Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Alvaro Alonso-Caballero"'
Autor:
Daniel T Peters, Antonio Reifs, Alvaro Alonso-Caballero, Azzeldin Madkour, Helen Waller, Brendan Kenny, Raul Perez-Jimenez, Jeremy H Lakey
Publikováno v:
PLoS Pathogens, Vol 18, Iss 3, p e1010447 (2022)
The pathogenic bacterium Yersina pestis is protected from macrophage engulfment by a capsule like antigen, F1, formed of long polymers of the monomer protein, Caf1. However, despite the importance of this pathogen, the mechanism of protection was not
Externí odkaz:
https://doaj.org/article/8a856613ebee42a4b3af58c3e5698a13
Publikováno v:
Royal Society Open Science, Vol 7, Iss 4 (2020)
The type 1 pilus is a bacterial filament consisting of a long coiled proteic chain of subunits joined together by non-covalent bonding between complementing β-strands. Its strength and structural stability are critical for its anchoring function in
Externí odkaz:
https://doaj.org/article/5a2c1149b48d4ba18f0539c55ff9c3e2
Autor:
Alvaro Alonso-Caballero, Jörg Schönfelder, Simon Poly, Fabiano Corsetti, David De Sancho, Emilio Artacho, Raul Perez-Jimenez
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
The pilus type 1 of uropathogenic E. coli must resist mechanical forces to remain attached to the epithelium. Here the authors use single-molecule force spectroscopy to demonstrate a hierarchy of mechanical stability among the pilus domains and show
Externí odkaz:
https://doaj.org/article/90d847fd94ed4db0be96ca5bbf74b922
Publikováno v:
Proc Natl Acad Sci U S A
Cells continually sample their mechanical environment using exquisite force sensors such as talin, whose folding status triggers mechanotransduction pathways by recruiting binding partners. Mechanical signals in biology change quickly over time and a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::098bcb3056c23c41e5e0a40aa70f81ad
https://doi.org/10.1073/pnas.2004091117
https://doi.org/10.1073/pnas.2004091117
Publikováno v:
Protein Folding ISBN: 9781071617151
Repositorio Institucional del Instituto Madrileño de Estudios Avanzados en Nanociencia
instname
Repositorio Institucional del Instituto Madrileño de Estudios Avanzados en Nanociencia
instname
Disulfide bonds play a pivotal role in the mechanical stability of proteins. Numerous proteins that are known to be exposed to mechanical forces in vivo contain disulfide bonds. The presence of cryptic disulfide bonds in a protein structure may be re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ace2d368b18608ea64311714ce14fee5
https://doi.org/10.1007/978-1-0716-1716-8_15
https://doi.org/10.1007/978-1-0716-1716-8_15
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2376
Disulfide bonds play a pivotal role in the mechanical stability of proteins. Numerous proteins that are known to be exposed to mechanical forces in vivo contain disulfide bonds. The presence of cryptic disulfide bonds in a protein structure may be re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e6b09c0f915efd2c1c8fa3123cb355e2
https://pubmed.ncbi.nlm.nih.gov/34845615
https://pubmed.ncbi.nlm.nih.gov/34845615
Autor:
Daniel T. Peters, Antonio Reifs, Alvaro Alonso-Caballero, Azzeldin Madkour, Helen Waller, Brendan Kenny, Raul Perez-Jimenez, Jeremy H. Lakey
Publikováno v:
PLoS pathogens. 18(3)
The pathogenic bacteriumYersina pestisis protected from macrophage engulfment by a capsule like antigen, F1, formed of long polymers of the monomer protein, Caf1. However, despite the importance of this pathogen, the mechanism of protection was not u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c2eb7789cc8b5b9bf6bee837dfe8f3f
https://pubmed.ncbi.nlm.nih.gov/35358289
https://pubmed.ncbi.nlm.nih.gov/35358289
The classical “one sequence, one structure, one function” paradigm has shaped much of our intuition of how proteins work inside the cell. Partially due to the insight provided by bulk biochemical assays, individual biomolecules are assumed to beh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f1eeadc973d4272dab8f538477cc215
https://doi.org/10.1101/2021.02.24.432730
https://doi.org/10.1101/2021.02.24.432730
Proteins that operate under force—cell adhesion, mechanosensing—exhibit a wide range of mechanostabilities. Single-molecule magnetic tweezers has enabled the exploration of the dynamics under force of these proteins with subpiconewton resolution
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a50b9b0b4bc7bb983afde4d6fa04c22
https://doi.org/10.1101/2021.01.04.425265
https://doi.org/10.1101/2021.01.04.425265
Autor:
Simon Poly, Emilio Artacho, Jörg Schönfelder, Raul Perez-Jimenez, Fabiano Corsetti, David De Sancho, Alvaro Alonso-Caballero
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Nature Communications
Nature Communications
Uropathogenic Escherichia coli attach to tissues using pili type 1. Each pilus is composed by thousands of coiled FimA domains followed by the domains of the tip fibrillum, FimF-FimG-FimH. The domains are linked by non-covalent β-strands that must r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2318b774d85c897415c0e158142c155b
http://link.springer.com/article/10.1038/s41467-018-05107-6
http://link.springer.com/article/10.1038/s41467-018-05107-6