Zobrazeno 1 - 10 of 40 pro vyhledávání: '"Nadine S. Henderson"'
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Akademický článek
Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis
Autor: Minge Du, Zuanning Yuan, Glenn T. Werneburg, Nadine S. Henderson, Hemil Chauhan, Amanda Kovach, Gongpu Zhao, Jessica Johl, Huilin Li, David G. Thanassi
Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Escherichia coli form pili structures in order to initiate infection of the urinary tract. Here, Thanassi et al., have solved the structures of pili assembly intermediates and provided insights into their biogenesis and assembly.
Externí odkaz: https://doaj.org/article/8a64b8abfd8d41f0a8749b5b52ff307e
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3
The Natural History and Composition of Urinary Catheter Biofilms: Early Uropathogen Colonization with Intraluminal and Distal Predominance
Autor: Raymond R. Rackley, Anh Nguyen, Annie J. Rohan, Daniel Shoskes, Aaron E. Katz, Jason Kim, Amanda L. Le Sueur, David G. Thanassi, Anthony T. Corcoran, Glenn T. Werneburg, Nadine S. Henderson
Publikováno v: J Urol
PURPOSE: To determine the composition and site of initiation of bacterial biofilm location on indwelling urinary catheters, and to track biofilm progression over time. MATERIALS & METHODS: Indwelling urinary catheters were collected from two tertiary
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c89614b3d2e05fcef55d6df5baf6d3e6
https://doi.org/10.1097/ju.0000000000000492
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5
Akademický článek
Allosteric signalling in the outer membrane translocation domain of PapC usher
Autor: Irene Farabella, Thieng Pham, Nadine S Henderson, Sebastian Geibel, Gilles Phan, David G Thanassi, Anne H Delcour, Gabriel Waksman, Maya Topf
Publikováno v: eLife, Vol 3 (2014)
PapC ushers are outer-membrane proteins enabling assembly and secretion of P pili in uropathogenic E. coli. Their translocation domain is a large β-barrel occluded by a plug domain, which is displaced to allow the translocation of pilus subunits acr
Externí odkaz: https://doaj.org/article/d13ab33701a7448fa6e5c303747f59c9
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6
Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis
Autor: Nadine S. Henderson, David G. Thanassi, Jessica Johl, Hemil Chauhan, Amanda Kovach, Gongpu Zhao, Huilin Li, Minge Du, Glenn T. Werneburg, Zuanning Yuan
Publikováno v: Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Uropathogenic Escherichia coli assemble surface structures termed pili or fimbriae to initiate infection of the urinary tract. P pili facilitate bacterial colonization of the kidney and pyelonephritis. P pili are assembled through the conserved chape
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72d0e1a25aa7a6f4c43ff366821ce58b
https://pubmed.ncbi.nlm.nih.gov/34471127
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8
Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD
Autor: Huilin Li, Gongpu Zhao, Nadine S. Henderson, Hongjun Yu, Minge Du, Glenn T. Werneburg, Zuanning Yuan, Samema Sarowar, David G. Thanassi
Publikováno v: Nature
Pathogenic bacteria such as Escherichia coli assemble surface structures termed pili, or fimbriae, to mediate binding to host-cell receptors1. Type 1 pili are assembled via the conserved chaperone–usher pathway2–5. The outer-membrane usher FimD r
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::458cf3d5f417a0d5730420bef0dbcd35
https://doi.org/10.1038/s41586-018-0587-z
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9
The small molecule nitazoxanide selectively disrupts BAM-mediated folding of the outer membrane usher protein
Autor: John J. Psonis, Peter Chahales, Paul S. Hoffman, Nadine S. Henderson, Nathan W. Rigel, David G. Thanassi
Publikováno v: J Biol Chem
Bacterial pathogens assemble adhesive surface structures termed pili or fimbriae to initiate and sustain infection of host tissues. Uropathogenic Escherichia coli, the primary causative agent of urinary tract infections, expresses type 1 and P pili r
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fa1df4be15525a85cd7ec5d620c0aeb
https://pubmed.ncbi.nlm.nih.gov/31391254
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