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Einav Tayeb-Fligelman
Researcher at Technion – Israel Institute of Technology
Publications - 18
Citations - 622
Einav Tayeb-Fligelman is an academic researcher from Technion – Israel Institute of Technology. The author has contributed to research in topics: Fibril & Amyloid. The author has an hindex of 8, co-authored 17 publications receiving 404 citations. Previous affiliations of Einav Tayeb-Fligelman include University of California, Los Angeles & Howard Hughes Medical Institute.
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Journal ArticleDOI
The cytotoxic Staphylococcus aureus PSMα3 reveals a cross-α amyloid-like fibril
Einav Tayeb-Fligelman,Orly Tabachnikov,Asher Moshe,Orit Goldshmidt-Tran,Michael R. Sawaya,Nicolas Coquelle,Jacques-Philippe Colletier,Meytal Landau +7 more
TL;DR: The fibril structure and function of the highly toxic, 22-residue phenol-soluble modulin α3 (PSMα3) peptide secreted by Staphylococcus aureus is determined and a distinctive “cross-α” amyloid-like architecture is revealed, in which amphipathic α helices stacked perpendicular to the fibrIL axis into tight self-associating sheets.
ComponentDOI
The cytotoxic Staphylococcus aureus PSM alpha 3 reveals a cross-alpha amyloid-like fibril.
Einav Tayeb-Fligelman,Orly Tabachnikov,Asher Moshe,Orit Goldshmidt-Tran,Michael R. Sawaya,Nicolas Coquelle,Jacques-Philippe Colletier,Meytal Landau +7 more
Journal ArticleDOI
Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents.
Sergei Perov,Ofir Lidor,Nir Salinas,Nimrod Golan,Einav Tayeb-Fligelman,Maya Deshmukh,Dieter Willbold,Meytal Landau +7 more
TL;DR: Crystal structures of amyloid-forming segments from the major curli subunit, CsgA, are presented, revealing steric zipper fibrils of tightly mated β-sheets, demonstrating a structural link between curli and human pathological amyloids.
Journal ArticleDOI
Staphylococcus aureus PSMα3 Cross-α Fibril Polymorphism and Determinants of Cytotoxicity.
TL;DR: It is demonstrated that massive T cell deformation and death are linked with PSM α3 aggregation and co-localization with cell membranes, and hypothesize that PSMα3 cytotoxicity is governed by the ability to form cross-α fibrils and involves a dynamic process of co-aggregation with the cell membrane, rupturing it.
Journal ArticleDOI
The GPSM2/LGN GoLoco motifs are essential for hearing.
Yoni Bhonker,Amal Abu-Rayyan,Kathy Ushakov,Liat Amir-Zilberstein,Shaked Shivatzki,Ofer Yizhar-Barnea,Tal Elkan-Miller,Einav Tayeb-Fligelman,Sun Myoung Kim,Meytal Landau,Moien Kanaan,Ping Helen Chen,Fumio Matsuzaki,David Sprinzak,Karen B. Avraham +14 more
TL;DR: The data provide a mechanism for the loss of hearing found in human patients with GPSM2/LGN variants, and support the role of Lgn as a PCP effector.