Zobrazeno 1 - 10 of 88 pro vyhledávání: '"J.L. McKimm-Breschkin"'
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Structural characterization of respiratory syncytial virus fusion inhibitor escape mutants: homology model of the F protein and a syncytium formation assay
Autor: Angela Luttick, Lynne J. Lawrence, Melinda Lowe, Bo Lin, Michael W. Parker, Jayne Sullivan, Rachel Cameron, Michael J. Smout, J.L. McKimm-Breschkin, Jane Ryan, Craig J. Morton, Simon P. Tucker, Paul R. Young, Anthony J. Mason
Publikováno v: Virology. 311:275-288
Respiratory syncytial virus (RSV) is a ubiquitous human pathogen and the leading cause of lower respiratory tract infections in infants. Infection of cells and subsequent formation of syncytia occur through membrane fusion mediated by the RSV fusion
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cce35eadcad8ca5ed073038bd32fd79
https://doi.org/10.1016/s0042-6822(03)00115-6
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2
The Structure of the Fusion Glycoprotein of Newcastle Disease Virus Suggests a Novel Paradigm for the Molecular Mechanism of Membrane Fusion
Autor: P.A. Tulloch, Brian J. Smith, Lynne J. Lawrence, J.L. McKimm-Breschkin, Jeffrey J Gorman, Peter M. Colman, Michael C. Lawrence, Lin Chen
Publikováno v: Structure. 9(3):255-266
Background: Membrane fusion within the Paramyxoviridae family of viruses is mediated by a surface glycoprotein termed the "F", or fusion, protein. Membrane fusion is assumed to involve a series of structural transitions of F from a metastable (prefus
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::766a2e7302964c5b9500f9b2d17b4992
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3
Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases
Autor: Peter M. Colman, Anjali Sahasrabudhe, Joseph N. Varghese, Tony J. Blick, J.L. McKimm-Breschkin, A. Van Donkelaar
Publikováno v: Proceedings of the National Academy of Sciences. 94:11808-11812
The x-ray structure of a complex of sialic acid (Neu5Ac) with neuraminidase N9 subtype from A/tern/Australia/G70C/75 influenza virus at 4°C has revealed the location of a second Neu5Ac binding site on the surface of the enzyme. At 18°C, only the en
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdb464a5a6418ee74f92ed94616abb90
https://doi.org/10.1073/pnas.94.22.11808
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4
Mutation in the Influenza Virus Neuraminidase Gene Resulting in Decreased Sensitivity to the Neuraminidase Inhibitor 4-Guanidino-Neu5Ac2en Leads to Instability of the Enzyme
Autor: Peter M. Colman, Tony J. Blick, Mandy McDonald, J.L. McKimm-Breschkin
Publikováno v: Virology. 225:240-242
We previously isolated a variant of the influenza virus NWS/G70C, with a decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu5Ac2en in vitro, which has a mutation in one of the conserved residues of the neuraminidase Glu 119
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da16ff70cc2f06b3684acf19e58b92f7
https://doi.org/10.1006/viro.1996.0595
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5
Affinity ranking of influenza neuraminidase mutants with monoclonal antibodies using an optical biosensor. Comparison with ELISA and slot blot assays
Autor: E.C. Nice, J.B. Caldwell, L.C. Gruen, J.L. McKimm-Breschkin
Publikováno v: Journal of immunological methods. 168(1)
A recently developed alternative to the more traditional techniques for studying antigen-antibody interactions has been examined. This method involves the use of an optical biosensor employing surface plasmon resonance detection. In this system one o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8be3742949d2acba4532000db5fbdb57
https://pubmed.ncbi.nlm.nih.gov/8288899
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6
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