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
Open accessAbstract
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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“Currently, the most well characterized mechanisms for substrate recognition by bacterial proteases are the N-end rule and the SsrA tag.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [54]
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“The N-end rule relates the half-life of a protein to the N-terminal amino acid while the SsrA tag is an eleven amino acid tag that is added to the carboxy-terminus of incompletely translated proteins relegating them to degradation [54–55].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [54]
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Cites
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Self-citationA multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
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Phosphorylation meets ubiquitination: the control of NF-κB activity
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Correlation between Protein and mRNA Abundance in Yeast
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The Canonical Notch Signaling Pathway: Unfolding the Activation Mechanism
Kopan, R., & Ilagan, M. X. G. (2009) · Cell · doi:10.1016/j.cell.2009.03.045 · Cited by 3,764
The ubiquitin–proteasome pathway: on protein death and cell life
Ciechanover, A. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7151 · Cited by 1,419
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
- 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
- green
- europepmc.org
- 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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