L. Vickery

发表

Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli.

D. Ta, L. Vickery, 1992, The Journal of biological chemistry.

Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations.

L. Vickery, M. Brandt, 1993, The Journal of biological chemistry.

Molecular recognition and electron transfer in mitochondrial steroid hydroxylase systems

L. Vickery, 1997, Steroids.

Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli.

J. Silberg, K. Hoff, L. Vickery, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Adrenodoxin with a COOH-terminal deletion (des 116-128) exhibits enhanced activity.

J. Cupp, L. Vickery, 1989, The Journal of biological chemistry.

Mitogen-activated protein/extracellular signal-regulated kinase kinase 1act/tubulin interaction is an important determinant of mitotic stability in cultured HT1080 human fibrosarcoma cells.

E. Stanbridge, Š. Kaluz, Jia-ning Cao, 2010, Cancer research.

Crystallization and preliminary X‐ray crystallographic properties of Hsc20, a J‐motif co‐chaperone protein from Escherichia coli

J. Cupp-Vickery, L. Vickery, 1997, Protein science : a publication of the Protein Society.

Aromatase cytochrome P-450. Purification and characterization of the enzyme from human placenta

J. Kellis, L. Vickery, 1987, Steroids.

Discriminatory inhibition of adrenocortical 17 alpha-hydroxylase activity by inhibitors of cholesterol side chain cleavage cytochrome P-450.

M. Waterman, L. Vickery, J. Sheets, 1985, Archives of biochemistry and biophysics.

The active site of aromatase cytochrome P-450. Differential effects of cyanide provide evidence for proximity of heme-iron and carbon-19 in the enzyme-substrate complex.

J. Kellis, L. Vickery, 1987, The Journal of biological chemistry.

Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c.

E. Johnson, L. Vickery, G. Schwab, 1988, The Journal of biological chemistry.

Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly.

S. Garland, K. Hoff, V. Culotta, 1999, Journal of molecular biology.

A spectrometer for the measurement of magnetic and natural circular dichroism

J. Sutherland, M. Klein, L. Vickery, 1974 .

1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins.

J. Markley, V. Coghlan, L. Vickery, 1991, Biochemistry.

Biochemisty A gene encoding a DnaK / hsp 79 homolog in Escherichia coli ( chaperone / heat shock cognate protein / ferredoxin operon )

L. Vickery, Brent L. Seaton, 2022 .

Preferential Substrate Binding Orientation by the Molecular Chaperone HscA*

L. Vickery, T. Tapley, Tim L. Tapley, 2004, Journal of Biological Chemistry.

Preliminary crystallographic analysis of the cysteine desulfurase IscS from Escherichia coli.

J. Cupp-Vickery, Hugo D. Urbina, L. Vickery, 2002, Acta crystallographica. Section D, Biological crystallography.

Electronic state of heme in cytochrome oxidase. I. Magnetic circular dichroism of the isolated enzyme and its derivatives.

G. Babcock, G. Palmer, L. Vickery, 1976, The Journal of biological chemistry.

The electronic state of heme in cytochrome oxidase II. Oxidation-reduction potential interactions and heme iron spin state behavior observed in reductive titrations.

G. Babcock, G. Palmer, L. Vickery, 1978, The Journal of biological chemistry.

Identification of free and [Fe2S2]-bound cysteine residues of adrenodoxin.

J. Cupp, L. Vickery, 1988, The Journal of biological chemistry.

A model for cytochrome oxidase.

G. Babcock, G. Palmer, L. Vickery, 1976, Proceedings of the National Academy of Sciences of the United States of America.

Preliminary crystallographic data for a basic copper-containing protein from cucumber seedlings.

J. Ramshaw, P. Colman, J. Guss, 1977, Journal of molecular biology.

Circular dichroism studies of human serum transferrin and chicken ovotransferrin and their copper complexes.

L. Vickery, Y. Tomimatsu, 1972, Biochimica et biophysica acta.

Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange.

S. Iametti, F. Bonomi, D. Ta, 2011, Biochemistry.

Three hydrophobic amino acids in Escherichia coli HscB make the greatest contribution to the stability of the HscB-IscU complex

J. Markley, A. K. Füzéry, D. Ta, 2011, BMC Biochemistry.

Solution Structure of the Iron−Sulfur Cluster Cochaperone HscB and Its Binding Surface for the Iron−Sulfur Assembly Scaffold Protein IscU†‡

Gabriel Cornilescu, J. Markley, M. Tonelli, 2008, Biochemistry.

Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC.

J. Cupp-Vickery, J. C. Peterson, D. Ta, 2004, Journal of molecular biology.

Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System*

K. Hoff, J. Cupp-Vickery, Jill R Cupp-Vickery, 2003, Journal of Biological Chemistry.

Crystal structure of IscS, a cysteine desulfurase from Escherichia coli.

J. Cupp-Vickery, Jill R Cupp-Vickery, Hugo Urbina, 2003, Journal of molecular biology.

Hsc66 Substrate Specificity Is Directed toward a Discrete Region of the Iron-Sulfur Cluster Template Protein IscU*

J. Silberg, K. Hoff, D. Ta, 2002, The Journal of Biological Chemistry.

Transfer of Sulfur from IscS to IscU during Fe/S Cluster Assembly*

Larry E. Vickery, Jonathan J. Silberg, J. Silberg, 2001, The Journal of Biological Chemistry.

MAGNETIC CIRCULAR DICHROISM STUDIES OF LOW-SPIN CYTOCHROMES. TEMPERATURE DEPENDENCE AND EFFECTS OF AXIAL COORDINATION ON THE SPECTRA OF CYTOCHROME C AND CYTOCHROME B5

T. Nozawa, K. Sauer, L. Vickery, 1976 .

Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB.

Jin Hae Kim, John L Markley, W. M. Westler, 2009, Biochemistry.

Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones.

S. Iametti, F. Bonomi, D. Ta, 2008, Biochemistry.

Molecular Chaperones HscA/Ssq1 and HscB/Jac1 and Their Roles in Iron-Sulfur Protein Maturation

J. Cupp-Vickery, L. Vickery, 2007, Critical reviews in biochemistry and molecular biology.

Multiple Turnover Transfer of [2Fe2S] Clusters by the Iron-Sulfur Cluster Assembly Scaffold Proteins IscU and IscA*

S. Iametti, F. Bonomi, D. Ta, 2005, Journal of Biological Chemistry.

Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli

J. Silberg, L E Vickery, J J Silberg, 1997, Protein science : a publication of the Protein Society.

Regulation of the HscA ATPase Reaction Cycle by the Co-chaperone HscB and the Iron-Sulfur Cluster Assembly Protein IscU*

Jonathan J Silberg, J. Silberg, K. Hoff, 2004, Journal of Biological Chemistry.

Suppressors of Superoxide Dismutase (SOD1) Deficiency in Saccharomyces cerevisiae

S. Garland, V. Culotta, Gromoslaw A. Smolen, 1998, The Journal of Biological Chemistry.

X-ray diffraction analysis of a crystal of HscA from Escherichia coli.

J. Cupp-Vickery, P. Aoto, D. Ta, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

The Fe/S Assembly Protein IscU Behaves as a Substrate for the Molecular Chaperone Hsc66 from Escherichia coli *

J. Silberg, K. Hoff, L E Vickery, 2001, The Journal of Biological Chemistry.

Kinetic Characterization of the ATPase Cycle of the Molecular Chaperone Hsc66 from Escherichia coli *

J. Silberg, L. Vickery, 2000, The Journal of Biological Chemistry.

Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli.

J. Silberg, J. Cupp-Vickery, D. Ta, 2004, Journal of molecular biology.

Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation.

T. Nozawa, K. Sauer, L. Vickery, 1976, Journal of the American Chemical Society.

Isolation of Indole-3-ethanol Oxidase from Cucumber Seedlings.

W. K. Purves, L. Vickery, 1972, Plant physiology.

Inhibition of human estrogen synthetase (aromatase) by flavones.

J. Kellis, L. Vickery, 1984, Science.

Amino-steroids as inhibitors and probes of the active site of cytochrome P-450scc. Effects on the enzyme from different sources.

J. Kellis, L. Vickery, J. Sheets, 1984, Journal of steroid biochemistry.

Purification and characterization of human placental aromatase cytochrome P-450.

J. Kellis, L E Vickery, J T Kellis, 1987, The Journal of biological chemistry.

Magnetic circular dichroism studies of low-spin cytochromes. Temperature dependence and effects of axial coordination on the spectra of cytochrome c and cytochrome b5.

T. Nozawa, K. Sauer, L. Vickery, 1976, Journal of the American Chemical Society.

Resonance Raman spectra of methemoglobin derivatives. Selective enhancement of axial ligand vibrations and lack of an effect of inositol hexaphosphate.

S. Asher, K. Sauer, S A Asher, 1977, Biochemistry.

Inhibition of human aromatase by mammalian lignans and isoflavonoid phytoestrogens

H. Adlercreutz, J. Kellis, T. Mäkelä, 1993, The Journal of Steroid Biochemistry and Molecular Biology.

Inhibition of aromatase cytochrome P-450 by 10-oxirane and 10-thiirane substituted androgens. Implications for the structure of the active site.

J. Kellis, W. Childers, L E Vickery, 1987, The Journal of biological chemistry.

The Hsc66-Hsc20 Chaperone System inEscherichia coli: Chaperone Activity and Interactions with the DnaK-DnaJ-GrpE System

J. Silberg, K. Hoff, L. Vickery, 1998, Journal of bacteriology.

Cooperativity and Dimerization of Recombinant Human Estrogen Receptor Hormone-binding Domain*

L. Vickery, M. Brandt, 1997, The Journal of Biological Chemistry.

Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone

J. Gargus, D. Ta, L. Vickery, 2003, Journal of Human Genetics.

Molecular cloning and sequence analysis of human placental ferredoxin.

Y. Z. Zhu, L. Vickery, S. Mittal, 1988, Archives of biochemistry and biophysics.

Purification and characterization of human placental ferredoxin.

V. Coghlan, J. Cupp, L. Vickery, 1988, Archives of biochemistry and biophysics.

Expression of human ferredoxin and assembly of the [2Fe-2S] center in Escherichia coli.

V. Coghlan, L. Vickery, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Expression of human ferredoxin and assembly of the [ 2 Fe2 S ] center in Escherichia coli ( mitochondrial iron-sulfur protein / electron transfer / adrenodoxin )

V. Coghlan, L. Vickery, 2022 .

Effects of aminoglutethimide and its metabolite, N-acetylaminoglutethimide, on bovine adrenocortical and human placental cytochromes P-450scc

L. Vickery, J. Sheets, 1982, Naunyn-Schmiedeberg's Archives of Pharmacology.

Inhibition of estrogen synthetase (aromatase) by 4-cyclohexylaniline.

J. Kellis, L. Vickery, 1984, Endocrinology.

Inhibition of adrenocortical cytochrome P-450scc by (20R)-20-phenyl-5-pregnene-3 beta,20-diol.

J. Kellis, L. Vickery, 1983, The Journal of biological chemistry.

Inhibition of bovine adrenocortical cytochrome P-450scc by 3,3'-dimethoxybenzidine

L. Vickery, J. F. Duval, 1981, Steroids.

3-methoxybenzidine: A potent inhibitor of cholesterol side chain cleavage cytochrome P-450

L. Vickery, J. F. Duval, 1980, Steroids.

Inhibition of Steroidogenesis in Cultured Leydig Tumor Cells by 22-Amino-23,24-Bisnor-5-Cholen-3β-Ol and (20R)20-Phenyl-5-Pregnene-3β,20-Diol

M. Ascoli, L. Vickery, J. Sheets, 1983 .

Transfer of Sulfur from IscS to IscU during Iron-Sulfur Cluster Assembly

J. Silberg, K. Hoff, Hugo D. Urbina, 2001 .

Modification of hemoglobin A with dimethyl adipimidate. Contribution of individual reacted subunits to changes in oxygen affinity.

B. Lubin, W. Mentzer, L. Vickery, 1979, Biochimica et biophysica acta.

Substitutions in an Active Site Loop of Escherichia coli IscS Result in Specific Defects in Fe-S Cluster and Thionucleoside Biosynthesis in Vivo*

D. Downs, E. Skovran, Hugo D. Urbina, 2004, Journal of Biological Chemistry.

Indole-3-ethanol Oxidase: Kinetics, Inhibition, and Regulation by Auxins.

W. K. Purves, L. Vickery, F. Percival, 1973, Plant physiology.

Enzymic Oxidation of Indole-3-Ethanol

W. K. Purves, L. Vickery, J. Sherwin, 1972 .

6α-Flurotestosterone: a nonaromatizable androgen inhibotor of aromatase cytochrome P450

J. Kellis, L. Vickery, 1990, Steroids.

Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli.

J. Cupp-Vickery, L. Vickery, 2000, Journal of molecular biology.

MAGNETIC CIRCULAR DICHROISM STUDIES ON MICROSOMAL ARYL HYDROCARBON HYDROXYLASE: COMPARISON WITH CYTOCHROME b5 AND CYTOCHROME P-450cam

A. Salmon, K. Sauer, L. Vickery, 1975 .

A gene encoding a DnaK/hsp70 homolog in Escherichia coli.

B. Seaton, L E Vickery, B L Seaton, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Interactive analysis of protein structure using a microcomputer spreadsheet

Larry E. Vickery, L. Vickery, 1987 .

Expression of human ferredoxin in Saccharomyces cerevisiae: mitochondrial import of the protein and assembly of the [2Fe-2S] center.

B. Seaton, L. Vickery, 1992, Archives of biochemistry and biophysics.

Expression and characterization of human mitochondrial ferredoxin reductase in Escherichia coli.

L. Vickery, M. Brandt, 1992, Archives of biochemistry and biophysics.

22-thio-23,24-bisnor-5-cholen-3 beta-ol: an active site-directed inhibitor of cytochrome P450scc.

L. Vickery, J. Singh, 1988, Journal of steroid biochemistry.

Sequence-dependent peptide binding orientation by the molecular chaperone DnaK.

J. Cupp-Vickery, L. Vickery, Tim L. Tapley, 2005, Biochemistry.

Cholesterol Side Chain Cleavage Cytochrome P450 (P450scc)

L. Vickery, 1993 .

Active site-directed inhibition of rabbit cytochrome P-450 1 by amino-substituted steroids.

L. Vickery, J. Singh, G. Schwab, 1986, The Journal of biological chemistry.

Active site-directed inhibitors of cytochrome P-450scc. Structural and mechanistic implications of a side chain-substituted series of amino-steroids.

L. Vickery, J. Sheets, 1983, The Journal of biological chemistry.

Inhibition of aromatase cytochrome P-450 (estrogen synthetase) by derivatives of α-naphthoflavone☆

S. Nesnow, J. Kellis, L. Vickery, 1986 .

Active site-directed inhibitors of steroid hydroxylase cytochromes P450.

L. Vickery, 1991, Methods in enzymology.

C-22-substituted steroid derivatives as substrate analogues and inhibitors of cytochrome P-450scc.

L. Vickery, J. Sheets, 1983, The Journal of biological chemistry.

NMR studies of cytochrome P-450scc. Effects of steroid binding on water proton access to the active site of the ferric enzyme.

L. Vickery, J. Singh, R. Jacobs, 1987, Biochemistry.

Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc.

V. Coghlan, Vincent, L. Vickery, 1991, The Journal of biological chemistry.

A vector for directional cloning and expression of polymerase chain reaction products in Escherichia coli.

L. Vickery, M. Brandt, A. H. Gabrik, 1991, Gene.

Heme c - heme d1 interaction in Pseudomonas cytochrome oxidase (nitrite reductase): a reappraisal of the spectroscopic evidence.

D. Wharton, G. Palmer, L. Vickery, 1978, Biochemical and biophysical research communications.

The nature of the axial ligands of spinach cytochrome.

J. Siedow, L. Vickery, G. Palmer, 1980, Archives of biochemistry and biophysics.

[17] Spin states of heme proteins by magnetic circular dichroism

L. Vickery, 1978 .

Magnetic and natural circular dichroism of metalloporphyrin complexes of human and rabbit hemopexin.

L. Vickery, W. Morgan, 1978, The Journal of biological chemistry.

Inhibition of cholesterol conversion to pregnenolone in submitochondrial particles from bovine adrenal cortex and bovine and human placenta by benzidine derivatives.

L. Vickery, J. Sheets, P. Moberg, 1981, Journal of steroid biochemistry.

Electrostatic interactions stabilizing ferredoxin electron transfer complexes. Disruption by "conservative" mutations.

V. Coghlan, L. Vickery, 1992, The Journal of biological chemistry.

Structural determinants of HscA peptide-binding specificity.

J. Cupp-Vickery, L. Vickery, Tim L. Tapley, 2006, Biochemistry.

Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin.

J. Markley, V. Coghlan, B. Xia, 1995, Biochemistry.