Polyubiquitin chains: polymeric protein signals

A 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

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.

Reyes-Turcu, F. E., Ventii, K. H., & Wilkinson, K. D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.082307.091526 · Cited by 1,396

Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling

Mukhopadhyay, D., & Riezman, H. (2007) · Science · doi:10.1126/science.1127085 · Cited by 1,221

Endocytosis and signalling: intertwining molecular networks

Sorkin, A., & von Zastrow, M. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2748 · Cited by 1,064

Building ubiquitin chains: E2 enzymes at work

Ye, Y., & Rape, M. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2780 · Cited by 989

Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation

Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767

Mitochondrial dysfunction in Parkinson's disease

Winklhofer, K. F., & Haass, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.013 · Cited by 688

Global changes to the ubiquitin system in Huntington's disease

Bennett, E. J., Shaler, T. A., Woodman, B., Ryu, K.-Y., Zaitseva, T. S., Becker, C. H., Bates, G. P., Schulman, H., & Kopito, R. R. (2007) · Nature · doi:10.1038/nature06022 · Cited by 497

Keap1 degradation by autophagy for the maintenance of redox homeostasis

Taguchi, K., Fujikawa, N., Komatsu, M., Ishii, T., Unno, M., Akaike, T., Motohashi, H., & Yamamoto, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121572109 · Cited by 482

MITOL Regulates Endoplasmic Reticulum-Mitochondria Contacts via Mitofusin2

Sugiura, A., Nagashima, S., Tokuyama, T., Amo, T., Matsuki, Y., Ishido, S., Kudo, Y., McBride, H. M., Fukuda, T., Matsushita, N., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.023 · Cited by 303

Targeting proteins for degradation.

Schrader, E. K., Harstad, K. G., & Matouschek, A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.250 · Cited by 287

Ubiquitin ligase Nedd4 promotes α-synuclein degradation by the endosomal–lysosomal pathway

Tofaris, G. K., Kim, H. T., Hourez, R., Jung, J.-W., Kim, K. P., & Goldberg, A. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109356108 · Cited by 271

The Ubiquitin Isopeptidase UBPY Regulates Endosomal Ubiquitin Dynamics and Is Essential for Receptor Down-regulation

Row, P. E., Prior, I. A., McCullough, J., Clague, M. J., & Urbé, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512615200 · Cited by 264

Linear Ubiquitin Assembly Complex Negatively Regulates RIG-I- and TRIM25-Mediated Type I Interferon Induction

Inn, K.-S., Gack, M. U., Tokunaga, F., Shi, M., Wong, L.-Y., Iwai, K., & Jung, J. U. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.029 · Cited by 209

Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics

Kirkpatrick, D. S., Denison, C., & Gygi, S. P. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-750 · Cited by 209

Structure-guided development of a potent and selective non-covalent active-site inhibitor of USP7.

Lamberto, I., Liu, X., Seo, H.-S., Schauer, N. J., Iacob, R. E., Hu, W., Das, D., Mikhailova, T., Weisberg, E. L., Engen, J. R., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.003 · Cited by 192

Parkin Mediates Neuroprotection through Activation of IκB Kinase/Nuclear Factor-κB Signaling

Henn, I. H., Bouman, L., Schlehe, J. S., Schlierf, A., Schramm, J. E., Wegener, E., Nakaso, K., Culmsee, C., Berninger, B., Krappmann, D., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.5537-06.2007 · Cited by 173

The mouse polyubiquitin gene UbC is essential for fetal liver development, cell‐cycle progression and stress tolerance

Ryu, K., Maehr, R., Gilchrist, C. A., Long, M. A., Bouley, D. M., Mueller, B., Ploegh, H. L., & Kopito, R. R. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601722 · Cited by 156

The pathophysiology of defective proteostasis in the hypothalamus — from obesity to ageing

Cavadas, C., Aveleira, C. A., Souza, G. F. P., & Velloso, L. A. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.107 · Cited by 105

A proteomics approach to identify the ubiquitinated proteins in mouse heart

Jeon, H. B., Choi, E. S., Yoon, J. H., Hwang, J. H., Chang, J. W., Lee, E. K., Choi, H. W., Park, Z.-Y., & Yoo, Y. J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.015 · Cited by 101

Histone methylation and ubiquitination with their cross-talk and roles in gene expression and stability

Shukla, A., Chaurasia, P., & Bhaumik, S. R. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8605-1 · Cited by 98

Catalysis of Lysine 48-Specific Ubiquitin Chain Assembly by Residues in E2 and Ubiquitin

Rodrigo-Brenni, M. C., Foster, S. A., & Morgan, D. O. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.027 · Cited by 91

Discovery of small-molecule inhibitors of ubiquitin specific protease 7 (USP7) using integrated NMR and in silico techniques

Di Lello, P., Pastor, R., Murray, J. M., Blake, R. A., Cohen, F., Crawford, T. D., Drobnick, J., Drummond, J., Kategaya, L., Kleinheinz, T., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01293 · Cited by 90

Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme

Durcan, T. M., Kontogiannea, M., Bedard, N., Wing, S. S., & Fon, E. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.288449 · Cited by 79

Characterization of selective ubiquitin and ubiquitin-like protease inhibitors using a fluorescence-based multiplex assay format.

Tian, X., Isamiddinova, N. S., Peroutka, R. J., Goldenberg, S. J., Mattern, M. R., Nicholson, B., & Leach, C. (2011) · ASSAY and Drug Development Technologies · doi:10.1089/adt.2010.0317 · Cited by 76

Lys6-modified Ubiquitin Inhibits Ubiquitin-dependent Protein Degradation

Shang, F., Deng, G., Liu, Q., Guo, W., Haas, A. L., Crosas, B., Finley, D., & Taylor, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414356200 · Cited by 74

A novel E3 ubiquitin ligase substrate screen identifies Rho guanine dissociation inhibitor as a substrate of gene related to anergy in lymphocytes

Su, L., Lineberry, N., Huh, Y., Soares, L., & Fathman, C. G. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.7559 · Cited by 61

Identification of eight novel proteasome variants in five unrelated cases of proteasome-associated autoinflammatory syndromes (PRAAS)

Papendorf, J. J., Ebstein, F., Alehashemi, S., Piotto, D. G. P., Kozlova, A., Terreri, M. T., Shcherbina, A., Rastegar, A., Rodrigues, M., Pereira, R., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1190104 · Cited by 38

PSMC3 proteasome subunit variants are associated with neurodevelopmental delay and type I interferon production

Ebstein, F., Küry, S., Most, V., Rosenfelt, C., Scott-Boyer, M.-P., van Woerden, G. M., Besnard, T., Papendorf, J. J., Studencka-Turski, M., Wang, T., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abo3189 · Cited by 36

An in silico model of the ubiquitin-proteasome system that incorporates normal homeostasis and age-related decline

Proctor, C. J., Tsirigotis, M., & Gray, D. A. (2007) · BMC Systems Biology · doi:10.1186/1752-0509-1-17 · Cited by 34

Major histocompatibility complex class I downregulation induced by equine herpesvirus type 1 pUL56 is through dynamin-dependent endocytosis.

Huang, T., Lehmann, M. J., Said, A., Ma, G., & Osterrieder, N. (2014) · Journal of Virology · doi:10.1128/jvi.02079-14 · Cited by 24

Active IKKβ promotes the stability of GLI1 oncogene in diffuse large B-cell lymphoma

Agarwal, N. K., Kim, C. H., Kunkalla, K., Konno, H., Tjendra, Y., Kwon, D., Blonska, M., Kozloski, G. A., Moy, V. T., Verdun, R. E., et al. (2016) · Blood · doi:10.1182/blood-2015-07-658781 · Cited by 23

Accurate and Sensitive Quantitation of the Dynamic Heat Shock Proteome Using Tandem Mass Tags

(2020) · doi:10.1021/acs.jproteome.9b00704 · Cited by 13

AlphaFold modeling of polyubiquitin complexes and covalently linked proteins

(2025) · doi:10.1016/j.xcrp.2025.102796 · Cited by 3