חוקר במחלקה לחקר התא ואימונולוגיה בפקולטה למדעי החיים ע"ש ג'ורג' ס. וייז באוניברסיטת תל-אביב
פרופ' ז'ררדו זלמר לדרקרמר
![פרופ' ז'ררדו זלמר לדרקרמר פרופ' ז'ררדו זלמר לדרקרמר](https://www.tau.ac.il/sites/default/files/styles/research_teaser_image_180_x_180/public/Gerrado180_0.png?itok=MlYFLXn8)
מידע כללי
Research Interests
Recent Publications
For the complete list, visit his lab website:
Sharma N, Patel C, Shenkman M, Kessel A, Ben-Tal N, Lederkremer GZ. The Sigma-1 receptor is an ER-localized type II membrane protein. J Biol Chem. 2021 Oct 11;297(5):101299.
Shenkman M, Geva M, Gershoni-Emek N, Hayden MR, Lederkremer GZ. Pridopidine reduces mutant huntingtin-induced endoplasmic reticulum stress by modulation of the Sigma-1 receptor. J Neurochem. 2021 Jul;158(2):467-481.
Shacham T, Patel C, Lederkremer GZ. PERK Pathway and Neurodegenerative Disease: To Inhibit or to Activate? Biomolecules. 2021 Feb 26;11(3):354.
Patel C, Saad H, Shenkman M, Lederkremer GZ. Oxidoreductases in Glycoprotein Glycosylation, Folding, and ERAD. Cells. 2020 Sep 22;9(9):2138. doi: 10.3390/cells9092138.
Ganz J, Shacham T, Kramer M, Shenkman M, Eiger H, Weinberg N, Iancovici O, Roy S, Simhaev L, Da'adoosh B, Engel H, Perets N, Barhum Y, Portnoy M, Offen D, Lederkremer GZ. A novel specific PERK activator reduces toxicity and extends survival in Huntington's disease models. Sci Rep. 10(1):6875. doi: 10.1038/s41598-020-63899-4. (2020)
Saad, H., Patel, C., Lederkremer, G.Z. (2019) Letting go of O-glycans. J.Biol.Chem. 294, 15912-3.
Shacham, T., Sharma, N. and Lederkremer GZ. Protein misfolding and ER stress in Huntington’s disease. Front Mol Biosci. 6:20. doi: 10.3389/fmolb.2019.00020. (2019).
Shenkman, M., and Lederkremer, G. Z. (2019)
Compartmentalization and Selective Tagging for Disposal of Misfolded Glycoproteins.
Trends in biochemical sciences 44, 827-836
Shenkman M, Ron E, Yehuda R, Benyair R, Khalaila I and Lederkremer GZ. (2018). Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates. Commun Biol. 1:172.
Ogen-Shtern, N., Ben-David, T. and Lederkremer, GZ. (2016). Protein Aggregation and ER Stress. Brain Res. 1648, 658-666.
Ogen-Shtern, N., Avezov, E., Shenkman, M., Benyair, R. and Lederkremer, GZ. (2016). Mannosidase IA is in quality control vesicles and participates in glycoprotein targeting to ERAD. J Mol Biol 428, 3194-205.
Benyair, R., Ogen-Shtern, N., Mazkereth, N., Shai, B., Ehrlich, M. and Lederkremer, G.Z. (2015). Mammalian ER mannosidase I resides in quality control vesicles where it encounters its glycoprotein substrates. Mol Biol Cell 26, 172-84.
Benyair, R., Ogen-Shtern, N. and Lederkremer, GZ. (2015). Glycan regulation of ER-associated degradation through compartmentalization. Seminars Cell Dev Biol 41:99-109.
Leitman, J., Barak, B., Benyair, R., Shenkman, M., Ashery, U., Hartl, F.U. and Lederkremer, G.Z. ER Stress-induced eIF2-alpha Phosphorylation Underlies Sensitivity of Striatal Neurons to Pathogenic Huntingtin. PLoS One 2014 9(3): e90803. pp. 1-10.
Leitman, J., Shenkman, M., Gofman, Y., Ben-Tal, N., Hendershot, L.M. and Lederkremer, G.Z. Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD. Mol Biol Cell. 2014 25(7):1050-60.
Leitman, J., Hartl, F.U. and Lederkremer, G.Z. Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress. Nature Commun 2013;4:2753. pp. 1-10.