| Year |
Citation |
Score |
| 2011 |
Bonomi F, Iametti S, Morleo A, Ta D, Vickery LE. Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange. Biochemistry. 50: 9641-50. PMID 21977977 DOI: 10.1021/Bi201123Z |
0.437 |
|
| 2011 |
Füzéry AK, Oh JJ, Ta DT, Vickery LE, Markley JL. Three hydrophobic amino acids in Escherichia coli HscB make the greatest contribution to the stability of the HscB-IscU complex. Bmc Biochemistry. 12: 3. PMID 21269500 DOI: 10.1186/1471-2091-12-3 |
0.446 |
|
| 2009 |
Kim JH, Füzéry AK, Tonelli M, Ta DT, Westler WM, Vickery LE, Markley JL. Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB. Biochemistry. 48: 6062-71. PMID 19492851 DOI: 10.1021/Bi9002277 |
0.434 |
|
| 2008 |
Bonomi F, Iametti S, Morleo A, Ta D, Vickery LE. Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones. Biochemistry. 47: 12795-801. PMID 18986169 DOI: 10.1021/Bi801565J |
0.409 |
|
| 2008 |
Füzéry AK, Tonelli M, Ta DT, Cornilescu G, Vickery LE, Markley JL. Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU. Biochemistry. 47: 9394-404. PMID 18702525 DOI: 10.1021/Bi800502R |
0.438 |
|
| 2007 |
Vickery LE, Cupp-Vickery JR. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Critical Reviews in Biochemistry and Molecular Biology. 42: 95-111. PMID 17453917 DOI: 10.1080/10409230701322298 |
0.505 |
|
| 2006 |
Tapley TL, Cupp-Vickery JR, Vickery LE. Structural determinants of HscA peptide-binding specificity. Biochemistry. 45: 8058-66. PMID 16800630 DOI: 10.1021/Bi0606187 |
0.79 |
|
| 2005 |
Aoto PC, Ta DT, Cupp-Vickery JR, Vickery LE. X-ray diffraction analysis of a crystal of HscA from Escherichia coli. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 61: 715-7. PMID 16511138 DOI: 10.1107/S1744309105019251 |
0.419 |
|
| 2005 |
Tapley TL, Cupp-Vickery JR, Vickery LE. Sequence-dependent peptide binding orientation by the molecular chaperone DnaK. Biochemistry. 44: 12307-15. PMID 16156644 DOI: 10.1021/Bi051145R |
0.787 |
|
| 2005 |
Bonomi F, Iametti S, Ta D, Vickery LE. Multiple turnover transfer of [2Fe2S] clusters by the iron-sulfur cluster assembly scaffold proteins IscU and IscA. The Journal of Biological Chemistry. 280: 29513-8. PMID 15964837 DOI: 10.1074/Jbc.M504344200 |
0.392 |
|
| 2004 |
Silberg JJ, Tapley TL, Hoff KG, Vickery LE. Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. The Journal of Biological Chemistry. 279: 53924-31. PMID 15485839 DOI: 10.1074/Jbc.M410117200 |
0.763 |
|
| 2004 |
Cupp-Vickery JR, Peterson JC, Ta DT, Vickery LE. Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. Journal of Molecular Biology. 342: 1265-78. PMID 15351650 DOI: 10.1016/J.Jmb.2004.07.025 |
0.481 |
|
| 2004 |
Tapley TL, Vickery LE. Preferential substrate binding orientation by the molecular chaperone HscA. The Journal of Biological Chemistry. 279: 28435-42. PMID 15100228 DOI: 10.1074/Jbc.M400803200 |
0.803 |
|
| 2004 |
Cupp-Vickery JR, Silberg JJ, Ta DT, Vickery LE. Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli. Journal of Molecular Biology. 338: 127-37. PMID 15050828 DOI: 10.1016/J.Jmb.2004.02.027 |
0.68 |
|
| 2004 |
Lauhon CT, Skovran E, Urbina HD, Downs DM, Vickery LE. Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo. The Journal of Biological Chemistry. 279: 19551-8. PMID 14978044 DOI: 10.1074/Jbc.M401261200 |
0.788 |
|
| 2004 |
Cupp-Vickery JR, Peterson JC, Ta DT, Vickery LE. Corrigendum to “Crystal Structure of the Molecular Chaperone HscA Substrate Binding Domain Complexed with the IscU Recognition Peptide ELPPVKIHC” [J. Mol. Biol. (2004) 342, 1265–1278] Journal of Molecular Biology. 344: 1163-1164. DOI: 10.1016/J.Jmb.2004.09.085 |
0.443 |
|
| 2003 |
Sun G, Gargus JJ, Ta DT, Vickery LE. Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone. Journal of Human Genetics. 48: 415-9. PMID 12938016 DOI: 10.1007/S10038-003-0048-9 |
0.318 |
|
| 2003 |
Hoff KG, Cupp-Vickery JR, Vickery LE. Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system. The Journal of Biological Chemistry. 278: 37582-9. PMID 12871959 DOI: 10.1074/Jbc.M305292200 |
0.74 |
|
| 2003 |
Cupp-Vickery JR, Urbina H, Vickery LE. Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. Journal of Molecular Biology. 330: 1049-59. PMID 12860127 DOI: 10.1016/S0022-2836(03)00690-9 |
0.762 |
|
| 2002 |
Urbina HD, Cupp-Vickery JR, Vickery LE. Preliminary crystallographic analysis of the cysteine desulfurase IscS from Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography. 58: 1224-5. PMID 12077450 DOI: 10.1107/S0907444902007370 |
0.745 |
|
| 2002 |
Hoff KG, Ta DT, Tapley TL, Silberg JJ, Vickery LE. Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU. The Journal of Biological Chemistry. 277: 27353-9. PMID 11994302 DOI: 10.1074/Jbc.M202814200 |
0.782 |
|
| 2001 |
Urbina HD, Silberg JJ, Hoff KG, Vickery LE. Transfer of sulfur from IscS to IscU during Fe/S cluster assembly. The Journal of Biological Chemistry. 276: 44521-6. PMID 11577100 DOI: 10.1074/Jbc.M106907200 |
0.768 |
|
| 2001 |
Silberg JJ, Hoff KG, Tapley TL, Vickery LE. The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli. The Journal of Biological Chemistry. 276: 1696-700. PMID 11053447 DOI: 10.1074/Jbc.M009542200 |
0.783 |
|
| 2000 |
Cupp-Vickery JR, Vickery LE. Crystal structure of Hsc20, a J-type co-chaperone from Escherichia coli Journal of Molecular Biology. 304: 835-845. PMID 11124030 DOI: 10.1006/Jmbi.2000.4252 |
0.42 |
|
| 2000 |
Hoff KG, Silberg JJ, Vickery LE. Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 97: 7790-5. PMID 10869428 DOI: 10.1073/Pnas.130201997 |
0.785 |
|
| 2000 |
Silberg JJ, Vickery LE. Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli. The Journal of Biological Chemistry. 275: 7779-86. PMID 10713091 DOI: 10.1074/Jbc.275.11.7779 |
0.681 |
|
| 1999 |
Garland SA, Hoff K, Vickery LE, Culotta VC. Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly. Journal of Molecular Biology. 294: 897-907. PMID 10588895 DOI: 10.1006/Jmbi.1999.3294 |
0.679 |
|
| 1998 |
Silberg JJ, Hoff KG, Vickery LE. The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system. Journal of Bacteriology. 180: 6617-24. PMID 9852006 DOI: 10.1128/Jb.180.24.6617-6624.1998 |
0.766 |
|
| 1998 |
Strain J, Lorenz CR, Bode J, Garland S, Smolen GA, Ta DT, Vickery LE, Culotta VC. Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. The Journal of Biological Chemistry. 273: 31138-44. PMID 9813017 DOI: 10.1074/Jbc.273.47.31138 |
0.375 |
|
| 1997 |
Vickery LE, Silberg JJ, Ta DT. Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli. Protein Science : a Publication of the Protein Society. 6: 1047-56. PMID 9144776 DOI: 10.1002/Pro.5560060511 |
0.687 |
|
| 1997 |
Brandt ME, Vickery LE. Cooperativity and dimerization of recombinant human estrogen receptor hormone-binding domain Journal of Biological Chemistry. 272: 4843-4849. PMID 9030541 DOI: 10.1074/Jbc.272.8.4843 |
0.607 |
|
| 1997 |
Vickery LE. Molecular recognition and electron transfer in mitochondrial steroid hydroxylase systems Steroids. 62: 124-127. PMID 9029726 DOI: 10.1016/S0039-128X(96)00170-5 |
0.41 |
|
| 1997 |
Silberg J, Hoff K, Vickery LE. HSC66 and HSC20, a New constitutive molecular chaperone system in escherichia coll Faseb Journal. 11: A1042. |
0.575 |
|
| 1995 |
Xia B, Cheng H, Skjeldal L, Coghlan VM, Vickery LE, Markley JL. Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin. Biochemistry. 34: 180-7. PMID 7819194 DOI: 10.1021/Bi00001A022 |
0.388 |
|
| 1994 |
Seaton BL, Vickery LE. A gene encoding a DnaK/hsp70 homolog in Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 91: 2066-2070. PMID 8134349 DOI: 10.1073/Pnas.91.6.2066 |
0.338 |
|
| 1993 |
Brandt ME, Vickery LE. Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations Journal of Biological Chemistry. 268: 17126-17130. PMID 8349601 |
0.349 |
|
| 1992 |
Brandt ME, Vickery LE. Expression and characterization of human mitochondrial ferredoxin reductase in Escherichia coli Archives of Biochemistry and Biophysics. 294: 735-740. PMID 1567230 DOI: 10.1016/0003-9861(92)90749-M |
0.595 |
|
| 1992 |
Seaton BL, Vickery LE. Expression of human ferredoxin in Saccharomyces cerevisiae: Mitochondrial import of the protein and assembly of the [2Fe-2S] center Archives of Biochemistry and Biophysics. 294: 603-608. PMID 1314545 DOI: 10.1016/0003-9861(92)90731-B |
0.379 |
|
| 1991 |
Brandt ME, Gabrik AH, Vickery LE. A vector for directional cloning and expression of polymerase chain reaction products in Escherichia coli Gene. 97: 113-117. PMID 1995421 DOI: 10.1016/0378-1119(91)90017-6 |
0.558 |
|
| 1991 |
Coghlan VM, Vickery LE. Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc Journal of Biological Chemistry. 266: 18606-18612. PMID 1917982 |
0.313 |
|
| 1991 |
Skjeldal L, Markley JL, Coghlan VM, Vickery LE. 1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins Biochemistry®. 30: 9078-9083. PMID 1909889 DOI: 10.1021/Bi00101A024 |
0.318 |
|
| 1990 |
Kellis JT, Vickery LE. 6α-Flurotestosterone: a nonaromatizable androgen inhibotor of aromatase cytochrome P450 Steroids. 55: 242-246. PMID 2360221 DOI: 10.1016/0039-128X(90)90023-5 |
0.309 |
|
| 1989 |
Coghlan VM, Vickery LE. Expression of human ferredoxin and assembly of the [2Fe-2S] center in Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 86: 835-839. PMID 2644647 DOI: 10.1073/Pnas.86.3.835 |
0.39 |
|
| 1988 |
Coghlan VM, Cupp JR, Vickery LE. Purification and characterization of human placental ferredoxin Archives of Biochemistry and Biophysics. 264: 376-382. PMID 3401007 DOI: 10.1016/0003-9861(88)90302-5 |
0.356 |
|
| 1988 |
Vickery LE, Singh J. 22-Thio-23,24-bisnor-5-cholen-3β-OL: An active site-directed inhibitor of cytochrome P450scc Journal of Steroid Biochemistry. 29: 539-543. PMID 3379962 DOI: 10.1016/0022-4731(88)90190-2 |
0.431 |
|
| 1988 |
Mittal S, Zhu YZ, Vickery LE. Molecular cloning and sequence analysis of human placental ferredoxin Archives of Biochemistry and Biophysics. 264: 383-391. PMID 2969697 DOI: 10.1016/0003-9861(88)90303-7 |
0.306 |
|
| 1987 |
Jacobs RE, Singh J, Vickery LE. NMR studies of cytochrome P-450scc. Effects of steroid binding on water proton access to the active site of the ferric enzyme. Biochemistry. 26: 4541-5. PMID 3663605 DOI: 10.1021/Bi00388A056 |
0.386 |
|
| 1987 |
Vickery LE, Kellis JT. Aromatase cytochrome P-450. Purification and characterization of the enzyme from human placenta Steroids. 50: 29-36. PMID 3504064 DOI: 10.1016/0039-128X(83)90059-4 |
0.304 |
|
| 1987 |
Vickery LE. Interactive analysis of protein structure using a microcomputer spreadsheet Trends in Biochemical Sciences. 12: 37-39. DOI: 10.1016/0968-0004(87)90021-1 |
0.387 |
|
| 1986 |
Kellis JT, Nesnow S, Vickery LE. Inhibition of aromatase cytochrome P-450 (estrogen synthetase) by derivatives of α-naphthoflavone Biochemical Pharmacology. 35: 2887-2891. PMID 3741479 DOI: 10.1016/0006-2952(86)90481-8 |
0.348 |
|
| 1985 |
Sheets JJ, Zuber MX, McCarthy JL, Vickery LE, Waterman MR. Discriminatory inhibition of adrenocortical 17α-hydroxylase activity by inhibitors of cholesterol side chain cleavage cytochrome P-450 Archives of Biochemistry and Biophysics. 242: 297-305. PMID 3876807 DOI: 10.1016/0003-9861(85)90505-3 |
0.328 |
|
| 1984 |
Kellis JT, Vickery LE. Inhibition of estrogen synthetase (aromatase) by 4-cyclohexylaniline Endocrinology. 114: 2128-2137. PMID 6723577 DOI: 10.1210/Endo-114-6-2128 |
0.336 |
|
| 1984 |
Kellis JT, Sheets JJ, Vickery LE. Amino-steroids as inhibitors and probes of the active site of cytochrome P-450scc. effects on the enzyme from different sources Journal of Steroid Biochemistry. 20: 671-676. PMID 6708544 DOI: 10.1016/0022-4731(84)90141-9 |
0.393 |
|
| 1982 |
Weeks CM, Strong PD, Daux WL, Vickery LE. The molecular structure of (20R)-20-phenyl-5-pregnene-3 beta, 20-diol, an inhibitor of cholesterol conversion to pregnenolone. Steroids. 40: 359-68. PMID 7184208 DOI: 10.1016/0039-128X(82)90047-2 |
0.333 |
|
| 1982 |
Sheets JJ, Vickery LE. Effects of aminoglutethimide and its metabolite, N-acetylaminoglutethimide, on bovine adrenocortical and human placental cytochromes P-450scc Naunyn-Schmiedeberg's Archives of Pharmacology. 321: 70-73. PMID 7144927 DOI: 10.1007/Bf00586352 |
0.329 |
|
| 1982 |
Sheets JJ, Vickery LE. Proximity of the substrate binding site and the heme-iron catalytic site in cytochrome P-450scc Proceedings of the National Academy of Sciences of the United States of America. 79: 5773-5777. PMID 6964388 DOI: 10.1073/Pnas.79.19.5773 |
0.438 |
|
| 1981 |
Duval JF, Vickery LE. Inhibition of bovine adrenocortical cytochrome P-450scc by 3,3'-dimethoxybenzidine Steroids. 37: 91-101. PMID 7222145 DOI: 10.1016/0039-128X(81)90011-8 |
0.315 |
|
| 1978 |
Vickery LE, Palmer G, Wharton DC. Heme c - heme d1 interaction in Pseudomonas cytochrome oxidase (nitrite reductase): A reappraisal of the spectroscopic evidence Biochemical and Biophysical Research Communications. 80: 458-463. PMID 203287 DOI: 10.1016/0006-291X(78)90699-X |
0.341 |
|
| 1973 |
Percival FW, Purves WK, Vickery LE. Indole-3-ethanol Oxidase: Kinetics, Inhibition, and Regulation by Auxins. Plant Physiology. 51: 739-43. PMID 16658401 DOI: 10.1104/Pp.51.4.739 |
0.697 |
|
| 1972 |
Vickery LE, Purves WK. Isolation of Indole-3-ethanol Oxidase from Cucumber Seedlings. Plant Physiology. 49: 716-21. PMID 16658035 DOI: 10.1104/Pp.49.5.716 |
0.663 |
|
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