Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Alan H. M. Wong"'
Autor:
Alan H. M. Wong, Aidan C. A. Tomlinson, Dongxia Zhou, Malathy Satkunarajah, Kevin Chen, Chetna Sharon, Marc Desforges, Pierre J. Talbot, James M. Rini
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Coronaviruses have a relatively high mutation rate, potentially allowing fast adaptation to changing pressures. Here, Wong et al. provide the structure of the receptor-binding domain (RBD) of the human coronavirus HCoV-229E and its receptor and analy
Externí odkaz:
https://doaj.org/article/f6588e45349a4419aa4c7ce1d24b3317
Autor:
Samir Benlekbir, Pierre J. Talbot, Dongxia Zhou, Aidan C. A. Tomlinson, John L. Rubinstein, Alan H. M. Wong, Zhijie Li, Marc Desforges, James M. Rini
Publikováno v:
eLife
eLife, Vol 8 (2019)
eLife, Vol 8 (2019)
The coronavirus S-protein mediates receptor binding and fusion of the viral and host cell membranes. In HCoV-229E, its receptor binding domain (RBD) shows extensive sequence variation but how S-protein function is maintained is not understood. Report
Autor:
James M. Rini, Mathieu Dubé, Alan H. M. Wong, Pierre J. Talbot, Marc Desforges, Alain Le Coupanec
Publikováno v:
Journal of Virology
Human coronaviruses (HCoVs) are recognized respiratory pathogens for which accumulating evidence indicates that in vulnerable patients the infection can cause more severe pathologies. HCoVs are not always confined to the upper respiratory tract and c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78f3ea16f2846e73249856b78275a59f
https://europepmc.org/articles/PMC6096804/
https://europepmc.org/articles/PMC6096804/
Autor:
Malathy Satkunarajah, James M. Rini, Kevin P. Chen, Chetna Sharon, Marc Desforges, Pierre J. Talbot, Aidan C. A. Tomlinson, Alan H. M. Wong, Dongxia Zhou
Publikováno v:
Nature Communications
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
RNA viruses are characterized by a high mutation rate, a buffer against environmental change. Nevertheless, the means by which random mutation improves viral fitness is not well characterized. Here we report the X-ray crystal structure of the recepto
Publikováno v:
Journal of Biological Chemistry. 287:36804-36813
Human aminopeptidase N (hAPN/hCD13) is a dimeric membrane protein and a member of the M1 family of zinc metallopeptidases. Within the rennin-angiotensin system, its enzymatic activity is responsible for processing peptide hormones angiotensin III and