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Sharon Amit
Researcher at Sheba Medical Center
Publications - 94
Citations - 7028
Sharon Amit is an academic researcher from Sheba Medical Center. The author has contributed to research in topics: Medicine & Internal medicine. The author has an hindex of 17, co-authored 64 publications receiving 4736 citations. Previous affiliations of Sharon Amit include Hebrew University of Jerusalem & Hadassah Medical Center.
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Journal ArticleDOI
NF-κB functions as a tumour promoter in inflammation-associated cancer
Eli Pikarsky,Rinnat M. Porat,Ilan Stein,Rinat Abramovitch,Sharon Amit,Shafika Kasem,Elena Gutkovich-Pyest,Simcha Urieli-Shoval,Eithan Galun,Yinon Ben-Neriah +9 more
TL;DR: It is shown that the inflammatory process triggers hepatocyte NF-κB through upregulation of tumour-necrosis factor-α (TNFα) in adjacent endothelial and inflammatory cells, and is therefore a potential target for cancer prevention in chronic inflammatory diseases.
Journal ArticleDOI
Covid-19 Breakthrough Infections in Vaccinated Health Care Workers.
Moriah Bergwerk,Tal Gonen,Yaniv Lustig,Sharon Amit,Marc Lipsitch,Carmit Cohen,Michal Mandelboim,Einav G Levin,Carmit Rubin,Victoria Indenbaum,Ilana Tal,Malka Zavitan,Neta S. Zuckerman,Adina Bar-Chaim,Yitshak Kreiss,Gili Regev-Yochay +15 more
TL;DR: Despite the high efficacy of the BNT162b2 messenger RNA vaccine against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), rare breakthrough infections have been reported.
Journal ArticleDOI
Axin-mediated CKI phosphorylation of β-catenin at Ser 45: a molecular switch for the Wnt pathway
Sharon Amit,Ada Hatzubai,Yaara Birman,Jens S. Andersen,Etti Ben-Shushan,Matthias Mann,Yinon Ben-Neriah,Irit Alkalay +7 more
TL;DR: Using mass spectrometry and phosphopeptide-specific antibodies, it is shown that a complex of axin and casein kinase I induces beta-catenin phosphorylation at a single site: serine 45 (S45), which serves as a molecular switch for the Wnt pathway.
Journal ArticleDOI
Identification of the receptor component of the IkappaBalpha-ubiquitin ligase.
Avraham Yaron,Ada Hatzubai,Matti Davis,Iris Lavon,Sharon Amit,Anthony M. Manning,Jens S. Andersen,Matthias Mann,Frank Mercurio,Yinon Ben-Neriah +9 more
TL;DR: The specific component of the ligase that recognizes the pIκBα degradation motif as an F-box/WD-domainprotein belonging to a recently distinguished family of β-TrCP/Slimb proteins is identified and designated E3RSIκBs, which represents a family of receptor proteins that are core components of a class of ubiquitin ligases.