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Cited by 859Ubiquitin and proteasome pathwaysAutophagy in Disease and TherapyProtein Structure and Dynamics

The DOI matches its Crossref record; 75 of the 77 references it cites were found in a registry or an index.

The N-end rule: functions, mysteries, uses

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Varshavsky, A·1996·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.93.22.12142PMC PMC37957
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Abstract

The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. Similar but distinct versions of the N-end rule operate in all organisms examined, from mammals to fungi and bacteria. In eukaryotes, the N-end rule pathway is a part of the ubiquitin system. I discuss the mechanisms and functions of this pathway, and consider its applications.

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Research works printed but not linked: 16

  1. [1]Lévy, F., Johnsson, N., Rümenapf, T. & Varshavsky, A. (1996) Proc. Natl. Acad. Sci. USA 93, 4907–4912.
  2. [3]Murray, A. & Hunt, T. (1993) in The Cell Cycle (Freeman, NY), pp. 60–62.
  3. [2]Baker, R. T. & Varshavsky, A. (1991) Proc. Natl. Acad. Sci. USA 88, 1090-1094.
  4. [22]Dohmen, R. J., Madura, K., Bartel, B. & Varshavsky, A. (1991) Proc. Natl. Acad. Sci. USA 88, 7351–7355.
  5. [32]Wickner, S., Gottesman, S., Skowyra, D., Hoskins, J., McKenney, K. & Maurizi, M. R. (1994) Proc. Natl. Acad. Sci. USA 91, 12218–12222.
  6. [33]Grigoryev, S., Stewart, A. E., Kwon, Y. T., Arfin, S. M., Bradshaw, R. A., Copeland, N. J. & Varshavsky, A. (1996) J. Biol. Chem. 271, in press.
  7. [37]Pickart, C. (1988) in Ubiquitin, ed. Rechsteiner, M. (Plenum, New York), pp. 77–99.
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  16. [79]Varshavsky, A. (1995) Proc. Natl. Acad. Sci. USA 92, 3663–3667.

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Metadata

Authors
Varshavsky, A.
Affiliations
California Institute of Technology (US)
Corresponding author
Varshavsky, A
ORCID
Varshavsky, A
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1996-10-29
Volume
93
Issue
22
Pages
12142-12149
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.93.22.12142
PMC
PMC37957
OpenAlex
W1983345237
Cited by
859
References
77
Citations by year
2026: 10 · 2025: 8 · 2024: 11 · 2023: 19 · 2022: 8 · 2021: 6 · 2020: 16 · 2019: 11 · 2018: 19 · 2017: 19 · 2016: 21 · 2015: 28 · 2014: 25 · 2013: 21 · 2012: 30
FWCI
9.34
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • CaltechAUTHORS (California Institute of Technology) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
N-end rule, protein half-life, N-terminal residues, ubiquitin system, protein degradation, ubiquitination, protein stability
MeSH terms
Acyltransferases, Amidohydrolases, Amino Acid Sequence, Animals, Female, Fungal Proteins, Half-Life, Ligases, Male, Models, Biological, Models, Chemical, Protein Conformation, Proteins, Rabbits, Proto-Oncogene Proteins c-mos, Evolution, Molecular, GTP-Binding Proteins, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases, Mice

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