Jeffrey T. Rubino, Ph.D. - Publications
Affiliations: | 2010 | Chemistry | Duke University, Durham, NC |
Area:
metal ion coordination in biological systemsYear | Citation | Score | |||
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2013 | Cafardi V, Biagini M, Martinelli M, Leuzzi R, Rubino JT, Cantini F, Norais N, Scarselli M, Serruto D, Unnikrishnan M. Identification of a novel zinc metalloprotease through a global analysis of Clostridium difficile extracellular proteins. Plos One. 8: e81306. PMID 24303041 DOI: 10.1371/journal.pone.0081306 | 0.312 | |||
2013 | Banci L, Cantini F, Kozyreva T, Rubino JT. Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants. Chembiochem : a European Journal of Chemical Biology. 14: 1839-44. PMID 23625804 DOI: 10.1002/Cbic.201300042 | 0.33 | |||
2012 | Rubino JT, Franz KJ. Coordination chemistry of copper proteins: how nature handles a toxic cargo for essential function. Journal of Inorganic Biochemistry. 107: 129-43. PMID 22204943 DOI: 10.1016/J.Jinorgbio.2011.11.024 | 0.592 | |||
2011 | Rubino JT, Chenkin MP, Keller M, Riggs-Gelasco P, Franz KJ. A comparison of methionine, histidine and cysteine in copper(I)-binding peptides reveals differences relevant to copper uptake by organisms in diverse environments. Metallomics : Integrated Biometal Science. 3: 61-73. PMID 21553704 DOI: 10.1039/c0mt00044b | 0.694 | |||
2011 | Rubino JT, Chenkin MP, Keller M, Riggs-Gelasco P, Franz KJ. A comparison of methionine, histidine and cysteine in copper(I)-binding peptides reveals differences relevant to copper uptake by organisms in diverse environments. Metallomics : Integrated Biometal Science. 3: 61-73. PMID 21305075 DOI: 10.1039/C0Mt00044B | 0.655 | |||
2010 | Rubino JT, Riggs-Gelasco P, Franz KJ. Methionine motifs of copper transport proteins provide general and flexible thioether-only binding sites for Cu(I) and Ag(I). Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 15: 1033-49. PMID 20437064 DOI: 10.1007/S00775-010-0663-9 | 0.649 | |||
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