Year |
Citation |
Score |
2022 |
Valer L, Rossetto D, Parkkila T, Sebastianelli L, Guella G, Hendricks AL, Cowan JA, Sang L, Mansy SS. Histidine Ligated Iron-Sulfur Peptides. Chembiochem : a European Journal of Chemical Biology. e202200202. PMID 35674331 DOI: 10.1002/cbic.202200202 |
0.683 |
|
2020 |
Yu Z, Thompson Z, Behnke SL, Fenk KD, Huang D, Shafaat HS, Cowan JA. Metalloglycosidase Mimics: Oxidative Cleavage of Saccharides Promoted by Multinuclear Copper Complexes under Physiological Conditions. Inorganic Chemistry. 59: 11218-11222. PMID 32799467 DOI: 10.1021/Acs.Inorgchem.0C01193 |
0.311 |
|
2020 |
Sen S, Hendricks AL, Cowan JA. Cluster exchange reactivity of [2Fe-2S]-bridged heterodimeric BOLA1-GLRX5. The Febs Journal. PMID 32542995 DOI: 10.1111/Febs.15452 |
0.419 |
|
2020 |
Thompson Z, Cowan JA. Artificial Metalloenzymes: Recent Developments and Innovations in Bioinorganic Catalysis. Small (Weinheim An Der Bergstrasse, Germany). e2000392. PMID 32372559 DOI: 10.1002/Smll.202000392 |
0.307 |
|
2020 |
Pearson SA, Wachnowsky C, Cowan JA. Defining the mechanism of the mitochondrial Atm1p [2Fe-2S] cluster exporter. Metallomics : Integrated Biometal Science. PMID 32337520 DOI: 10.1039/C9Mt00286C |
0.431 |
|
2020 |
Jia M, Sen S, Wachnowsky C, Fidai I, Cowan JA, Wysocki V. Characterization of [2Fe-2S]-Cluster-Bridged Protein Complexes and Reaction Intermediates by use of Robust Native Mass Spectrometric Methods. Angewandte Chemie (International Ed. in English). PMID 32031732 DOI: 10.1002/Anie.201915615 |
0.429 |
|
2019 |
Lewis BE, Mason Z, Rodrigues AV, Nuth M, Dizin E, Cowan JA, Stemmler TL. Unique roles of iron and zinc binding to the yeast Fe-S cluster scaffold assembly protein "Isu1". Metallomics : Integrated Biometal Science. PMID 31532427 DOI: 10.1039/C9Mt00172G |
0.724 |
|
2019 |
Wachnowsky C, Rao B, Sen S, Fries B, Howard CJ, Ottesen JJ, Cowan JA. Reconstitution, characterization, and [2Fe-2S] cluster exchange reactivity of a holo human BOLA3 homodimer. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 31486956 DOI: 10.1007/S00775-019-01713-X |
0.43 |
|
2019 |
Wachnowsky C, Hendricks AL, Wesley NA, Ferguson C, Fidai I, Cowan JA. Understanding the Mechanism of [4Fe-4S] Cluster Assembly on Eukaryotic Mitochondrial and Cytosolic Aconitase Inorganic Chemistry. 58: 13686-13695. PMID 31436962 DOI: 10.1021/Acs.Inorgchem.9B01278 |
0.358 |
|
2019 |
Alexander JL, Thompson Z, Yu Z, Cowan JA. Cu-ATCUN Derivatives of Sub5 Exhibit Enhanced Antimicrobial Activity via Multiple Modes of Action. Acs Chemical Biology. PMID 30742402 DOI: 10.1021/Acschembio.8B01087 |
0.335 |
|
2019 |
Li D, Agarwal A, Cowan JA. Evaluation of Solvent Accessibility to the [Fe(4)S(4)] Binding Pocket in Native and Tyr19 Mutant High Potential Iron Proteins by (1)H-(15)N HMQC and (19)F NMR Experiments. Inorganic Chemistry. 35: 1121-1125. PMID 11666298 DOI: 10.1021/ic951160s |
0.305 |
|
2018 |
Pinkham AM, Yu Z, Cowan JA. Broad-spectrum catalytic metallopeptide inactivators of Zika and West Nile virus NS2B/NS3 proteases. Chemical Communications (Cambridge, England). PMID 30324214 DOI: 10.1039/C8Cc07448H |
0.315 |
|
2018 |
Sen S, Rao B, Wachnowsky C, Cowan JA. Cluster exchange reactivity of [2Fe-2S] cluster-bridged complexes of BOLA3 with monothiol glutaredoxins. Metallomics : Integrated Biometal Science. PMID 30137089 DOI: 10.1039/C8Mt00128F |
0.414 |
|
2018 |
Olive JA, Cowan JA. Role of the HSPA9/HSC20 chaperone pair in promoting directional human iron-sulfur cluster exchange involving monothiol glutaredoxin 5. Journal of Inorganic Biochemistry. 184: 100-107. PMID 29689452 DOI: 10.1016/J.Jinorgbio.2018.04.007 |
0.403 |
|
2018 |
Pinkham AM, Yu Z, Cowan JA. Attenuation of West Nile Virus NS2B/NS3 Protease by Amino Terminal Copper and Nickel Bind-ing (ATCUN) Peptides. Journal of Medicinal Chemistry. PMID 29301071 DOI: 10.1021/Acs.Jmedchem.7B01409 |
0.384 |
|
2018 |
Wachnowsky C, Fidai I, Cowan JA. Iron–sulfur cluster biosynthesis and trafficking – impact on human disease conditions Metallomics. 10: 9-29. PMID 29019354 DOI: 10.1039/C7Mt00180K |
0.383 |
|
2017 |
Sen S, Bonfio C, Mansy SS, Cowan JA. Investigation of glutathione-derived electrostatic and hydrogen-bonding interactions and their role in defining Grx5 [2Fe-2S] cluster optical spectra and transfer chemistry. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 29264659 DOI: 10.1007/S00775-017-1525-5 |
0.807 |
|
2017 |
Wachnowsky C, Liu Y, Yoon T, Cowan JA. Regulation of Human Nfu Activity in Fe-S Cluster Delivery - Characterization of the Interaction between Nfu and the HSPA9/Hsc20 Chaperone Complex. The Febs Journal. PMID 29211945 DOI: 10.1111/Febs.14353 |
0.637 |
|
2017 |
Alexander JL, Yu Z, Cowan JA. Amino Terminal Copper and Nickel Binding Motif Derivatives of Ovispirin-3 Display Increased Antimicrobial Activity via Lipid Oxidation. Journal of Medicinal Chemistry. 60: 10047-10055. PMID 29172482 DOI: 10.1021/Acs.Jmedchem.7B01117 |
0.337 |
|
2017 |
Yu Z, Cowan JA. Metal complexes promoting catalytic cleavage of nucleic acids-biochemical tools and therapeutics. Current Opinion in Chemical Biology. 43: 37-42. PMID 29153936 DOI: 10.1016/J.Cbpa.2017.10.029 |
0.316 |
|
2017 |
Wesley NA, Wachnowsky C, Fidai I, Cowan JA. Understanding the Molecular Basis for Multiple Mitochondrial Dysfunctions Syndrome 1 (MMDS1): Impact of a Disease-Causing Gly189Arg Substitution on NFU1. The Febs Journal. PMID 28906594 DOI: 10.1111/Febs.14271 |
0.42 |
|
2017 |
Wesley NA, Wachnowsky C, Fidai I, Cowan JA. Analysis of NFU-1 Metallocofactor Binding Site Substitutions: Impacts on Iron-Sulfur Cluster Coordination and Protein Structure and Function. The Febs Journal. PMID 28906593 DOI: 10.1111/Febs.14270 |
0.429 |
|
2017 |
Wachnowsky C, Cowan JA. In Vitro Studies of Cellular Iron-Sulfur Cluster Biosynthesis, Trafficking, and Transport. Methods in Enzymology. 595: 55-82. PMID 28882208 DOI: 10.1016/Bs.Mie.2017.06.045 |
0.445 |
|
2017 |
Sen S, Cowan JA. Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe-2S] cluster chirality, ligand exchange and transfer chemistry. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 28836015 DOI: 10.1007/S00775-017-1485-9 |
0.436 |
|
2017 |
Cowan JA, Yu Z. Catalytic Metallodrugs: Substrate-Selective Metal Catalysts as Therapeutics. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 28688119 DOI: 10.1002/Chem.201701714 |
0.314 |
|
2017 |
Ross MJ, Fidai I, Cowan JA. Analysis of Structure-Activity Relationships Based on the HCV SLIIb IRES RNA-Targeting GGHYRFK-Cu Complex. Chembiochem : a European Journal of Chemical Biology. PMID 28628737 DOI: 10.1002/Cbic.201700228 |
0.344 |
|
2017 |
Wachnowsky C, Wesley NA, Fidai I, Cowan JA. Understanding the Molecular Basis of Multiple Mitochondrial Dysfunctions Syndrome 1 (MMDS1)-Impact of a Disease-Causing Gly208Cys Substitution on Structure and Activity of NFU1 in the Fe/S Cluster Biosynthetic Pathway. Journal of Molecular Biology. 429: 790-807. PMID 28161430 DOI: 10.1016/J.Jmb.2017.01.021 |
0.418 |
|
2016 |
Fidai I, Wachnowsky C, Cowan JA. Mapping cellular Fe-S cluster uptake and exchange reactions - divergent pathways for iron-sulfur cluster delivery to human ferredoxins. Metallomics. 8: 1283-1293. PMID 27878189 DOI: 10.1039/C6Mt00193A |
0.396 |
|
2016 |
Wachnowsky C, Fidai I, Cowan JA. Cytosolic iron-sulfur cluster transfer-a proposed kinetic pathway for reconstitution of glutaredoxin 3. Febs Letters. PMID 27859051 DOI: 10.1002/1873-3468.12491 |
0.433 |
|
2016 |
Scintilla S, Bonfio C, Belmonte L, Forlin M, Rossetto D, Li J, Cowan JA, Galliani A, Arnesano F, Assfalg M, Mansy SS. Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin. Chemical Communications (Cambridge, England). PMID 27790655 DOI: 10.1039/C6Cc07912A |
0.779 |
|
2016 |
Fidai I, Wachnowsky C, Cowan JA. Glutathione-complexed [2Fe-2S] clusters function in Fe–S cluster storage and trafficking Journal of Biological Inorganic Chemistry. 21: 887-901. PMID 27590019 DOI: 10.1007/S00775-016-1387-2 |
0.433 |
|
2016 |
Wachnowsky C, Fidai I, Cowan JA. Iron-sulfur cluster exchange reactions mediated by the human Nfu protein. Journal of Biological Inorganic Chemistry. 21: 825-836. PMID 27538573 DOI: 10.1007/S00775-016-1381-8 |
0.39 |
|
2015 |
Ross MJ, Bradford SS, Cowan JA. Catalytic metallodrugs based on the LaR2C peptide target HCV SLIV IRES RNA. Dalton Transactions (Cambridge, England : 2003). PMID 26583601 DOI: 10.1039/C5Dt02837J |
0.68 |
|
2014 |
Fidai I, Hocharoen L, Bradford S, Wachnowsky C, Cowan JA. Inactivation of sortase A mediated by metal ATCUN complexes. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 19: 1327-39. PMID 25217034 DOI: 10.1007/S00775-014-1190-X |
0.778 |
|
2014 |
Bradford SS, Ross MJ, Fidai I, Cowan JA. Insight into the recognition, binding, and reactivity of catalytic metallodrugs targeting stem loop IIb of hepatitis C IRES RNA. Chemmedchem. 9: 1275-85. PMID 24756921 DOI: 10.1002/Cmdc.201400070 |
0.679 |
|
2014 |
Amick J, Schlanger SE, Wachnowsky C, Moseng MA, Emerson CC, Dare M, Luo WI, Ithychanda SS, Nix JC, Cowan JA, Page RC, Misra S. Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone. Protein Science : a Publication of the Protein Society. 23: 833-42. PMID 24687350 DOI: 10.1002/Pro.2466 |
0.608 |
|
2014 |
Bradford SS, Cowan JA. From Traditional Drug Design to Catalytic Metallodrugs: A Brief History of the Use of Metals in Medicine Metallodrugs. 1. DOI: 10.2478/medr-2014-0002 |
0.643 |
|
2014 |
Luo WI, Cowan JA. The role of mortalin in iron homeostasis Mortalin Biology: Life, Stress and Death. 2147483647: 31-54. DOI: 10.1007/978-94-007-3027-4_3 |
0.592 |
|
2014 |
Bradford SS, Ross MJ, Fidai I, Cowan JA. Inside Cover: Insight into the Recognition, Binding, and Reactivity of Catalytic Metallodrugs Targeting Stem Loop IIb of Hepatitis C IRES RNA (ChemMedChem 6/2014) Chemmedchem. 9: 1086-1086. DOI: 10.1002/Cmdc.201490021 |
0.679 |
|
2013 |
Hocharoen L, Joyner JC, Cowan JA. N- versus C-domain selectivity of catalytic inactivation of human angiotensin converting enzyme by lisinopril-coupled transition metal chelates. Journal of Medicinal Chemistry. 56: 9826-36. PMID 24228790 DOI: 10.1021/Jm4009345 |
0.756 |
|
2013 |
Joyner JC, Cowan JA. Target-directed catalytic metallodrugs. Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas MéDicas E BiolóGicas / Sociedade Brasileira De BiofíSica ... [Et Al.]. 46: 465-85. PMID 23828584 DOI: 10.1590/1414-431X20133086 |
0.752 |
|
2013 |
Joyner JC, Keuper KD, Cowan JA. Kinetics and Mechanisms of Oxidative Cleavage of HIV RRE RNA by Rev-Coupled Transition Metal Chelates. Chemical Science (Royal Society of Chemistry : 2010). 4: 1707-1718. PMID 23626900 DOI: 10.1039/C3Sc22135K |
0.75 |
|
2013 |
Joyner JC, Hodnick WF, Cowan AS, Tamuly D, Boyd R, Cowan JA. Antimicrobial metallopeptides with broad nuclease and ribonuclease activity. Chemical Communications (Cambridge, England). 49: 2118-20. PMID 23380915 DOI: 10.1039/C3Cc38977D |
0.738 |
|
2013 |
Joyner JC, Keuper KD, Cowan JA. Analysis of RNA cleavage by MALDI-TOF mass spectrometry. Nucleic Acids Research. 41: e2. PMID 22941655 DOI: 10.1093/Nar/Gks811 |
0.723 |
|
2012 |
Qi W, Li J, Chain CY, Pasquevich GA, Pasquevich AF, Cowan JA. Glutathione complexed Fe-S centers. Journal of the American Chemical Society. 134: 10745-8. PMID 22687047 DOI: 10.1021/Ja302186J |
0.411 |
|
2012 |
Joyner JC, Keuper KD, Cowan JA. DNA nuclease activity of Rev-coupled transition metal chelates. Dalton Transactions (Cambridge, England : 2003). 41: 6567-78. PMID 22450234 DOI: 10.1039/C2Dt00026A |
0.757 |
|
2012 |
Bradford S, Cowan JA. Catalytic metallodrugs targeting HCV IRES RNA. Chemical Communications (Cambridge, England). 48: 3118-20. PMID 22343977 DOI: 10.1039/C2Cc17377H |
0.674 |
|
2012 |
Joyner JC, Hocharoen L, Cowan JA. Targeted catalytic inactivation of angiotensin converting enzyme by lisinopril-coupled transition-metal chelates. Journal of the American Chemical Society. 134: 3396-410. PMID 22200082 DOI: 10.1021/Ja208791F |
0.773 |
|
2011 |
Joyner JC, Reichfield J, Cowan JA. Factors influencing the DNA nuclease activity of iron, cobalt, nickel, and copper chelates. Journal of the American Chemical Society. 133: 15613-26. PMID 21815680 DOI: 10.1021/Ja2052599 |
0.759 |
|
2011 |
Joyner JC, Cowan JA. Targeted cleavage of HIV RRE RNA by Rev-coupled transition metal chelates. Journal of the American Chemical Society. 133: 9912-22. PMID 21585196 DOI: 10.1021/Ja203057Z |
0.774 |
|
2011 |
Qi W, Cowan JA. Structural, Mechanistic and Coordination Chemistry of Relevance to the Biosynthesis of Iron-Sulfur and Related Iron Cofactors. Coordination Chemistry Reviews. 255: 688-699. PMID 21499539 DOI: 10.1016/J.Ccr.2010.10.016 |
0.433 |
|
2011 |
Wu SP, Bellei M, Mansy SS, Battistuzzi G, Sola M, Cowan JA. Redox chemistry of the Schizosaccharomyces pombe ferredoxin electron-transfer domain and influence of Cys to Ser substitutions. Journal of Inorganic Biochemistry. 105: 806-11. PMID 21497579 DOI: 10.1016/J.Jinorgbio.2011.03.004 |
0.745 |
|
2011 |
Qi W, Cowan JA. Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange. Chemical Communications (Cambridge, England). 47: 4989-91. PMID 21437321 DOI: 10.1039/C0Cc05079B |
0.409 |
|
2011 |
Patwardhan A, Cowan JA. Influence of charge and structure on the coordination chemistry of copper aminoglycosides. Dalton Transactions (Cambridge, England : 2003). 40: 1795-801. PMID 21218243 DOI: 10.1039/C0Dt00704H |
0.624 |
|
2010 |
Bellei M, Battistuzzi G, Wu SP, Mansy SS, Cowan JA, Sola M. Control of reduction thermodynamics in [2Fe-2S] ferredoxins Entropy-enthalpy compensation and the influence of surface mutations. Journal of Inorganic Biochemistry. 104: 691-6. PMID 20362339 DOI: 10.1016/J.Jinorgbio.2010.03.001 |
0.724 |
|
2010 |
Luo WI, Dizin E, Yoon T, Cowan JA. Kinetic and structural characterization of human mortalin. Protein Expression and Purification. 72: 75-81. PMID 20152901 DOI: 10.1016/J.Pep.2010.02.003 |
0.729 |
|
2010 |
Kondapalli KC, Bencze KZ, Dizin E, Cowan JA, Stemmler TL. NMR assignments of a stable processing intermediate of human frataxin. Biomolecular Nmr Assignments. 4: 61-4. PMID 20108066 DOI: 10.1007/S12104-010-9209-X |
0.369 |
|
2010 |
Qi W, Cowan JA. A structural and functional homolog supports a general role for frataxin in cellular iron chemistry. Chemical Communications (Cambridge, England). 46: 719-21. PMID 20087498 DOI: 10.1039/B911975B |
0.345 |
|
2009 |
Liu Y, Cowan JA. Iron-sulfur cluster biosynthesis: characterization of a molten globule domain in human NFU. Biochemistry. 48: 7512-8. PMID 19722697 DOI: 10.1021/Bi9002524 |
0.415 |
|
2009 |
Hocharoen L, Cowan JA. Metallotherapeutics: novel strategies in drug design. Chemistry (Weinheim An Der Bergstrasse, Germany). 15: 8670-6. PMID 19685535 DOI: 10.1002/Chem.200900821 |
0.775 |
|
2009 |
Huang J, Cowan JA. Iron-sulfur cluster biosynthesis: role of a semi-conserved histidine. Chemical Communications (Cambridge, England). 3071-3. PMID 19462090 DOI: 10.1039/B902676B |
0.544 |
|
2009 |
Bradford S, Kawarasaki Y, Cowan JA. Copper.Lys-Gly-His-Lys mediated cleavage of tRNA(Phe): studies of reaction mechanism and cleavage specificity. Journal of Inorganic Biochemistry. 103: 871-5. PMID 19386364 DOI: 10.1016/J.Jinorgbio.2009.03.003 |
0.695 |
|
2009 |
Nuth M, Cowan JA. Iron-sulfur cluster biosynthesis: characterization of IscU-IscS complex formation and a structural model for sulfide delivery to the [2Fe-2S] assembly site. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 829-39. PMID 19308466 DOI: 10.1007/S00775-009-0495-7 |
0.736 |
|
2009 |
Liu Y, Qi W, Cowan JA. Iron-sulfur cluster biosynthesis: functional characterization of the N- and C-terminal domains of human NFU. Biochemistry. 48: 973-80. PMID 19146390 DOI: 10.1021/Bi801645Z |
0.394 |
|
2008 |
Huang J, Dizin E, Cowan JA. Mapping iron binding sites on human frataxin: implications for cluster assembly on the ISU Fe-S cluster scaffold protein. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 825-36. PMID 18425540 DOI: 10.1007/S00775-008-0369-4 |
0.565 |
|
2008 |
Gokhale NH, Bradford S, Cowan JA. Catalytic inactivation of human carbonic anhydrase I by a metallopeptide-sulfonamide conjugate is mediated by oxidation of active site residues. Journal of the American Chemical Society. 130: 2388-9. PMID 18251475 DOI: 10.1021/Ja0778038 |
0.687 |
|
2007 |
Liu Y, Cowan JA. Iron sulfur cluster biosynthesis. Human NFU mediates sulfide delivery to ISU in the final step of [2Fe-2S] cluster assembly. Chemical Communications (Cambridge, England). 3192-4. PMID 17653385 DOI: 10.1039/B704928E |
0.421 |
|
2007 |
Gokhale NH, Bradford S, Cowan JA. Stimulation and oxidative catalytic inactivation of thermolysin by copper.Cys-Gly-His-Lys. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 12: 981-7. PMID 17618468 DOI: 10.1007/S00775-007-0270-6 |
0.708 |
|
2007 |
Jin Y, Lewis MA, Gokhale NH, Long EC, Cowan JA. Influence of stereochemistry and redox potentials on the single- and double-strand DNA cleavage efficiency of Cu(II) and Ni(II) Lys-Gly-His-derived ATCUN metallopeptides. Journal of the American Chemical Society. 129: 8353-61. PMID 17552522 DOI: 10.1021/Ja0705083 |
0.351 |
|
2007 |
Bencze KZ, Yoon T, Millán-Pacheco C, Bradley PB, Pastor N, Cowan JA, Stemmler TL. Human frataxin: iron and ferrochelatase binding surface. Chemical Communications (Cambridge, England). 1798-800. PMID 17476391 DOI: 10.1039/B703195E |
0.59 |
|
2007 |
Jin Y, Cowan JA. Cellular activity of Rev response element RNA targeting metallopeptides. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 12: 637-44. PMID 17356872 DOI: 10.1007/S00775-007-0221-2 |
0.345 |
|
2007 |
Yoon T, Dizin E, Cowan JA. N-terminal iron-mediated self-cleavage of human frataxin: regulation of iron binding and complex formation with target proteins. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 12: 535-42. PMID 17285345 DOI: 10.1007/S00775-007-0205-2 |
0.615 |
|
2007 |
Wu SP, Cowan JA. Iron-sulfur cluster stability. Kinetics and mechanism of ligand-promoted cluster degradation. Chemical Communications (Cambridge, England). 82-4. PMID 17279268 DOI: 10.1039/B610665J |
0.579 |
|
2006 |
Chen CA, Cowan JA. Characterization of Saccharomyces cerevisiae Atm1p: functional studies of an ABC7 type transporter. Biochimica Et Biophysica Acta. 1760: 1857-65. PMID 16963188 DOI: 10.1016/j.bbagen.2006.08.002 |
0.44 |
|
2006 |
Gokhale NH, Cowan JA. Metallopeptide-promoted inactivation of angiotensin-converting enzyme and endothelin-converting enzyme 1: Toward dual-action therapeutics. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 937-47. PMID 16874470 DOI: 10.1007/S00775-006-0145-2 |
0.376 |
|
2005 |
Gokhale NH, Cowan JA. Inactivation of human angiotensin converting enzyme by copper peptide complexes containing ATCUN motifs. Chemical Communications (Cambridge, England). 5916-8. PMID 16317474 DOI: 10.1039/B511081E |
0.334 |
|
2005 |
Wu SP, Mansy SS, Cowan JA. Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity. Biochemistry. 44: 4284-93. PMID 15766257 DOI: 10.1021/Bi0483007 |
0.739 |
|
2004 |
Mansy SS, Cowan JA. Iron-sulfur cluster biosynthesis: toward an understanding of cellular machinery and molecular mechanism. Accounts of Chemical Research. 37: 719-25. PMID 15379587 DOI: 10.1021/Ar0301781 |
0.712 |
|
2004 |
Yoon T, Cowan JA. Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. The Journal of Biological Chemistry. 279: 25943-6. PMID 15123683 DOI: 10.1074/Jbc.C400107200 |
0.613 |
|
2004 |
Venturoli G, Mamedov MD, Mansy SS, Musiani F, Strocchi M, Francia F, Semenov AY, Cowan JA, Ciurli S. Electron transfer from HiPIP to the photooxidized tetraheme cytochrome subunit of Allochromatium vinosum reaction center: new insights from site-directed mutagenesis and computational studies. Biochemistry. 43: 437-45. PMID 14717598 DOI: 10.1021/Bi035384V |
0.67 |
|
2004 |
Mansy SS, Wu SP, Cowan JA. Iron-sulfur cluster biosynthesis: biochemical characterization of the conformational dynamics of Thermotoga maritima IscU and the relevance for cellular cluster assembly. The Journal of Biological Chemistry. 279: 10469-75. PMID 14688265 DOI: 10.1074/Jbc.M312051200 |
0.729 |
|
2003 |
Chen CA, Cowan JA. Characterization of the soluble domain of the ABC7 type transporter Atm1. The Journal of Biological Chemistry. 278: 52681-8. PMID 14514697 DOI: 10.1074/Jbc.M306472200 |
0.516 |
|
2003 |
Bertini I, Cowan JA, Del Bianco C, Luchinat C, Mansy SS. Thermotoga maritima IscU. Structural characterization and dynamics of a new class of metallochaperone. Journal of Molecular Biology. 331: 907-24. PMID 12909018 DOI: 10.1016/S0022-2836(03)00768-X |
0.689 |
|
2003 |
Yoon T, Cowan JA. Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. Journal of the American Chemical Society. 125: 6078-84. PMID 12785837 DOI: 10.1021/ja027967i |
0.6 |
|
2003 |
Wu SP, Cowan JA. Iron-sulfur cluster biosynthesis. A comparative kinetic analysis of native and Cys-substituted ISA-mediated [2Fe-2S]2+ cluster transfer to an apoferredoxin target. Biochemistry. 42: 5784-91. PMID 12741836 DOI: 10.1021/Bi026939+ |
0.562 |
|
2003 |
Cowan JA. Bioinorganic Chemistry: A Short Course. Rosette M. Roat-Malone. Hoboken, NJ: Wiley-Interscience, A John Wiley & Sons Inc. Publication, 2002, 366 pp., $89.95, softcover. ISBN 0-471-15976-X. Clinical Chemistry. 49: 1565-1566. DOI: 10.1373/49.9.1565 |
0.344 |
|
2002 |
Nuth M, Yoon T, Cowan JA. Iron-sulfur cluster biosynthesis: characterization of iron nucleation sites for assembly of the [2Fe-2S]2+ cluster core in IscU proteins. Journal of the American Chemical Society. 124: 8774-5. PMID 12137512 DOI: 10.1021/Ja0264596 |
0.771 |
|
2002 |
Chen CA, Cowan JA. In vivo cleavage of a target RNA by copper kanamycin A. Direct observation by a fluorescence assay. Chemical Communications (Cambridge, England). 196-7. PMID 12120364 DOI: 10.1039/B108439A |
0.479 |
|
2002 |
Wu SP, Wu G, Surerus KK, Cowan JA. Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate. Biochemistry. 41: 8876-85. PMID 12102630 DOI: 10.1021/Bi0256781 |
0.578 |
|
2002 |
Battistuzzi G, Borsari M, Cowan JA, Ranieri A, Sola M. Control of cytochrome C redox potential: axial ligation and protein environment effects. Journal of the American Chemical Society. 124: 5315-24. PMID 11996572 DOI: 10.1021/Ja017479V |
0.351 |
|
2002 |
Wu G, Mansy SS, Hemann C, Hille R, Surerus KK, Cowan JA. Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 526-32. PMID 11941510 DOI: 10.1007/S00775-001-0330-2 |
0.702 |
|
2002 |
Wu G, Mansy SS, Wu Sp SP, Surerus KK, Foster MW, Cowan JA. Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe. Biochemistry. 41: 5024-32. PMID 11939799 DOI: 10.1021/Bi016073S |
0.709 |
|
2002 |
Mansy SS, Wu G, Surerus KK, Cowan JA. Iron-sulfur cluster biosynthesis. Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein Journal of Biological Chemistry. 277: 21397-21404. PMID 11934893 DOI: 10.1074/Jbc.M201439200 |
0.677 |
|
2002 |
Mansy SS, Xiong Y, Hemann C, Hille R, Sundaralingam M, Cowan JA. Crystal structure and stability studies of C77S HiPIP: a serine ligated [4Fe-4S] cluster. Biochemistry. 41: 1195-201. PMID 11802718 DOI: 10.1021/Bi011811Y |
0.669 |
|
2001 |
Sau AK, Chen CA, Cowan JA, Mazumdar S, Mitra S. Steady-state and time-resolved fluorescence studies on wild type and mutant chromatium vinosum high potential iron proteins: holo- and apo-forms. Biophysical Journal. 81: 2320-30. PMID 11566801 DOI: 10.1016/S0006-3495(01)75878-X |
0.539 |
|
2001 |
Puapaiboon U, Jai-nhuknan J, Cowan JA. Characterization of a multi-functional metal-mediated nuclease by MALDI-TOF mass spectrometry Nucleic Acids Research. 29: 3652-3656. PMID 11522836 DOI: 10.1093/Nar/29.17.3652 |
0.307 |
|
2001 |
Sreedhara A, Cowan JA. Catalytic hydrolysis of DNA by metal ions and complexes Journal of Biological Inorganic Chemistry. 6: 337-347. PMID 11372193 DOI: 10.1007/S007750100209 |
0.331 |
|
2001 |
Foster MW, Bian S, Surerus KK, Cowan JA. Elucidation of a [4Fe-4S] cluster degradation pathway: Rapid kinetic studies of the degradation of Chromatium vinosum HiPIP Journal of Biological Inorganic Chemistry. 6: 266-274. PMID 11315562 DOI: 10.1007/S007750000196 |
0.424 |
|
2001 |
Sreedhara A, Cowan JA. Targeted site-specific cleavage of HIV-1 viral Rev responsive element by copper aminoglycosides Journal of Biological Inorganic Chemistry. 6: 166-172. PMID 11293410 DOI: 10.1007/S007750000187 |
0.318 |
|
2001 |
Patwardhan A, Cowan JA. Highly specific oxidative damage of double-strand DNA by copper aminoglycosides Chemical Communications. 1490-1491. DOI: 10.1039/B103789G |
0.562 |
|
2000 |
Cowan JA, Ohyama T, Wang D, Natarajan K. Recognition of a cognate RNA aptamer by neomycin B: Quantitative evaluation of hydrogen bonding and electrostatic interactions Nucleic Acids Research. 28: 2935-2942. PMID 10908357 DOI: 10.1093/Nar/28.15.2935 |
0.32 |
|
2000 |
Cowan JA, Ohyama T, Howard K, Rausch JW, Cowan SM, Le Grice SF. Metal-ion stoichiometry of the HIV-1 RT ribonuclease H domain: evidence for two mutually exclusive sites leads to new mechanistic insights on metal-mediated hydrolysis in nucleic acid biochemistry. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 67-74. PMID 10766438 DOI: 10.1007/S007750050009 |
0.343 |
|
2000 |
Sreedhara A, Freed JD, Cowan JA. Efficient inorganic deoxyribonucleases. Greater than 50-million-fold rate enhancement in enzyme-like DNA cleavage Journal of the American Chemical Society. 122: 8814-8824. DOI: 10.1021/Ja994411V |
0.309 |
|
2000 |
Foster MW, Mansy SS, Hwang J, Penner-Hahn JE, Surerus KK, Cowan JA. A mutant human IscU protein contains a stable [2Fe-2S]2+ center of possible functional significance [21] Journal of the American Chemical Society. 122: 6805-6806. DOI: 10.1021/Ja000800+ |
0.662 |
|
2000 |
Chen CA, Chi-Hung L, Cowan JA. Functional role of a conserved tryptophan residue of Chromatium vinosum high potential iron protein Inorganica Chimica Acta. 300: 91-95. DOI: 10.1016/S0020-1693(99)00532-0 |
0.57 |
|
1999 |
Battistuzzi G, Borsari M, Cowan JA, Eicken C, Loschi L, Sola M. Redox chemistry and acid-base equilibria of mitochondrial plant cytochromes c. Biochemistry. 38: 5553-62. PMID 10220343 DOI: 10.1021/Bi982429X |
0.307 |
|
1999 |
Foster MW, Cowan JA. Chemistry of nitric oxide with protein-bound iron sulfur centers. Insights on physiological reactivity Journal of the American Chemical Society. 121: X. DOI: 10.1021/Ja9901056 |
0.433 |
|
1999 |
Bian S, Cowan JA. Protein-bound iron-sulfur centers. Form, function, and assembly Coordination Chemistry Reviews. 190: 1049-1066. DOI: 10.1016/S0010-8545(99)00157-5 |
0.348 |
|
1998 |
Suga H, Cowan JA, Szostak JW. Unusual metal ion catalysis in an acyl-transferase ribozyme. Biochemistry. 37: 10118-25. PMID 9665717 DOI: 10.1021/Bi980432A |
0.528 |
|
1998 |
Natarajan K, Cowan JA. Solution structure of a synthetic lytic peptide: the perforin amino terminus. Chemistry & Biology. 5: 147-54. PMID 9545423 DOI: 10.1016/S1074-5521(98)90059-X |
0.3 |
|
1998 |
Cowan JA. Magnesium activation of nuclease enzymes—the importance of water Inorganica Chimica Acta. 24-27. DOI: 10.1016/S0020-1693(98)00073-5 |
0.342 |
|
1998 |
Black CB, Cowan JA. A critical evaluation of metal-promoted Klenow 3′-5′ exonuclease activity: calorimetric and kinetic analyses support a one-metal-ion mechanism Journal of Biological Inorganic Chemistry. 3: 292-299. DOI: 10.1007/S007750050234 |
0.326 |
|
1997 |
Bertini I, Cowan JA, Luchinat C, Natarajan K, Piccioli M. Characterization of a partially unfolded high potential iron protein. Biochemistry. 36: 9332-9. PMID 9235975 DOI: 10.1021/Bi970810W |
0.404 |
|
1997 |
Black CB, Cowan JA. Inert chromium and cobalt complexes as probes of magnesium-dependent enzymes. Evaluation of the mechanistic role of the essential metal cofactor in Escherichia coli exonuclease III. European Journal of Biochemistry. 243: 684-9. PMID 9057832 DOI: 10.1111/J.1432-1033.1997.00684.X |
0.333 |
|
1997 |
Natarajan K, Cowan JA. Identification of a Key Intermediate of Relevance to Iron−Sulfur Cluster Biosynthesis. Mechanism of Cluster Assembly and Implications for Protein Folding Journal of the American Chemical Society. 119: 4082-4083. DOI: 10.1021/Ja9639729 |
0.348 |
|
1997 |
Cowan JA. Metal-mediated hydrolysis of biological phosphate esters: A critical analysis of the essential metal ion stoichiometry for magnesium-dependent nuclease activation Journal of Biological Inorganic Chemistry. 2: 168-176. DOI: 10.1007/S007750050121 |
0.328 |
|
1996 |
Bian S, Hemann CF, Hille R, Cowan JA. Characterization of an autoreduction pathway for the [Fe4S4]3+ cluster of mutant Chromatium vinosum high-potential iron proteins. Site-directed mutagenesis studies to probe the role of phenylalanine 66 in defining the stability of the [Fe4S4] center provide evidence for oxidative degradation via a [Fe3S4] cluster Biochemistry. 35: 14544-14552. PMID 8931551 DOI: 10.1021/Bi961658L |
0.427 |
|
1996 |
Soriano A, Li D, Bian S, Agarwal A, Cowan JA. Factors influencing redox thermodynamics and electron self-exchange for the [Fe4S4] cluster in Chromatium vinosum high potential iron protein: the role of core aromatic residues in defining cluster redox chemistry. Biochemistry. 35: 12479-86. PMID 8823183 DOI: 10.1021/Bi960974X |
0.428 |
|
1996 |
Agarwal A, Li D, Cowan JA. Influence of Oxygen Ligation on [Fe4S4] Cluster Properties. Characterization of the Cys77Ser Mutant ofChromatium vinosumHiPIP Journal of the American Chemical Society. 118: 927-928. DOI: 10.1021/Ja953447U |
0.303 |
|
1996 |
Li D, Soriano A, Cowan JA. 19F NMR Studies of Fluorine-LabeledChromatium vinosumHigh-Potential Iron Protein† Inorganic Chemistry. 35: 1980-1987. DOI: 10.1021/Ic951159T |
0.341 |
|
1996 |
Soriano A, Cowan J. Phenylalanine 48 of Chromatium vinosum high potential iron protein is essential for stability of the oxidized [Fe4S4] cluster. Site-directed mutagenesis and NMR studies as a probe of cluster chemistry Inorganica Chimica Acta. 251: 285-290. DOI: 10.1016/S0020-1693(96)05281-4 |
0.421 |
|
1996 |
Man Lui S, Cowan J. Optical and EPR characterization of Desulfovibrio vulgaris (Hildenborough) sulfite reductase and ligand adducts Inorganica Chimica Acta. 242: 25-30. DOI: 10.1016/0020-1693(95)04845-6 |
0.322 |
|
1996 |
Aono S, Bertini I, Cowan JA, Luchinat C, Rosato A, Viezzoli MS. 1H NMR studies of the Fe7S8 ferredoxin from Bacillus schlegelii: a further attempt to understand Fe3S4 clusters Jbic Journal of Biological Inorganic Chemistry. 1: 523-528. DOI: 10.1007/S007750050087 |
0.359 |
|
1996 |
Ohyama T, Cowan JA. Influence of monovalent cations on magnesium binding to poly-RNA by solution titration calorimetry: an analysis of the salt dependence of binding enthalpies and entropies Journal of Biological Inorganic Chemistry. 1: 111-116. DOI: 10.1007/S007750050029 |
0.309 |
|
1995 |
Agarwal A, Li D, Cowan JA. Role of aromatic residues in stabilization of the [Fe4S4] cluster in high-potential iron proteins (HiPIPs): physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP. Proceedings of the National Academy of Sciences of the United States of America. 92: 9440-4. PMID 7568150 DOI: 10.1073/Pnas.92.21.9440 |
0.385 |
|
1994 |
Huang HW, Cowan JA. Metallobiochemistry of the magnesium ion - Characterization of the essential metal-binding site in Escherichia coli ribonuclease H European Journal of Biochemistry. 219: 253-260. PMID 8306992 DOI: 10.1111/J.1432-1033.1994.Tb19936.X |
0.359 |
|
1994 |
Wolfe BM, Lui SM, Cowan JA. Desulfoviridin, a multimeric-dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Purification, characterization, kinetics and EPR studies European Journal of Biochemistry. 223: 79-89. PMID 8033912 DOI: 10.1111/J.1432-1033.1994.Tb18968.X |
0.361 |
|
1993 |
Agarwal A, Tan J, Eren M, Tevelev A, Lui SM, Cowan JA. Synthesis, Cloning and Expression of a Synthetic Gene for High Potential Iron Protein from Chromatium vinosum Biochemical and Biophysical Research Communications. 197: 1357-1362. PMID 7916611 DOI: 10.1006/Bbrc.1993.2626 |
0.345 |
|
1993 |
Cowan JA. Metallobiochemistry of RNA. Co(NH3)6(3+) as a probe for Mg2+(aq) binding sites. Journal of Inorganic Biochemistry. 49: 171-5. PMID 7679435 DOI: 10.1016/0162-0134(93)80002-Q |
0.341 |
|
1993 |
Lui SM, Soriano A, Cowan JA. Enzymic reduction of inorganic anions. Pre-steady-state kinetic analysis of the dissimilatory sulfite reductase (desulfoviridin) from Desulfovibrio vulgaris (Hildenborough). Mechanistic implications Journal of the American Chemical Society. 115: 10483-10486. DOI: 10.1021/Ja00076A003 |
0.307 |
|
1992 |
Sola M, Cowan JA. Assignment of heme resonances in the 1H NMR spectrum of oxidized Desulfovibrio vulgaris (Hildenborough) cytochrome c3 Inorganica Chimica Acta. 202: 241-251. DOI: 10.1016/S0020-1693(00)86841-3 |
0.326 |
|
1991 |
Tan J, Cowan JA. Enzymatic redox chemistry: a proposed reaction pathway for the six-electron reduction of SO3(2-) to S2- by the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Biochemistry. 30: 8910-7. PMID 1888748 DOI: 10.1021/Bi00100A027 |
0.362 |
|
1991 |
Reid SS, Cowan JA. Metallobiochemistry of a ribosomal RNA. A possible role for Na+ and K+ in the regulation of Mg2+ binding sites on Escherichia coli 5S rRNA : implications for activity Journal of the American Chemical Society. 113: 673-675. DOI: 10.1021/Ja00002A045 |
0.317 |
|
1991 |
Borsari M, Sola M, Cowan JA. Polarographic studies of Chromatium vinosum high-potential iron protein Bioelectrochemistry and Bioenergetics. 26: 123-129. DOI: 10.1016/0302-4598(91)87039-J |
0.349 |
|
1990 |
Cowan JA, Sola M. 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements. Biochemistry. 29: 5633-7. PMID 2386791 DOI: 10.1021/Bi00475A031 |
0.313 |
|
1990 |
Reid SS, Cowan JA. Biostructural chemistry of magnesium ion: characterization of the weak binding sites on tRNA(Phe)(yeast). Implications for conformational change and activity. Biochemistry. 29: 6025-32. PMID 2383570 DOI: 10.1021/Bi00477A021 |
0.322 |
|
1989 |
Sola M, Cowan JA, Gray HB. 1H NMR characterization of Chromatium gracile high-potential iron protein and its ruthenium-modified derivatives. Modulation of the reduction potentials in low- and high-potential [Fe4S4] ferredoxins. Biochemistry. 28: 5261-8. PMID 2765533 DOI: 10.1021/Bi00438A051 |
0.452 |
|
1988 |
Cowan JA, Upmacis RK, Beratan DN, Onuchic JN, Gray HB. Long-range electron transfer in myoglobin. Annals of the New York Academy of Sciences. 550: 68-84. PMID 3245652 DOI: 10.1111/J.1749-6632.1988.Tb35324.X |
0.323 |
|
1986 |
Cowan JA, Sanders JK. Reductive demetallation of porphyrins: Evidence for peripheral and axial modes of reduction Tetrahedron Letters. 27: 1201-1204. DOI: 10.1016/S0040-4039(00)84216-1 |
0.485 |
|
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