Výsledky vyhledávání - "Travis Nieusma"

Akademický článek

Small Molecule Microcrystal Electron Diffraction for the Pharmaceutical Industry–Lessons Learned From Examining Over Fifty Samples

Publikováno v: Frontiers in Molecular Biosciences, Vol 8 (2021)

The emerging field of microcrystal electron diffraction (MicroED) is of great interest to industrial researchers working in the drug discovery and drug development space. The promise of being able to routinely solve high-resolution crystal structures

Externí odkaz: https://doaj.org/article/4e8f74f2a00c436abdbb1fc0f9db7a2d

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Akademický článek

A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA

Autor: Sandhya Bangaru, Heng Zhang, Iuliia M. Gilchuk, Thomas G. Voss, Ryan P. Irving, Pavlo Gilchuk, Pranathi Matta, Xueyong Zhu, Shanshan Lang, Travis Nieusma, Juergen A. Richt, Randy A. Albrecht, Hillary A. Vanderven, Robin Bombardi, Stephen J. Kent, Andrew B. Ward, Ian A. Wilson, James E. Crowe

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)

Broadly neutralizing antibodies are potential therapeutics and can aid rational vaccine development. Here, the authors show that the human monoclonal antibody H3v-47 recognizes a highly conserved epitope in HA of H3N2 viruses, inhibits virus replicat

Externí odkaz: https://doaj.org/article/ed7f5c4471db479d99f688c74abaa776

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Akademický článek

A Computationally Designed Hemagglutinin Stem-Binding Protein Provides In Vivo Protection from Influenza Independent of a Host Immune Response.

Autor: Merika Treants Koday, Jorgen Nelson, Aaron Chevalier, Michael Koday, Hannah Kalinoski, Lance Stewart, Lauren Carter, Travis Nieusma, Peter S Lee, Andrew B Ward, Ian A Wilson, Ashley Dagley, Donald F Smee, David Baker, Deborah Heydenburg Fuller

Publikováno v: PLoS Pathogens, Vol 12, Iss 2, p e1005409 (2016)

Broadly neutralizing antibodies targeting a highly conserved region in the hemagglutinin (HA) stem protect against influenza infection. Here, we investigate the protective efficacy of a protein (HB36.6) computationally designed to bind with high affi

Externí odkaz: https://doaj.org/article/fd1ee080cfd1498393ace6eeda4b5e3c

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A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA

Autor: Ryan P. Irving, Robin G. Bombardi, Randy A. Albrecht, Ian A. Wilson, Sandhya Bangaru, Shanshan Lang, Heng Zhang, Hillary A. Vanderven, Pavlo Gilchuk, Iuliia M. Gilchuk, Stephen J. Kent, Travis Nieusma, Pranathi Matta, James E. Crowe, Thomas G. Voss, Xueyong Zhu, Juergen A. Richt, Andrew B. Ward

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Nature Communications

The high rate of antigenic drift in seasonal influenza viruses necessitates frequent changes in vaccine composition. Recent seasonal H3 vaccines do not protect against swine-origin H3N2 variant (H3N2v) strains that recently have caused severe human i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7b25d168b923eb482e8c9e2486e0d3c
http://link.springer.com/article/10.1038/s41467-018-04704-9

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Computational design of trimeric influenza-neutralizing proteins targeting the hemagglutinin receptor binding site

Publikováno v: Nature biotechnology

Many viral surface glycoproteins and cell surface receptors are homo-oligomers1-4, and hence can potentially be targeted by geometrically matched homo-oligomers that engage all subunits simultaneously to attain high avidity and/or lock subunits toget

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d8d7f1631b78fd47df0e19759fad522
https://doi.org/10.1038/nbt.3907

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Structural flexibility at a major conserved antibody target on hepatitis C virus E2 antigen

Autor: Sheng Li, Tong Liu, David E. Lee, Rameshwar U. Kadam, Virgil L. Woods, Andrew B. Ward, Erick Giang, Travis Nieusma, Fernando Garces, Mansun Law, Leopold Kong, Netanel Tzarum, Ian A. Wilson

Publikováno v: Proceedings of the National Academy of Sciences. 113:12768-12773

Hepatitis C virus (HCV) is a major cause of liver disease, affecting over 2% of the world's population. The HCV envelope glycoproteins E1 and E2 mediate viral entry, with E2 being the main target of neutralizing antibody responses. Structural investi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59467057f3813943c57f29d6770347d3
https://doi.org/10.1073/pnas.1609780113

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Structure of Hepatitis C Virus Envelope Glycoprotein E1 Antigenic Site 314–324 in Complex with Antibody IGH526

Autor: Rameshwar U. Kadam, Leopold Kong, Robyn L. Stanfield, Jeffrey C. Culhane, Travis Nieusma, Erick Giang, Mansun Law, Philip E. Dawson, Tinashe B. Ruwona, Ian A. Wilson

Publikováno v: Journal of Molecular Biology. 427:2617-2628

Hepatitis C virus (HCV) is a positive-strand RNA virus within the Flaviviridae family. The viral "spike" of HCV is formed by two envelope glycoproteins, E1 and E2, which together mediate viral entry by engaging host receptors and undergoing conformat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1742a629c35018711ad15ad306d4d97f
https://doi.org/10.1016/j.jmb.2015.06.012

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