James C. Paulson
Affiliations: | Immunology & Microbiology | Scripps Research Institute, La Jolla, La Jolla, CA, United States |
Website:
http://www.scripps.edu/paulson/paulson.cv.htmlGoogle:
"James Paulson"Bio:
http://hdl.handle.net/2142/64192
DOI: 10.1083/jcb.67.2.461
https://pdfs.semanticscholar.org/8afe/88e971a0034e41247f1dc547106648080312.pdf
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Parents
Sign in to add mentorWilliam Owen McClure | grad student | 1974 | UIUC | |
(Detection and Quantitation of Drug-Induced Inhibition of Rapid Axoplasmic Transport: Microtubules and Axoplasmic Transport.) | ||||
Robert L. Hill | post-doc | 1974-1978 | Duke |
Children
Sign in to add traineeCory D. Rillahan | grad student | 2012 | Scripps Institute |
Corwin M. Nycholat | post-doc | 2008-2011 | Scripps Institute |
Robert P de Vries | post-doc | 2012-2014 | TSRI |
Landon J Edgar | post-doc | 2016-2021 | The Scripps Research Institute, California, USA |
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Publications
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Santos JJS, Wang S, McBride R, et al. (2025) Bovine H5N1 binds poorly to human-type sialic acid receptors. Nature. 640: E18-E20 |
Lin TH, Zhu X, Wang S, et al. (2024) A single mutation in bovine influenza H5N1 hemagglutinin switches specificity to human receptors. Science (New York, N.Y.). 386: 1128-1134 |
Huang K, Bashian EE, Zong G, et al. (2024) Chemoenzymatic Synthesis of Sulfated -Glycans Recognized by Siglecs and Other Glycan-Binding Proteins. Jacs Au. 4: 2966-2978 |
Santos JJS, Wang S, McBride R, et al. (2024) Bovine H5N1 influenza virus binds poorly to human-type sialic acid receptors. Biorxiv : the Preprint Server For Biology |
Atxabal U, Fernández A, Moure MJ, et al. (2024) Quantifying Siglec-sialylated ligand interactions: a versatile F-T CPMG filtered competitive NMR displacement assay. Chemical Science. 15: 10612-10624 |
Lei R, Liang W, Ouyang WO, et al. (2024) Epistasis mediates the evolution of the receptor binding mode in recent human H3N2 hemagglutinin. Nature Communications. 15: 5175 |
Atxabal U, Nycholat C, Pröpster JM, et al. (2024) Unraveling Molecular Recognition of Glycan Ligands by Siglec-9 via NMR Spectroscopy and Molecular Dynamics Modeling. Acs Chemical Biology |
Thompson AJ, Wu NC, Canales A, et al. (2024) Evolution of human H3N2 influenza virus receptor specificity has substantially expanded the receptor-binding domain site. Cell Host & Microbe |
Kikuchi C, Antonopoulos A, Wang S, et al. (2023) Glyco-engineered MDCK cells display preferred receptors of H3N2 influenza absent in eggs used for vaccines. Nature Communications. 14: 6178 |
Canales A, Sastre J, Orduña JM, et al. (2023) Revealing the Specificity of Human H1 Influenza A Viruses to Complex -Glycans. Jacs Au. 3: 868-878 |