Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Blanca Echeverria"'
Publikováno v:
J Biol Chem
Journal of Biological Chemistry, 295 (35)
Journal of Biological Chemistry, 295 (35)
FimA is the main structural subunit of adhesive type 1 pili from uropathogenic Escherichia coli strains. Up to 3000 copies of FimA assemble to the helical pilus rod through a mechanism termed donor strand complementation, in which the incomplete immu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d62829ba408ca57025f7b6f2a7797d1
https://doi.org/10.1074/jbc.ra120.014324
https://doi.org/10.1074/jbc.ra120.014324
Autor:
Charles A. R. Cotton, Doryen Bubeck, Burak V. Kabasakal, Blanca Echeverria, Ciaran McFarlane, James W. Murray, Nita R. Shah
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The Calvin–Benson (CB) cycle in plants, algae, and cyanobacteria fixes most of the carbon in most of the biomass on Earth. The CB cycle is regulated by the redox state, which enables it to be turned off in the dark. One part of this re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4047492bfec333c0cc89b2e6f18c78fa
https://doi.org/10.1073/pnas.1906722116
https://doi.org/10.1073/pnas.1906722116
Autor:
Blanca Echeverria, Katharina Schubert, Volker Thiel, Alain Scaiola, Evangelos D. Karousis, Lukas Adrian Gurzeler, Marc Leibundgut, Ahmad Jomaa, Nenad Ban, Oliver Mühlemann
Publikováno v:
Nature Structural & Molecular Biology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f8ab69c4ada6a6e02c34e75f8109036
Autor:
Alain Scaiola, Oliver Mühlemann, Marc Leibundgut, Ahmad Jomaa, Volker Thiel, Evangelos D. Karousis, Blanca Echeverria, Lukas Adrian Gurzeler, Katharina Schubert, Nenad Ban
Publikováno v:
Nature Structural & Molecular Biology, 27 (10)
Nature Structural & Molecular Biology
Nature Structural & Molecular Biology
The SARS-CoV-2 non-structural protein 1 (Nsp1), also referred to as the host shutoff factor, suppresses host innate immune functions. By combining cryo-electron microscopy and biochemistry, we show that SARS-CoV-2 Nsp1 binds to the human 40S subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cf8f76b79e2c4e1da2e331cee3349d6
https://hdl.handle.net/20.500.11850/443711
https://hdl.handle.net/20.500.11850/443711
Autor:
Marc Leibundgut, Katharina Schubert, Blanca Echeverria, Lukas-Adrian Gurzeler, Ahmad Jomaa, Oliver Mühlemann, Alain Scaiola, Volker Thiel, Evangelos D. Karousis, Nenad Ban
The non-structural protein 1 (Nsp1), also referred to as the host shutoff factor, is the first viral protein that is synthesized in SARS-CoV-2 infected human cells to suppress host innate immune functions1,2. By combining cryo-electron microscopy and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7459080da4e69e610c0c519418334928
https://doi.org/10.1101/2020.07.07.191676
https://doi.org/10.1101/2020.07.07.191676