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Paolo Rossi
Researcher at Rutgers University
Publications - 48
Citations - 2863
Paolo Rossi is an academic researcher from Rutgers University. The author has contributed to research in topics: Structural genomics & Protein structure. The author has an hindex of 23, co-authored 48 publications receiving 2658 citations. Previous affiliations of Paolo Rossi include Center for Advanced Biotechnology and Medicine & University of Nebraska–Lincoln.
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Journal ArticleDOI
Consistent blind protein structure generation from NMR chemical shift data
Yang Shen,Oliver F. Lange,Frank Delaglio,Paolo Rossi,James M. Aramini,Gaohua Liu,Alexander Eletsky,Yibing Wu,Kiran Kumar Singarapu,Alexander Lemak,Alexandr Ignatchenko,Cheryl H. Arrowsmith,Thomas Szyperski,Gaetano T. Montelione,David Baker,Ad Bax +15 more
TL;DR: The chemical shift based structure determination protocol uses an empirically optimized procedure to select protein fragments from the Protein Data Bank, in conjunction with the standard ROSETTA Monte Carlo assembly and relaxation methods, and potentially provides a new direction for high-throughput NMR structure determination.
Journal ArticleDOI
NMR Structure Determination for Larger Proteins Using Backbone-Only Data
Srivatsan Raman,Oliver F. Lange,Paolo Rossi,Michael D. Tyka,Xu Wang,James M. Aramini,Gaohua Liu,Theresa Ramelot,Alexander Eletsky,Thomas Szyperski,Michael A. Kennedy,James H. Prestegard,Gaetano T. Montelione,David Baker,David Baker +14 more
TL;DR: It is shown that structures can be accurately determined without nuclear magnetic resonance (NMR) information on the side chains for proteins up to 25 kilodaltons by incorporating backbone chemical shifts, residual dipolar couplings, and amide proton distances into the Rosetta protein structure modeling methodology.
Journal ArticleDOI
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
Tomohide Saio,Xiao Guan,Paolo Rossi,Anastassios Economou,Anastassios Economou,Charalampos G. Kalodimos +5 more
TL;DR: The structural data reveal a multivalent binding mechanism between the chaperone and its protein substrate that enables chaperones to function as holdases and unfoldases by exerting forces to retain proteins in the unfolded state and at the same time protect them from aggregation by shielding their exposed hydrophobic regions.
Journal ArticleDOI
Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples
Oliver F. Lange,Paolo Rossi,Nikolaos G. Sgourakis,Yifan Song,H. Lee,James M. Aramini,Asli Ertekin,Rong Xiao,Thomas Acton,Gaetano T. Montelione,Gaetano T. Montelione,David Baker +11 more
TL;DR: The incorporation of sparse distance restraints into RASREC Rosetta allows routine determination of high-quality solution NMR structures for proteins up to 40 kDa, and should be broadly useful in structural biology.
Journal ArticleDOI
The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium
Rong Xiao,Stephen Anderson,James M. Aramini,R.L. Belote,W.A. Buchwald,Colleen Ciccosanti,Ken Conover,John K. Everett,Keith Hamilton,Yuanpeng J. Huang,Haleema Janjua,Mei Jiang,G. Kornhaber,D. Lee,Jessica Y. Locke,Li Chung Ma,Melissa Maglaqui,Lei Mao,Saheli Mitra,Dayaban Patel,Paolo Rossi,Seema Sahdev,Seema Sharma,Ritu Shastry,G. V. T. Swapna,Saichu N. Tong,Dongyan Wang,Huang Wang,Li Zhao,Gaetano T. Montelione,Thomas Acton +30 more
TL;DR: The core Protein Production Platform of the Northeast Structural Genomics Consortium (NESG) is described and the strategies used for producing high-quality protein samples are outlined, centered on the cloning, expression and purification of 6X-His-tagged proteins using T7-based Escherichia coli systems.