Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Tyler D. R. Vance"'
Autor:
Tyler D. R. Vance, Patrick Yip, Elisabet Jiménez, Sheng Li, Diana Gawol, James Byrnes, Isabel Usón, Ahmed Ziyyat, Jeffrey E. Lee
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-14 (2022)
The crystal structure of sperm-expressed surface protein SPACA6 shows similarities to IZUMO1 though their functions are not redundant. Structural homology search in the AlphaFold human proteome and sequence search suggest a superfamily of mammalian g
Externí odkaz:
https://doaj.org/article/5103ed85da4846eba054e5b2109b21e5
Autor:
Farshad C. Azimi, Trevor T. Dean, Karine Minari, Luis G. M. Basso, Tyler D. R. Vance, Vitor Hugo B. Serrão
Publikováno v:
Biomolecules, Vol 13, Iss 7, p 1130 (2023)
Viral entry and fertilization are distinct biological processes that share a common mechanism: membrane fusion. In viral entry, enveloped viruses attach to the host cell membrane, triggering a series of conformational changes in the viral fusion prot
Externí odkaz:
https://doaj.org/article/f08b0b660ffc488da8a100b74ddfd162
Autor:
Shuaiqi Guo, Tyler D. R. Vance, Hossein Zahiri, Robert Eves, Corey Stevens, Jan-Hendrik Hehemann, Silvia Vidal-Melgosa, Peter L. Davies
Publikováno v:
mBio, Vol 12, Iss 2 (2021)
Bacterial adhesins are key virulence factors that are essential for the pathogen-host interaction and biofilm formation that cause most infections. Many of the adhesin-driven cell-cell interactions are mediated by lectins.
Externí odkaz:
https://doaj.org/article/7dd6c85e360047f09aa5083c8d95df3d
Publikováno v:
PLoS ONE, Vol 14, Iss 7, p e0220045 (2019)
Bacterial adhesins attach their hosts to surfaces through one or more ligand-binding domains. In RTX adhesins, which are localized to the outer membrane of many Gram-negative bacteria via the type I secretion system, we see several examples of a puta
Externí odkaz:
https://doaj.org/article/d1cf730e59894dd6873334a6d57debd6
Publikováno v:
PLoS ONE, Vol 14, Iss 8, p e0221101 (2019)
[This corrects the article DOI: 10.1371/journal.pone.0220045.].
Externí odkaz:
https://doaj.org/article/c35d623c9fdf4faf9a294f8d78eab4cb
Publikováno v:
PLoS ONE, Vol 12, Iss 4, p e0174682 (2017)
To gain insight into the relationship between protein structure and mechanical stability, single molecule force spectroscopy experiments on proteins with diverse structure and topology are needed. Here, we measured the mechanical stability of extende
Externí odkaz:
https://doaj.org/article/d143bbc676674d0ab9c62593e9d60f19
Autor:
Robert Eves, Hossein Zahiri, Jan-Hendrik Hehemann, Tyler D. R. Vance, Silvia Vidal-Melgosa, Corey A. Stevens, Peter L. Davies, Shuaiqi Guo
Publikováno v:
mBio
mBio, Vol 12, Iss 2 (2021)
mBio, Vol 12, Iss 2 (2021)
Bacterial adhesins are key virulence factors that are essential for the pathogen-host interaction and biofilm formation that cause most infections. Many of the adhesin-driven cell-cell interactions are mediated by lectins.
Carbohydrate recogniti
Carbohydrate recogniti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3af9c64485154fa5a721db0233580308
https://pubmed.ncbi.nlm.nih.gov/33824212
https://pubmed.ncbi.nlm.nih.gov/33824212
Autor:
Shuaiqi Guo, Corey A. Stevens, Silvia Vidal-Melgosa, Peter L. Davies, Jan-Hendrik Hehemann, Robert Eves, Tyler D. R. Vance, Hossein Zahiri
Carbohydrate recognition by lectins governs critical host-microbe interactions. MpPA14 lectin is a domain of a 1.5-MDa adhesin responsible for a symbiotic bacterium-diatom interaction in Antarctica. Here we show MpPA14 binds various monosaccharides,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21a65c4235d32aaa4d2e32851230e40d
https://doi.org/10.1101/2020.11.18.389155
https://doi.org/10.1101/2020.11.18.389155
Publikováno v:
Journal of Structural Biology: X
Journal of Structural Biology: X, Vol 4, Iss, Pp 100036-(2020)
Journal of Structural Biology: X, Vol 4, Iss, Pp 100036-(2020)
Graphical abstract
Highlights • Elongated beta-sandwich repeats are a major part of bacterial RTX adhesins. • The repeats are arranged in tandem to extend away from the bacterial surface. • Calcium ions are coordinated in the linkers betwe
Highlights • Elongated beta-sandwich repeats are a major part of bacterial RTX adhesins. • The repeats are arranged in tandem to extend away from the bacterial surface. • Calcium ions are coordinated in the linkers betwe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99bee3d6c6d2b49d35fcf94071dc824f
http://europepmc.org/articles/PMC7493085
http://europepmc.org/articles/PMC7493085
Publikováno v:
The FEBS Journal. 285:1511-1527
Out of the dozen different ice-binding protein (IBP) structures known, the DUF3494 domain is the most widespread, having been passed many times between prokaryotic and eukaryotic microorganisms by horizontal gene transfer. This ~25-kDa β-solenoid do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5697eb17a5f7498b7648f9be01e51ff2
https://doi.org/10.1111/febs.14424
https://doi.org/10.1111/febs.14424