Year |
Citation |
Score |
2023 |
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. Communications Biology. 6: 385. PMID 37031316 DOI: 10.1038/s42003-023-04763-9 |
0.351 |
|
2020 |
Tabachnick-Cherny S, Pinto S, Berko D, Curato C, Wolf Y, Porat Z, Karmona R, Tirosh B, Jung S, Navon A. Polyglutamine-Related Aggregates Can Serve as a Potent Antigen Source for Cross-Presentation by Dendritic Cells. Journal of Immunology (Baltimore, Md. : 1950). PMID 33067378 DOI: 10.4049/jimmunol.1901535 |
0.76 |
|
2020 |
Ferro ES, Gewehr MCF, Navon A. Thimet Oligopeptidase Biochemical and Biological Significances: Past, Present, and Future Directions. Biomolecules. 10. PMID 32847123 DOI: 10.3390/biom10091229 |
0.309 |
|
2017 |
Demishtein A, Fraiberg M, Berko D, Tirosh B, Elazar Z, Navon A. SQSTM1/p62-mediated autophagy compensates for loss of proteasome polyubiquitin recruiting capacity. Autophagy. 0. PMID 28792301 DOI: 10.1080/15548627.2017.1356549 |
0.776 |
|
2015 |
Altun M, Walter TS, Kramer HB, Herr P, Iphöfer A, Boström J, David Y, Komsany A, Ternette N, Navon A, Stuart DI, Ren J, Kessler BM. The human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages. Plos One. 10: e0115344. PMID 25590432 DOI: 10.1371/Journal.Pone.0115344 |
0.727 |
|
2015 |
Altun M, Walter TS, Kramer HB, Herr P, Iphöfer A, Boström J, David Y, Komsany A, Ternette N, Navon A, Stuart DI, Ren J, Kessler BM. OTUB2 has a broader cleavage profile than OTUB1. Plos One. DOI: 10.1371/Journal.Pone.0115344.G005 |
0.626 |
|
2014 |
Piterman R, Braunstein I, Isakov E, Ziv T, Navon A, Cohen S, Stanhill A. VWA domain of S5a restricts the ability to bind ubiquitin and Ubl to the 26S proteasome. Molecular Biology of the Cell. 25: 3988-98. PMID 25318673 DOI: 10.1091/Mbc.E13-11-0697 |
0.438 |
|
2014 |
Raule M, Cerruti F, Benaroudj N, Migotti R, Kikuchi J, Bachi A, Navon A, Dittmar G, Cascio P. PA28αβ reduces size and increases hydrophilicity of 20S immunoproteasome peptide products. Chemistry & Biology. 21: 470-80. PMID 24631123 DOI: 10.1016/J.Chembiol.2014.02.006 |
0.382 |
|
2014 |
Tsvetkov P, Myers N, Eliav R, Adamovich Y, Hagai T, Adler J, Navon A, Shaul Y. NADH Binds and stabilizes the 26S proteasomes independent of ATP Journal of Biological Chemistry. 289: 11272-11281. PMID 24596095 DOI: 10.1074/Jbc.M113.537175 |
0.44 |
|
2014 |
Berko D, Herkon O, Braunstein I, Isakov E, David Y, Ziv T, Navon A, Stanhill A. Inherent asymmetry in the 26S proteasome is defined by the ubiquitin receptor RPN13. The Journal of Biological Chemistry. 289: 5609-18. PMID 24429290 DOI: 10.1074/Jbc.M113.509380 |
0.714 |
|
2012 |
Berko D, Tabachnick-Cherny S, Shental-Bechor D, Cascio P, Mioletti S, Levy Y, Admon A, Ziv T, Tirosh B, Goldberg AL, Navon A. The direction of protein entry into the proteasome determines the variety of products and depends on the force needed to unfold its two termini. Molecular Cell. 48: 601-11. PMID 23041283 DOI: 10.1016/J.Molcel.2012.08.029 |
0.76 |
|
2012 |
Pomerantz Y, Elbaz J, Ben-Eliezer I, Reizel Y, David Y, Galiani D, Nevo N, Navon A, Dekel N. From ubiquitin-proteasomal degradation to CDK1 inactivation: requirements for the first polar body extrusion in mouse oocytes. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 26: 4495-505. PMID 22859367 DOI: 10.1096/Fj.12-209866 |
0.685 |
|
2011 |
David Y, Ternette N, Edelmann MJ, Ziv T, Gayer B, Sertchook R, Dadon Y, Kessler BM, Navon A. E3 ligases determine ubiquitination site and conjugate type by enforcing specificity on E2 enzymes. The Journal of Biological Chemistry. 286: 44104-15. PMID 21965653 DOI: 10.1074/Jbc.M111.234559 |
0.698 |
|
2011 |
Shimshon L, Michaeli A, Hadar R, Nutt SL, David Y, Navon A, Waisman A, Tirosh B. SUMOylation of Blimp-1 promotes its proteasomal degradation. Febs Letters. 585: 2405-9. PMID 21722636 DOI: 10.1016/J.Febslet.2011.06.022 |
0.691 |
|
2011 |
Kario E, Amar N, Elazar Z, Navon A. A new autophagy-related checkpoint in the degradation of an ERAD-M target. The Journal of Biological Chemistry. 286: 11479-91. PMID 21228276 DOI: 10.1074/Jbc.M110.177618 |
0.743 |
|
2010 |
Li X, Wood TE, Sprangers R, Jansen G, Franke NE, Mao X, Wang X, Zhang Y, Verbrugge SE, Adomat H, Li ZH, Trudel S, Chen C, Religa TL, Jamal N, ... ... Navon A, et al. Effect of noncompetitive proteasome inhibition on bortezomib resistance. Journal of the National Cancer Institute. 102: 1069-82. PMID 20505154 DOI: 10.1093/Jnci/Djq198 |
0.346 |
|
2010 |
David Y, Ziv T, Admon A, Navon A. The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. The Journal of Biological Chemistry. 285: 8595-604. PMID 20061386 DOI: 10.1074/Jbc.M109.089003 |
0.702 |
|
2010 |
Navon A, Gatushkin A, Zelcbuch L, Shteingart S, Farago M, Hadar R, Tirosh B. Direct proteasome binding and subsequent degradation of unspliced XBP-1 prevent its intracellular aggregation. Febs Letters. 584: 67-73. PMID 19941857 DOI: 10.1016/J.Febslet.2009.11.069 |
0.457 |
|
2009 |
Lavelin I, Beer A, Kam Z, Rotter V, Oren M, Navon A, Geiger B. Discovery of novel proteasome inhibitors using a high-content cell-based screening system. Plos One. 4: e8503. PMID 20041034 DOI: 10.1371/Journal.Pone.0008503 |
0.647 |
|
2009 |
Navon A, Ciechanover A. The 26 S proteasome: from basic mechanisms to drug targeting. The Journal of Biological Chemistry. 284: 33713-8. PMID 19812037 DOI: 10.1074/Jbc.R109.018481 |
0.482 |
|
2009 |
Medalia N, Beer A, Zwickl P, Mihalache O, Beck M, Medalia O, Navon A. Architecture and molecular mechanism of PAN, the archaeal proteasome regulatory ATPase. The Journal of Biological Chemistry. 284: 22952-60. PMID 19363223 DOI: 10.1074/Jbc.M809643200 |
0.642 |
|
2008 |
Kario E, Tirosh B, Ploegh HL, Navon A. N-linked glycosylation does not impair proteasomal degradation but affects class I major histocompatibility complex presentation Journal of Biological Chemistry. 283: 244-254. PMID 17951257 DOI: 10.1074/Jbc.M706237200 |
0.754 |
|
2007 |
Horwitz AA, Navon A, Groll M, Smith DM, Reis C, Goldberg AL. ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea. The Journal of Biological Chemistry. 282: 22921-9. PMID 17553803 DOI: 10.1074/Jbc.M702846200 |
0.511 |
|
2005 |
Costanzi J, Sidransky D, Navon A, Goldsweig H. Ribonucleases as a novel pro-apoptotic anticancer strategy: review of the preclinical and clinical data for ranpirnase. Cancer Investigation. 23: 643-50. PMID 16305992 DOI: 10.1080/07357900500283143 |
0.309 |
|
2001 |
Navon A, Goldberg AL. Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome Molecular Cell. 8: 1339-1349. PMID 11779508 DOI: 10.1016/S1097-2765(01)00407-5 |
0.554 |
|
2001 |
Gomes MD, Lecker SH, Jagoe RT, Navon A, Goldberg AL. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proceedings of the National Academy of Sciences of the United States of America. 98: 14440-5. PMID 11717410 DOI: 10.1073/Pnas.251541198 |
0.5 |
|
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