(list of publications, titles, and DOI will be updated once they are on-line)

Palayam, M., Ganapathy, J., Guercio, AM., Tal, L., Deck, SL., and Shabek, N (2020). Structural Insights into Photoactivation of Plant Cryptochrome-2. BioRxiv doi.org/10.1101/2020.07.30.227371

Kuppu, S., Marimuthu, M., Ron, M., Li, G., Huddleson, A., Siddeek, MH., Terry, J., Buchner, R., Shabek, N., Comai, L., and Britt, AB (2020). A variety of changes, including CRISPR/Cas9 mediated deletions, in CENH3 lead to uniparental genome elimination and haploid induction on outcrossing. Plant Biotechnology Journal. 10.1111/pbi.13365

Tal, L., Anleu-Gil, MX., Guercio, AM., and Shabek, N (2020). Structural Aspects of Plant Hormone Signal Perception and Regulation by Ubiquitin Ligases. Plant Physiology. 10.1104/pp.19.01282

Shabek, N., Ticchiarelli, F., Mao, H., Hinds, TR., Leyser, O. & Zheng, N. (2018). Structural plasticity of D3-D14 Ub ligase in strigolactone signalling. Nature. 10.1038/s41586-018-0743-5

Shabek, N., Ruble, J., Waston CJ, Garbutt KC, Hinds, TR., and Zheng, N. (2018). Structural insights into DDA1 function as a core component of the CRL4-DDB1 ubiquitin ligase. Nature – Cell Discovery. 10.1038/s41421-018-0064-8

Zheng, N., Shabek, N. (2017).  Ubiquitin ligases:  structure, function, and regulation. Annu Rev Biochem. 86, 129-157. 10.1146/annurev-biochem-060815-014922

Shabek, N., Zheng, N. (2014). Plant ubiquitin ligases as signaling hubs. Nat Struct Mol Biol 21, 293-296. 10.1038/nsmb.2804

Zhou, F., Lin, Q., Zhu, L., Ren, Y., Zhou, K., Shabek, N., et al. (2013). D14-SCF(D3)-dependent degradation of D53 regulates strigolactone signaling. Nature. 504, 406-410. 10.1038/nature12878

Shabek, N., Herman-Bachinsky, Y., Buchsbaum, S., Lewinson, O., Haj-Yahya, M., Hejjaoui, M., Lashuel, HA., 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. 10.1016/j.molcel.2012.07.011.

  • RESEARCH HIGHLIGHT –  Nature Reviews Molecular Cell Biology. Protein Metabolism: Length Matters (2012). doi.org/10.1038/nrm3445

Braten O., Shabek, N., Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2011).  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. 10.1042/BJ20111840

Weissman, AM., Shabek, N., and Ciechanover, A. (2011).  The predator becomes the prey: regulation of the ubiquitin system by ubiquitylation and degradation. Nat Rev Mol Cell Biol 12, 605-620. 10.1038/nrm3173

Shabek, N., Ciechanover, A. (2010). The degradation of ubiquitin: the fate of the cellular reaper. Cell Cycle 9, 523-530. 10.4161/cc.9.3.11152

Shabek, N., Herman-Bachinsky, Y., and Ciechanover, A. (2009). Ubiquitin degradation with its substrate, or as a monomer in a ubiquitination-independent mode, provides clues to proteasome regulation. Proc Natl Acad Sci U S A 106, 11907-11912. 10.1073/pnas.0905746106

Shabek, N., Iwai, K., and Ciechanover, A. (2007). Ubiquitin is degraded by the ubiquitin system as a monomer and as part of its conjugated target. Biochem Biophys Res Commun 363, 425-431. 10.1016/j.bbrc.2007.08.185

Ivantsiv, Y., Kaplun, L., Tzirkin-Goldin, R., Shabek, N., and Raveh, D. (2006). Unique role for the UbL-UbA protein Ddi1 in turnover of SCFUfo1 complexes. Mol Cell Biol 26, 1579-1588. 10.1128/MCB.25.13.5355-5362.2005

Kaplun, L., Ivantsiv, Y., Bakhrat, A., Tzirkin, R., Baranes, K., Shabek, N., and Raveh, D. (2006). The F-box protein, Ufo1, maintains genome stability by recruiting the yeast mating switch endonuclease, Ho, for rapid proteasome degradation. Isr Med Assoc J 8, 246-248.

Kaplun, L., Tzirkin, R., Bakhrat, A., Shabek, N., Ivantsiv, Y., and Raveh, D. (2005). The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease. Mol Cell Biol 25, 5355-5362. 10.1128/MCB.25.13.5355-5362.2005

 

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