M
Michal Sharon
Researcher at Weizmann Institute of Science
Publications - 126
Citations - 8023
Michal Sharon is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Protein subunit & Proteasome. The author has an hindex of 39, co-authored 121 publications receiving 6850 citations. Previous affiliations of Michal Sharon include Tel Aviv University & University of Cambridge.
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Journal ArticleDOI
Mechanism of auxin perception by the TIR1 ubiquitin ligase
Xu Tan,Luz Irina A. Calderon-Villalobos,Michal Sharon,Changxue Zheng,Carol V. Robinson,Mark Estelle,Ning Zheng +6 more
TL;DR: These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket, establishing the first structural model of a plant hormone receptor.
Journal ArticleDOI
Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-receptor
Laura B. Sheard,Xu-Hui Tan,Haibin Mao,John Withers,Gili Ben-Nissan,Thomas R. Hinds,Yuichi Kobayashi,Fong-Fu Hsu,Michal Sharon,John Browse,Sheng Yang He,Josep Rizo,Gregg A. Howe,Ning Zheng +13 more
TL;DR: The mechanism of jasmonate perception is unraveled, the ability of F-box proteins to evolve as multi-component signalling hubs is highlighted and inositol pentakisphosphate is identified, which interacts with both COI1 and JAZ adjacent to the ligand.
Journal ArticleDOI
The role of mass spectrometry in structure elucidation of dynamic protein complexes.
Michal Sharon,Carol V. Robinson +1 more
TL;DR: The applications described herein not only confirm the status of mass spectrometry as a structural biology approach to complement X-ray analysis or electron microscopy, but also highlight unique attributes of the methodology.
Journal ArticleDOI
Regulating the 20S Proteasome Ubiquitin-Independent Degradation Pathway
Gili Ben-Nissan,Michal Sharon +1 more
TL;DR: The current understanding of the regulatory mechanisms that coordinate 20S proteasome-mediated degradation are described, and gaps in knowledge are highlighted that remain to be bridged.
Journal ArticleDOI
Structural organization of the 19S proteasome lid: insights from MS of intact complexes.
TL;DR: The findings allow us to identify a scaffold for the assembly of the particle and to propose a regulatory mechanism that prevents exposure of the active site until assembly is complete, and highlight the potential of mass spectrometry to add crucial insight into the structural organization of an endogenous, wild-type complex.