S
Scott J. Hultgren
Researcher at Washington University in St. Louis
Publications - 393
Citations - 42958
Scott J. Hultgren is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Pilus & Bacterial adhesin. The author has an hindex of 109, co-authored 380 publications receiving 38674 citations. Previous affiliations of Scott J. Hultgren include University College London & Vrije Universiteit Brussel.
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Journal ArticleDOI
Structural Homology between the C-Terminal Domain of the PapC Usher and Its Plug
Bradley Ford,Ana Toste Rêgo,Timothy J. Ragan,Jerome S. Pinkner,Karen W. Dodson,Paul C. Driscoll,Scott J. Hultgren,Gabriel Waksman +7 more
TL;DR: A stable and folded fragment of the C-terminal region of the PapC usher is identified and its structure is determined, revealing a beta-sandwich fold very similar to that of the plug domain, a domain of PapC obstructing its translocation domain that suggests similar functions in usher-mediated pilus biogenesis.
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Pilicides regulate pili expression in E. coli without affecting the functional properties of the pilus rod.
TL;DR: A potential use of pilicides as chemical tools to study important biological processes e.g. adhesion, pilus biogenesis and the role of pili in infections and biofilm formation is established.
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Molecular dissection of PapD interaction with PapG reveals two chaperone-binding sites
Zheng Xu,C. Hal Jones,David B. Haslam,Jerome S. Pinkner,Karen W. Dodson,Jan Kihlberg,Scott J. Hultgren +6 more
TL;DR: A chaperone‐binding assay was developed using fusions of the C‐terminus of PapG to maltose‐binding protein (MBP/G fusions) to investigate whether chaper one‐subunit complex formation requires additional interactions.
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Binding of pili from uropathogenic Escherichia coli to membranes secreted by human colonocytes and enterocytes.
TL;DR: It is reported that surfactant-like particles secreted by the human intestine contain receptors for PapG adhesins and may provide an intestinal habitat for uropathogenic bacteria.
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Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation
Roger D. Klein,Qin Shu,Zachary T. Cusumano,Kanna Nagamatsu,Nathaniel C. Gualberto,Aaron J L Lynch,Chao Wu,Wenjie Wang,Neha Jain,Jerome S. Pinkner,Gaya K. Amarasinghe,Scott J. Hultgren,Carl Frieden,Matthew George Chapman +13 more
TL;DR: A series of finely tuned nonpolar and charge-charge interactions that facilitate the oligomerization of CsgE and its ability to transport unfolded CsgA to CsgG for translocation are elucidated to elucidate possible targets for biofilm-associated bacterial infections.