Zobrazeno 1 - 10
of 15
pro vyhledávání: '"L. J. Calder"'
Publikováno v:
Virology. 257:415-423
In influenza infections, haemagglutinin (HA) mediates the fusion of virus and cellular membranes at endosomal pH, between pH 5 and 6. In vitro , when reconstituted into virosomes, efficient fusion requires target membranes to contain sialic acid rece
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40ffea2e12b5a3d5f05be8fc1d46b580
https://doi.org/10.1006/viro.1999.9624
https://doi.org/10.1006/viro.1999.9624
Autor:
Don C. Wiley, Andréa Dessen, Stephen C. Harrison, John J. Skehel, Winfried Weissenhorn, L. J. Calder
Publikováno v:
Molecular Membrane Biology. 16:3-9
Enveloped viruses such as HIV-1, influenza virus, and Ebola virus express a surface glycoprotein that mediates both cell attachment and fusion of viral and cellular membranes. The membrane fusion process leads to the release of viral proteins and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d2340b0ac0c98b6c4b5278f37267da4
https://doi.org/10.1080/096876899294706
https://doi.org/10.1080/096876899294706
Autor:
S Wharton, B Barrere, Walter Fiers, Willy Min Jou, Peter Vanlandschoot, B Millar, Els Beirnaert, L. J. Calder
Publikováno v:
Journal of General Virology. 79:1781-1791
A monoclonal antibody, LMBH6, was derived from mice which had been sequentially immunized with bromelain-cleaved haemagglutinin (BHA) from influenza virus A/Aichi/2/68, A/Victoria/3/75 and A/Philippines/2/82 (all H3N2). LMBH6 recognizes the haemagglu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c83742cabf5152e538b9bbed251a920
https://doi.org/10.1099/0022-1317-79-7-1781
https://doi.org/10.1099/0022-1317-79-7-1781
Autor:
L. J. Calder, Winfried Weissenhorn, B. Moss, J. J. Skehel, S. A. Wharton, P. L. Earl, E. Aliprandis, Don C. Wiley
Publikováno v:
The EMBO Journal. 15:1507-1514
The human immunodeficiency virus-1 (HIV-1) envelope glycoprotein is composed of a soluble glycopolypeptide gp120 and a transmembrane glycopolypeptide gp41. These subunits form non-covalently linked oligomers on the surface of infected cells, virions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4954cb14ee48791ebb5f4be269f3a0af
https://doi.org/10.1002/j.1460-2075.1996.tb00494.x
https://doi.org/10.1002/j.1460-2075.1996.tb00494.x
Autor:
Don C. Wiley, John J. Skehel, Stephen A. Wharton, David A. Steinhauer, Rob W.H. Ruigrok, L. J. Calder
Publikováno v:
The EMBO Journal. 14:240-246
Activation of the membrane fusion potential of influenza haemagglutinin (HA) at endosomal pH requires changes in its structure. X-ray analysis of TBHA2, a proteolytic fragment of HA in the fusion pH conformation, indicates that at the pH of fusion th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c07e8e1fd3ebff6549f29c421314779f
https://doi.org/10.1002/j.1460-2075.1995.tb06997.x
https://doi.org/10.1002/j.1460-2075.1995.tb06997.x
Publikováno v:
Novel and Re-Emerging Respiratory Viral Diseases: Novartis Foundation Symposium 290
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::700877c7ae2bb837e60802efd0dca94a
https://doi.org/10.1002/9780470770672.ch6
https://doi.org/10.1002/9780470770672.ch6
Publikováno v:
Journal of General Virology. 71:1181-1188
A number of different influenza C virus strains were tested for their fusion properties using a resonance energy assay which allows direct monitoring of fusion between virus membranes and artificial lipid vesicles. The fusion pH of various strains wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a6bda000f10e6ff1a0284f876dff87b
https://doi.org/10.1099/0022-1317-71-5-1181
https://doi.org/10.1099/0022-1317-71-5-1181
Autor:
C. Barbey-Martin, J.J. Skehel, Marcel Knossow, Stephen A. Wharton, B. Gigant, L. J. Calder, Thierry Bizebard
Publikováno v:
Virology. 294(1)
We have determined the structure of a complex of influenza hemagglutinin (HA) with an antibody that binds simultaneously to the membrane-distal domains of two HA monomers, effectively cross-linking them. The antibody prevents the low pH structural tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8e512f8a7183e352b179e90248fd806
https://pubmed.ncbi.nlm.nih.gov/11886266
https://pubmed.ncbi.nlm.nih.gov/11886266
Autor:
Juan Antonio López, L. J. Calder, Blanca García-Barreno, M B Ruiz-Argüello, Luis González-Reyes, Don C. Wiley, Juan Pablo Albar, José A. Melero, John J. Skehel
Publikováno v:
Repisalud
Instituto de Salud Carlos III (ISCIII)
Instituto de Salud Carlos III (ISCIII)
Preparations of purified full-length fusion (F) protein of human respiratory syncytial virus (HRSV) expressed in recombinant vaccinia-F infected cells, or of an anchorless mutant (F(TM(-))) lacking the C-terminal 50 amino acids secreted from vaccinia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9566c896ce1c14536888274522e4c93
https://pubmed.ncbi.nlm.nih.gov/11493675
https://pubmed.ncbi.nlm.nih.gov/11493675
Autor:
Blanca García-Barreno, José A. Melero, Steve A. Wharton, Don C. Wiley, Luis González-Reyes, John J. Skehel, L. J. Calder
Publikováno v:
Virology. 271(1)
Full-length fusion (F) glycoprotein of human respiratory syncytial virus (HRSV) and a truncated anchorless mutant lacking the C-terminal 50 amino acids were expressed from vaccinia recombinants and purified by immunoaffinity chromatography and sucros
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7310d4ab8009b3b96acc2eca3920632e
https://pubmed.ncbi.nlm.nih.gov/10814577
https://pubmed.ncbi.nlm.nih.gov/10814577