Publications (2011- )

Original Papers:Ubiquitin Image

  1. Kashuba, E., Yurchenko, M., Yenamandra, S.P., Snopok, B., Szekely, L., Bercovich, B.,  Ciechanover, A., and Klein, G. (2011). Epstein-Barr Virus-Encoded EBNA-5 Forms Trimolecular Protein Complexes with MDM2 and p53 and inhibits the transactivating function of p53.  Int. J. Cancer 128, 817-825.
  2. de Bie P, Zaaroor-Regev D, and Ciechanover A. (2010). Regulation of the Polycomb protein RING1B ubiquitination by USP7. Biochem. Biophys. Res. Commun. 400, 389-395.
  3. Kravtsova-Ivantsiv, Y., Cohen, S., and Ciechanover A. (2011). Modification by Single Ubiquitin Moieties Rather Than Polyubiquitination is Sufficient for Proteasomal Processing of the p105 NF-κB Precursor.  Adv. Exp. Med. Biol. 691, 95-106.
  4. Moyal, L., Lerenthal, Y., Gana-Weisz, M., Mass, G., So, S., Wang, S.Y., Eppink, B., Chung, Y.M., Shalev, G., Shema, E., Shkedy, D., Smorodinsky, N.I., van Vliet, N., Kuster, B., Mann, M., Ciechanover, A., Dahm-Daphi, J., Kanaar, R., Hu, M.C., Chen, D.J., Oren, M., and Shiloh, Y. (2011). Requirement of ATM-Dependent Monoubiquitylation of Histone H2B for Timely Repair of DNA Double-Strand Breaks.  Mol. Cell 41, 529-542.
  5. Kühnle, S., Kogel, U., Glockzin, S., Marquardt, A., Ciechanover, A., Matentzoglu, K., and Scheffner, M. (2011). Physical and functional interaction of the HECT ubiquitin-protein ligases E6AP and HERC2. J. Biol. Chem. 286, 19410-19416.
  6. Zoaby, M., Sadeh, R., and Ciechanover, A. (2011). PRAJA1 is a Ubiquitin Ligase for the Polycomb Repressive Complex 2 Proteins. Biochem. Biophys. Res. Commun. 408, 393-398.
  7. Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2011). Ubiquitination and   Degradation of Proteins.  Methods Mol. Biol. 753, 335-357.
  8. Ciechanover, A., Shoenfeld, Y., Shemer, J., Eidelman, L., and Borow, M. (2011). Response to Health in the Occupied Palestinian Territory.  The Lancet 378, e1.
  9. Nguyen, L.K., Muñoz-García, J., Maccario, H., Ciechanover, A., Kolch, W., and Kholodenko, B.N. (2011).  Switches, Excitable Responses and Oscillations in the Ring1B/Bmi1 Ubiquitination System.  PLoS Comput Biol. 7, e1002317 
  10. Buchsbaum, S., Bercovich, B., and Ciechanover, A. (2012).  FAT10 is a Proteasomal Degradation Signal which is itself Regulated by Ubiquitination. Mol. Biol. Cell 23, 225-232.
  11. Craxton, A., Butterworth, M., Harper, N., Fairall, L., Schwabe, J., Ciechanover, A., and Cohen, G.M. (2012). NOXA, a sensor of proteasome integrity, is degraded by 26S proteasomes by an ubiquitin-independent pathway that is blocked by MCL-1. Cell Death Differ. 19, 1424-1434.
  12. Noy, T., Suad, O., Taglicht, D., and Ciechanover, A. (2012). HUWE1 ubiquitinates MyoD and targets it for proteasomal degradation. Biochem Biophys Res Commun.  418, 408-413.
  13. Braten, O., Shabek, N., Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2012). Generation of free ubiquitin chains is upregulated in stress, and facilitated by the HECT domain ubiquitin ligases UFD4 and HUL5.  Biochem J. 444, 611-617.
  14. Shabek, N., Herman-Bachinsky, Y., Buchsbaum, S., Lewinson, O., Haj-Yahya, M., Hejjaoui, M., Lashuel, H.A., Sommer, T., Brik, A., and Ciechanover, A. (2012). The Size of the Proteasomal Substrate Determines whether its Degradation will be Mediated by Mono- or Polyubiquitylation. Mol. Cell 48, 87-97. Reviewed by F1000. Reviewed by Nature Reviews in Cell and Molecular Biology 
  15. De Bie, Prim, and Ciechanover, A. (2012). RING1B ubiquitination and stability are regulated by ARF. Biochem. Biophys. Res. Commun. 426, 49-53.
  16. Ciechanover, A. (2012).  Reprint of “A Heat-Sstable Polypeptide Component of an ATP-Dependent Proteolytic System from Reticulocytes”. Biochem. Biophys. Res. Commun. 425, 565-570.
  17. Buchsbaum, S., Bercovich, B., Ziv, T., and Ciechanover A. (2012). Modification of the Inflammatory Mediator LRRFIP2 by the Ubiquitin-Like Protein FAT10 Inhibits its Activity During Cellular Response to LPS.  Biochem. Biophys. Res. Commun. 428, 11-16.
  18. Bagola, K., von Delbrück, M., Dittmar, G., Scheffner, M., Ziv, I., Glickman, M.H., Ciechanover, A., and Sommer, T. (2013). Ubiquitin Binding by a CUE Domain Regulates Ubiquitin Chain Formation by ERAD E3 Ligases. Mol. Cell 50, 528-539.
  19. Haj-Yahya, N., Haj-Yahya, M., CastaÇeda, C. A., Spasser, L., Hemantha, H. P., Jbara, M., Penner, M., Ciechanover, A., Fushman, D., and Brik, A. (2013). Modifying the Vicinity of the Isopeptide Bond to Reveal Differential Behavior of Ubiquitin Chains with Interacting roteins. Angew. Chem. Int. Ed. Engl. 52, 11149-11153. 
  20. Haj-Yahyaa, M., Fauvet, B., Herman-Bachinsky, Y., Hejjaoui, M., Bavikar, S. N., Karthikeyan, S. V., Ciechanover, A.* , Lashuel, H. A.*, and Brik, A.* (2013). Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating pathophysiology. Proc. Natl. Acad. Sci. USA 110, 17726-17731.
    *Corresponding authors
  21. Hemantha, H.P., Bavikar, S.N., Herman-Bachinsky, Y., Haj-Yahya, N., Bondalapati, S., Ciechanover, A., and Brik, A. (2014).  Nonenzymatic polyubiquitination of expressed proteins.  J. Am. Chem. Soc. 136, 2665-2673.
  22. Belogurov, A., Kudriaeva, A. K., Kuzina, E., Smirnov, A., Boblik, T., Ponomarenko, N., Kravtsova-Ivantsiv, Y., Ciechanover, A.*, and Gabibov, A.* (2014).  Multiple Sclerosis Autoantigen Myelin Basic Protein Escapes Control by Ubiquitination During Proteasomal Degradation.  J. Biol. Chem. 289, 17758-17766.
  23. Rossi, M., Rotblat, B., Ansell, K., Amelio, I., Caraglia, M., Misso, G., Bernassola, F., Cavasotto, C.N., Knight, R.A., Ciechanover, A.*, and Melino, G.* (2014). High Throughput Screening for Inhibitors of the HECT Ubiquitin E3 Ligase ITCH Identifies Antidepressant Drugs as Regulators of Autophagy. Cell Death Dis. 1;5:e1203. doi: 10.1038/cddis.2014.113: PMID: 24787015].
    *Corresponding authors
  24. Queisser, M.A., Dada, L.A., Deiss-Yehiely, N., Angulo, M., Zhou, G., Kouri, F.M., Knab, L.M., Liu, J., Stegh, A.H., DeCamp, M.M., Budinger, G.R., Chandel, N.S., Ciechanover, A., Iwai, K., and Sznajder, J.I. (2014). HOIL-1L Functions as the PKCζ Ubiquitin Ligase to Promote Lung Tumor Growth.  Am. J. Respir. Crit. Care Med. 190, 688-698.
  25. Ahmed, Q., Avidan, A.Y., Ciechanover, A., Shechtman, D., Zajfman, D., Reichman, U., Kornberg, R., Hershko, A., and Lavie, P. (2014). Israel-Gaza Conflict. Lancet 384, 9945. e34-7. doi: 10.1016/S0140-6736(14)61314-3. Epub August 18, 2014.    PMID:  25145777
  26. Kravtsova-Ivantsiv, Y., Shomer, I., Cohen-Kaplan, V., Snijder, B., Superti-Furga, G., Gonen, H., Sommer, T., Ziv, T., Admon, A., Naroditky, I., Jbara, M., Brik, A., Pikarsky, E., Kwon, Y.T. Doweck, I., and Ciechanover, A.  (2015). KPC1-mediated ubiquitination and Proteasomal Processing of NF-κB p105 to p50 Restricts Tumor Growth. Cell 161, 333-347.
  27. Cha-Molstad, H., Sung, K.S., Hwang, J., Kim, K.A., Yu, J.E., Yoo, Y.D., Jang, J.M., Han, D.H., Molstad, M., Kim, J.G., Lee, Y.J., Zakrzewska, A., Kim, S.H., Kim, S.T., Kim, S.Y., Lee, H.G., Soung, N.K., Ahn, J.S., Ciechanover, A., Kim, B.Y., and Kwon, Y.T. (2015). Amino-Terminal Arginylation Targets Endoplasmic Reticulum Chaperone BiP for Autophagy Through p62 Binding.  Nat. Cell Biol. 17, 917-929.
  28. Cha-Molstad, H., Yu, J.E., Lee, S.H., Kim, J.G., Sung, K.S., Hwang, J., Yoo, Y.D., Lee, Y.J., Kim, S.T., Lee, D.H., Ciechanover, A., Kim, B.Y., and Kwon, Y.T. (2016). Modulation of SQSTM1/p62 Activity by N-Terminal Arginylation of the Endoplasmic Reticulum Chaperone HSPA5/GRP78/BiP.  Autophagy 12, 426-428. 
  29. Lehmann, G., Udasin, R.G., and Ciechanover, A. (2016). On the Linkage Between the Ubiquitin-Proteasome System and the Mitochondria. Biochem. Biophys. Res. Commun. 473, 80-86. doi: 10.1016/j.bbrc.2016.03.055. Epub 2016 Mar 18.  PMID: 26996128
  30. Lehmann, G., Ziv, T., Braten, O., Admon, A., Udasin, R.G., and Ciechanover, A. (2016).  Ubiquitination of Specific Mitochondrial Matrix Proteins.  Biochem. Biophys. Res. Commun. 475, 13-18. pii: S0006-291X(16)30699-4. doi: 10.1016/j.bbrc.2016.04.150. [Epub ahead of print].  PMID: 27157140
  31. Braten, O., Livneh, I., Ziv, T., Admon, A., Kehat, I., Caspi, L., Gonen, H., Bercovich, B., Godzik, A., Jahandideh, S., Jaroszewski, L. Sommer, T., Kwon, Y.T. Guharoy, M., Tompa, P., and Ciechanover, A. (2016). Numerous Proteins with Unique Characteristics are Degraded by the 26S Proteasome Following Monoubiquitination. Proc. Natl. Acad. Sci. USA 113 (32): E4639-47. doi: 10.1073/pnas.1608644113. Epub 2016 Jul 6.
    Highlighted in:
    Ronai, Z.A. (2016). Monoubiquitination in Proteasomal Degradation.  Proc. Natl. Acad. Sci. USA. 113, 8894-8896. doi: 10.1073/pnas.1610186113. Epub 2016 Aug 1.
  32. Cohen-Kaplan, V., Livneh, I., Avni, N., Fabre, B., Ziv, T., Kwon, Y. T., Ciechanover, A. (2016). p62- and Ubiquitin-Dependent Stress-Induced Autophagy of the Mammalian 26S Proteasome. Proc. Natl. Acad. Sci. USA E7490-E7499. www.pnas.org/cgi/dpi/10.1073/pnas.1615455113.
    Highlighted in:
    1) Hoeller, D., and Dikic, I. (2016). How the Proteasome is Degraded. Proc. Natl. Acad. Sci. USA 113, 13266-13268.
    2) Cohen-Kaplan, V., Ciechanover, A.,* and Livneh, I. (2016). p62 at the crossroad of the ubiquitin-proteasome system and autophagy. Oncotarget doi: 10.18632/oncotarget.13805. PMID: 27974671
    *Corresponding author  
  33. Lahav-Baratz, S., Kravtsova-Ivantsiv, Y., Golan, S., and Ciechanover, A. (2016). The testis-specific USP26 is a deubiquitinating enzyme of the ubiquitin ligase Mdm2. Biochem. Biophys. Res. Commun. 482, 106-111. doi: 10.1016/j.bbrc.2016.10.135. PMID: 27810359
  34. Yoo, Y.D., Lee, D.H., Cha-Molstad, H., Kim, H., Mun, S.R., Ji, C., Park, S.H., Sung, K.S., Choi, S.A., Hwang, J., Park, D.M., Kim, S.K., Park, K.J., Kang, S.H., Oh, S.C., Ciechanover, A., Lee, Y.J., Kim, B.Y., and Kwon Y.T. (2017). Glioma-derived cancer stem cells are hypersensitive to proteasomal inhibition. EMBO Rep. 18, 150-168. doi: 10.15252/embr.201642360. PMID: 27993939.
  35. Lehmann, G., Udasin, R.G., Livneh, I., and Ciechanover, A. (2017). Identification of UBact, a Ubiquitin-Like Protein, Along With Other Homologous Components of a Conjugation System and the Proteasome in Different Gram-Negative Bacteria. Biochem. Biophys. Res. Commun.  DOI information: 10.1016/j.bbrc.2017.01.037 PMID: 28087277.
  36. Shim, S.-M., Choi, H.-R., Sung, K.-W., Yoon, J.-L., Sung, T.-K., Kim, D., Mun, S.-R., Hwang, J., Cha-Molstad,H., Ciechanover, A., Kim, B.-Y., and Kwon, Y.-T. (2018).  The Endoplasmic Reticulum–Residing Caperone BiP is Short-Lived and Metabolized through N-Terminal Arginylation Sci. Signaling 11(511). pii: eaan0630. doi: 10.1126/scisignal.aan0630. PMID: 29295953.
  37. Cha-Molstad, H., Lee, S-.H., Kim, J.-G., Sung,. K.-W., Hwang, J., Shim, S.-M.,  Ganipisetti, S., McGuire, T., Mook-Jung, I., Ciechanover, A., Xie, X.Q., Kim, B.Y., and Kwon, Y.-T. (2017). Regulation of Autophagic Proteolysis by the N-Recognin SQSTM1/p62 of the N-End Rule Pathway. Autophagy 20, 1-6. doi: 10.1080/15548627.2017.1415190. PMID: 26797053.
  38. Yoo, Y.D., Mun, S.R., Ji, C.H., Sung, K.W., Kang, K.Y., Heo, A.J., Lee, S.H., An, J.Y., Hwang, J., Xie, X.Q., Ciechanover, A., Kim, B.Y., and Kwon, Y.T. (2018). N-Terminal Arginylation Generates a Bimodal Degron that Modulates Autophagic Proteolysis. Proc. Natl. Acad .Sci. USA pii: 201719110. doi: 10.1073/pnas.1719110115. PMID: 29507222.
  39. Yoo, Y.D., Lee, D.H., Cha-Molstad, H., Kim, H., Mun, S.R., Ji, C., Park, S.H.,Sung, K.S., Choi, S.A., Hwang, J., Park, D.M., Kim, S.K., Park, K.J., Kang, S.H., Oh, S.C., Ciechanover, A., Lee, Y.J., Kim, B.Y., and Kwon, Y.T. (2018).  Glioma-derived cancer stem cells are hypersensitive to proteasomal inhibition. EMBO Rep. 19, pii: e46380. doi: 10.15252/embr.201846380. PMID: 30185565.
  40. Sun, H., Mali, S.M., Singh, S.K., Meledin, R., Brik, A., Kwon, Y. T., Kravtsova-Ivantsiv Y., Bercovich, B., and Ciechanover, A. (2019). Diverse fate of ubiquitin chain moieties: The proximal is degraded with the target, and the distal protects the proximal from removal and recycles. Proc. Natl. Acad. Sci. USA 116, 7805-7812.
  41. Nawatha, M., Rogers, J.M., Bonn, S.M., Livneh, I., Lemma, B., Mali, S.M.,Vamisetti, G.B., Sun, H., Bercovich, B., Huang, Y., Ciechanover, A.,  Fushman, D., Suga, H., and Brik, A. (2019). Nature Chem.  doi.org/10.1038/s41557-019-0278-x. Fabre, B., I. Livneh, Ziv, T., and Ciechanover, A. (2019). Identification of proteins regulated by the proteasome following induction of endoplasmic reticulum stress.  Biochem. Biophys. Res. Commun. https://doi.org/10.1016/j.bbrc.2019.07.040
  42. Ji, C.H., Kim, H.Y., Heo, A.J., Lee, S.H., Lee, M.J., Kim, S.B., Srinivasrao, G., Mun, S.R., Cha-Molstad, H., Ciechanover, A., Choi, C.Y., Lee, H.G., Kim, B.Y., and Kwon, Y.T. (2019). The N-Degron Pathway Mediates ER-phagy. Mol. Cell 75, 1058-1072. e9. doi: 10.1016/j.molcel.2019.06.028.
  43. Pasca, S., Tomuleasa, C., Teodorescu, P., Ghiaur, G., Dima, D., Moisoiu, V., Berce, C., Stefan, C., Ciechanover, A., and Einsele, H. (2019). KRAS/NRAS/BRAF Mutations as Potential Targets in Multiple Myeloma. Front. Oncol. 9:1137. doi: 10.3389/fonc.2019.01137. eCollection 2019. PMID: 31709194.
  44. Wang, X., Bustos, M.A., Zhang, X., Ramos, R.I.,  Tan, C.,  Iida, Y., Chang, S.-C.,  Salomon, M.P., Tran, K., Gentry, R., Kravtsova-Ivantsiv, Y., Kelly, D.F., Mills, G.B., Ciechanover, A., Mao, Y., and Hoon, D.S.B. (2020). Downregulation of the Ubiquitin-E3 Ligase RNF123 Promotes Upregulation of the NF-κB1 Target SerpinE1 in Aggressive Glioblastoma Tumors Cancers 12, 1081; https://doi.org/10.3390/cancers12051081 (registering DOI).
  45. Huang, Y., Nawatha, M., Livneh, I., Rogers, J.M., Sun, H., Singh, S.K., Ciechanover, A., Brik, A., and Suga, H. (2020). Affinity Maturation of Macrocyclic Peptide Modulators of Lys48-Linked Diubiquitin by a Twofold Strategy. Chemistry 26, 8022-8027. doi: 10.1002/chem.202000273. Epub June 8, 2020.
  46. Hakim-Eshed, V., Boulos, A., Cohen-Rosenzweig, C., Libo Yu-Taegerd, L., Ziv, T., Kwon, Y.-T., Riess, O., Nguyen, H.H.P., Ziv, N.E., and Ciechanover, A. (2020). Site-specific ubiquitination of pathogenic huntingtin attenuates its deleterious effects. Proc. Natl. Acad. Sci,  USA. www.pnas.org/cgi/doi/10.1073/pnas.2007667117.
  47. Kravtsova-Ivantsiv, Y., Goldhirsh, G., Ivantsiv A., Ben Itzhak, O., Kwon, Y.-T., Pikarsky, E., and Ciechanover, A. (2020). Excess of the NF-ĸB p50 subunit generated by the ubiquitin ligase KPC1 suppresses tumors via PD-L1– and chemokines-mediated mechanisms. Proc. Natl. Acad. Sci,  USA. www.pnas.org/cgi/doi/10.1073/pnas.2019604117.
  48. Udasin, R.G., Gottfried, Y., Fabre, B., Bercovich, B., Ziv, T., and Ciechanover, A. (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 proliferation. Biochem. Biophys. Res. Commun. https://doi.org/10.1016/j.bbrc.2020.08.098.
  49. Fu, A., Cohen-Kaplan, V., Avni, N., Livneh, I., and Ciechanover, A. (2021). p62-containing, proteolytically active nuclear condensates, increase the efficiency of the ubiquitin-proteasome system. Proc. Natl. Acad. Sci. USA 118:e2107321118. DOI: 10.1073/pnas.2107321118. PMID: 34385323

    Review Articles:

  1. de Bie, P. and Ciechanover, A. (2011). Ubiquitination of E3 Ligases: Self-Regulation of the Ubiquitin System via Proteolytic and Non-Proteolytic Mechanisms. Cell Death Differ. 18, 1393-1402.  Mar 4, 2011  [Epub ahead of print].
  2. Ciechanover, A. (2011).  Intracellular Protein Degradation: From a Vague Idea thru the Lysosome and the Ubiquitin-Proteasome System and onto Human Diseases and Drug Targeting.  Biochim. Biophys. Acta.  1824, 3-13 [Epub ahead of print, 22 March 2011].
  3. Weissman, A.M., Shabek, N., and Ciechanover, A.  (2011).  The Predator Becomes the Prey: Regulating the Ubiquitin System by Ubiquitylation and Degradation. Nature Rev. Mol. Cell. Biol. 12, 605-620.
  4. Kravtsova-Ivantsiv, Y., and Ciechanover A. (2011). Ubiquitination and Degradation of Proteins.  Methods Mol. Biol. (Gel-Free Proteomics Methods and Protocols; Kris Gevaert, ed.).  Humana Press, Inc.  753, 335-357.
  5. Ciechanover, A. (2011). On the Wings of Imagination.  Nature 478 (7368), S4. doi: 10.1038/478S4a.  PMID:  21993824
  6. Ciechanover, A.J., and Sznajder, J.I. (2011).  Innate and Adaptive Immunity:  The 2011 Nobel Prize in Physiology or Medicine.  Am. J. Respir. Crit. Care Med. 184, i-ii.
  7. Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2012). Non-Canonical Ubiquitin-Based Signals for Proteasomal Degradation.  J. Cell Sci. 125 (Pt 3), 539-548.
  8. Ciechanover, A. (2012). Intracellular Protein Degradation: From a Vague Idea through the Lysosome and the Ubiquitin-Proteasome System and onto Human Diseases and Drug Targeting.  Neurodegener. Dis. 10, 7-22.
  9. Ciechanover, A. (2012). Why Our Proteins Have to Die So We Shall Live? The Ubiquitin Proteolytic System – From Basic Mechanisms Thru Pathogenesis of Diseases and Onto Drug Targeting.  Allergol. Immunol. 12, 197-201.
  10. Sznajder, J.I., and Ciechanover, A. (2012).  Personalized Medicine:  The Road Ahead.  Am. J. Respir. Crit. Care Med. 186, 945–947.
  11. Kravtsova-Ivantsiv, Y., Sommer, T., and Ciechanover, A. (2013).  The Lysine48-Based Polyubiquitin Chain Proteasomal Signal: Not a Single Child Anymore. Angew. Chem. Int. Ed. Engl. 52, 192-198.
  12. Ciechanover, A. (2013). Intracellular Protein Degradation: From a Vague Idea through the Lysosome and the Ubiquitin-Proteasome System and onto Human Diseases and Drug Targeting.  Bioorg. Med. Chem.  21, 3400-3410.
  13. Ciechnaover, A. (2013). An Interview with Aaron Ciechanover. Trends Biochem. Sci.  38, 219-221.
  14. Ciechanover, A. (2013). A conversation with Aaron Ciechanover. Interview by Ushma S. Neill. J. Clin. Invest. 123, 4093-4094.
  15. Ciechanover, A. (2013). Intracellular Protein Degradation: From a Vague Idea Through the Lysosome and the Ubiquitin-Proteasome System, and on to Human Diseases and Drug targeting.  Eur. J. Neurodegener. Dis. 2, 113-132
  16. Ciechanover, A., and Stanhill, A. (2014). The Complexity of Recognition of Ubiquitinated Substrates by the 26S Proteasome. Biochim Biophys Acta. 1843, 86-96.
  17. Ciechanover, A. (2015). The Unraveling of the Ubiquitin System. Nature Rev. Mol. Cell. Biol. 16, 322-324.
  18. Ciechanover, A., and Kwon, Y.T. (2015). Degradation of Misfolded Proteins in Neurodegenerative Diseases: Therapeutic Targets and Strategies. Exptl. and Mol. Med. 47, e147; doi:10:1038/emm.2014.117
  19. Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2015). The Ubiquitin-Proteasome System and Activation of NF-kB: Involvement of the Ubiquitin Ligase KPC1 in p105 Processing and Tumor Suppression.  Mol. Cell. Oncol.; (e1054552-1) ISSN: (Print) 2372-3556 (Online) Journal homepage.
  20. Mollereau, B., Rzechorzek, N.M., Roussel, B.D., Sedru, M., Van denBrink, D., Bailly-Maitre, B., Palladino, F., Medinas, D.B., Domingos, P.M., Hunot, S., Chandran, S., Birman, S., Baron, T., Vivien, D., Duarte, C.B., Ryoo, H.-D., Steller, H., Urano, F., Chevet, E., Kroemer, G., Ciechanover, A., Calabrese, E.J., Kaufman, R.J., and Hetz, C. (2016). Adaptive Preconditioning in Neurological Diseases: Therapeutic Insights from Proteostatic Perturbations.  Brain Research. pii: S0006-8993(16)30092-0. doi: 10.1016/j.brainres.2016.02.033. [Epub ahead of print] Review.  PMID: 26923166
  21. Eisenberg-Lerner, A., Ciechanover, A*., and Merbl, Y*. (2016). Post-translational modification profiling – A novel tool for mapping the protein modification landscape in cancer.  Exptl. Biol. Med. (Maywood) 241, 1475-1482. pii: 1535370216651732. PMID: 27229346 doi: 10.1177/1535370216651732.
  22. Cohen-Kaplan, V., Livneh, I., Avni, N., Cohen-Rosenzweig, C., and Ciechanover, A. (2016). The Ubiquitin-Proteasome System and Autophagy: Coordinated and Independent Activities.  Int. J. Biochem. Cell Biol. pii: S1357-2725(16)30193-5. doi: 10.1016/j.biocel.2016.07.019. [Epub ahead of print]
  23. Livneh, I., Cohen-Kaplan, V., Cohen-Rosenzweig, C., Avni, N., and Ciechanover, A. (2016). The Life Cycle of the 26S Proteasome – From Birth, through Regulation and Function, and on to its Death.  Cell Res. 26(8):869-85. doi: 10.1038/cr.2016.86. Epub 2016 Jul 22.
  24. Kosik, K.S., Sejnowski, T.J., Raichle, M.E., Ciechanover, A., and Baltimore D. (2016). A Path Toward Understanding Neurodegeneration. Science 353, 872-873. doi: 10.1126/science.aai7622
  25. Cohen-Kaplan, V., Ciechanover, A.*, and Livneh, I. (2016). p62 at the Crossroad of the Ubiquitin-Proteasome System and Autophagy.  Oncotarget 7, 83833-83834. doi: 10.18632/oncotarget.13805.                                                                                             *Corresponding author
  26. Cohen-Kaplan, V., Ciechanover, A.*, and Livneh, I. (2017). Stress-induced Polyubiquitination of Proteasomal Ubiquitin Receptors Targets the Proteolytic Complex for Autophagic Degradation. Autophagy .                                                                                                                       *Corresponding author 
  27. Etzioni, A.*, Ciechanover, A.*, and Pikarsky, E.* (2017). Immune defects caused by mutations in the ubiquitin system. J. Allerg. Clin. Immunol. 139, 743-753.*equal contributing authors
  28.   Barac, Y.D., Emrich, F., Krutzwakd-Josefson, E., Schrepfer, S., Sampaio, L.C., Willerson, J.T., Robbins, R.C., Ciechanover, A., Mohr, F.W., Aravot, D., and Taylor, D.A.. (2017). The ubiquitin-proteasome system: A potential therapeutic target for heart failure. J Heart Lung Transplant. pii: S1053-2498(17)31621-2. doi: 10.1016/j.healun. 2017.02.012ץ
  29. Ciechanover, A., and Kwon, Y.-T. (2017). Protein Quality Control by Molecular
    Chaperones in Neurodegeneration. Front. Neurosci. 11 (article 185).
    doi: 10.3389/fnins.2017.00185. Epub, April 6, 2017.
  30. Livneh, I., Kravtsova-Ivantsiv, Y., Braten, O., Kwon, Y. T., and Ciechanover, A. (2017). Monoubiquitination Joins Polyubiquitination as an Esteemed Proteasomal Targeting Signal. BioEssays 39, DOI 10.1002/bies.201700027 PMID: 28493408 Was selected as the highlight of the issue:  http://onlinelibrary.wiley.com/doi/10.1002/bies.v39.6/issuetocWas highlighted on the news website “Advanced Science News” (http://www.advancedsciencenews.com/).Accessing the highlight article here: http://www.advancedsciencenews.com/monoubiquitination-new-signal-proteasomal-degradation/
  31. Kwon, Y.T., and Ciechanover, A. (2017). The Ubiquitin Code in the Ubiquitin-Proteasom system and Autophagy. Trends Biochem Sci. pii: S0968-0004(17)30169-X. doi: 10.1016/j.tibs.2017.09.002.
  32. Ciechanover, A. (2017). Intracellular Protein Degradation: From a Vague Idea thru the Lysosome and the Ubiquitin-Proteasome System and Onto Human Diseases and Drug Targeting. Best Pract. Res. Clin. Haematol. 30, 341-355. doi: 10.1016/j.beha.2017.09.001. PMID: 29156207.
  33. Galuzzi, L., Vitale, I., et al. (2018). Molecular Mechanisms of Cell Death: Recommendations of the Nomenclature Committee on Cell Death 2018.
    Cell Death and Differentiation. https://doi.org/10.1038/s41418-017-0012-4.              Complete list of authors: Galluzzi, L., Vitale, I., Aaronson, S.A., Abrams, J.M. Adam, D., Agostinis, P.,  Alnemri, E.S., Altucci, L., Amelio, I., Andrews, D.W., Annicchiarico-Petruzzelli, M., Antonov, A.V., Arama, E., Baehrecke, E.H., Barlev, N.A., Bazan, N.G., Bernassola, F., Bertrand, M.J.M., Bianchi, M., Blagosklonny, M.V., Blomgren, K., Borner, C., Boya, P., Brenner, C., Campanella, M., Candi, E., Carmona-Gutierrez, D., Cecconi, F., Chang, F. K.-M., Chandel, N.S., Cheng, E.H, Chipuk, J.E., Cidlowski, J.A., Ciechanover, A., Cohen, G.M.,  Conrad, M., Cubillos-Ruiz, J.R., Czabotar, P.E., D’Angiolella, V., Dawson, T.M., Dawson, V.L., De Laurenzi, V., De Maria, R., Debatin, K.M. DeBerardinis, R.J., Deshmukh, M.,  a Di Daniele, N., Di Virgilio, F., Dixit, V.M., Dixon, S.J., Duckett, C.S., Dynlacht, B.D., El-Deiry, W.S., Elrod, J.W., Fimia, G.M., Fulda, S., García-Sáez, A.J.,  Garg, A.D.,  Garrido, C., Gavathiotis, E., Golstein, P., Gottlieb, E., Green, D.R.,  Greene, L.A., Gronemeyer, H., Gross, A., Hajnoczky, G., Hardwick, J.M., Harris, I.S., Hengartner, M.O., Hetz, C., Ichijo, H., Jäättelä, M., Joseph, B., Jost, P.J.,  Juin, P.P., Kaiser, W.J., Karin, M., Kaufmann, T., Kepp, O., Kimchi, A., Kitsis, R.N., Klionsky, D.J., Knight, R.A., Kumar, S., Lee, S.W., Lemasters, J.J.,  Levine, B., Linkermann, A., Lipton, S.A., Lockshin, R.A., López-Otín, C., Lowe, S.W.,  Luedde, t., Lugli, l., MacFarlane, M., Madeo, F., Malewicz, M., Malorni, W.,  Manic, G., Marine, J.-C., Martin, S.J., Martinou, J.-C., Medema, J.P., Mehlen, P.,  Meier, P., Melino, S., Miao, E.A., Molkentin, J.D., Moll, U.M., Muñoz-Pinedo, C., Nagata, S., Nuñez, G., Oberst, A., Oren, M., Overholtzer, M., Pagano, M., Panaretakis, T., Pasparakis, M., Penninger, J.M., Pereira, D.M., Pervaiz, S., Peter, M.E., Piacentini, M., Pinton, P., Prehn, J.H.M., Puthalakath, H.,  Rabinovich, G.A., Rehm, M., Rizzuto, R., Rodrigues, C.M.P., Rubinsztein, D.C., Rudel, T.,  Ryan, K.M., Sayan, E., Scorrano, L., Shao, F., Shi, Y., Silke, J., Simon, H.-U.,  Sistigu, A., Stockwell, S.R., Strasser, A., Szabadkai, G., Tait, S.W.G., Tang, D.,    Tavernarakis, N., Thorburn, A., Tsujimoto, Y., Turk, B., Vanden Berghe, T.,  Vandenabeele, P., Vander Heiden, M.G., Villunger, A., Virgin, H.W.,  Vousden, K.H., Vucic, D., Wagner, E.F., Walczak, H., Wallach, D., Wang, Y., Wells, J.A., Wood, W., Yuan, J., Zakeri, Z., Zhivotovsky, B., Zitvogel, L., Melino, G. and   Kroemer, G.
  34. Cohen-Kaplan, V., Livneh, I., Kwon, Y.T., and Ciechanover, A. (2019). Monitoring Stress-Induced Autophagic Engulfment and Degradation of the 26S Proteasome in Mammalian Cell. In: Methods in Enzymology: Ubiquitination and Protein Stability, 619, 337-366. doi: 10.1016/bs.mie.2018.12.022. Elsevier Publishing.
  35. Cohen-Kaplan, V., Livneh, I., and Ciechanover, A. (2020).  Proteasome phase separation: a novel layer of quality control. Cell Res. 30, 374-375, doi: 10.1038/s41422-020-0306-9. PMID: 32265504                                                                                

Book Chapters:

  1. Ciechanover, A. (2011).  Intracellular Protein Degradation: From a Vague Idea thru the Lysosome and the Ubiquitin-Proteasome System and onto Human Diseases and Drug Targeting.  In:  The Scientific Legacy of the 20th Century: Proceedings of the Plenary Session of the Pontifical Academy of Sciences, Vatican City, October 28th – November 1st, 2010.  Volume 21, pp. 286-310, 372-376.
  2. Kravtsova-Ivantsiv, Y., and Ciechanover A. (2011). Ubiquitination and Degradation of Proteins.  In: Methods in Molecular Biology: Gel-Free Proteomics Methods and Protocols (Kris Gevaert, ed.).  Humana Press, Inc.  Totowa, NJ, USA 753, 335-357.