N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals

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 · see citing works

The N-end rule: functions, mysteries, uses

Varshavsky, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12142 · Cited by 859 · see citing works

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans

Arnesen, T., Damme, P. V., Polevoda, B. V., Helsens, K., Evjenth, R., Colaert, N., Varhaug, J. E., Vandekerckhove, J. S., Lillehaug, J. R., Sherman, F., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901931106 · Cited by 539 · see citing works

A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradationPreprint

Swanson, R. J., Locher, M., & Hochstrasser, M. (2001) · Genes & Development · doi:10.1101/gad.933301 · Cited by 456 · see citing works

N-terminal Acetyltransferases and Sequence Requirements for N-terminal Acetylation of Eukaryotic Proteins

Polevoda, B. V., & Sherman, F. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01269-x · Cited by 440 · see citing works

The degradation signal in a short-lived protein

Bachmair, A., & Varshavsky, A. J. (1989) · Cell · doi:10.1016/0092-8674(89)90635-1 · Cited by 431 · see citing works

Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor

Chen, P., Johnson, P. R., Sommer, T., Jentsch, S., & Hochstrasser, M. (1993) · Cell · doi:10.1016/0092-8674(93)90426-q · Cited by 392 · see citing works

The Proteomics of N-terminal Methionine Cleavage

Frottin, F., Martinez, A., Peynot, P., Mitra, S., Holz, R. C., Giglione, C., & Meinnel, T. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600225-mcp200 · Cited by 385 · see citing works

Identification and characterization of genes and mutants for an N‐terminal acetyltransferase from yeast.

Mullen, J. R., Kayne, P. S., Moerschell, R. P., Tsunasawa, S., Gribskov, M., Colavito-Shepanski, M., Grunstein, M. R., Sherman, F., & Sternglanz, R. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03615.x · Cited by 323 · see citing works

The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators

Hu, R., Sheng, J., Qi, X., Xu, Z., Takahashi, T. T., & Varshavsky, A. J. (2005) · Nature · doi:10.1038/nature04027 · Cited by 316 · see citing works

Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways

Ravid, T., Kreft, S. G., & Hochstrasser, M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600946 · Cited by 271 · see citing works

The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies

Mogk, A., Schmidt, R., & Bukau, B. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.02.001 · Cited by 261 · see citing works

In vivo degradation of a transcriptional regulator: The yeast α2 repressor

Hochstrasser, M., & Varshavsky, A. J. (1990) · Cell · doi:10.1016/0092-8674(90)90481-s · Cited by 240 · see citing works

The Yeast Nα-Acetyltransferase NatA Is Quantitatively Anchored to the Ribosome and Interacts with Nascent Polypeptides

Gautschi, M., Just, S., Mun, A., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7403-7414.2003 · Cited by 217 · see citing works

Molecular mechanisms of cell-type determination in budding yeast

Johnson, A. D. (1995) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(95)80022-0 · Cited by 189 · see citing works

Acetylation of protein N-terminal amino groups structural observations on α-amino acetylated proteins

Jörnvall, H. (1975) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(75)80105-6 · Cited by 184 · see citing works

TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum

Hassink, G. C., Kikkert, M., van Voorden, S., Lee, S., Spaapen, R. M., van Laar, T., Coleman, C. S., Bartee, E., Früh, K., Chau, V., et al. (2005) · Biochemical Journal · doi:10.1042/bj20041241 · Cited by 172 · see citing works

ARD1 and NAT1 proteins form a complex that has N‐terminal acetyltransferase activity.

Park, E. C., & Szostak, J. W. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05267.x · Cited by 169 · see citing works

The mammalian N-end rule pathway: new insights into its components and physiological roles

Tasaki, T., & Kwon, Y. T. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.08.010 · Cited by 167 · see citing works

Identification and Functional Characterization of N-Terminally Acetylated Proteins in Drosophila melanogaster

Goetze, S., Qeli, E., Mosimann, C., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000236 · Cited by 167 · see citing works

Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase

Deng, M., & Hochstrasser, M. (2006) · Nature · doi:10.1038/nature05170 · Cited by 161 · see citing works

The N-end rule pathway is a sensor of heme

Hu, R., Wang, H., Xia, Z., & Varshavsky, A. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710568105 · Cited by 116 · see citing works

Degradation of Proteins with Acetylated Amino Termini by the Ubiquitin System

Mayer, A., Siegel, N. R., Schwartz, A. L., & Ciechanover, A. J. (1989) · Science · doi:10.1126/science.2544030 · Cited by 106 · see citing works

Ubiquitin Fusion Technique and Related Methods

Varshavsky, A. J. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)99051-4 · Cited by 105 · see citing works

Discovery of Cellular Regulation by Protein Degradation

Varshavsky, A. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.x800009200 · Cited by 99 · see citing works

Glutamine-Specific N-Terminal Amidase, a Component of the N-End Rule Pathway

Wang, H., Piatkov, K. I., Brower, C. S., & Varshavsky, A. J. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.032 · Cited by 81 · see citing works

Two proteolytic pathways regulate DNA repair by cotargeting the Mgt1 alkylguanine transferase

Hwang, C., Shemorry, A., & Varshavsky, A. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812316106 · Cited by 77 · see citing works

Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway

Hwang, C., & Varshavsky, A. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808891105 · Cited by 40 · see citing works

Interspecies variation reveals a conserved repressor of α-specific genes in Saccharomyces yeastsPreprint

Zill, O. A., & Rine, J. (2008) · Genes & Development · doi:10.1101/gad.1640008 · Cited by 29 · see citing works

The proteostasis network and its decline in ageing

Hipp, M. S., Kasturi, P., & Hartl, F. U. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0101-y · Cited by 1,642 · see citing works

Protein Analysis by Shotgun/Bottom-up Proteomics

Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491 · see citing works

N-degron and C-degron pathways of protein degradation

Varshavsky, A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1816596116 · Cited by 544 · see citing works

Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms

Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483 · see citing works

Protein acetylation and deacetylation: An important regulatory modification in gene transcription (Review)

Xia, C., Tao, Y., Li, M., Che, T., & Qu, J. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.9073 · Cited by 136 · see citing works

Molecular basis of GID4-mediated recognition of degrons for the Pro/N-end rule pathway

Dong, C., Zhang, H., Li, L., Tempel, W., Loppnau, P., & Min, J. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0036-1 · Cited by 111 · see citing works

Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus

Lamoth, F., Juvvadi, P. R., Soderblom, E. J., Moseley, M. A., Asfaw, Y. G., & Steinbach, W. J. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02286-13 · Cited by 74 · see citing works

DEGRONOPEDIA: a web server for proteome-wide inspection of degrons

Szulc, N. A., Stefaniak, F., Piechota, M., Soszyńska, A., Piórkowska, G., Cappannini, A., Bujnicki, J. M., Maniaci, C., & Pokrzywa, W. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae238 · Cited by 35 · see citing works

Dispersed Sites of HIV Vif-Dependent Polyubiquitination in the DNA Deaminase APOBEC3F

Albin, J. S., Anderson, J. S., Johnson, J. R., Harjes, E., Matsuo, H., Krogan, N. J., & Harris, R. S. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.01.010 · Cited by 25 · see citing works

Cellular maintenance of nuclear protein homeostasis.

Gallagher, P. S., Oeser, M. L., Abraham, A.-C., Kaganovich, D., & Gardner, R. G. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1530-y · Cited by 22 · see citing works

Reprograming of the ubiquitin ligase Ubr1 by intrinsically disordered Roq1 through cooperating multifunctional motifs

Peters, N., Kanngießer, S., Pajonk, O., Salazar Claros, R., Mogk, A., & Schuck, S. (2024) · doi:10.1101/2024.07.24.604893 · Cited by 2 · see citing works

The structural basis of Indisulam-mediated recruitment of RBM39 to the DCAF15-DDB1-DDA1 E3 ligase complexPreprint

Bussiere, D. E., Xie, L., Srinivas, H., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/737510 · Cited by 3 · see citing works

Peptidic degron in EID1 is recognized by an SCF E3 ligase complex containing the orphan F-box protein FBXO21

Zhang, C., Li, X., Adelmant, G., Dobbins, J., Geisen, C., Oser, M. G., Wucherpfenning, K. W., Marto, J. A., & Kaelin, W. G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522006112 · Cited by 30 · see citing works

Pac-Man for biotechnology: co-opting degrons for targeted protein degradation to control and alter cell function

Yu, G., Rosenberg, J. N., Betenbaugh, M. J., & Oyler, G. A. (2015) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2015.08.023 · Cited by 10 · see citing works

Ubiquitylation of unphosphorylated c-myc by novel E3 ligase SCFFbxl8

Bajpai, S., Jin, H. R., Mucha, B., & Diehl, J. A. (2022) · Cancer Biology & Therapy · doi:10.1080/15384047.2022.2061279 · Cited by 6 · see citing works