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Proteomics|September 15, 2015
The making of an embryo in a basal metazoan: Proteomic analysis in the sea anemone Nematostella vectensisShimrit Levitan, Noa Sher, Vera Brekhman, et al.
Biomacromolecules|September 23, 2008
Nanofibers made of globular proteinsYael Dror, Tamar Ziv, Vadim Makarov, et al.
The Journal of Biological Chemistry|February 12, 2020
Opposing effects of polysulfides and thioredoxin on apoptosis through caspase persulfidationIlana Braunstein, Rotem Engelman, Ofer Yitzhaki, et al.
The EMBO Journal|September 11, 2016
The effects of proteasomal inhibition on synaptic proteostasisVicky Hakim, Laurie D Cohen, Rina Zuchman, et al.
Cancer Biomarkers : Section a of Disease Markers|February 1, 2007
Comparative proteomics of small cell lung carcinomaTamar Ziv, Eilon Barnea, Hava Segal, et al.
Circulation Research|December 15, 2025
Subcellular In Vivo Cardiac Proteomics Reveals Sarcomere and Ribosome Interactomes and skNAC's Impact on Cardiac ProteostasisRami Haddad, Omer Sadeh, Tamar Ziv, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 7, 2021
A short binding site in the KPC1 ubiquitin ligase mediates processing of NF-κB1 p105 to p50: A potential for a tumor-suppressive PROTACGilad Goldhirsh, Yelena Kravtsova-Ivantsiv, Gandhesiri Satish, et al.
Biochimica Et Biophysica Acta|January 3, 2014
Identification of proteins that form specific complexes with the highly conserved protein Translin in Schizosaccharomyces pombeElad Eliahoo, Phyana Litovco, Ron Ben Yosef, et al.
Biochemical and Biophysical Research Communications|September 16, 2020
The p105 NF-ĸB precursor is a pseudo substrate of the ubiquitin ligase FBXO7, and its binding to the ligase stabilizes it and results in stimulated cell proliferationRonald G Udasin, Yossi Gottfried, Bertrand Fabre, et al.
Molecules (Basel, Switzerland)|August 12, 2022
Antibody for Serine 65 Phosphorylated Ubiquitin Identifies PLK1-Mediated Phosphorylation of Mitotic Proteins and APC1Guy Mann, Prasad Sulkshane, Pradeep Sadhu, et al.
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