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Research Publications

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  1. Shenkman M,  Ogen-Shtern N,  Patel C,  Groisman B,  Pasmanik-Chor M,  Schermann SM,  Körner R,  Lederkremer GZ. Oligosaccharyltransferase is involved in targeting to ER-associated degradation. (2024). bioRxiv 2024 Pages 2024.05.12.593735. DOI: 10.1101/2024.05.12.593735. PREPRINT

  2. Shacham T, Offen, D. and Lederkremer GZ. Efficacy of therapy by MK-28 PERK activation in the Huntington’s disease R6/2 mouse model. (2023). Neurotherapeutics 2024 Vol. 21 Issue 2 Pages e00335. DOI: 10.1016/j.neurot.2024.e00335

  3. Legesse A, Kaushansky N, Braunstein I, Saad H, Lederkremer G, Navon A, Stanhill A. The role of RNF149 in the pre-emptive quality control substrate ubiquitination. (2023). Commun Biol. 2023 Apr 8;6(1):385. doi: 10.1038/s42003-023-04763-9.

  4. Ogen-Shtern, N., C. Chang, H. Saad, N. Mazkereth, C. Patel, M. Shenkman, and G.Z. Lederkremer. COP I and II dependent trafficking controls ER-associated degradation. (2023) iScience, Volume 26, 106232, ,https://doi.org/10.1016/j.isci.2023.106232.

  5. 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. doi: 10.1016/j.jbc.2021.101299. PMID: 34648767 

  6. Shacham T, Patel C, Lederkremer GZ. PERK Pathway and Neurodegenerative Disease: To Inhibit or to Activate? Biomolecules. 2021 Feb 26;11(3):354. doi: 10.3390/biom11030354. PMID: 33652720 Free PMC article. Review.

  7. 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. doi: 10.1111/jnc.15366. Epub 2021 Apr 28.PMID: 33871049

  8. Patel C, Saad H, Shenkman M, Lederkremer GZ. Oxidoreductases in Glycoprotein Glycosylation, Folding, and ERAD. Cells. 2020 Sep 22;9(9):2138. doi:m 10.3390/cells9092138.

  9. García-Huerta P, Troncoso-Escudero P, Wu D, Thiruvalluvan A, Cisternas-Olmedo M, Henríquez DR, Plate L, Chana-Cuevas P, Saquel C, Thielen P, Longo KA, Geddes BJ, Lederkremer GZ, Sharma N, Shenkman M, Naphade S, Sardi SP, Spichiger C, Richter HG, Court FA, Tshilenge KT, Ellerby LM, Wiseman RL, Gonzalez-Billault C, Bergink S, Vidal RL, Hetz C. Insulin-like growth factor 2 (IGF2) protects against Huntington's disease through the extracellular disposal of protein aggregates. Acta Neuropathol. 140(5):737-764 doi: 10.1007/s00401-020-02183-1. (2020)

  10. 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)

  11. Saad, H., Patel, C., Lederkremer, G.Z. (2019) Letting go of O-glycans. J.Biol.Chem. 294, 15912-3.

  12. Shenkman, M., and Lederkremer, G. Z. (2019). Compartmentalization and Selective Tagging for Disposal of Misfolded Glycoproteins. Trends in biochemical sciences 44, 827-836

  13. 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).

  14. 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.

  15. Shenkman, M., Ogen-Shtern, N. and Lederkremer, GZ. (2017) [2-3H]Mannose-labeling and Analysis of N-linked Oligosaccharides. Bio-protocol 7(14): e2393.

  16. Ogen-Shtern, N., Ben-David, T. and Lederkremer, GZ. (2016). Protein Aggregation and ER Stress. Brain Res. 1648, 658-666.

  17. Benyair, R. and Lederkremer, GZ. (2016). Common fixation-permeabilization methods cause artifactual localization of a type II transmembrane protein. Microscopy (Oxford) 2016,517-21.

  18. 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.

  19. Shenkman, M., Eiger, H. and Lederkremer, GZ. (2015). Genesis of ER Stress in Huntington’s Disease. ER Stress in Diseases 2, 94-106.

  20. Lurie, Y., Webb, M., Cytter-Kuint, R., Shteingert, S., Lederkremer, GZ. (2015). Non-invasive diagnosis of liver fibrosis and cirrhosis. World J Gastroenterol 21, 11567-83.

  21. Benyair, R., Ogen-Shtern, N. and Lederkremer, GZ. (2015). Glycan regulation of ER-associated degradation through compartmentalization. Seminars Cell Dev Biol 41:99-109.

  22. 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.

  23. Leitman, J., Shenkman, M., Gofman, Y., Ben-Tal, N., Hendershot, L.M. and Lederkremer, G.Z. (2014). Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD. Mol Biol Cell. 25(7):1050-60.

  24. Leitman, J., Barak, B., Benyair, R., Shenkman, M., Ashery, U., Hartl, F.U. and Lederkremer, G.Z. (2014). ER Stress-induced eIF2-alpha Phosphorylation Underlies Sensitivity of Striatal Neurons to Pathogenic Htt. PLoS One 9(3): e90803. pp. 1-10. Note: Featured in Nature Rev Neurology.

  25. Leitman, J., Hartl, F.U. and Lederkremer, G.Z. (2013). Soluble forms of polyQ-expanded Htt rather than large aggregates cause endoplasmic reticulum stress. Nature Commun 2013;4:2753. pp. 1-10.

  26. Lynes, E. M., Raturi, A., Shenkman, M., Sandoval, C. O., Yap, M. C., Wu, J., Janowicz, A., Myhill, N., Benson, M. D., Campbell, R. E., Berthiaume, L. G., Lederkremer, G. Z., and Simmen, T. (2013). Palmitoylation is the switch that assigns calnexin to quality control or ER Ca2+ signaling. J Cell Sci 126, 3893-3903

  27. Shenkman, M., Groisman, B., Ron, E., Avezov, E., Hendershot, L.M. and Lederkremer, G.Z. (2013). A shared ER-associated degradation pathway involving EDEM1 for glycosylated and nonglycosylated proteins. J Biol Chem 288, 2167-78.

  28. Leitman, J., Ron, E., Ogen-Shtern, N. and Lederkremer, G.Z. (2013). Compartmentalization of ER quality control and ERAD factors. DNA and Cell Biology 32, 2-7. Note: Featured in cover of issue.

  29. Benyair, R., Ron, E. and Lederkremer, G.Z. (2011). Protein quality control, retention and degradation at the endoplasmic reticulum. Int Rev Cell Mol Biol 292,197-280.

  30. Veselkin, E., Kondratyev, M., Lurie, Y., Ron, E., Santo, M., Reif, S., Elashvili, I., Bar, L. and Lederkremer, G.Z. (2011). A secreted form of the asialoglycoprotein receptor, sH2a, as a novel potential non-invasive marker for liver fibrosis. PLoS One 6, e27210.

  31. Benyair, R., Kondratyev, M., Veselkin, E., Tolchinsky, S., Shenkman, M., Lurie, Y., and Lederkremer, G.Z. (2011). Constant serum levels of secreted asialoglycoprotein receptor sH2a and decrease with cirrhosis. World J Gastroenterol 17:5305-5309.

  32. Ron, E., Shenkman, M., Groisman, B., Izenshtein, Y., Leitman, J. and Lederkremer, G.Z.  (2011). Bypass of glycan-dependent glycoprotein delivery to ERAD by upregulated EDEM1. Mol Biol Cell 22:3945-54. Note: Featured in Mol Biol Cell highlights, Nov. 2011.

  33. Groisman, B., Shenkman, M., Ron, E. and Lederkremer, G.Z. (2011). Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late ER-associated degradation steps. J Biol Chem 286 :1292-300. Note: Featured in Nature Functional Glycomics Gateway Dec. 2010.

  34. Benyair, R. and Lederkremer, G.Z. (2010). Precursor N-Linked Oligosaccharides as Codes for Glycoprotein Folding Status. In: Oligosaccharides: Sources, Properties and Applications. ISBN 978-1-61122-193-0. Editor: Nicole S. Gordon. Nova Science Publishers, Inc.

  35. Avezov, E., Ron, E., Izenshtein, Y., Adan, Y., and Lederkremer, G.Z. (2010). Pulse-chase analysis of N-linked sugar chains from glycoproteins in mammalian cells. J Vis Exp 38, 1899-1904.

  36. Lederkremer, G.Z., Glycoprotein folding, quality control and ER-associated degradation, Curr. Op. Str. Biol. 2009. 19, 515-23.

  37. Avezov, A., Frenkel, Z., Ehrlich, M., Herscovics, A. and Lederkremer, G.Z. ER mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation.  Mol Biol Cell, 2008. 19,  216-225.

  38. Kondratyev, M., Avezov, E., Shenkman, M., Groisman, B. and Lederkremer, G.Z. PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress. Exp Cell Res, 2007. 313, 3395-3407.

  39. Shenkman, M., Tolchinsky, S. and Lederkremer, G.Z. Prolonged ER stress and Translational Inhibition Induce Alternative Non-Proteasomal Degradation Pathways for ER but not Cytosolic Substrates.  Cell Stress and Chaperones, 2007. 12, 373-383.

  40. Shenkman, M., Tolchinsky, S., Kondratyev, M. and Lederkremer, G.Z.. Transient arrest in proteasomal degradation during inhibition of translation in the unfolded protein response. Biochem J, 2007. 404, 509-516.

  41. Lederkremer, G.Z. Intracellular Lectin Involvement in Glycoprotein Maturation and Quality Control in the Secretory Pathway. In Glycobiology, Ed. by Sansom, C.  and Markman, O. Scion Publishing Ltd., Oxfordshire (2007) p. 123-134.

  42. Groisman, B., Avezov, E. and G.Z. Lederkremer, The E3 ubiquitin ligases HRD1 and SCFFbs2 recognize the protein moiety and sugar chains respectively of an ER-associated degradation substrate. Isr J Chem 2006. 46, p. 189-196.  Note: Issue in honor of A. Hershko and A. Ciechanover.

  43. Lederkremer, G.Z. and M.H. Glickman, A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem Sci. 2005. 30(6): p. 297-303.

  44. Frenkel, Z., M. Shenkman, M. Kondratyev, and G.Z. Lederkremer, Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains. Mol Biol Cell, 2004. 15(5): p. 2133-42. Epub 2004 Feb 20.

  45. Frenkel, Z., W. Gregory, S. Kornfeld, and G.Z. Lederkremer, Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2. J Biol Chem, 2003. 278(36): p. 34119-24.

  46. Lederkremer, G.Z., Y. Cheng, B.M. Petre, E. Vogan, S. Springer, R. Schekman, T. Walz, and T. Kirchhausen, Structure of the Sec23p/24p and Sec13p/31p complexes of COPII. PNAS, 2001. 98(19): p. 10704-10709.

  47. Kamhi-Nesher, S., M. Shenkman, S. Tolchinsky, S.V. Fromm, R. Ehrlich, and G.Z. Lederkremer, A novel quality control compartment derived from the endoplasmic reticulum. Mol Biol Cell, 2001. 12(6): p. 1711-23.

  48. Shenkman, M., M. Ehrlich, and G.Z. Lederkremer, Masking of an Endoplasmic Reticulum Retention Signal by Its Presence in the Two Subunits of the Asialoglycoprotein Receptor. J. Biol. Chem., 2000. 275(4): p. 2845-2851.

  49. Ayalon-Soffer, M., M. Shenkman, and G.Z. Lederkremer, Differential role of mannose and glucose trimming in the ER degradation of asialoglycoprotein receptor subunits. J Cell Sci, 1999. 112(Pt 19): p. 3309-3318.

  50. Ayalon-Soffer, M., S. Kamhi-Nesher, and G.Z. Lederkremer, Folding and self-assembly do not prevent ER retention and proteasomal degradation of asialoglycoprotein receptor H2a. FEBS letters, 1999. 460: p. 112-116.

  51. Shenkman, M., Ayalon, M. and Lederkremer, G. Z. (1997).  Endoplasmic reticulum quality control of asialoglycoprotein receptor H2a involves a determinant for retention and not retrieval. Proc Natl Acad Sci. 94, 11363-11368.

  52. Tolchinsky, S., Yuk, M., Ayalon, M., Lodish, H. F. and Lederkremer, G. Z. (1996).  Membrane bound versus secreted forms of human asialoglycoprotein receptor subunits: role of a juxtamembrane pentapeptide.  J Biol Chem. 271, 14496-14503.

  53. Scherer P.E., Lederkremer, G.Z., Williams, S., Fogliano, M., Baldini, G. and Lodish, H.F. (1996). Cab45, a novel Ca2+-binding protein localized to the Golgi lumen. J Cell Biol. 133, 257-268. Note: Featured in cover of issue.

  54. Neumann, D., Yuk, M. H., Lodish, H. F. and Lederkremer, G. Z. (1996). Blocking intracellular degradation of the erythropoietin and asialoglycoprotein receptors by calpain inhibitors does not result in the same increase in the levels of their membrane and secreted forms.  Biochem J. 313, 391-399.

  55. Khier, S., Tolchinsky, S., Lederkremer, G.Z. and Shaanan, B. (1994) Modeling the combining site of the human asialoglycoprotein receptor.  Isr. J. Chem. 34, 177-184.

  56. Lederkremer, G.Z. and Lodish, H.F. (1991) An alternatively spliced miniexon alters the subcellular fate of the human asialoglycoprotein receptor H2 subunit: Endoplasmic reticulum retention and degradation or cell surface expression. J. Biol. Chem. 266, 1237-1244.

  57. Amara, J.E., Lederkremer, G., and Lodish, H.F. (1989) Intracellular degradation of unassembled asialoglycoprotein receptor subunits: a pre-Golgi, non-lysosomal endoproteolytic cleavage. J. Cell Biol. 109, 3315-3324.

  58. Eshhar, N., Lederkremer, G. & Teichberg, V.I. (1989) The use of Kainyl-bovine serum albumin in the visualization by autoradiography and immunoperoxidase staining of kainate binding sites. in Excitatory amino acids 1988 Plenum Press. J. Lehmann, L. Turski and E.A. Cavalheiro editors.

  59. Eshhar, N., Lederkremer, G, Beaujean, M., Goldberg, 0., Gregor P., Ortega, A., Triller, A. & Teichberg, V.I. (1989) Kainyl-bovine serum albumin: a novel ligand of the kainate sub-type of glutamate receptor with a very high binding affinity. Brain Research 476, 57-70.

  60. Lederkremer, G.Z. & Parodi, A.J. (1986) Processing of asparagine-linked saccharides in Mucor rouxii. Biochim. Biophys. Acta 884, 363-369.

  61. Lederkremer, G.Z. & Parodi, A.J. (1986) The structure of the main dolichol-P-P linked oligosaccharide present in Mucor rouxii. Anal. As. Quim. Arg. 74, 643. Note: In honor of Luis F. Leloir.

  62. Lederkremer, G.Z. & Parodi, A.J. (1984) 3-0-Methylation of mannose residues. A novel reaction in the processing of N-linked oligosaccharides occurring in Mucor rouxii. J. Biol. Chem. 259, 12514-12518.

  63. Parodi, A.J., Mendelzon, D.H., Lederkremer, G.Z. & Martin-Barrientos, J. (1984) Evidence that transient glucosylation of protein-linked Man9GlcNAc2, Man8GlcNAc2 and Man7GlcNAc2 occurs in rat liver and Phaseolus vulgaris cells. J. Biol. Chem. 259, 6351-6357.

  64. Lederkremer, G.Z. & Parodi, A.J. (1983) Separation of dolichol monophosphate mannose and dolichol monophosphate glucose by thin-layer chromatography. J. Chromatogr. 262, 299-304.

  65. Parodi, A.J., Mendelzon, D.H. & Lederkremer, G.Z. (1983) Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2 and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins. J. Biol. Chem. 258, 8260-8265.

  66. Parodi, A.J., Lederkremer, G.Z. & Mendelzon, D.H. (1983) Protein glycosylation in Trypanosoma cruzi. The mechanism of glycosylation and structure of protein-bound oligosaccharides. J. Biol. Chem. 258, 5589-5595.

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