 1987 |
Tung HY, Reed LJ. Identification and purification of a cytosolic phosphotyrosyl protein phosphatase from bovine spleen. Analytical Biochemistry. 161: 412-9. PMID 3034101 DOI: 10.1016/0003-2697(87)90469-6 |
0.334 |
|
| 1987 |
Damuni Z, Reed LJ. Purification and properties of the catalytic subunit of the branched-chain alpha-keto acid dehydrogenase phosphatase from bovine kidney mitochondria. The Journal of Biological Chemistry. 262: 5129-32. PMID 3031042 |
0.311 |
|
| 1987 |
Reed LJ, Yeaman SJ. 3 Pyruvate Dehydrogenase Enzymes. 18: 77-95. DOI: 10.1016/S1874-6047(08)60254-1 |
0.391 |
|
| 1986 |
Uhlinger DJ, Yang CY, Reed LJ. Phosphorylation-dephosphorylation of pyruvate dehydrogenase from bakers' yeast. Biochemistry. 25: 5673-7. PMID 3535883 DOI: 10.1021/Bi00367A049 |
0.412 |
|
| 1986 |
Damuni Z, Humphreys JS, Reed LJ. A potent, heat-stable protein inhibitor of [branched-chain alpha-keto acid dehydrogenase]-phosphatase from bovine kidney mitochondria. Proceedings of the National Academy of Sciences of the United States of America. 83: 285-9. PMID 3455764 DOI: 10.1073/Pnas.83.2.285 |
0.349 |
|
| 1985 |
Stepp LR, Reed LJ. Active-site modification of mammalian pyruvate dehydrogenase by pyridoxal 5'-phosphate. Biochemistry. 24: 7187-91. PMID 4084575 DOI: 10.1021/Bi00346A026 |
0.375 |
|
| 1985 |
Reed LJ, Damuni Z, Merryfield ML. Regulation of mammalian pyruvate and branched-chain alpha-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation. Current Topics in Cellular Regulation. 27: 41-9. PMID 3004826 DOI: 10.1016/B978-0-12-152827-0.50011-6 |
0.438 |
|
| 1985 |
Damuni Z, Lim Tung HY, Reed LJ. Specificity of the heat-stable protein inhibitor of the branched-chain alpha-keto acid dehydrogenase phosphatase. Biochemical and Biophysical Research Communications. 133: 878-83. PMID 3002373 DOI: 10.1016/0006-291X(85)91217-3 |
0.335 |
|
| 1985 |
Mullinax TR, Stepp LR, Brown JR, Reed LJ. Synthetic peptide substrates for mammalian pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase. Archives of Biochemistry and Biophysics. 243: 655-9. PMID 3002277 DOI: 10.1016/0003-9861(85)90543-0 |
0.368 |
|
| 1984 |
Damuni Z, Merryfield ML, Humphreys JS, Reed LJ. Purification and properties of branched-chain alpha-keto acid dehydrogenase phosphatase from bovine kidney. Proceedings of the National Academy of Sciences of the United States of America. 81: 4335-8. PMID 6589597 DOI: 10.1073/Pnas.81.14.4335 |
0.382 |
|
| 1984 |
Wu TL, Reed LJ. Subunit binding in the pyruvate dehydrogenase complex from bovine kidney and heart. Biochemistry. 23: 221-6. PMID 6546521 DOI: 10.1021/Bi00297A008 |
0.314 |
|
| 1983 |
Hackert ML, Oliver RM, Reed LJ. Evidence for a multiple random coupling mechanism in the alpha-ketoglutarate dehydrogenase multienzyme complex of Escherichia coli: a computer model analysis. Proceedings of the National Academy of Sciences of the United States of America. 80: 2226-30. PMID 6403946 DOI: 10.1073/Pnas.80.8.2226 |
0.36 |
|
| 1983 |
Pettit FH, Yeaman SJ, Reed LJ. Pyruvate dehydrogenase kinase from bovine kidney. Methods in Enzymology. 99: 331-6. PMID 6358789 DOI: 10.1016/0076-6879(83)99068-7 |
0.382 |
|
| 1983 |
Hackert ML, Oliver RM, Reed LJ. A computer model analysis of the active-site coupling mechanism in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 80: 2907-11. PMID 6344073 DOI: 10.1073/Pnas.80.10.2907 |
0.357 |
|
| 1982 |
Pettit FH, Reed LJ. Pyruvate dehydrogenase complex from bovine kidney and heart. Methods in Enzymology. 89: 376-86. PMID 7144580 DOI: 10.1016/S0076-6879(82)89067-8 |
0.388 |
|
| 1982 |
Pettit FH, Humphreys J, Reed LJ. Regulation of pyruvate dehydrogenase kinase activity by protein thiol-disulfide exchange. Proceedings of the National Academy of Sciences of the United States of America. 79: 3945-8. PMID 6955781 DOI: 10.1073/Pnas.79.13.3945 |
0.387 |
|
| 1982 |
Reed LJ, Oliver RM. Structure-function relationships in pyruvate and alpha-ketoglutarate dehydrogenase complexes. Advances in Experimental Medicine and Biology. 148: 231-41. PMID 6751042 DOI: 10.1007/978-1-4615-9281-5_19 |
0.419 |
|
| 1982 |
Pettit FH, Teague WM, Reed LJ. Pyruvate dehydrogenase phosphatase from bovine heart. Methods in Enzymology. 90: 402-7. PMID 6296618 DOI: 10.1016/S0076-6879(82)90163-X |
0.381 |
|
| 1982 |
Teague WM, Pettit FH, Wu TL, Silberman SR, Reed LJ. Purification and properties of pyruvate dehydrogenase phosphatase from bovine heart and kidney. Biochemistry. 21: 5585-92. PMID 6293549 DOI: 10.1021/Bi00265A031 |
0.326 |
|
| 1981 |
Reed LJ. Regulation of mammalian pyruvate dehydrogenase complex by a phosphorylation-dephosphorylation cycle Current Topics in Cellular Regulation. 18: 95-106. PMID 7273851 DOI: 10.1016/B978-0-12-152818-8.50012-8 |
0.338 |
|
| 1981 |
Stepp LR, Bleile DM, McRorie DK, Pettit FH, Reed LJ. Use of trypsin and lipoamidase to study the role of lipoic acid moieties in the pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli. Biochemistry. 20: 4555-60. PMID 6794598 DOI: 10.1021/Bi00519A007 |
0.334 |
|
| 1980 |
White RH, Bleile DM, Reed LJ. Lipoic acid content of dihydrolipoyl transacylases determined by isotope dilution analysis Biochemical and Biophysical Research Communications. 94: 78-84. PMID 6770865 DOI: 10.1016/S0006-291X(80)80190-2 |
0.389 |
|
| 1979 |
Fuller CC, Reed LJ, Oliver RM, Hackert ML. Crystallization of a dihydrolipoyl transacetylase--dihydrolipoyl dehydrogenase subcomplex and its implications regarding the subunit structure of the pyruvate dehydrogenase complex from Escherichia coli. Biochemical and Biophysical Research Communications. 90: 431-8. PMID 389239 DOI: 10.1016/0006-291X(79)91253-1 |
0.348 |
|
| 1979 |
Bleile D, Munk P, Oliver RM, Reed LJ. Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 76: 4385-4389. PMID 388441 DOI: 10.1073/Pnas.76.9.4385 |
0.314 |
|
| 1978 |
Yeaman SJ, Hutcheson ET, Roche TE, Pettit FH, Brown JR, Reed LJ, Watson DC, Dixon GH. Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart. Biochemistry. 17: 2364-70. PMID 678513 DOI: 10.1021/Bi00605A017 |
0.347 |
|
| 1978 |
Pettit FH, Yeaman SJ, Reed LJ. Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney Proceedings of the National Academy of Sciences of the United States of America. 75: 4881-4885. PMID 283398 DOI: 10.1073/Pnas.75.10.4881 |
0.413 |
|
| 1977 |
Collins JH, Reed LJ. Acyl group and electron pair relay system: a network of interacting lipoyl moieties in the pyruvate and α-ketoglutarate dehydrogenase complexes from Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 74: 4223-4227. PMID 200908 DOI: 10.1073/Pnas.74.10.4223 |
0.365 |
|
| 1977 |
Davis PF, Pettit FH, Reed LJ. Peptides derived from pyruvate dehydrogenase as substrates for pyruvate dehydrogenase kinase and phosphatase. Biochemical and Biophysical Research Communications. 75: 541-9. PMID 193491 DOI: 10.1016/0006-291X(77)91506-6 |
0.339 |
|
| 1977 |
Butler JR, Pettit RH, Davis PF, Reed LJ. Binding of thiamin thiazolone pyrophosphate to mammalian pyruvate dehydrogenase and its effects of kinase and phosphatase activities. Biochemical and Biophysical Research Communications. 74: 1667-74. PMID 191033 DOI: 10.1016/0006-291X(77)90636-2 |
0.363 |
|
| 1975 |
Reed LJ, Pettit FH, Eley MH, Hamilton L, Collins JH, Oliver RM. Reconstitution of the Escherichia coli pyruvate dehydrogenase complex Proceedings of the National Academy of Sciences of the United States of America. 72: 3068-3072. PMID 1103138 DOI: 10.1073/Pnas.72.8.3068 |
0.372 |
|
| 1975 |
Pettit FH, Pelley JW, Reed LJ. Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios Biochemical and Biophysical Research Communications. 65: 575-582. PMID 167775 DOI: 10.1016/S0006-291X(75)80185-9 |
0.358 |
|
| 1974 |
Roche TE, Reed LJ. Monovalent cation requirement for ADP inhibition of pyruvate dehydrogenase kinase Biochemical and Biophysical Research Communications. 59: 1341-1348. PMID 4370205 DOI: 10.1016/0006-291X(74)90461-6 |
0.309 |
|
| 1972 |
Roche TE, Reed LJ. Function of the nonidentical subunits of mammalian pyruvate dehydrogenase Biochemical and Biophysical Research Communications. 48: 840-846. PMID 4564641 DOI: 10.1016/0006-291X(72)90684-5 |
0.375 |
|
| 1972 |
Eley MH, Namihira G, Hamilton L, Munk P, Reed LJ. α-Keto acid dehydrogenase complexes. XVIII. Subunit composition of the Escherichia coli pyruvate dehydrogenase complex Archives of Biochemistry and Biophysics. 152: 655-669. PMID 4564450 DOI: 10.1016/0003-9861(72)90262-7 |
0.377 |
|
| 1972 |
Barrera CR, Namihira G, Hamilton L, Munk P, Eley MH, Linn TC, Reed LJ. α-Keto acid dehydrogenase complexes. XVI. Studies on the subunit structure of the pyruvate dehydrogenase complexes from bovine kidney and heart Archives of Biochemistry and Biophysics. 148: 343-358. PMID 4553418 DOI: 10.1016/0003-9861(72)90152-X |
0.417 |
|
| 1972 |
Linn TC, Pelley JW, Pettit FH, Hucho F, Randall DD, Reed LJ. -Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart. Archives of Biochemistry and Biophysics. 148: 327-42. PMID 4401694 DOI: 10.1016/0003-9861(72)90151-8 |
0.588 |
|
| 1972 |
Pettit FH, Roche TE, Reed LJ. Function of calcium ions in pyruvate dehydrogenase phosphatase activity Biochemical and Biophysical Research Communications. 49: 563-571. PMID 4344895 DOI: 10.1016/0006-291X(72)90448-2 |
0.333 |
|
| 1972 |
Hucho F, Randall DD, Roche TE, Burgett MW, Pelley JW, Reed LJ. -Keto acid dehydrogenase complexes. XVII. Kinetic and regulatory properties of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase from bovine kidney and heart. Archives of Biochemistry and Biophysics. 151: 328-40. PMID 4339797 DOI: 10.1016/0003-9861(72)90504-8 |
0.559 |
|
| 1971 |
Derosier DJ, Oliver RM, Reed LJ. Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex. Proceedings of the National Academy of Sciences of the United States of America. 68: 1135-7. PMID 4942179 DOI: 10.1073/Pnas.68.6.1135 |
0.317 |
|
| 1970 |
Schwartz ER, Reed LJ. Regulation of the activity of the pyruvate dehydrogenase complex of Escherichia coli. Biochemistry. 9: 1434-9. PMID 4907331 DOI: 10.1021/Bi00808A019 |
0.36 |
|
| 1970 |
Reed LJ, Cox DJ. 4 Multienzyme Complexes Enzymes. 1: 213-240. DOI: 10.1016/S1874-6047(08)60167-5 |
0.337 |
|
| 1969 |
Linn TC, Pettit FH, Hucho F, Reed LJ. Alpha-keto acid dehydrogenase complexes. XI. Comparative studies of regulatory properties of the pyruvate dehydrogenase complexes from kidney, heart, and liver mitochondria. Proceedings of the National Academy of Sciences of the United States of America. 64: 227-34. PMID 4312751 DOI: 10.1073/Pnas.64.1.227 |
0.584 |
|
| 1969 |
Linn TC, Pettit FH, Reed LJ. Alpha-keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation Proceedings of the National Academy of Sciences of the United States of America. 62: 234-241. PMID 4306045 DOI: 10.1073/Pnas.62.1.234 |
0.427 |
|
| 1969 |
Reed LJ. Pyruvate Dehydrogenase Complex Current Topics in Cellular Regulation. 1: 233-251. DOI: 10.1016/B978-0-12-152801-0.50014-6 |
0.351 |
|
| 1969 |
Reed LJ, Mukherjee BB. [12] α-ketoglutarate dehydrogenase complex from Escherichia coli Methods in Enzymology. 13: 55-61. DOI: 10.1016/0076-6879(69)13016-5 |
0.391 |
|
| 1968 |
Reed LJ. Oxidation of alpha-keto acids The Journal of Vitaminology. 14: Suppl:77-85. PMID 4877191 DOI: 10.5925/Jnsv1954.14.Supplement_77 |
0.426 |
|
| 1966 |
Ishikawa E, Oliver RM, Reed LJ. Alpha-Keto acid dehydrogenase complexes, V. Macromolecular organization of pyruvate and alpha-ketoglutarate dehydrogenase complexes isolated from beef kidney mitochondria Proceedings of the National Academy of Sciences of the United States of America. 56: 534-541. PMID 5229976 DOI: 10.1073/Pnas.56.2.534 |
0.358 |
|
| 1966 |
Reed LJ, Willms CR. [50] Purification and resolution of the pyruvate dehydrogenase complex (Escherichia coli) Methods in Enzymology. 9: 247-265. DOI: 10.1016/0076-6879(66)09057-8 |
0.386 |
|
| 1962 |
Daigo K, Reed LJ. The Amino Acid Sequence Around the Nϵ-Lipoyllysine Residue in α-Keto Acid Dehydrogenation Complexes Journal of the American Chemical Society. 84: 666-671. DOI: 10.1021/Ja00863A032 |
0.372 |
|
| 1962 |
Reed LJ. Biochemistry of Lipoic Acid Vitamins and Hormones. 20: 1-38. DOI: 10.1016/S0083-6729(08)60714-1 |
0.363 |
|
| 1960 |
Nawa H, Brady WT, Koike M, Reed LJ. Studies on the Nature of Protein-bound Lipoic Acid Journal of the American Chemical Society. 82: 896-903. DOI: 10.1021/Ja01489A033 |
0.319 |
|
| 1959 |
Nawa H, Brady WT, Koike M, Reed LJ. ON THE NATURE OF PROTEIN-BOUND LIPOIC ACID Journal of the American Chemical Society. 81: 2908-2909. DOI: 10.1021/Ja01520A075 |
0.319 |
|
| 1956 |
Thomas RC, Reed LJ. Synthesis of DL-1,2-Dithiolane-3-caproic Acid and DL-1,2-Dithiolane-3-butyric Acid, Homologs of α-Lipoic Acid Journal of the American Chemical Society. 78: 6151-6153. DOI: 10.1021/Ja01604A055 |
0.353 |
|
| 1956 |
Thomas RC, Reed LJ. Synthesis of DL-1,2-Dithiolane-3-butanesulfonamide, an Analog of α-Lipoic Acid Journal of the American Chemical Society. 78: 6150-6151. DOI: 10.1021/Ja01604A054 |
0.345 |
|
| 1955 |
LEACH FR, YASUNOBU K, REED LJ. Lipoic acid activation of the alpha-ketobutyrate oxidation system in cell-free extracts of Streptococcus faecalis. Biochimica Et Biophysica Acta. 18: 297-8. PMID 13276384 DOI: 10.1016/0006-3002(55)90077-9 |
0.611 |
|
| 1955 |
Thomas RC, Reed LJ. Synthesis and Properties of High Specific Activity DL-α-Lipoic Acid-S235 Journal of the American Chemical Society. 77: 5446-5448. DOI: 10.1021/Ja01625A092 |
0.354 |
|
| 1953 |
Hornberger CS, Heitmiller RF, Gunsalus IC, Schnakenberg GHF, Reed LJ. Synthesis of DL-α-Lipoic Acid Journal of the American Chemical Society. 75: 1273-1277. DOI: 10.1021/Ja01102A003 |
0.341 |
|
| 1953 |
Reed LJ, DeBusk BG, Hornberger CS, Gunsalus IC. Interrelationships of Lipoic Acids Journal of the American Chemical Society. 75: 1271-1273. DOI: 10.1021/Ja01102A002 |
0.324 |
|
| 1953 |
Reed LJ, Gunsalus IC, Schnakenberg GHF, Soper QF, Boaz HE, Kern SF, Parke TV. Isolation, Characterization and Structure of α-Lipoic Acid1 Journal of the American Chemical Society. 75: 1267-1270. DOI: 10.1021/Ja01102A001 |
0.318 |
|
| 1952 |
Reed LJ, DeBusk BG. LIPOIC ACID CONJUGASE Journal of the American Chemical Society. 74: 4727-4728. DOI: 10.1021/Ja01138A530 |
0.324 |
|
| 1952 |
Reed LJ, DeBusk BG. LIPOTHIAMIDE PYROPHOSPHATE: COENZYME FOR OXIDATIVE DECARBOXYLATION OF α-KETO ACIDS Journal of the American Chemical Society. 74: 3964-3965. DOI: 10.1021/Ja01135A532 |
0.324 |
|
| 1952 |
Reed LJ, DeBusk BG. LIPOTHIAMIDE AND ITS RELATION TO A THIAMIN COENZYME REQUIRED FOR OXIDATIVE DECARBOXYLATION OF α-KETO ACIDS Journal of the American Chemical Society. 74: 3457-3457. DOI: 10.1021/Ja01133A541 |
0.324 |
|
| 1952 |
Hornberger CS, Heitmiller RF, Gunsalus IC, Schnakenberg GHF, Reed LJ. SYNTHETIC PREPARATION OF LIPOIC ACID Journal of the American Chemical Society. 74: 2382-2382. DOI: 10.1021/Ja01129A511 |
0.347 |
|
| 1951 |
Reed LJ, Debusk BG, Gunsalus IC, Hornberger CS. Crystalline α-lipoic acid: A catalytic agent associated with pyruvate dehydrogenase Science. 114: 93-94. PMID 14854913 DOI: 10.1126/Science.114.2952.93 |
0.338 |
|
| 1951 |
Reed LJ, DeBusk BG, Gunsalus IC, Schnakenberg GHF. CHEMICAL NATURE OF α-LIPOIC ACID Journal of the American Chemical Society. 73: 5920-5920. DOI: 10.1021/Ja01156A567 |
0.312 |
|
| 1950 |
RACHELE JR, REED LJ, KIDWAI AR, FERGER MF, du VIGNEAUD V. Conversion of cystathionine labeled with S35 to cystine in vivo. The Journal of Biological Chemistry. 185: 817-26. PMID 14774428 |
0.422 |
|
| 1949 |
REED LJ, KIDWAI AR, DU VIGNEAUD V. Preparation of the optically active isomers of S-benzylhomocysteine by enzymatic resolution. The Journal of Biological Chemistry. 180: 571-4. PMID 18135790 |
0.446 |
|
| 1947 |
Fuson R, Parham W, Reed L. Additions and Corrections - The Synthesis of 7-Chloro-4-(1-ethyl-4-piperidylamino)-quinoline (SN-13,425). Journal of the American Chemical Society. 69: 3153-3153. DOI: 10.1021/Ja01204A606 |
0.623 |
|
| 1946 |
FUSON RC, PARHAM WE, REED LJ. Alkylation of ethyl malonate with diethoxymethyl acetate. The Journal of Organic Chemistry. 11: 194-8. PMID 21018792 DOI: 10.1021/Jo01172A014 |
0.612 |
|
| 1946 |
FUSON RC, PARHAM WE, REED LJ. The synthesis of 7-chloro-4-(l-ethyl-4-piperidylamino)-quinoline (SN-13,425). Journal of the American Chemical Society. 68: 1239. PMID 20990959 DOI: 10.1021/Ja01211A028 |
0.611 |
|
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