Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lawrence G. Welch"'
Autor:
Jérôme Cattin-Ortolá, Lawrence G. Welch, Sarah L. Maslen, Guido Papa, Leo C. James, Sean Munro
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
The Spike protein of SARS-CoV-2 has a C-terminal cytoplasmic tail. Here the authors show that this tail binds trafficking machinery via sequences that appear optimised to ensure that Spike accumulates at the site of viral budding in the Golgi but tha
Externí odkaz:
https://doaj.org/article/fbd2667f0c0d43b0837fb514639c3ee9
Autor:
Lawrence G. Welch, Sarah L. Maslen, Guido Papa, Jérôme Cattin-Ortolá, Leo C. James, Sean Munro
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
The Spike (S) protein of SARS-CoV-2 binds ACE2 to direct fusion with host cells. S comprises a large external domain, a transmembrane domain, and a short cytoplasmic tail. Understanding the intracellular trafficking of S is relevant to SARS-CoV-2 inf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00ab5b02c7e0f1aefc02444a42527210
A tale of short tails, through thick and thin: investigating the sorting mechanisms of Golgi enzymes
Autor:
Sean Munro, Lawrence G. Welch
Publikováno v:
FEBS Letters. 593:2452-2465
The Golgi apparatus is an important site for the modification of most secreted and membrane proteins. Glycan processing is the major class of modification and is mediated by a large number of Golgi-resident glycosyltransferases and glycosidases. Thes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1063ce2f3f52d55facb9caacf2f2009f
https://doi.org/10.1002/1873-3468.13553
https://doi.org/10.1002/1873-3468.13553
Publikováno v:
The Journal of cell biology. 220(10)
Glycosylation is a diverse and abundant modification of proteins, lipids and RNA. The fidelity of glycosylation is, in part, assured by the correct compartmentalisation of Golgi-resident glycosylation enzymes within the Golgi stack. The COPI adaptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65118507de31df0aaef3fd56bfe8368b
https://pubmed.ncbi.nlm.nih.gov/34477810
https://pubmed.ncbi.nlm.nih.gov/34477810
Autor:
Jérôme Cattin-Ortolá, Sarah L. Maslen, Leo C. James, Sean Munro, Guido Papa, Lawrence G. Welch, J. Mark Skehel
The Spike (S) protein of SARS-CoV-2 binds ACE2 to direct fusion with host cells. S comprises a large external domain, a transmembrane domain (TMD) and a short cytoplasmic tail. Understanding the intracellular trafficking of S is relevant to SARS-CoV-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e207483f99efc1a061aa7cdc8c2393e
https://doi.org/10.1101/2020.10.12.335562
https://doi.org/10.1101/2020.10.12.335562
Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusion.
Autor:
Guido Papa, Donna L Mallery, Anna Albecka, Lawrence G Welch, Jérôme Cattin-Ortolá, Jakub Luptak, David Paul, Harvey T McMahon, Ian G Goodfellow, Andrew Carter, Sean Munro, Leo C James
Publikováno v:
PLoS Pathogens, Vol 17, Iss 1, p e1009246 (2021)
Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) infects cells by binding to the host cell receptor ACE2 and undergoing virus-host membrane fusion. Fusion is triggered by the protease TMPRSS2, which processes the viral Spike (S) protein t
Externí odkaz:
https://doaj.org/article/e7f61576d1094208b86f915b6e68af06