J
James C. Paulson
Researcher at Scripps Research Institute
Publications - 460
Citations - 56432
James C. Paulson is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Sialic acid & Glycan. The author has an hindex of 126, co-authored 443 publications receiving 52152 citations. Previous affiliations of James C. Paulson include University of California, Los Angeles & Pasteur Institute.
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Journal ArticleDOI
Siglecs and their roles in the immune system
TL;DR: The postulated functions of the recently discovered CD33-related Siglecs are discussed and the factors that seem to be driving their rapid evolution are considered.
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ELAM-1 mediates cell adhesion by recognition of a carbohydrate ligand, sialyl-Lex
M. L. Phillips,Edward Nudelman,Federico C. A. Gaeta,Perez Mary S,A. K. Singhal,Sen-itiroh Hakomori,James C. Paulson,James C. Paulson +7 more
TL;DR: Cell adhesion by ELAM-1 is shown to be mediated by a carbohydrate ligand, sialyl-Lewis X (SLex; NeuAc alpha 2,3Gal beta 1,4(Fuc alpha 1,3)-GlcNAc-), a terminal structure found on cell-surface glycoprotein and glycolipid carbohydrate groups of neutrophils.
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New world bats harbor diverse influenza A viruses.
Suxiang Tong,Xueyong Zhu,Yan Li,Mang Shi,Jing Zhang,Melissa Bourgeois,Hua Yang,Xianfeng Chen,Sergio Recuenco,Jorge Gomez,Li-Mei Chen,Adam Johnson,Ying Tao,C. Dreyfus,Wenli Yu,Ryan McBride,Paul J. Carney,Amy T. Gilbert,Jessie Chang,Zhu Guo,Charles T. Davis,James C. Paulson,James Stevens,Charles E. Rupprecht,Charles E. Rupprecht,Edward C. Holmes,Edward C. Holmes,Ian A. Wilson,Ruben O. Donis +28 more
TL;DR: Using consensus degenerate RT-PCR, a novel influenza A virus is identified in a flat-faced fruit bat from Peru, indicating that bats constitute a potentially important and likely ancient reservoir for a diverse pool of influenza viruses.
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Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
William I. Weis,Jerry H. Brown,Stephen Cusack,Stephen Cusack,James C. Paulson,John J. Skehel,Don C. Wiley +6 more
TL;DR: The three-dimensional structures of influenza virus haemagglutinins complexed with cell receptor analogues show sialic acids bound to a pocket of conserved amino acids surrounded by antibody-binding sites, suggesting that antibodies neutralize virus infectivity by preventing virus-to-cell binding.
Journal ArticleDOI
Printed covalent glycan array for ligand profiling of diverse glycan binding proteins
Ola Blixt,Steve Head,Tony S. Mondala,Christopher N. Scanlan,Margaret E. Huflejt,Richard Alvarez,Marian C. Bryan,Fabio Fazio,Daniel A. Calarese,James Stevens,Nahid Razi,D.J. Stevens,John J. Skehel,Irma van Die,Dennis R. Burton,Ian A. Wilson,Richard D. Cummings,Nicolai V. Bovin,Chi-Huey Wong,James C. Paulson +19 more
TL;DR: A glycan microarray constructed by using standard robotic microarray printing technology to couple amine functionalized glycans to an amino-reactive glass slide has remarkable utility for profiling the specificity of a diverse range of glycan binding proteins.