| Year |
Citation |
Score |
| 2003 |
Dunham WR, Sands RH. g-Strain, ENDOR, and structure of active centers of two-iron ferredoxins Biochemical and Biophysical Research Communications. 312: 255-261. PMID 14630052 DOI: 10.1016/J.Bbrc.2003.09.228 |
0.672 |
|
| 1997 |
Hoover DM, Jarrett JT, Sands RH, Dunham WR, Ludwig ML, Matthews RG. Interaction of Escherichia coli cobalamin-dependent methionine synthase and its physiological partner flavodoxin: binding of flavodoxin leads to axial ligand dissociation from the cobalamin cofactor. Biochemistry. 36: 127-38. PMID 8993326 DOI: 10.1021/Bi961693S |
0.611 |
|
| 1996 |
Jarrett JT, Amaratunga M, Drennan CL, Scholten JD, Sands RH, Ludwig ML, Matthews RG. Mutations in the B12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity. Biochemistry. 35: 2464-75. PMID 8652590 DOI: 10.1021/Bi952389M |
0.32 |
|
| 1996 |
Stone JR, Sands RH, Dunham WR, Marletta MA. Spectral and ligand-binding properties of an unusual hemoprotein, the ferric form of soluble guanylate cyclase Biochemistry. 35: 3258-3262. PMID 8605161 DOI: 10.1021/bi952386 |
0.644 |
|
| 1996 |
Filter WF, Sands RH, Dunham WR. An ultra-high-stability Mössbauer spectrometer drive using a type-2 feedback system Nuclear Instruments and Methods in Physics Research, Section B: Beam Interactions With Materials and Atoms. 119: 565-582. DOI: 10.1016/S0168-583X(96)00466-1 |
0.609 |
|
| 1996 |
Moon N, Coffin CT, Steinke DC, Sands RH, Dunham WR. A high-sensitivity Mössbauer spectrometer facilitates the study of iron proteins at natural abundance Nuclear Instruments and Methods in Physics Research, Section B: Beam Interactions With Materials and Atoms. 119: 555-564. DOI: 10.1016/S0168-583X(96)00457-0 |
0.647 |
|
| 1995 |
Stone JR, Sands RH, Dunham WR, Marletta MA. Electron paramagnetic resonance spectral evidence for the formulation of a pentacoordinate nitrosyl-heme complex on soluble guanylate cyclase Biochemical and Biophysical Research Communications. 207: 572-577. PMID 7864845 DOI: 10.1006/Bbrc.1995.1226 |
0.614 |
|
| 1994 |
Kramer JA, Johnson KR, Dunham WR, Sands RH, Funk MO. Position 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3 Biochemistry. 33: 15017-15022. PMID 7999759 DOI: 10.1021/Bi00254A010 |
0.681 |
|
| 1993 |
Dunham WR, Harding LJ, Sands RH. Mossbauer spectroscopy of metalloproteins and the use of Fourier transforms European Journal of Biochemistry. 214: 1-8. PMID 8508782 DOI: 10.1111/J.1432-1033.1993.Tb17889.X |
0.587 |
|
| 1993 |
Hunt J, Massey V, Dunham WR, Sands RH. Redox potentials of milk xanthine dehydrogenase. Room temperature measurement of the FAD and 2Fe/2S center potentials. The Journal of Biological Chemistry. 268: 18685-91. PMID 8395516 |
0.319 |
|
| 1993 |
Carroll RT, Muller J, Grimm J, Dunham WR, Sands RH, Funk MO. Rapid purification of rabbit reticulocyte lipoxygenase for electron paramagnetic spectroscopy characterization of the non-heme iron Lipids. 28: 241-244. PMID 8385258 DOI: 10.1007/Bf02536646 |
0.701 |
|
| 1992 |
Pierik AJ, Hagen WR, Redeker JS, Wolbert RB, Boersma M, Verhagen MF, Grande HJ, Veeger C, Mutsaers PH, Sands RH. Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough). European Journal of Biochemistry / Febs. 209: 63-72. PMID 1396719 DOI: 10.1111/J.1432-1033.1992.Tb17261.X |
0.44 |
|
| 1992 |
Pierik AJ, Hagen WR, Dunham WR, Sands RH. Multi-frequency EPR and high-resolution Mössbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). Characterization of a supercluster and superspin model protein. European Journal of Biochemistry / Febs. 206: 705-19. PMID 1318833 DOI: 10.1111/J.1432-1033.1992.Tb16977.X |
0.497 |
|
| 1992 |
Haddy A, Dunham WR, Sands RH, Aasa R. Multifrequency EPR investigations into the origin of the S2-state signal at g = 4 of the O2-evolving complex Bba - Bioenergetics. 1099: 25-34. PMID 1310873 DOI: 10.1016/0005-2728(92)90183-3 |
0.613 |
|
| 1992 |
Pierik AJ, Hagen WR, Dunham WR, Sands RH. Multi-frequency EPR and high-resolution Mossbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). Characterization of a supercluster and superspin model protein European Journal of Biochemistry. 206: 705-719. DOI: 10.1111/j.1432-1033.1992.tb16977.x |
0.605 |
|
| 1992 |
Larson E, Haddy A, Kirk ML, Sands RH, Hatfield WE, Pecoraro VL. Asymmetric mixed-valent complex {[Mn(2-OH-3,5-Cl2-SALPN)]2(THF)}ClO4 shows a temperature-dependent interconversion between g = 2 multiline and low-field EPR signals Journal of the American Chemical Society. 114: 6263-6265. DOI: 10.1021/Ja00041A065 |
0.308 |
|
| 1991 |
Dunham WR, Hagen WR, Fee JA, Sands RH, Dunbar JB, Humblet C. An investigation of Chromatium vinosum high-potential irondashsulfur protein by EPR and Mossbauer spectroscopy; evidence for a freezing-induced dimerization in NaCl solutions Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1079: 253-262. PMID 1655037 DOI: 10.1016/0167-4838(91)90066-9 |
0.683 |
|
| 1991 |
Finnen DC, Alan Pinkerton A, Dunham WR, Sands RH, Funk MO. Structures aad spectroscopic characteristics of iron(III) diethylenetriaminepentaacetic acid complexes. A non-heme iron(III) complex with relevance to the iron environment in lipoxygenases Inorganic Chemistry. 30: 3960-3964. DOI: 10.1021/Ic00020A034 |
0.673 |
|
| 1990 |
Dunham WR, Carroll RT, Thompson JF, Sands RH, Funk MO. The initial characterization of the iron environment in lipoxygenase by Mössbauer spectroscopy. European Journal of Biochemistry. 190: 611-617. PMID 2164931 DOI: 10.1111/J.1432-1033.1990.Tb15616.X |
0.718 |
|
| 1990 |
Funk MO, Carroll RT, Thompson JF, Sands RH, Dunham WR. Role of iron in lipoxygenase catalysis Journal of the American Chemical Society. 112: 5375-5376. DOI: 10.1021/Ja00169A069 |
0.662 |
|
| 1989 |
Newton WE, Gheller SF, Sands RH, Dunham WR. Mössbauer spectroscopy applied to the oxidized and semi-reduced states of the iron-molybdenum cofactor of nitrogenase Biochemical and Biophysical Research Communications. 162: 882-891. PMID 2757645 DOI: 10.1016/0006-291X(89)92392-9 |
0.679 |
|
| 1989 |
Draheim JE, Carroll RT, McNemar TB, Dunham WR, Sands RH, Funk MO. Lipoxygenase isoenzymes: A spectroscopic and structural characterization of soybean seed enzymes Archives of Biochemistry and Biophysics. 269: 208-218. PMID 2537058 DOI: 10.1016/0003-9861(89)90102-1 |
0.699 |
|
| 1989 |
COUCOUVANIS D, AL-AHMAD S, SALIFOGLOU A, DUNHAM WR, SANDS RH. ChemInform Abstract: A Cubane Cluster with the (MoFe3S4)0 Core and Its Possible Relevance Concerning the Fe3 Centers in Ferredoxins: The (Fe3S4(SEt)3Mo(CO)3)3- Ion. Cheminform. 20. DOI: 10.1002/CHIN.198902246 |
0.587 |
|
| 1988 |
Frasca V, Banerjee RV, Dunham WR, Sands RH, Matthews RG. Cobalamin-dependent methionine synthase from Escherichia coli B: Electron paramagnetic resonance spectra of the inactive form and the active methylated form of the enzyme Biochemistry. 27: 8458-8465. PMID 2853966 DOI: 10.1021/Bi00422A025 |
0.626 |
|
| 1988 |
Day EP, David SS, Peterson J, Dunham WR, Bonvoisin JJ, Sands RH, Que L. Magnetization and electron paramagnetic resonance studies of reduced uteroferrin and its 'EPR-silent' phosphate complex Journal of Biological Chemistry. 263: 15561-15567. PMID 2844817 |
0.345 |
|
| 1988 |
Ghosh DK, Peegel H, Dunham WR, Sands RH, Menon KMJ. Modulation of progesterone synthesis and cytochrome P450 levels in rat luteal cells during human chorionic gonadotropin-induced desensitized state Endocrinology. 123: 514-522. PMID 2838263 |
0.615 |
|
| 1988 |
Coucouvanis D, Al-Ahmad S, Salifoglou A, Dunham WR, Sands RH. A New Cubane Cluster with the[MoFe3S4]0 Core and Possible Relevance to the Fe3-Centers in Ferredoxins. The Synthesis, Structure and Properties of the[Fe3S4(SEt)3Mo(CO)3]3⊖ Anion Angewandte Chemie International Edition in English. 27: 1353-1355. DOI: 10.1002/Anie.198813531 |
0.623 |
|
| 1988 |
Coucouvanis D, Al-Ahmad S, Salifoglou A, Dunham WR, Sands RH. Ein Cubancluster mit dem [MoFe3S4]0-Gerüst und seine mögliche Relevanz im Hinblick auf die Fe3-Zentren in Ferredoxinen: das [Fe3S4(SEt)3Mo(CO)3]3⊖-Ion Angewandte Chemie. 100: 1404-1406. DOI: 10.1002/Ange.19881001022 |
0.332 |
|
| 1987 |
Ghosh DK, Dunham WR, Sands RH, Menon KMJ. Regulation of cholesterol side-chain cleavage enzyme activity by gonadotropin in rat corpus luteum Endocrinology. 121: 21-27. PMID 3036468 |
0.553 |
|
| 1986 |
Stevenson RC, Dunham WR, Sands RH, Singer TP, Beinert H. Studies on the spin-spin interaction between flavin and iron-sulfur cluster in an iron-sulfur flavoprotein. Biochimica Et Biophysica Acta. 869: 81-8. PMID 3002478 DOI: 10.1016/0167-4838(86)90313-4 |
0.682 |
|
| 1986 |
Hearshen DO, Hagen WR, Sands RH, Grande HJ, Crespi HL, Gunsalus IC, Dunham WR. An analysis of g strain in the EPR of two [2Fe2S] ferredoxins. Evidence for a protein rigidity model Journal of Magnetic Resonance (1969). 69: 440-459. DOI: 10.1016/0022-2364(86)90156-3 |
0.684 |
|
| 1985 |
Hagen WR, Hearshen DO, Sands RH, Dunham WR. A statistical theory for powder EPR in distributed systems Journal of Magnetic Resonance (1969). 61: 220-232. DOI: 10.1016/0022-2364(85)90077-0 |
0.561 |
|
| 1984 |
Hagen WR, Dunham WR, Sands RH, Shaw RW, Beinert H. Dual-mode EPR spectrometry of O2-pulsed cytochrome c oxidase. Biochimica Et Biophysica Acta. 765: 399-402. PMID 6329275 DOI: 10.1016/0005-2728(84)90181-6 |
0.581 |
|
| 1983 |
Grande HJ, Dunham WR, Averill B, Van Dijk C, Sands RH. Electron paramagnetic resonance and other properties of hydrogenases isolated from Desulfovibrio vulgaris (strain Hildenborough) and Megasphaera elsdenii. European Journal of Biochemistry. 136: 201-207. PMID 6311546 DOI: 10.1111/J.1432-1033.1983.Tb07727.X |
0.693 |
|
| 1983 |
Dunham WR, Sands RH, Shaw RW, Beinert H. Multiple frequency EPR studies on three forms of oxidized cytochrome c oxidase. Biochimica Et Biophysica Acta. 748: 73-85. PMID 6311273 DOI: 10.1016/0167-4838(83)90029-8 |
0.657 |
|
| 1982 |
van Camp HL, Sands RH, Fee JA. An examination of the cyanide derivative of bovine superoxide dismutase with electron-nuclear double resonance Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 704: 75-89. PMID 6284238 DOI: 10.1016/0167-4838(82)90134-0 |
0.391 |
|
| 1981 |
Van Camp HL, Sands RH, Fee JA. Electron-nuclear double resonance on copper (II) tetraimidazole The Journal of Chemical Physics. 75: 2098-2107. DOI: 10.1063/1.442313 |
0.301 |
|
| 1977 |
Dunham WR, Wu CT, Polichar RM, Sands RH, Harding LJ. Added precision in 57Fe Mössbauer spectroscopy Nuclear Instruments and Methods. 145: 537-553. DOI: 10.1016/0029-554X(77)90585-7 |
0.641 |
|
| 1975 |
Anderson RE, Dunham WR, Sands RH, Bearden AJ, Crespi HL. On the nature of the iron sulfur cluster in a deuterated algal ferredoxin. Biochimica Et Biophysica Acta. 408: 306-18. PMID 172131 DOI: 10.1016/0005-2728(75)90132-2 |
0.675 |
|
| 1975 |
Ruzicka FJ, Beinert H, Schepler KL, Dunham WR, Sands RH. Interaction of ubisemiquinone with a paramagnetic component in heart tissue Proceedings of the National Academy of Sciences of the United States of America. 72: 2886-2890. PMID 171646 DOI: 10.1073/Pnas.72.8.2886 |
0.642 |
|
| 1975 |
Schepler KL, Dunham WR, Sands RH, Fee JA, Abeles RH. A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B12. Biochimica Et Biophysica Acta. 397: 510-8. PMID 168925 DOI: 10.1016/0005-2744(75)90141-2 |
0.629 |
|
| 1974 |
Sands RH, Dunham WR. Spectroscopic studies on two iron ferredoxins Quarterly Reviews of Biophysics. 7: 443-504. PMID 4376247 |
0.645 |
|
| 1974 |
Mathews R, Charlton S, Sands RH, Palmer G. On the nature of the spin coupling between the iron sulfur clusters in the eight iron ferredoxins Journal of Biological Chemistry. 249: 4326-4328. PMID 4368981 |
0.364 |
|
| 1971 |
Palmer G, Dunham WR, Fee JA, Sands RH, Iizuka T, Yonetani T. The magnetic susceptibility of spinach ferredoxin from 77-250°K: A measurement of the antiferromagnetic coupling between the two iron atoms Bba - Bioenergetics. 245: 201-207. PMID 5132472 DOI: 10.1016/0005-2728(71)90022-3 |
0.631 |
|
| 1971 |
Dunham WR, Palmer G, Sands RH, Bearden AJ, Beinert H, Orme-Johnson WH. Comments on "the interpretation of the EPR and Mössbauer spectra of two-iron, one-electron iron-sulfur proteins". Biochemical and Biophysical Research Communications. 45: 1119-26. PMID 4332592 DOI: 10.1016/0006-291X(71)90135-5 |
0.689 |
|
| 1971 |
Dunham WR, Palmer G, Sands RH, Bearden AJ. On the structure of the iron-sulfur complex in the two-iron ferredoxins. Biochimica Et Biophysica Acta. 253: 373-84. PMID 4332306 DOI: 10.1016/0005-2728(71)90041-7 |
0.688 |
|
| 1971 |
Dunham WR, Bearden AJ, Salmeen IT, Palmer G, Sands RH, Orme-Johnson WH, Beinert H. The two-iron ferredoxins in spinach, parsley, pig adrenal cortex, Azotobacter vinelandii, and Clostridium pasteurianum: studies by magnetic field Mössbauer spectroscopy. Biochimica Et Biophysica Acta. 253: 134-52. PMID 4331269 DOI: 10.1016/0005-2728(71)90240-4 |
0.706 |
|
| 1971 |
Fritz J, Anderson R, Fee J, Palmer G, Sands RH, Tsibris JC, Gunsalus IC, Orme-Johnson WH, Beinert H. The iron electron-nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida. Biochimica Et Biophysica Acta. 253: 110-33. PMID 4331268 DOI: 10.1016/0005-2728(71)90239-8 |
0.453 |
|
| 1966 |
Palmer G, Sands RH, Mortenson LE. Electron paramagnetic resonance studies on the ferredoxin from Clostridiumpasteurianum Biochemical and Biophysical Research Communications. 23: 357-362. PMID 4289757 DOI: 10.1016/0006-291X(66)90733-9 |
0.386 |
|
| 1966 |
Brintzinger H, Palmer G, Sands RH. On the ligand field of iron in ferredoxin from spinach chloroplasts and related nonheme iron enzymes. Proceedings of the National Academy of Sciences of the United States of America. 55: 397-404. PMID 4287558 DOI: 10.1073/Pnas.55.2.397 |
0.445 |
|
| 1966 |
Brintzinger H, Palmer G, Sands RH. An electron paramagnetic resonance study of metal-aromatic bonding in bis(hexamethylbenzene)iron(I) [17] Journal of the American Chemical Society. 88: 623. DOI: 10.1021/Ja00955A053 |
0.386 |
|
| 1964 |
Moos HW, Sands RH. Study of spin-exchange collisions in vapors of Rb85, Rb87, and Cs133 by paramagnetic resonance Physical Review. 135: A591-A602. DOI: 10.1103/PhysRev.135.A591 |
0.462 |
|
| 1960 |
Beinert H, Sands RH. Studies on succinic and DPNH dehydrogenase preparations by paramagnetic resonance (EPR) spectroscopy Biochemical and Biophysical Research Communications. 3: 41-46. DOI: 10.1016/0006-291X(60)90100-5 |
0.318 |
|
| 1959 |
Beinert H, Sands RH. On the function of iron in DPNH cytochrome c reductase Biochemical and Biophysical Research Communications. 1: 171-174. DOI: 10.1016/0006-291X(59)90012-9 |
0.404 |
|
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