| Year |
Citation |
Score |
| 2010 |
Hirota S, Tanaka N, Micetic I, Di Muro P, Nagao S, Kitagishi H, Kano K, Magliozzo RS, Peisach J, Beltramini M, Bubacco L. Structural basis of the lactate-dependent allosteric regulation of oxygen binding in arthropod hemocyanin. The Journal of Biological Chemistry. 285: 19338-45. PMID 20406810 DOI: 10.1074/Jbc.M109.076067 |
0.323 |
|
| 2009 |
Vergara A, Franzese M, Merlino A, Bonomi G, Verde C, Giordano D, di Prisco G, Lee HC, Peisach J, Mazzarella L. Correlation between hemichrome stability and the root effect in tetrameric hemoglobins. Biophysical Journal. 97: 866-74. PMID 19651045 DOI: 10.1016/J.Bpj.2009.04.056 |
0.333 |
|
| 2009 |
Colaneri MJ, Vitali J, Peisach J. Aspects of structure and bonding in copper-amino acid complexes revealed by single-crystal EPR/ENDOR spectroscopy and density functional calculations. The Journal of Physical Chemistry. A. 113: 5700-9. PMID 19378965 DOI: 10.1021/Jp811249S |
0.399 |
|
| 2008 |
Hirota S, Kawahara T, Beltramini M, Di Muro P, Magliozzo RS, Peisach J, Powers LS, Tanaka N, Nagao S, Bubacco L. Molecular basis of the Bohr effect in arthropod hemocyanin. The Journal of Biological Chemistry. 283: 31941-8. PMID 18725416 DOI: 10.1074/Jbc.M803433200 |
0.354 |
|
| 2007 |
Vergara A, Franzese M, Merlino A, Vitagliano L, Verde C, di Prisco G, Lee HC, Peisach J, Mazzarella L. Structural characterization of ferric hemoglobins from three antarctic fish species of the suborder notothenioidei. Biophysical Journal. 93: 2822-9. PMID 17545238 DOI: 10.1529/Biophysj.107.105700 |
0.361 |
|
| 2005 |
Chattopadhyay M, Walter ED, Newell DJ, Jackson PJ, Aronoff-Spencer E, Peisach J, Gerfen GJ, Bennett B, Antholine WE, Millhauser GL. The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4. Journal of the American Chemical Society. 127: 12647-56. PMID 16144413 DOI: 10.1021/Ja053254Z |
0.777 |
|
| 2003 |
Burns CS, Aronoff-Spencer E, Legname G, Prusiner SB, Antholine WE, Gerfen GJ, Peisach J, Millhauser GL. Copper coordination in the full-length, recombinant prion protein. Biochemistry. 42: 6794-803. PMID 12779334 DOI: 10.1021/Bi027138+ |
0.784 |
|
| 2003 |
Peisach J. An appreciation of William H. Orme-Johnson III. Journal of Inorganic Biochemistry. 93: 6-10. PMID 12538047 DOI: 10.1016/S0162-0134(02)00434-8 |
0.331 |
|
| 2002 |
Legler PM, Lee HC, Peisach J, Mildvan AS. Kinetic and magnetic resonance studies of the role of metal ions in the mechanism of Escherichia coli GDP-mannose mannosyl hydrolase, an unusual nudix enzyme. Biochemistry. 41: 4655-68. PMID 11926828 DOI: 10.1021/Bi012118D |
0.333 |
|
| 2002 |
Burns CS, Aronoff-Spencer E, Dunham CM, Lario P, Avdievich NI, Antholine WE, Olmstead MM, Vrielink A, Gerfen GJ, Peisach J, Scott WG, Millhauser GL. Molecular features of the copper binding sites in the octarepeat domain of the prion protein. Biochemistry. 41: 3991-4001. PMID 11900542 DOI: 10.1021/Bi011922X |
0.784 |
|
| 2000 |
Aronoff-Spencer E, Burns CS, Avdievich NI, Gerfen GJ, Peisach J, Antholine WE, Ball HL, Cohen FE, Prusiner SB, Millhauser GL. Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochemistry. 39: 13760-71. PMID 11076515 DOI: 10.1021/Bi001472T |
0.785 |
|
| 2000 |
Lee HC, Goroncy AK, Peisach J, Cavada BS, Grangeiro TB, Ramos MV, Sampaio AH, Dam TK, Brewer CF. Demonstration of a conserved histidine and two water ligands at the Mn2+ site in Diocleinae lectins by pulsed EPR spectroscopy. Biochemistry. 39: 2340-6. PMID 10694401 DOI: 10.1021/Bi992102B |
0.439 |
|
| 2000 |
Colaneri MJ, Vitali J, Peisach J. Electron spin-echo envelope modulation study of multicrystalline Cu(2+)-insulin: effects of Cd(2+) on the nuclear quadrupole interaction of the Cu(2+)-coordinated imidazole remote nitrogen. Biochemistry. 39: 584-91. PMID 10642183 DOI: 10.1021/Bi991613V |
0.402 |
|
| 1999 |
Das TK, Couture M, Lee HC, Peisach J, Rousseau DL, Wittenberg BA, Wittenberg JB, Guertin M. Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: evidence for ligation of tyrosine-63 (B10) to the heme. Biochemistry. 38: 15360-8. PMID 10563822 DOI: 10.1021/Bi991237E |
0.406 |
|
| 1999 |
Couture M, Das TK, Lee HC, Peisach J, Rousseau DL, Wittenberg BA, Wittenberg JB, Guertin M. Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands. The Journal of Biological Chemistry. 274: 6898-910. PMID 10066743 DOI: 10.1074/Jbc.274.11.6898 |
0.354 |
|
| 1999 |
Das TK, Lee HC, Duff SM, Hill RD, Peisach J, Rousseau DL, Wittenberg BA, Wittenberg JB. The heme environment in barley hemoglobin. The Journal of Biological Chemistry. 274: 4207-12. PMID 9933618 DOI: 10.1074/Jbc.274.7.4207 |
0.335 |
|
| 1999 |
Lippai I, Magliozzo RS, Peisach J. EPR spectroscopic reinvestigation of the activation of iron complexes of PMAH as a bleomycin model Journal of the American Chemical Society. 121: 780-784. DOI: 10.1021/Ja980458P |
0.353 |
|
| 1998 |
Sam JW, Takahashi S, Lippai I, Peisach J, Rousseau DL. Sequence-specific changes in the metal site of ferric bleomycin induced by the binding of DNA. The Journal of Biological Chemistry. 273: 16090-7. PMID 9632661 DOI: 10.1074/Jbc.273.26.16090 |
0.332 |
|
| 1998 |
Bender CJ, Peisach J. Electron spin-echo modulation spectroscopic study of the type I copper center associated with stellacyanin from Rhus vernicifera: Examination of the graphical analysis of ESEEM spectra for two dissimilar weakly coupled 14N nuclei Journal of the Chemical Society - Faraday Transactions. 94: 375-386. DOI: 10.1039/A706120J |
0.441 |
|
| 1997 |
Bender CJ, Casimiro DR, Peisach J, Jane Dyson H. Electron spin echo modulation study of the Type I copper protein rusticyanin and its mutant variant His85Ala Implications for the general analysis of weak14N superhyperfine interactions Journal of the Chemical Society - Faraday Transactions. 93: 3967-3980. DOI: 10.1039/A704541G |
0.409 |
|
| 1997 |
Lee HC, Scheuring E, Peisach J, Chance MR. Electron spin echo envelope modulation and extended X-ray absorption fine structure studies of active site models of oxygenated cobalt-substituted hemoproteins: Correlating electron-nuclear couplings and metal-ligand bond lengths Journal of the American Chemical Society. 119: 12201-12209. DOI: 10.1021/Ja9717166 |
0.393 |
|
| 1996 |
Lu Y, Roe JA, Bender CJ, Peisach J, Banci L, Bertini I, Gralla EB, Valentine JS. New Type 2 Copper-Cysteinate Proteins. Copper Site Histidine-to-Cysteine Mutants of Yeast Copper-Zinc Superoxide Dismutase. Inorganic Chemistry. 35: 1692-1700. PMID 11666393 DOI: 10.1021/Ic9513189 |
0.401 |
|
| 1996 |
Bubacco L, Magliozzo RS, Beltramini M, Peisach J, Salvato B. Nitrite Reductase Activity of Deoxy Carcinus maenas Hemocyanin: Formation of the Half-Met Derivative. Inorganic Chemistry. 35: 1393-1394. PMID 11666340 DOI: 10.1021/Ic951008Q |
0.318 |
|
| 1996 |
Nersissian AM, Mehrabian ZB, Nalbandyan RM, Hart PJ, Fraczkiewicz G, Czernuszewicz RS, Bender CJ, Peisach J, Herrmann RG, Valentine JS. Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form. Protein Science : a Publication of the Protein Society. 5: 2184-92. PMID 8931137 DOI: 10.1002/Pro.5560051105 |
0.332 |
|
| 1996 |
Tipton PA, Quinn TP, Peisach J, Cook PF. Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex. Protein Science : a Publication of the Protein Society. 5: 1648-54. PMID 8844853 DOI: 10.1002/Pro.5560050818 |
0.358 |
|
| 1996 |
Coffino AR, Peisach J. Simulation of Mn (II) EPR spectra using a full spin-Hamiltonian approach. Journal of Magnetic Resonance. Series B. 111: 127-34. PMID 8661270 DOI: 10.1006/Jmrb.1996.0071 |
0.35 |
|
| 1996 |
Hüber M, Bubacco L, Beltramini M, Salvato B, Elias H, Peisach J, Larsen E, Harnung SE, Haase W. Cobalt(II) Substituted Derivatives of Carcinus maenas Hemocyanin: Magnetic Characterization, Magnetooptic, and Kinetic Studies Regarding the Geometry of the Active Site Inorganic Chemistry. 35: 7482-7492. DOI: 10.1021/Ic951587Z |
0.313 |
|
| 1995 |
Bubacco L, Magliozzo RS, Wirt MD, Beltramini M, Salvato B, Peisach J. Structural characterization of mononuclear Cu(II) and its nitrite complex in the active site of Carcinus maenas hemocyanin. Biochemistry. 34: 1524-33. PMID 7849011 DOI: 10.1021/Bi00005A008 |
0.35 |
|
| 1995 |
Bubacco L, Magliozzo RS, Wirt MD, Beltramini M, Salvato B, Peisach J. Structural characterization of mononuclear Cu(II) and its nitrite complex in the active site of Carcinus maenas hemocyanin. Biochemistry. 34: 1524-33. PMID 7849011 DOI: 10.1021/Bi00005A008 |
0.35 |
|
| 1995 |
Magliozzo RS, Bubacco L, McCracken J, Jiang F, Beltramini M, Salvato B, Peisach J. Cu(II) coordination in arthropod and mollusk green half-methemocyanins analyzed by electron spin-echo envelope modulation spectroscopy. Biochemistry. 34: 1513-23. PMID 7849010 DOI: 10.1021/Bi00005A007 |
0.699 |
|
| 1995 |
Parast CV, Wong KK, Kozarich JW, Peisach J, Magliozzo RS. Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate. Biochemistry. 34: 5712-7. PMID 7727431 DOI: 10.1021/Bi00017A002 |
0.31 |
|
| 1995 |
Theodorakis JL, Garber EA, McCracken J, Peisach J, Schejter A, Margoliash E. A chemical modification of cytochrome-c lysines leading to changes in heme iron ligation. Biochimica Et Biophysica Acta. 1252: 103-13. PMID 7548152 DOI: 10.1016/0167-4838(95)00097-E |
0.607 |
|
| 1995 |
Colaneri MJ, Peisach J. A single crystal EPR and ESEEM analysis of Cu(II)-doped bis(L-histidinato)cadmium dihydrate Journal of the American Chemical Society. 117: 6308-6315. DOI: 10.1021/Ja00128A021 |
0.356 |
|
| 1995 |
Crowder MW, Stewart JD, Roberts VA, Bender CJ, Tevelrakh E, Peisach J, Getzoff ED, Gaffney BJ, Benkovic SJ. Spectroscopic Studies on the Designed Metal-Binding Sites of the 43C9 Single Chain Antibody Journal of the American Chemical Society. 117: 5627-5634. DOI: 10.1021/Ja00126A003 |
0.38 |
|
| 1995 |
Wirt MD, Bubacco L, Peisach J. Investigation of solid and solution structures of N-substituted Cu(II) salicyldimines by X-ray absorption spectroscopy Inorganic Chemistry. 34: 2377-2381. DOI: 10.1021/Ic00113A019 |
0.398 |
|
| 1995 |
Wirt MD, Bender CJ, Peisach J. Electron spin echo envelope modulation (ESEEM) spectroscopy of cobalt(II) bis(dimethylglyoximes): Equatorial Co-N coupling parameters Inorganic Chemistry. 34: 1663-1667. DOI: 10.1021/Ic00111A010 |
0.402 |
|
| 1994 |
Balasubramanian S, Carr RT, Bender CJ, Peisach J, Benkovic SJ. Identification of metal ligands in Cu(II)-inhibited Chromobacterium violaceum phenylalanine hydroxylase by electron spin echo envelope modulation analysis of histidine to serine mutations. Biochemistry. 33: 8532-7. PMID 8031788 DOI: 10.1021/Bi00194A019 |
0.495 |
|
| 1994 |
Jiang F, Peisach J. Electron Spin Echo Envelope Modulation (ESEEM) study of CuII(dien)-pyrazole (dien = diethylenetriamine) and -pyridazine complexes Inorganic Chemistry. 33: 1348-1353. DOI: 10.1021/Ic00085A023 |
0.429 |
|
| 1993 |
Magliozzo RS, Peisach J. Evaluation of nitrogen nuclear hyperfine and quadrupole coupling parameters for the proximal imidazole in myoglobin-azide, -cyanide, and -mercaptoethanol complexes by electron spin echo envelope modulation spectroscopy. Biochemistry. 32: 8446-56. PMID 8395204 DOI: 10.1021/Bi00084A009 |
0.434 |
|
| 1993 |
Longa SD, Bianconi A, Palladino L, Simonelli B, Castellano AC, Borghi E, Barteri M, Beltramini M, Rocco GP, Salvato B, Bubacco L, Magliozzo RS, Peisach J. An x-ray absorption near edge structure spectroscopy study of metal coordination in Co(II)-substituted Carcinus maenas hemocyanin Biophysical Journal. 65: 2680-2691. PMID 8312502 DOI: 10.1016/S0006-3495(93)81330-4 |
0.307 |
|
| 1993 |
Balasubramanian S, Carr RT, Bender CJ, Peisach J, Benkovic SJ. Histidines 138 and 143 are copper binding ligands in Chromobacterium violaceum phenylalanine hydroxylase. Advances in Experimental Medicine and Biology. 338: 67-70. PMID 8304204 DOI: 10.1007/978-1-4615-2960-6_13 |
0.369 |
|
| 1993 |
Balasubramanian S, Carr RT, Bender CJ, Peisach J, Benkovic SJ. Histidines 138 and 143 are copper binding ligands in Chromobacterium violaceum phenylalanine hydroxylase. Advances in Experimental Medicine and Biology. 338: 67-70. PMID 8304204 DOI: 10.1007/978-1-4615-2960-6_13 |
0.369 |
|
| 1993 |
Van de Kamp M, Canters GW, Andrew CR, Sanders-Loehr J, Bender CJ, Peisach J. Effect of lysine ionization on the structure and electrochemical behaviour of the Met44-->Lys mutant of the blue-copper protein azurin from Pseudomonas aeruginosa. European Journal of Biochemistry / Febs. 218: 229-38. PMID 8243468 DOI: 10.1111/J.1432-1033.1993.Tb18369.X |
0.387 |
|
| 1993 |
Lu Y, LaCroix LB, Lowery MD, Solomon EI, Bender CJ, Peisach J, Roe JA, Gralla EB, Valentine JS. Construction of a blue copper site at the native zinc site of yeast copper-zinc superoxide dismutase Journal of the American Chemical Society. 115: 5907-5918. DOI: 10.1021/Ja00067A003 |
0.398 |
|
| 1993 |
Jiang F, Conry RR, Bubacco L, Tyeklar Z, Jacobson RR, Karlin KD, Peisach J. Crystal structure and electron spin echo envelope modulation study of [Cu(II)(TEPA)(NO2)]PF6 (TEPA = tris[2-(2-pyridyl)ethyl]amine): a model for the purported structure of the nitrite derivative of hemocyanin Journal of the American Chemical Society. 115: 2093-2102. DOI: 10.1021/Ja00059A001 |
0.477 |
|
| 1993 |
Jiang F, Karlin KD, Peisach J. An electron spin echo envelope modulation (ESEEM) study of electron-nuclear hyperfine and nuclear quadrupole interactions of dz2 ground state copper(II) complexes with substituted imidazoles Inorganic Chemistry. 32: 2576-2582. DOI: 10.1021/Ic00063A060 |
0.428 |
|
| 1993 |
Gurbiel RJ, Peoples R, Doan PE, Cline JF, McCracken J, Peisach J, Hoffman BM, Valentine JS. ENDOR and ESEEM investigation of AgI2CuII2 bovine superoxide dismutase Inorganic Chemistry. 32: 1813-1819. DOI: 10.1021/Ic00061A044 |
0.637 |
|
| 1993 |
Magliozzo RS, Peisach J. Evaluation of electronic changes in the axial ligand bonds of low spin myoglobin complexes by simulation of electron spin echo envelope modulation (ESEEM) spectra. Journal of Inorganic Biochemistry. 51: 179. DOI: 10.1016/0162-0134(93)85215-T |
0.393 |
|
| 1993 |
Gurbiel RJ, Peoples R, Doan PE, Cline JF, McCracken J, Peisach J, Hoffman BM, Valentine JS. ENDOR and ESEEM investigation of AgI 2CuII 2 bovine superoxide dismutase Inorganic Chemistry. 32: 1813-1819. |
0.514 |
|
| 1993 |
Jiang F, Karlin KD, Peisach J. An Electron Spin Echo Envelope Modulation (ESEEM) study of electron-nuclear hyperfine and nuclear quadrupole interactions of dz2 ground state copper(II) complexes with substituted imidazoles Inorganic Chemistry. 32: 2576-2582. |
0.313 |
|
| 1993 |
Jiang F, Conry RR, Bubacco L, Tyeklár Z, Jacobson RR, Karlin KD, Peisach J. Crystal structure and electron spin echo envelope modulation study of [Cu(II)(TEPA)(NO2)]PF6 (TEPA = tris[2-(2-pyridyl)ethyl]amine): A model for the purported structure of the nitrite derivative of hemocyanin Journal of the American Chemical Society. 115: X-2101. |
0.321 |
|
| 1992 |
Lu J, Bender CJ, McCracken J, Peisach J, Severns JC, McMillin DR. Pulsed EPR studies of the type 2 copper binding site in the mercury derivative of laccase. Biochemistry. 31: 6265-72. PMID 1320933 DOI: 10.1021/Bi00142A014 |
0.664 |
|
| 1992 |
Magliozzo RS, Peisach J. Electron spin echo envelope modulation spectroscopic study of iron-nitrogen interactions in myoglobin hydroxide and Fe(III) tetraphenylporphyrin models. Biochemistry. 31: 189-99. PMID 1310029 DOI: 10.1021/Bi00116A028 |
0.437 |
|
| 1992 |
Coffino AR, Peisach J. Nuclear modulation effects in high-spin electron systems with small zero-field splittings The Journal of Chemical Physics. 97: 3072-3091. DOI: 10.1063/1.462995 |
0.358 |
|
| 1992 |
Colaneri MJ, Peisach J. An electron spin-echo envelope modulation study of Cu(II)-doped single crystals of L-histidine hydrochloride monohydrate Journal of the American Chemical Society. 114: 5335-5341. DOI: 10.1021/Ja00039A051 |
0.458 |
|
| 1992 |
McCracken J, Peisach J, Cote CE, McGuirl MA, Dooley DM. Pulsed EPR studies of the semiquinone state of copper-containing amine oxidases Journal of the American Chemical Society. 114: 3715-3720. DOI: 10.1021/Ja00036A021 |
0.63 |
|
| 1992 |
Peisach J. Pulsed EPR studies of copper proteins Journal of Inorganic Biochemistry. 47: 21-33. DOI: 10.1007/978-94-011-6875-5_2 |
0.331 |
|
| 1991 |
Zer H, Freedman JH, Peisach J, Chevion M. Inverse correlation between resistance towards copper and towards the redox-cycling compound paraquat: a study in copper-tolerant hepatocytes in tissue culture. Free Radical Biology & Medicine. 11: 9-16. PMID 1937132 DOI: 10.1016/0891-5849(91)90182-3 |
0.325 |
|
| 1991 |
McCracken J, Peisach J, Bhattacharyya L, Brewer F. Electron spin echo envelope modulation studies of lectins: evidence for a conserved Mn(2+)-binding site. Biochemistry. 30: 4486-91. PMID 1850625 DOI: 10.1021/Bi00232A016 |
0.646 |
|
| 1991 |
Tipton PA, Peisach J. Pulsed EPR analysis of tartrate dehydrogenase active-site complexes. Biochemistry. 30: 739-44. PMID 1846305 DOI: 10.1021/Bi00217A024 |
0.405 |
|
| 1991 |
Jiang F, Peisach J, Ming LJ, Que L, Chen VJ. Electron spin echo envelope modulation studies of the Cu(II)-substituted derivative of isopenicillin N synthase: a structural and spectroscopic model. Biochemistry. 30: 11437-45. PMID 1660301 DOI: 10.1021/Bi00112A010 |
0.491 |
|
| 1991 |
Cammack R, Chapman A, McCracken J, Peisach J. Electron spin-echo spectroscopy of the iron-sulphur clusters of xanthine oxidase from milk Journal of the Chemical Society, Faraday Transactions. 87: 3203-3206. DOI: 10.1039/Ft9918703203 |
0.593 |
|
| 1991 |
Lee H, Magliozzo RS, Peisach J. Electron-nuclear coupling in cobaltous myoglobin and Glycera dibranchiata hemoglobin Journal of Inorganic Biochemistry. 43: 326. DOI: 10.1016/0162-0134(91)84313-X |
0.307 |
|
| 1990 |
Morgan TV, McCracken J, Orme-Johnson WH, Mims WB, Mortenson LE, Peisach J. Pulsed electron paramagnetic resonance studies of the interaction of Mg-ATP and D2O with the iron protein of nitrogenase. Biochemistry. 29: 3077-82. PMID 2159783 DOI: 10.1021/Bi00464A026 |
0.601 |
|
| 1990 |
Colaneri MJ, Potenza JA, Schugar HJ, Peisach J. Single-crystal electron spin-echo envelope modulation study of copper(II)-doped zinc bis(1,2-dimethylimidazole) dichloride Journal of the American Chemical Society. 112: 9451-9458. DOI: 10.1021/Ja00182A002 |
0.426 |
|
| 1990 |
Jiang F, McCracken J, Peisach J. Nuclear quadrupole interactions in copper(II)-diethylenetriamine-substituted imidazole complexes and in copper(II) proteins Journal of the American Chemical Society. 112: 9035-9044. DOI: 10.1021/Ja00181A002 |
0.632 |
|
| 1990 |
Cornelius JB, McCracken J, Clarkson RB, Belford RL, Peisach J. Electron spin echo envelope modulation angle selection studies of axial pyridine coordination to copper(II) benzoylacetonate Journal of Physical Chemistry. 94: 6977-6982. DOI: 10.1021/J100381A013 |
0.651 |
|
| 1990 |
Colaneri MJ, Potenza JA, Schugar HJ, Peisach J. Single-crystal electron spin echo envelope modulation study of Cu(II)-doped zinc bis(1,2-dimethylimidazole) dichloride Journal of the American Chemical Society. 112: 9451-9458. |
0.334 |
|
| 1989 |
Freedman JH, Peisach J. Intracellular copper transport in cultured hepatoma cells. Biochemical and Biophysical Research Communications. 164: 134-40. PMID 2553012 DOI: 10.1016/0006-291X(89)91693-8 |
0.402 |
|
| 1989 |
Tipton PA, McCracken J, Cornelius JB, Peisach J. Electron spin echo envelope modulation studies of pyruvate kinase active-site complexes. Biochemistry. 28: 5720-8. PMID 2550061 DOI: 10.1021/Bi00440A004 |
0.637 |
|
| 1989 |
Cunningham RP, Asahara H, Bank JF, Scholes CP, Salerno JC, Surerus K, Münck E, McCracken J, Peisach J, Emptage MH. Endonuclease III is an iron-sulfur protein. Biochemistry. 28: 4450-5. PMID 2548577 DOI: 10.1021/Bi00436A049 |
0.595 |
|
| 1989 |
Freedman JH, Peisach J. Resistance of cultured hepatoma cells to copper toxicity. Purification and characterization of the hepatoma metallothionein. Biochimica Et Biophysica Acta. 992: 145-54. PMID 2547449 DOI: 10.1016/0304-4165(89)90003-2 |
0.323 |
|
| 1989 |
Cammack R, Kovacs KL, McCracken J, Peisach J. Spectroscopic characterization of the nickel and iron-sulphur clusters of hydrogenase from the purple photosynthetic bacterium Thiocapsa roseopersicina. 2. Electron spin-echo spectroscopy. European Journal of Biochemistry / Febs. 182: 363-6. PMID 2544425 DOI: 10.1111/J.1432-1033.1989.Tb14839.X |
0.636 |
|
| 1989 |
Salvato B, Giacometti GM, Beltramini M, Zilio F, Giacometti G, Magliozzo RS, Peisach J. The oxidation of Octopus vulgaris hemocyanin by nitrogen oxides. Biochemistry. 28: 680-4. PMID 2540804 DOI: 10.1021/Bi00428A040 |
0.321 |
|
| 1989 |
Magliozzo R, McCracken J, Cornelius J, Lu J, Peisach J. EPR and pulsed EPR studies of low spin ferric porphyrin complexes Journal of Inorganic Biochemistry. 36: 269. DOI: 10.1016/0162-0134(89)84363-6 |
0.611 |
|
| 1989 |
McCracken J, Tipton P, Peisach J. Direct observation of Mn(II)-17O ligand hyperfine couplings using electron spin echo envelope modulation Journal of Inorganic Biochemistry. 36: 248. DOI: 10.1016/0162-0134(89)84298-9 |
0.635 |
|
| 1989 |
Peisach J, Tipton P, Cornelius J, McCracken J. Electron spin echo envelope modulation (ESEEM) studies of univalent metal coordination to pyruvate kinase Journal of Inorganic Biochemistry. 36: 247. DOI: 10.1016/0162-0134(89)84297-7 |
0.598 |
|
| 1989 |
Shugar H, Colaneri M, Peisach J. A single crystal electron spin echo envelope modulation (ESEEM) study of CU(II)-doped bis (1,2-dimethyllimidazole) Zinc(II) dichloride Journal of Inorganic Biochemistry. 36: 247. DOI: 10.1016/0162-0134(89)84295-3 |
0.329 |
|
| 1988 |
Serpersu EH, McCracken J, Peisach J, Mildvan AS. Electron spin echo modulation and nuclear relaxation studies of staphylococcal nuclease and its metal-coordinating mutants. Biochemistry. 27: 8034-44. PMID 2852950 DOI: 10.1021/Bi00421A010 |
0.584 |
|
| 1988 |
Serpersu EH, McCracken J, Peisach J, Mildvan AS. Electron spin echo modulation and nuclear relaxation studies of staphylococcal nuclease and its metal-coordinating mutants. Biochemistry. 27: 8034-44. PMID 2852950 DOI: 10.1021/Bi00421A010 |
0.584 |
|
| 1988 |
Chapman A, Cammack R, Hatchikian CE, McCracken J, Peisach J. A pulsed EPR study of redox-dependent hyperfine interactions for the nickel centre of Desulfovibrio gigas hydrogenase. Febs Letters. 242: 134-8. PMID 2849556 DOI: 10.1016/0014-5793(88)81001-9 |
0.617 |
|
| 1988 |
Cammack R, Chapman A, McCracken J, Cornelius JB, Peisach J, Weiner JH. Electron spin-echo spectroscopic studies of Escherichia coli fumarate reductase. Biochimica Et Biophysica Acta. 956: 307-12. PMID 2844272 DOI: 10.1016/0167-4838(88)90148-3 |
0.591 |
|
| 1988 |
Cammack R, Chapman A, McCracken J, Cornelius JB, Peisach J, Weiner JH. Electron spin-echo spectroscopic studies of Escherichia coli fumarate reductase. Biochimica Et Biophysica Acta. 956: 307-12. PMID 2844272 DOI: 10.1016/0167-4838(88)90148-3 |
0.591 |
|
| 1988 |
McCracken J, Desai PR, Papadopoulos NJ, Villafranca JJ, Peisach J. Electron spin-echo studies of the copper(II) binding sites in dopamine beta-hydroxylase. Biochemistry. 27: 4133-7. PMID 2843225 DOI: 10.1021/Bi00411A034 |
0.654 |
|
| 1988 |
McCracken J, Desai PR, Papadopoulos NJ, Villafranca JJ, Peisach J. Electron spin-echo studies of the copper(II) binding sites in dopamine beta-hydroxylase. Biochemistry. 27: 4133-7. PMID 2843225 DOI: 10.1021/Bi00411A034 |
0.654 |
|
| 1988 |
Doi K, McCracken J, Peisach J, Aisen P. The binding of molybdate to uteroferrin. Hyperfine interactions of the binuclear center with 95Mo, 1H, and 2H. The Journal of Biological Chemistry. 263: 5757-63. PMID 2833515 |
0.591 |
|
| 1988 |
Nakamura M, Peisach J. Self-inactivation of Fe(II)-bleomycin. The Journal of Antibiotics. 41: 638-47. PMID 2454908 DOI: 10.7164/Antibiotics.41.638 |
0.338 |
|
| 1988 |
Traylor TG, Hill KW, Tian ZQ, Rheingold AL, Peisach J, McCracken J. Ene diimidazoles: Ligands for biomimetic chemistry Journal of the American Chemical Society. 110: 5571-5573. DOI: 10.1021/Ja00224A052 |
0.563 |
|
| 1988 |
McCracken J, Pember S, Benkovic SJ, Villafranca JJ, Miller RJ, Peisach J. Electron spin-echo studies of the copper binding site in phenylalanine hydroxylase from Chromobacterium violaceum Journal of the American Chemical Society. 110: 1069-1074. DOI: 10.1021/Ja00212A012 |
0.65 |
|
| 1988 |
MCCRACKEN J, PEMBER S, BENKOVIC SJ, VILLAFRANCA JJ, MILLER RJ, PEISACH J. ChemInform Abstract: Electron Spin-Echo Studies of the Copper Binding Site in Phenylalanine Hydroxylase from Chromobacterium violaceum Cheminform. 19. DOI: 10.1002/chin.198823340 |
0.333 |
|
| 1988 |
McCracken J, Pember S, Benkovic SJ, Villafranca JJ, Miller RJ, Peisach J. Electron spin-echo studies of the copper binding site in phenylalanine hydroxylase from Chromobacterium violaceum Journal of the American Chemical Society. 110: 1069-1074. |
0.616 |
|
| 1987 |
Dooley DM, McGuirl MA, Peisach J, McCracken J. The generation of an organic free radical in substrate-reduced pig kidney diamine oxidase-cyanide. Febs Letters. 214: 274-8. PMID 3106087 DOI: 10.1016/0014-5793(87)80069-8 |
0.58 |
|
| 1987 |
Antanaitis BC, Brown RD, Chasteen ND, Freedman JH, Koenig SH, Lilienthal HR, Peisach J, Brewer CF. Electron paramagnetic resonance and magnetic susceptibility studies of dimanganese concanavalin A. Evidence for antiferromagnetic exchange coupling. Biochemistry. 26: 7932-7. PMID 2827763 DOI: 10.1021/Bi00398A058 |
0.372 |
|
| 1987 |
Magliozzo RS, McCracken J, Peisach J. Electron-nuclear coupling in nitrosyl heme proteins and in nitrosyl ferrous and oxy cobaltous tetraphenylporphyrin complexes. Biochemistry. 26: 7923-31. PMID 2827762 DOI: 10.1021/Bi00398A057 |
0.623 |
|
| 1987 |
Mondovi B, Morpurgo L, Agostinelli E, Befani O, McCracken J, Peisach J. A comparison of the local environment of Cu(II) in native and half-Cu-depleted bovine serum amine oxidase. European Journal of Biochemistry / Febs. 168: 503-7. PMID 2822417 DOI: 10.1111/J.1432-1033.1987.Tb13446.X |
0.669 |
|
| 1987 |
McCracken J, Peisach J, Dooley DM. Cu(II) Coordination chemistry of amine oxidases: Pulsed EPR studies of histidine imidazole, water, and exogenous ligand coordination Journal of the American Chemical Society. 109: 4064-4072. DOI: 10.1021/Ja00247A037 |
0.639 |
|
| 1987 |
Melnyk DL, Band Horwitz S, Peisach J. The oxidation-reduction potential of copper-bleomycin Inorganica Chimica Acta. 138: 75-78. DOI: 10.1016/S0020-1693(00)81184-6 |
0.331 |
|
| 1986 |
Freedman JH, Powers L, Peisach J. Structure of the copper cluster in canine hepatic metallothionein using X-ray absorption spectroscopy. Biochemistry. 25: 2342-9. PMID 3718956 DOI: 10.1021/Bi00357A007 |
0.398 |
|
| 1986 |
Salvato B, Beltramini M, Piazzesi A, Alviggi M, Ricchelli F, Magliozzo RS, Peisach J. Preparation, spectroscopic characterization and anion binding studies of a mononuclear Co(II) derivative of carcinus maenas hemocyanin Inorganica Chimica Acta. 125: 55-62. DOI: 10.1016/S0020-1693(00)85484-5 |
0.448 |
|
| 1985 |
Malikayil JA, Sweeney WV, McCracken J, Peisach J. The lack of a solvent accessible hydroxide or water ligand to iron at the 3Fe center of Azotobacter vinelandii ferredoxin I. Biochemical and Biophysical Research Communications. 133: 1119-24. PMID 3002366 DOI: 10.1016/0006-291X(85)91252-5 |
0.57 |
|
| 1985 |
Malikayil JA, Sweeney WV, McCracken J, Peisach J. The lack of a solvent accessible hydroxide or water ligand to iron at the 3Fe center of Azotobacter vinelandii ferredoxin I. Biochemical and Biophysical Research Communications. 133: 1119-24. PMID 3002366 DOI: 10.1016/0006-291X(85)91252-5 |
0.57 |
|
| 1984 |
Mims WB, Davis JL, Peisach J. The accessibility of type I Cu(II) centers in laccase, azurin, and stellacyanin to exchangeable hydrogen and ambient water. Biophysical Journal. 45: 755-66. PMID 6326878 DOI: 10.1016/S0006-3495(84)84219-8 |
0.345 |
|
| 1984 |
Di Iorio EE, Winterhalter KH, Mansouri A, Blumberg WE, Peisach J. Studies on the oxidation of hemoglobin Zurich (beta 63 E7 Arg). European Journal of Biochemistry / Febs. 145: 549-54. PMID 6096143 DOI: 10.1111/J.1432-1033.1984.Tb08591.X |
0.311 |
|
| 1984 |
Roberts JE, Cline JF, Lum V, Gray HB, Freeman H, Peisach J, Reinhammar B, Hoffman BM. Comparative ENDOR study of six blue copper proteins Journal of the American Chemical Society. 106: 5324-5330. DOI: 10.1021/Ja00330A048 |
0.363 |
|
| 1983 |
Burger RM, Peisach J. Photoreduction of ferric bleomycin Inorganica Chimica Acta. 79: 304. DOI: 10.1016/S0020-1693(00)95355-6 |
0.313 |
|
| 1983 |
Peisach J, Burger RM, Horwitz SB, Kent TA, Münck E. The electronic structure of iron complexes of bleomycin Inorganica Chimica Acta. 79: 33. DOI: 10.1016/S0020-1693(00)95054-0 |
0.4 |
|
| 1982 |
Peisach J, Powers L, Blumberg WE, Chance B. Stellacyanin. Studies of the metal-binding site using x-ray absorption spectroscopy. Biophysical Journal. 38: 277-85. PMID 7104439 DOI: 10.1016/S0006-3495(82)84559-1 |
0.431 |
|
| 1982 |
Freedman JH, Pickart L, Weinstein B, Mims WB, Peisach J. Structure of the Glycyl-L-histidyl-L-lysine--copper(II) complex in solution. Biochemistry. 21: 4540-4. PMID 6291585 DOI: 10.1021/Bi00262A004 |
0.441 |
|
| 1982 |
Zweier JL, Peisach J, Mims WB. Electron spin echo studies of the copper complexes of conalbumin. The Journal of Biological Chemistry. 257: 10314-6. PMID 6286648 |
0.383 |
|
| 1982 |
Freedman JH, Horwitz SB, Peisach J. Reduction of copper(II)-bleomycin: A model for in vivo drug activity Biochemistry. 21: 2203-2210. PMID 6178433 DOI: 10.1021/Bi00538A032 |
0.403 |
|
| 1981 |
Burger RM, Adler AD, Horwitz SB, Mims WB, Peisach J. Demonstration of nitrogen coordination in metal--bleomycin complexes by electron spin--echo envelope spectroscopy. Biochemistry. 20: 1701-4. PMID 6164390 |
0.336 |
|
| 1980 |
Mims WB, Peisach J, Shaw RW, Beinert H. Electron spin echo studies of cytochrome c oxidase. The Journal of Biological Chemistry. 255: 6843-6. PMID 6248535 |
0.338 |
|
| 1980 |
Kosman DJ, Peisach J, Mims WB. Pulsed electron paramagnetic resonance studies of the copper(II) site in galactose oxidase Biochemistry. 19: 1304-1308. PMID 6248103 DOI: 10.1021/Bi00548A007 |
0.406 |
|
| 1980 |
Roberts JE, Brown TG, Hoffman BM, Peisach J. Electron nuclear double resonance spectra of stellacyanin, a blue copper protein Journal of the American Chemical Society. 102: 825-829. DOI: 10.1021/Ja00522A063 |
0.369 |
|
| 1979 |
Powers L, Blumberg WE, Chance B, Barlow CH, Leigh JS, Smith J, Yonetani T, Vik S, Peisach J. The nature of the copper atoms of cytochrome c oxidase as studied by optical and x-ray absorption edge spectroscopy. Biochimica Et Biophysica Acta. 546: 520-38. PMID 222313 DOI: 10.1016/0005-2728(79)90085-9 |
0.389 |
|
| 1979 |
Mims WB, Peisach J. Measurement of 14N superhyperfine frequencies in stellacyanin by an electron spin echo method Journal of Biological Chemistry. 254: 4321-4323. PMID 220240 |
0.316 |
|
| 1978 |
Blumberg WE, Peisach J, Eisenberger P, Fee JA. Superoxide dismutase, a study of the electronic properties of the copper and zinc by X-ray absorption spectroscopy. Biochemistry. 17: 1842-6. PMID 566111 |
0.33 |
|
| 1978 |
Peisach J, Mims WB. The linear electric field effect in stellacyanin, azurin and in some simple model compounds European Journal of Biochemistry. 84: 207-214. PMID 206431 DOI: 10.1111/J.1432-1033.1978.Tb12158.X |
0.426 |
|
| 1978 |
Sausville EA, Peisach J, Horwitz SB. Effect of chelating agents and metal ions on the degradation of dna by bleomycin Biochemistry. 17: 2740-2746. PMID 80226 DOI: 10.1021/Bi00607A007 |
0.333 |
|
| 1978 |
Chevion M, Stern A, Peisach J, Blumberg WE, Simon S. Analogous effect of protons and inositol hexaphosphate on the alteration of structure of nitrosyl fetal human hemoglobin. Biochemistry. 17: 1745-50. PMID 26386 DOI: 10.1021/Bi00602A025 |
0.302 |
|
| 1977 |
Mondoví B, Graziani MT, Mims WB, Oltzik R, Peisach J. Pulsed electron paramagnetic resonance studies of types I and II copper of Rhus vernicifera laccase and porcine ceruloplasmin Biochemistry. 16: 4198-4202. PMID 197989 |
0.33 |
|
| 1976 |
Stern JO, Peisach J. A model compound for nitrosyl cytochrome P-450; further evidence for mercaptide sulfur ligation to heme Febs Letters. 62: 364-368. PMID 1278381 DOI: 10.1016/0014-5793(76)80095-6 |
0.358 |
|
| 1976 |
Appleby CA, Blumberg WE, Peisach J, Wittenberg BA, Wittenberg JB. Leghemoglobin. An electron paramagnetic resonance and optical spectral study of the free protein and its complexes with nicotinate and acetate. The Journal of Biological Chemistry. 251: 6090-6. PMID 184092 |
0.318 |
|
| 1976 |
Mims WB, Peisach J. Assignment of a ligand in stellacyanin by a pulsed electron paramagnetic resonance method. Biochemistry. 15: 3863-9. PMID 182220 DOI: 10.1021/BI00662A033 |
0.391 |
|
| 1976 |
Sausville EA, Peisach J, Horwitz SB. A role for ferrous ion and oxygen in the degradation of DNA by bleomycin Biochemical and Biophysical Research Communications. 73: 814-822. PMID 64249 DOI: 10.1016/0006-291X(76)90882-2 |
0.304 |
|
| 1976 |
Chevion M, Salhany JM, Peisach J, Castillo CL, Blumberg WE. Iron-Nitrosyl Bond Configuration in Nitrosyl-Hemoproteins: A Comparative EPR Study of Hemoglobin A and Hemoglobin Kansas Israel Journal of Chemistry. 15: 311-317. DOI: 10.1002/Ijch.197600053 |
0.341 |
|
| 1975 |
Stern JO, Peisach E, Peisach J, Blumberg WE, Lu AY, Ryan WD, Levin W, West S. Studies on the spin state of 3-methylcholanthrene induced cytochrome P-450 from rat liver. Advances in Experimental Medicine and Biology. 58: 189-202. PMID 168749 DOI: 10.1007/978-1-4615-9026-2_13 |
0.333 |
|
| 1973 |
Stern JO, Peisach J, Blumberg WE, Lu AY, Levin W. A low-temperature EPR study of partially purified, soluble ferric cytochromes P-450 and P-448 from rat liver microsomes. Archives of Biochemistry and Biophysics. 156: 404-13. PMID 4352418 DOI: 10.1016/0003-9861(73)90289-0 |
0.347 |
|
| 1972 |
Peisach J, Appleby CA, Blumberg WE. Electron paramagnetic resonance and temperature dependent spin state studies of ferric cytochrome P-450 from Rhizobium japonicum. Archives of Biochemistry and Biophysics. 150: 725-32. PMID 4339738 DOI: 10.1016/0003-9861(72)90091-4 |
0.373 |
|
| 1970 |
Wittenberg JB, Wittenberg BA, Peisach J, Blumberg WE. On the state of the iron and the nature of the ligand in oxyhemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 67: 1846-53. PMID 4321348 DOI: 10.1073/Pnas.67.4.1846 |
0.357 |
|
| 1970 |
Tsai R, Yu CA, Gunsalus IC, Peisach J, Blumberg W, Orme-Johnson WH, Beinert H. Spin-state changes in cytochrome P-450cam on binding of specific substrates. Proceedings of the National Academy of Sciences of the United States of America. 66: 1157-63. PMID 4319883 DOI: 10.1073/Pnas.66.4.1157 |
0.383 |
|
| 1967 |
Brumer P, Levine WG, Peisach J. Some properties of denatured horse heart cytochrome c. Archives of Biochemistry and Biophysics. 117: 232-8. PMID 4291460 DOI: 10.1016/0003-9861(66)90407-3 |
0.304 |
|
| 1966 |
Blumberg WE, Peisach J. The optical and magnetic properties of copper in Chenopodium album plastocyanin. Biochimica Et Biophysica Acta. 126: 269-73. PMID 4291366 DOI: 10.1016/0926-6585(66)90063-X |
0.354 |
|
| 1965 |
Blumberg W, Horecker B, Kelly-Falcoz F, Peisach J. The role of copper in galactose oxidase Biochimica Et Biophysica Acta (Bba) - Enzymology and Biological Oxidation. 96: 336-338. DOI: 10.1016/0926-6593(65)90019-6 |
0.357 |
|
| 1964 |
Blumberg WE, Levine WG, Margolis S, Peisach J. On the nature of copper in two proteins obtained from Rhus vernicifera latex. Biochemical and Biophysical Research Communications. 15: 277-83. PMID 4284280 DOI: 10.1016/0006-291X(64)90160-3 |
0.349 |
|
| 1963 |
Peisach J, Levine WG. On the mechanism of ceruloplasmin-catalyzed oxidations Biochimica Et Biophysica Acta. 77: 615-628. DOI: 10.1016/0006-3002(63)90546-8 |
0.343 |
|
| 1963 |
Levine WG, Peisach J. Ethylenediaminetetraacetate, iron and ceruloplasmin activity Biochimica Et Biophysica Acta. 77: 602-614. DOI: 10.1016/0006-3002(63)90545-6 |
0.324 |
|
| 1958 |
Walling C, Peisach J. Organic Reactions Under High Pressure. IV. The Dimerization of Isoprene1 Journal of the American Chemical Society. 80: 5819-5824. DOI: 10.1021/Ja01554A058 |
0.469 |
|
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