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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
Scheffner, M., Werness, B. A., Huibregtse, J. M., Levine, A. J., & Howley, P. M. (1990) · Cell · doi:10.1016/0092-8674(90)90409-8 · Cited by 3,995
A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J. G., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,613
The alphaviruses: gene expression, replication, and evolution.
Strauss, J. H., & Strauss, E. G. (1994) · Microbiological Reviews · doi:10.1128/mmbr.58.3.491-562.1994 · Cited by 2,221
Mechanisms And Functions Of Cell Death
Ellis, R. E., Yuan, J., & Horvitz, H. R. (1991) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.07.110191.003311 · Cited by 2,088
In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal Residue
Bachmair, A., Finley, D. J., & Varshavsky, A. J. (1986) · Science · doi:10.1126/science.3018930 · Cited by 1,976
Self-citationA multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535
Self-citationCommon Principles of Protein Translocation Across Membranes
Schatz, G., & Dobberstein, B. (1996) · Science · doi:10.1126/science.271.5255.1519 · Cited by 1,116
Wiertz, E. J. H. J., Jones, T. R., Sun, L., Bogyo, M. S., Geuze, H. J., & Ploegh, H. L. (1996) · Cell · doi:10.1016/s0092-8674(00)81054-5 · Cited by 1,073
A two-component system that regulates an osmosensing MAP kinase cascade in yeast
Maeda, T., Wurgler‐Murphy, S. M., & Saito, H. (1994) · Nature · doi:10.1038/369242a0 · Cited by 1,072
Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascade
Scheffner, M., Nuber, U. A., & Huibregtse, J. M. (1995) · Nature · doi:10.1038/373081a0 · Cited by 1,017
Flagged first, then by citations
2 of the 77 references couldn’t be matched to a known paper.
Research works printed but not linked: 16
- [1]Lévy, F., Johnsson, N., Rümenapf, T. & Varshavsky, A. (1996) Proc. Natl. Acad. Sci. USA 93, 4907–4912.
- [3]Murray, A. & Hunt, T. (1993) in The Cell Cycle (Freeman, NY), pp. 60–62.
- [2]Baker, R. T. & Varshavsky, A. (1991) Proc. Natl. Acad. Sci. USA 88, 1090-1094.
- [22]Dohmen, R. J., Madura, K., Bartel, B. & Varshavsky, A. (1991) Proc. Natl. Acad. Sci. USA 88, 7351–7355.
- [32]Wickner, S., Gottesman, S., Skowyra, D., Hoskins, J., McKenney, K. & Maurizi, M. R. (1994) Proc. Natl. Acad. Sci. USA 91, 12218–12222.
- [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.
- [37]Pickart, C. (1988) in Ubiquitin, ed. Rechsteiner, M. (Plenum, New York), pp. 77–99.
- [43]Negrutskii, B. S. & Deutscher, M. P. (1991) Proc. Natl. Acad. Sci. USA 88, 4991-4995.
- [48]Li, X. & Chang, Y. H. (1995) Proc. Natl. Acad. Sci. USA 92, 12357–12361.
- [54]Scherer, D. C., Brockman, J. A., Chen, Z. J., Maniatis, T. & Ballard, D. (1995) Proc. Natl. Acad. Sci. USA 92, 11259–11263.
- [58]Ota, I. M. & Varshavsky, A. (1992) Proc. Natl. Acad. Sci. USA 89, 2355–2359.
- [64]Aizenman, E., Engelberg-Kulka, H. & Glaser, G. (1996) Proc. Natl. Acad. Sci. USA 93, 6059–6063.
- [65]Kayalar, C., Örd, T., Testa, M. P., Zhong, L.-T. & Bredesen, D. E. (1996) Proc. Natl. Acad. Sci. USA 93, 2234–2238.
- [69]Levis, M. J. & Bourne, H. R. (1992) J. Cell Biol. 119, 1297–1307. deGroot, R. J., Rümenapf, T., Kuhn, R. J., Strauss, E. G. & Strauss, J. H. (1991) Proc. Natl. Acad. Sci. USA 88, 8967–8971.
- [77]Park, E. C., Finley, D. & Szostak, J. W. (1992) Proc. Natl. Acad. Sci. USA 89, 1249–1252.
- [79]Varshavsky, A. (1995) Proc. Natl. Acad. Sci. USA 92, 3663–3667.
Cited by
Sorted by citations
Items 501–600 of 856
Sequence elements that contribute to the degradation of yeast Gα
Schauber, C., Chen, L., Tongaonkar, P., Vega, I. E., & Madura, K. (1998) · Genes to Cells · doi:10.1046/j.1365-2443.1998.00192.x · Cited by 20
Kim, L., Kwon, D. H., Heo, J., Park, M. R., & Song, H. K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010912 · Cited by 19
Nabu, S., Lawung, R., Isarankura-Na-Ayudhya, P., Isarankura‐Na‐Ayudhya, C., Roytrakul, S., & Prachayasittikul, V. (2014) · Journal of Medical Microbiology · doi:10.1099/jmm.0.067595-0 · Cited by 19
A ubiquitin‐based vector for the co‐ordinated synthesis of multiple proteins in plants
Walker, J. M., & Vierstra, R. D. (2007) · Plant Biotechnology Journal · doi:10.1111/j.1467-7652.2007.00250.x · Cited by 19
Reichel, C., & Johnsson, N. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)99050-2 · Cited by 19
Masdehors, P., Glaisner, S., Maciorowski, Z., Magdelénat, H., & Delić, J. (2000) · Experimental Cell Research · doi:10.1006/excr.2000.4870 · Cited by 19
Ubiquitylation in apoptosis: DIAP1's (N-)en(d)igma
Ditzel, M., & Meier, P. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401711 · Cited by 19
Essentials in the Life Process Indicated by the Self-Referential Genetic Code
Guimarães, R. C. (2014) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-014-9380-7 · Cited by 18
Brandsma, M. E., Wang, X., Diao, H., Kohalmi, S. E., Jevnikar, A. M., & Ma, S. (2009) · The Open Biotechnology Journal · doi:10.2174/1874070700903010057 · Cited by 18
Wang, Q., Kang, L., & Wang, X. (2009) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2009.00138.x · Cited by 18
Chua, C. S., Low, H., Lehming, N., & Sim, T. S. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.10.021 · Cited by 18
Chen, S., Ko, C.-Y., Yen, C.-W., & Wang, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804378200 · Cited by 18
Fast protein-depletion system utilizing tetracycline repressible promoter and N-end rule in yeast
Gnanasundram, S. V., & Koš, M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-07-1186 · Cited by 18
Synthetic biology approaches for targeted protein degradation
Chen, R. P., Gaynor, A. S., & Chen, W. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107446 · Cited by 18
Bulik, S., Peters, B., & Holzhütter, H. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.12.7957 · Cited by 18
Chen, E., Lim, M. S., Rosic-Kablar, S., Liu, J., Jolicoeur, P., Dubé, I. D., & Hough, M. R. (2005) · Oncogene · doi:10.1038/sj.onc.1209285 · Cited by 18
A Standard Parts List for Biological Circuitry
Arkin, A. P., & Endy, D. (1999) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 18
Hockerman, G. H., Dethrow, N. M., Hameed, S., Doran, M., Jaeger, C. B., Wang, W., & Pond, A. L. (2014) · European Journal of Translational Myology · doi:10.4081/ejtm.2014.3319 · Cited by 17
Pharmacological Modulation of the N-End Rule Pathway and Its Therapeutic Implications
Lee, J. H., Jiang, Y., Kwon, Y. T., & Lee, M. J. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.07.004 · Cited by 17
Wang, Q., Lei, C.-X., Wan, H., & Liu, Q. (2011) · DNA and Cell Biology · doi:10.1089/dna.2011.1309 · Cited by 17
“In Silico” Characterization of 3-Phytase A and 3-Phytase B fromAspergillus niger
Niño-Gómez, D. C., Rivera-Hoyos, C. M., Morales-Álvarez, E. D., Reyes-Montaño, E. A., Alejo, N. E. V., Ramírez-Casallas, I. N., Türkmen, K. E., Sáenz-Suárez, H., Sáenz-Moreno, J. A., Poutou‐Piñales, R. A., et al. (2017) · Enzyme Research · doi:10.1155/2017/9746191 · Cited by 17
Structural basis for the N‐degron specificity of ClpS1 from Arabidopsis thaliana
Kim, L., Heo, J., Kwon, D. H., Shin, J. S., Jang, S. H., Park, Z., & Song, H. K. (2020) · Protein Science · doi:10.1002/pro.4018 · Cited by 17
In Vivo Chemoenzymatic Control of N‐Terminal Processing in Recombinant Human Epidermal Growth Factor
Merkel, L., Cheburkin, Y. V., Wiltschi, B., & Budiša, N. (2007) · ChemBioChem · doi:10.1002/cbic.200700540 · Cited by 17
Song, X., Zhou, T., Hao, J., Guo, X., Zhang, X., Han, P., & Sha, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027836 · Cited by 17
Involvement of exopeptidases in dehydration tolerance of spring wheat seedlings
Miazek, A., & Zagdańska, B. (2008) · Biologia Plantarum · doi:10.1007/s10535-008-0133-1 · Cited by 17
de Farías, S. T., Moreira, C. H. C., & Guimarães, R. C. (2006) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-006-9008-7 · Cited by 17
Condò, I., Ruggero, D., Reinhardt, R., & Londei, P. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00971.x · Cited by 17
Piechocki, M. P., Pilon, S. A., Kelly, C., & Wei, W. (2001) · Cellular Immunology · doi:10.1006/cimm.2001.1853 · Cited by 17
Srb7p is essential for the activation of a subset of genes
Gromöller, A., & Lehming, N. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02123-2 · Cited by 17
Liu, D., & Bhunia, A. K. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00323 · Cited by 16
Fu, F., Li, X., YuJu, Y., YuJu, Y., Tong, G., Li, G., Zhou, Y., & Li, X. (2011) · Virology Journal · doi:10.1186/1743-422x-8-264 · Cited by 16
Chimeric RNA-binding protein-based killing switch targeting hepatocellular carcinoma cells
Yang, J., & Ding, S. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.08.012 · Cited by 16
ProtNet: a tool for stochastic simulations of protein interaction networks dynamics
Bernaschi, M., Castiglione, F., Ferranti, A., Gavrila, C., Tinti, M., & Cesareni, G. (2007) · BMC Bioinformatics · doi:10.1186/1471-2105-8-s1-s4 · Cited by 16
Engineering L7Ae for RNA-Only Delivery Kill Switch Targeting CMS2 Type Colorectal Cancer Cells
Yang, J., & Ding, S. (2021) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00612 · Cited by 16
Liu, W., Wang, J., Mitsui, K., Shen, H., & Tsurugi, K. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03047.x · Cited by 16
Structure of tomato wound-induced leucine aminopeptidase sheds light on substrate specificity
DuPrez, K. T., Scranton, M. A., Walling, L. L., & Fan, L. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714006245 · Cited by 16
Enhanced detection of tRNA isoacceptors by combinatorial oligonucleotide hybridization
Buvoli, A. E., Buvoli, M., & Leinwand, L. A. (2000) · RNA · doi:10.1017/s1355838200000339 · Cited by 16
Mint virus X: a novel potexvirus associated with symptoms in ‘Variegata’ mint
Tzanetakis, I. E., Postman, J., & Martín, R. R. (2005) · Archives of Virology · doi:10.1007/s00705-005-0586-x · Cited by 16
Kanno, T., Kitano, M., Kato, R., Omori, A., Endo, Y., & Tozawa, Y. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.09.007 · Cited by 16
Replication strategies and applications of Semliki Forest virus
Lulla, V. (2007) · DSpace repository (University of Tartu) · Cited by 16
Baiden, N., Gandini, C., Goddard, P., & Sayanova, O. V. (2022) · Algal Research · doi:10.1016/j.algal.2022.102927 · Cited by 15
New Insights into the Role of Ubiquitin Networks in the Regulation of Antiapoptosis Pathways
Asaoka, T., & Ikeda, F. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.05.003 · Cited by 15
Fluorescent reporters for the ubiquitin–proteasome system
Salomons, F. A., Verhoef, L. G. G. C., & Dantuma, N. P. (2005) · Essays in Biochemistry · doi:10.1042/bse0410113 · Cited by 15
Deubiquitination by proteasome is coordinated with substrate translocation for proteolysis in vivo
Zhu, Q., Wani, G., Wang, Q., Elmahdy, M., Snapka, R. M., & Wani, A. A. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.03.031 · Cited by 15
Expression and Biochemical Characterization of the Human Enzyme N-Terminal Asparagine Amidohydrolase
Cantor, J. R., Stone, E. M., & Georgiou, G. (2011) · Biochemistry · doi:10.1021/bi101832w · Cited by 15
Bae, S. M., Kim, H. J., Lee, J., Choi, J. B., Shin, T. Y., Koo, H. N., Choi, J. Y., Lee, K. S., Je, Y. H., Jin, B. R., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060835 · Cited by 15
N‐terminal residues regulate proteasomal degradation of AANAT
Huang, Z., Liu, T., & Borjigin, J. (2010) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2010.00753.x · Cited by 15
Exploration of degrons and their ability to mediate targeted protein degradation
Harris, T. J., & Trader, D. J. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00787e · Cited by 15
Paltansing, S., Tengeler, A. C., Kraakman, M. E. M., Claas, E. C. J., & Bernards, A. T. (2013) · Microbial Drug Resistance · doi:10.1089/mdr.2013.0058 · Cited by 14
Singh, A., Borah, A. K., Deka, K., Gogoi, A. P., Verma, K., Barah, P., & Saha, S. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.12.015 · Cited by 14
Kimata, Y., Higashio, H., & Kohno, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10655 · Cited by 14
Yang, S., Proctor, A., Cline, L. L., Houston, K. M., Waters, M. L., & Allbritton, N. L. (2013) · The Analyst · doi:10.1039/c3an00874f · Cited by 14
Beenukumar, R., Goedderz, D., Palanimurugan, R., & Dohmen, R. J. (2015) · Microbial Cell · doi:10.15698/mic2015.06.206 · Cited by 14
Structure of proteins: Evolution with unsolved mysteries
Upadhyay, A. (2019) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2019.04.007 · Cited by 14
Three Decades of Studies to Understand the Functions of the Ubiquitin Family
Varshavsky, A. J. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-474-2_1 · Cited by 14
Self-citationHow Do Endogenous Proteins Become Peptides and Reach the Endoplasmic Reticulum
Nandi, D., Marusina, K., & Monaco, J. J. (1998) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-72045-1_2 · Cited by 14
Saito, T., Mitsui, K., Hamada, Y., & Tsurugi, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201909200 · Cited by 14
Pasquo, A., Nardi, M. C., Dimasi, N., Tomei, L., Steinkühler, C., Delmastro, P., Tramontano, A. L., & Francesco, R. D. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00060-1 · Cited by 14
Ubiquitin Ligases in Malignant Lymphoma
Lim, M. S., & Elenitoba‐Johnson, K. S. J. (2004) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428190410001663635 · Cited by 14
Frontiers of protein expression control with conditional degrons
Kanemaki, M. T. (2012) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-012-1203-y · Cited by 13
Leveraging nature’s biomolecular designs in next-generation protein sequencing reagent development
Tullman, J. A., Marino, J. P., & Kelman, Z. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10745-2 · Cited by 13
Delayed Protein Changes During Seed Germination
Bai, B., van der Horst, N., Cordewener, J. H. G., America, A. H. P., Nijveen, H., & Bentsink, L. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.735719 · Cited by 19
UBR‐1 ubiquitin ligase regulates the balance between GABAergic and glutamatergic signaling
Li, Y., Chitturi, J., Yu, B., Zhang, Y., Wu, J., Ti, P., Hung, W., Zhen, M., & Gao, S. (2023) · EMBO Reports · doi:10.15252/embr.202357014 · Cited by 13
Deciphering the Roles of Multicomponent Recognition Signals by the AAA + Unfoldase ClpX
Ling, L., Montaño, S. P., Sauer, R. T., Rice, P. A., & Baker, T. A. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.03.008 · Cited by 13
Jiang, Y., Pore, S. K., Lee, J. H., Sriram, S., Mai, B. K., Han, D. H., Agarwalla, P., Zakrzewska, A., Kim, Y., Banerjee, R., et al. (2013) · Chemical Science · doi:10.1039/c3sc51059j · Cited by 13
Blueprints for the rational design of therapeutic mutacin 1140 variants
Kers, J. A., Sharp, R. E., Muley, S., Mayo, M., Colbeck, J. C., Zhu, Y., DeFusco, A. W., Park, J. H., & Handfield, M. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13365 · Cited by 13
Jeon, J. H., Oh, T. R., Park, S., Huh, S., Kim, J. H., Mai, B. K., Lee, J. H., Kim, S. H., & Lee, M. J. (2021) · Neurotherapeutics · doi:10.1007/s13311-021-01039-0 · Cited by 13
Combs, L. R., Spires, L. M., Alonso, J. D., Papp, B., & Tóth, Z. (2022) · Journal of Virology · doi:10.1128/jvi.00101-22 · Cited by 13
Shemesh, R., Novik, A., & Cohen, Y. (2010) · Genomics Proteomics & Bioinformatics · doi:10.1016/s1672-0229(10)60020-4 · Cited by 13
Schüller, J., & Lehming, N. (2003) · Microbial Physiology · doi:10.1159/000071071 · Cited by 13
Alam, S. I., Bansod, S., Goel, A. K., & Singh, L. (2010) · Current Microbiology · doi:10.1007/s00284-010-9743-x · Cited by 13
Bueno, K. O., Resende, L. D. S., Ribeiro, A. F., dos Santos, D. M., Gonçalves, E. C., Vigil, F. A. B., Silva, I. F. D. O., Ferreira, L. F., Pimenta, A. M. C., & Ribeiro, A. M. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.03.001 · Cited by 13
Sit4 Phosphatase Is Functionally Linked to the Ubiquitin-Proteasome System
Singer, T., Haefner, S., Hoffmann, M., Fischer, M., Ilyina, J., & Hilt, W. (2003) · Genetics · doi:10.1093/genetics/164.4.1305 · Cited by 13
Starodubova, E. S., Boberg, A., Kashuba, E., Wahrén, B., Карпов, В. Л., & Isaguliants, M. G. (2005) · Vaccine · doi:10.1016/j.vaccine.2005.08.020 · Cited by 13
Chen, E., Kwon, Y. T., Lim, M. S., Dubé, I. D., & Hough, M. R. (2006) · Oncogene · doi:10.1038/sj.onc.1209573 · Cited by 13
Rana, A., Minz, R. W., Aggarwal, R., Sharma, S., Pasricha, N., Anand, S., & Singh, S. (2012) · Pediatric Rheumatology · doi:10.1186/1546-0096-10-24 · Cited by 12
Improved Fitness of Arabidopsis thaliana Nitrilase 2
Schreiner, U., Steinkellner, G., Rozzell, J. D., Glieder, A., & Winkler, M. (2010) · ChemCatChem · doi:10.1002/cctc.200900212 · Cited by 12
Jarmalavicius, S., Trefzer, U., & Walden, P. (2009) · The FASEB Journal · doi:10.1096/fj.09-136283 · Cited by 12
Relationships between stress, protein damage, nutrition, and age-related eye diseases
Taylor, A., Shang, F., & Obin, M. S. (1997) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(95)00049-6 · Cited by 12
Lety, M. A., Fréhel, C., Béretti, J., Berche, P., & Charbit, A. (2003) · Microbiology · doi:10.1099/mic.0.26072-0 · Cited by 12
Page, A. M., Aneliunas, V., Lamb, J. R., & Hieter, P. (2005) · Genetics · doi:10.1534/genetics.104.040105 · Cited by 12
Physiological functions and clinical implications of the N-end rule pathway
Liu, Y., Liu, C., Dong, W., & Li, W. (2016) · Frontiers of Medicine · doi:10.1007/s11684-016-0458-7 · Cited by 13
Sikora, S., & Godzik, A. (2004) · Protein Science · doi:10.1110/ps.03454904 · Cited by 12
Lippi, G., Franchini, M., Montagnana, M., & Guidi, G. C. (2007) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-2007-1000366 · Cited by 12
Miletic, S., Hünerberg, M., Kaldis, A., MacDonald, J., Leuthreau, A., McAllister, T. A., & Menassa, R. (2017) · Biotechnology Journal · doi:10.1002/biot.201700405 · Cited by 11
The Structure of Saccharomyces cerevisiae Arginyltransferase 1 (ATE1)
Van, V., Ejimogu, E., Bui, T. S., & Smith, A. T. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167816 · Cited by 11
Pettersen, V. K., Skancke, J., Brautaset, T., & Valla, S. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.01676-13 · Cited by 11
Thomas, S., Besset, C., Courtin, P., & Rul, F. (2009) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2009.04400.x · Cited by 13
Hockerman, G. H., Dethrow, N. M., Hameed, S., Doran, M., Jaeger, C. B., Wang, W., & Pond, A. L. (2014) · European Journal of Translational Myology · doi:10.4081/bam.2014.3.173 · Cited by 11
Cellular control of ubiquitin-proteasome-dependent proteolysis1
Attaix, D., Combaret, L., Pouch-Pélissier, M.-N., & Taillandier, D. (2002) · Journal of Animal Science · doi:10.2527/animalsci2002.80e-suppl_2e56x · Cited by 11
Co- and Posttranslational Processing: The Removal of Methionine
Bradshaw, R. A., Hope, C. J., Yi, E., & Walker, K. W. (2002) · The Enzymes · doi:10.1016/s1874-6047(02)80015-4 · Cited by 11
Han, H. J., Park, H. C., Byun, H., Lee, S. M., Kim, H. S., Yun, D., Cho, M. J., & Chung, W. S. (2012) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2012.02530.x · Cited by 11
Expression of cyclooxygenase genes in the jejunum of horses during low-flow ischemia and reperfusion
Hilton, H. G., Nieto, J. E., Moore, P. F., Harmon, F. A., Naydan, D. K., & Snyder, J. R. (2011) · American Journal of Veterinary Research · doi:10.2460/ajvr.72.5.681 · Cited by 11
Mishra, P., Prabha, C. R., Rao, C. M., & Srinivas, V. (2011) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-011-9247-8 · Cited by 11
Lawson, T. G., Sweep, M. E., Schlax, P. E., Bohnsack, R. N., & Haas, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102659200 · Cited by 11
Subunit S5a of the 26S proteasome is regulated by antiapoptotic signals
Gus, Y., Karni, R., & Levitzki, A. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05815.x · Cited by 11
Cadmium and Secondary Structure-dependent Function of a Degron in the Pca1p Cadmium Exporter
Smith, N., Wei, W., Zhao, M., Qin, X., Seravalli, J., Kim, H., & Lee, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.724930 · Cited by 11
Gelfi, C., Viganò, A., Ripamonti, M., Wait, R., Begum, S., Biguzzi, E., Castaman, G., & Faioni, E. M. (2004) · PROTEOMICS · doi:10.1002/pmic.200300724 · Cited by 11
The N-End Rule Pathway inXenopusEgg Extracts
Davydov, I. V., Patra, D., & Varshavsky, A. J. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0829 · Cited by 11
Self-citation
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review