Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Joyce J W, Wong"'
Autor:
Joyce J. W. Wong, Tracy A. Young, Jiayan Zhang, Shiheng Liu, George P. Leser, Elizabeth A. Komives, Robert A. Lamb, Z. Hong Zhou, Joshua Salafsky, Theodore S. Jardetzky
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Nipah virus causes encephalitis in humans. Here the authors use a multidisciplinary approach to study the binding of the viral attachment protein G to its host receptor ephrinB2 and show that monomeric and dimeric receptors activate distinct conforma
Externí odkaz:
https://doaj.org/article/6bf2cd0a2e484c86a8eb86d2ea0a7ae4
Publikováno v:
Science Advances
The reconstitution of Nipah virus fusion activation provides new insights into the dynamics of the viral entry glycoproteins.
Paramyxovirus membrane fusion requires an attachment protein that binds to a host cell receptor and a fusion protein th
Paramyxovirus membrane fusion requires an attachment protein that binds to a host cell receptor and a fusion protein th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b50eb6c4b640c177289e2c014ef1e892
https://doi.org/10.1126/sciadv.abe1235
https://doi.org/10.1126/sciadv.abe1235
Autor:
Tracy A. Young, Elizabeth A. Komives, Joyce J. W. Wong, George P. Leser, Jiayan Zhang, Joshua Salafsky, Theodore S. Jardetzky, Shiheng Liu, Robert A. Lamb, Z. Hong Zhou
Publikováno v:
Nature Communications
Nature communications, vol 8, iss 1
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Nature communications, vol 8, iss 1
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Nipah virus is an emergent paramyxovirus that causes deadly encephalitis and respiratory infections in humans. Two glycoproteins coordinate the infection of host cells, an attachment protein (G), which binds to cell surface receptors, and a fusion (F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cef1572fc87ddf3b1ac813229bd67200
https://pubmed.ncbi.nlm.nih.gov/28974687
https://pubmed.ncbi.nlm.nih.gov/28974687
Publikováno v:
Journal of Molecular Biology. 426:3783-3795
The conjugative transfer of bacterial F plasmids relies on TraM, a plasmid-encoded protein that recognizes multiple DNA sites to recruit the plasmid to the conjugative pore. In spite of the high degree of amino acid sequence conservation between TraM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::475db0bd6d6abcfaec5f338b1778a880
https://doi.org/10.1016/j.jmb.2014.09.018
https://doi.org/10.1016/j.jmb.2014.09.018
Relaxosome function and conjugation regulation in F-like plasmids - a structural biology perspective
Publikováno v:
Molecular Microbiology. 85:602-617
Summary The tra operon of the prototypical F plasmid and its relatives enables transfer of a copy of the plasmid to other bacterial cells via the process of conjugation. Tra proteins assemble to form the transferosome, the transmembrane pore through
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6852d9776662b28794824481bfa48adb
https://doi.org/10.1111/j.1365-2958.2012.08131.x
https://doi.org/10.1111/j.1365-2958.2012.08131.x
Publikováno v:
Nucleic Acids Research
The conjugative transfer of F-like plasmids such as F, R1, R100 and pED208, between bacterial cells requires TraM, a plasmid-encoded DNA-binding protein. TraM tetramers bridge the origin of transfer (oriT) to a key component of the conjugative pore,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::783aae22896520fd171a51357b3592c4
https://doi.org/10.1093/nar/gkr296
https://doi.org/10.1093/nar/gkr296
Publikováno v:
Molecular Microbiology. 70:89-99
F plasmid-mediated bacterial conjugation requires interactions between a relaxosome component, TraM, and the coupling protein TraD, a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore. Here we present the crystal structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fef5278ba2d7942bf22078738b35b320
https://doi.org/10.1111/j.1365-2958.2008.06391.x
https://doi.org/10.1111/j.1365-2958.2008.06391.x
Autor:
J. N. Mark Glover, Paul G. Scott, Jan Manchak, Jun Lu, Laura S. Frost, Joyce J. W. Wong, Ross A. Edwards
Publikováno v:
The EMBO Journal. 25:2930-2939
TraM is essential for F plasmid-mediated bacterial conjugation, where it binds to the plasmid DNA near the origin of transfer, and recognizes a component of the transmembrane DNA transfer complex, TraD. Here we report the 1.40 Å crystal structure o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5a3c9b48851d9323eba8b34d4aa4e62
https://doi.org/10.1038/sj.emboj.7601151
https://doi.org/10.1038/sj.emboj.7601151
Publikováno v:
Journal of Cutaneous Medicine and Surgery. 16:375-377
Background: Basaloid squamous cell carcinoma is a rare aggressive variant of squamous cell carcinoma, with a predilection for the head and neck region. There are only two case reports in the literature documenting a nasal cavity squamous cell carcino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1869c1bfdfc84411e66a2df620bd002e
https://doi.org/10.1177/120347541201600520
https://doi.org/10.1177/120347541201600520
Relaxosome function and conjugation regulation in F-like plasmids - a structural biology perspective
Publikováno v:
Molecular microbiology. 85(4)
The tra operon of the prototypical F plasmid and its relatives enables transfer of a copy of the plasmid to other bacterial cells via the process of conjugation. Tra proteins assemble to form the transferosome, the transmembrane pore through which th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1678727b7fddc83c9602b51cdd9ed8fe
https://pubmed.ncbi.nlm.nih.gov/22788760
https://pubmed.ncbi.nlm.nih.gov/22788760