Research Topics
| Benjamin W NeumanSummaryAffiliation: The Scripps Research Institute Country: USA Publications
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Detail Information
Publications
Antisense morpholino-oligomers directed against the 5' end of the genome inhibit coronavirus proliferation and growthBenjamin W Neuman
The Scripps Research Institute, Department of Neuropharmacology, Division of Virology, 10550 North Torrey Pines Rd, La Jolla, CA 92037, USA
J Virol 78:5891-9. 2004..These results suggest that this composition of antisense compound has therapeutic potential for control of coronavirus infection...- Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysisBenjamin W Neuman
Department of Neuropharmacology, The Scripps Research Institute, 10550 N Torrey Pines Rd, La Jolla, CA 92037, USA
J Virol 79:3822-30. 2005..The structural proteins of retroviruses and arenaviruses assemble with similar radial density distributions, using common cellular components... - Inhibition, escape, and attenuated growth of severe acute respiratory syndrome coronavirus treated with antisense morpholino oligomersBenjamin W Neuman
The Scripps Research Institute, Division of Virology, Department of Neuropharmacology, La Jolla, CA 92037, USA
J Virol 79:9665-76. 2005..Those partially resistant viruses grew more slowly and formed smaller plaques than wild-type SARS-CoV. These results suggest PMO compounds have powerful therapeutic and investigative potential toward coronavirus infection... - Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopyBenjamin W Neuman
Department of Molecular and Integrative Neuroscience, The Scripps Research Institute, 10550 N Torrey Pines Rd, La Jolla, CA 92037, USA
J Virol 80:7918-28. 2006..Our results contribute to the understanding of the assembly pathway used by coronaviruses and other pleomorphic viruses and provide the first detailed view of coronavirus ultrastructure... - Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3Pedro Serrano
Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd, MB 44, La Jolla, CA 92037, USA
J Virol 83:12998-3008. 2009..This binding site is similar to the ssRNA-binding site of the sterile alpha motif domain of the Saccharomyces cerevisiae Vts1p protein, although the two proteins do not share a common globular fold... - Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirusPedro Serrano
Department of Molecular Biology, MB 44, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
J Virol 81:12049-60. 2007..Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence... - Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain foldAmarnath Chatterjee
Department of Molecular Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
J Virol 83:1823-36. 2009..The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection... - Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N proteinKumar Singh Saikatendu
Department of Cell Biology, 10550 N Torrey Pines Rd, CB265, The Scripps Research Institute, La Jolla, CA 92037, USA
J Virol 81:3913-21. 2007.... - SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA bindingMargaret A Johnson
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
J Mol Biol 400:724-42. 2010..Overall, the present data provide evidence for molecular mechanisms involving the concerted actions of SUD-M and SUD-C, which result in specific RNA binding that might be unique to the SUD and, thus, to the SARS coronavirus... 
Ultrastructure of SARS-CoV, FIPV, and MHV revealed by electron cryomicroscopyBenjamin W Neuman
The Scripps Research Institute, La Jolla, California, USA
Adv Exp Med Biol 581:181-5. 2006- Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switchJeremiah S Joseph
Department of Cell Biology, 10550 N Torrey Pines Road, CB265, The Scripps Research Institute, La Jolla, CA 92037, USA
J Virol 81:6700-8. 2007.... - Inhibition and escape of SARS-CoV treated with antisense morpholino oligomersBenjamin W Neuman
The Scripps Research Institute, La Jolla, California, USA
Adv Exp Med Biol 581:567-71. 2006 - Antiviral effects of antisense morpholino oligomers in murine coronavirus infection modelsRenaud Burrer
The Scripps Research Institute, Department of Molecular and Integrative Neurosciences, Mail Drop SP30 2020, 10550 N Torrey Pines Rd, La Jolla, CA 92037, USA
J Virol 81:5637-48. 2007..However, the strong antiviral effect observed suggests that with further development, P-PMO may provide an effective therapeutic approach against a broad range of coronavirus infections... - Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3Benjamin W Neuman
Molecular and Integrative Neurosciences Department, Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 N Torrey Pines Road, La Jolla, California 92037, USA
J Virol 82:5279-94. 2008..Overall, the ensemble of data surveyed here paint a more complete picture of nsp3 as a conserved component of the viral protein processing machinery, which is intimately associated with viral RNA in its role as a virion component... - Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifsJeremiah S Joseph
Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA
J Virol 80:7894-901. 2006..It is possible that nsp10 functions within a larger RNA-binding protein complex. However, its exact role within the replicase complex is still not clear... - Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3Kumar Singh Saikatendu
Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Structure 13:1665-75. 2005..Sequence and structure comparison of all known macro-H2A domains combined with available functional data suggests that proteins of this superfamily form an emerging group of nucleotide phosphatases that dephosphorylate Appr-1''-p... 
Purification and electron cryomicroscopy of coronavirus particlesBenjamin W Neuman
The Scripps Research Institute, La Jolla, CA, USA
Methods Mol Biol 454:129-36. 2008..Two virus purification procedures are described...- Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domainsApril A Saunders
The Scripps Research Institute, Molecular and Integrative Neurosciences Department, Mailstop SP30 2020, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA
J Virol 81:5649-57. 2007.... - Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7Wolfgang Peti
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
J Virol 79:12905-13. 2005..Each of these three areas is thus implicated as a potential site for protein-protein interactions...