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Christopher M. Barbieri
Researcher at Rutgers University
Publications - 5
Citations - 143
Christopher M. Barbieri is an academic researcher from Rutgers University. The author has contributed to research in topics: Aminoglycoside & Replication protein A. The author has an hindex of 5, co-authored 5 publications receiving 138 citations.
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Journal ArticleDOI
Differential Selectivity of Natural and Synthetic Aminoglycosides towards the Eukaryotic and Prokaryotic Decoding A Sites.
Jiro Kondo,Mariana Hainrichson,Igor Nudelman,Dalia Shallom-Shezifi,Christopher M. Barbieri,Daniel S. Pilch,Eric Westhof,Timor Baasov +7 more
TL;DR: This work has used a combination of biochemical and structural analysis to compare and contrast the molecular mechanisms of action and the structure–activity relationships of a new synthetic aminoglycoside, NB33, and a structurally similar natural aminglycoside apramycin, and demonstrates the general molecular principles that determine the decreased selectivity of apramYcin for the prokaryotic decoding site, and the increased selectivity for NB33.
Journal ArticleDOI
A hybrid NMR/SAXS-based approach for discriminating oligomeric protein interfaces using Rosetta
Paolo Rossi,Lei Shi,Gaohua Liu,Christopher M. Barbieri,H. Lee,Thomas D. Grant,Joseph R. Luft,Rong Xiao,Thomas Acton,Edward H. Snell,Gaetano T. Montelione,David Baker,Oliver F. Lange,Nikolaos G. Sgourakis +13 more
TL;DR: This work highlights a new approach for studying minor conformational changes due to structural plasticity within a single dimeric interface in solution, and uses sparse data to limit conformational search during optimization of a physically realistic energy function.
A hybrid NMR/SAXS-based approach for discriminating oligomeric protein interfaces
Paolo Rossi,Lei Shi,Gaohua Liu,Christopher M. Barbieri,Hsiau-Wei Lee,Thomas D. Grant,Joseph R. Luft,Rong Xiao,Thomas Acton,Edward H. Snell,Gaetano T. Montelione,David Baker,Oliver F. Lange,Nikolaos G. Sgourakis +13 more
TL;DR: In this paper, the authors focus on a member of the bet-V1 superfamily, Aha1 from Colwellia psychrerythraea, and highlight a new approach for studying minor conformational changes due to structural plasticity within a single dimeric interface in solution.
Journal ArticleDOI
Structures of apo- and ssDNA-bound YdbC from Lactococcus lactis uncover the function of protein domain family DUF2128 and expand the single-stranded DNA-binding domain proteome.
Paolo Rossi,Christopher M. Barbieri,James M. Aramini,Elisabetta Bini,Hsiau-Wei Lee,Haleema Janjua,Rong Xiao,Thomas Acton,Gaetano T. Montelione +8 more
TL;DR: The molecular function of protein domain family domain of unknown function DUF2128 (PF09901) as a novel ss DNA binding domain is uncovered and this bacterial domain strongly associates into a dimer and presents a highly positively charged surface that is consistent with its function in non-specific ssDNA binding.