Standout Papers

In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal Residue 1986 2026 1999 2012 1.6k
  1. In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal Residue (1986)
    Andreas Bachmair, Daniel Finley et al. Science
  2. A Multiubiquitin Chain Is Confined to Specific Lysine in a Targeted Short-Lived Protein (1989)
    Vincent Chau, John W. Tobias et al. Science
  3. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses (1987)
    Daniel Finley, Engin Özkaynak et al. Cell
  4. A Proteolytic Pathway That Recognizes Ubiquitin as a Degradation Signal (1995)
    Erica S. Johnson, Irene M. Ota et al. Journal of Biological Chemistry
  5. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme (1987)
    Stefan Jentsch, John P. McGrath et al. Nature
  6. A protein binds to a satellite DNA repeat at three specific sites that would be brought into mutual proximity by DNA folding in the nucleosome (1984)
    François Strauss, Alexander Varshavsky Cell
  7. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis (1989)
    Daniel Finley, Bonnie Bartel et al. Nature
  8. Split ubiquitin as a sensor of protein interactions in vivo. (1994)
    Nils Johnsson, Alexander Varshavsky Proceedings of the National Academy of Sciences
  9. The N‐end rule pathway and regulation by proteolysis (2011)
    Alexander Varshavsky Protein Science
  10. N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals (2010)
    Cheol‐Sang Hwang, Anna Shemorry et al. Science
  11. The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein (1989)
    John P. McGrath, Alexander Varshavsky Nature
  12. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85 (1984)
    Aaron Ciechanover, Daniel Finley et al. Cell
  13. Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85 (1984)
    Daniel Finley, Aaron Ciechanover et al. Cell
  14. N-degron and C-degron pathways of protein degradation (2019)
    Alexander Varshavsky Proceedings of the National Academy of Sciences

Immediate Impact

68 by Nobel laureates 80 from Science/Nature 119 standout
Sub-graph 1 of 16

Citing Papers

Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants
2019 StandoutScienceNobel
In vivo aspects of protein folding and quality control
2016 StandoutScience
49 intermediate papers

Works of Alexander Varshavsky being referenced

Control of Protein Quality and Stoichiometries by N-Terminal Acetylation and the N-End Rule Pathway
2013
Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms
2006
and 52 more

Author Peers

Author Last Decade Papers Cites
Alexander Varshavsky 25282 7457 5170 206 29.4k
Raymond J. Deshaies 27065 6615 8929 167 30.0k
Bruce Stillman 29056 7114 4029 221 33.6k
Steven I. Reed 22514 11199 7777 208 27.1k
Marc Vidal 23844 2944 2916 196 30.2k
Mike Tyers 22834 2767 5162 185 26.8k
Michael B. Yaffe 23446 5655 7854 278 30.4k
Nikola P. Pavletich 24832 9099 3578 77 29.5k
Stanley Fields 27133 2111 3822 186 32.6k
Anne‐Claude Gingras 25271 2809 5411 317 31.4k
Thomas M. Roberts 19460 7514 3566 305 28.5k

All Works

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2026