Mechanisms Underlying Ubiquitination

Mdm2 promotes the rapid degradation of p53

Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506

Regulation of p53 stability by Mdm2

Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024

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

RING Finger Proteins

Joazeiro, C. A. P., & Weissman, A. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00077-5 · Cited by 1,249

Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53

Honda, R., & Yasuda, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.22 · Cited by 724

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679

RING Domain E3 Ubiquitin Ligases

Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679

The F-box protein TIR1 is an auxin receptor

Dharmasiri, N., Dharmasiri, S., & Estelle, M. (2005) · Nature · doi:10.1038/nature03543 · Cited by 2,083

Ubiquitin ligases: structure, function, and regulation

Zheng, N., & Shabek, N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014922 · Cited by 1,499

Negative regulation of Toll-like receptor-mediated immune responses

Liew, F. Y., Xu, D., Brint, E. K., & O'Neill, L. A. J. (2005) · Nature Reviews Immunology · doi:10.1038/nri1630 · Cited by 1,509

Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507

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

Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress

Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480

A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF β-TRCP

Zhao, B., Li, L., Tumaneng, K., Wang, C.-Y., & Guan, K.-L. (2010) · Genes & Development · doi:10.1101/gad.1843810 · Cited by 1,418

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

Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications

Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092

p53 ubiquitination: Mdm2 and beyond

Brooks, C. L., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.020 · Cited by 924

Cellular and Molecular Basis of Deiodinase-Regulated Thyroid Hormone Signaling1

Gereben, B., Zavacki, A. M., Ribich, S., Kim, B. W., Huang, S. A., Simonides, W. S., Zeöld, A., & Bianco, A. C. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0019 · Cited by 891

Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2

Li, M., Brooks, C. L., Wu-Baer, F., Chen, D., Baer, R., & Gu, W. (2003) · Science · doi:10.1126/science.1091362 · Cited by 804

Epigenetic mechanisms in memory formation

Levenson, J. M., & Sweatt, J. D. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1604 · Cited by 767

Molecular architecture and assembly of the DDB1–CUL4A ubiquitin ligase machinery

Angers, S., Li, T., Yi, X., MacCoss, M. J., Moon, R. T., & Zheng, N. (2006) · Nature · doi:10.1038/nature05175 · Cited by 674

Auxin Receptors and Plant Development: A New Signaling Paradigm

Mockaitis, K., & Estelle, M. (2008) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123214 · Cited by 651

Structure of a β-TrCP1-Skp1-β-Catenin Complex

Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612

Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family

Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588

CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein

Murata, S., Minami, Y., Minami, M., Chiba, T., & Tanaka, K. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve246 · Cited by 574

Acetylation of p53 inhibits its ubiquitination by Mdm2

Li, M., Luo, J., Brooks, C. L., & Gu, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200578200 · Cited by 503

Control of Mammalian Circadian Rhythm by CKIε-Regulated Proteasome-Mediated PER2 Degradation

Eide, E. J., Woolf, M. F., Kang, H., Woolf, P., Hurst, W., Camacho, F., Vielhaber, E. L., Giovanni, A., & Virshup, D. M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2795-2807.2005 · Cited by 495

An unstructured initiation site is required for efficient proteasome-mediated degradation

Prakash, S., Tian, L., Ratliff, K. S., Lehotzky, R. E., & Matouschek, A. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb814 · Cited by 458

p53 modifications: exquisite decorations of the powerful guardian

Liu, Y., Tavana, O., & Gu, W. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz060 · Cited by 392

Feedback regulation of cholesterol synthesis: Sterol-accelerated ubiquitination and degradation of HMG-CoA reductase

DeBose-Boyd, R. A. (2008) · Cell Research · doi:10.1038/cr.2008.61 · Cited by 391

The Cbl interactome and its functions

Schmidt, M. H. H., & Dikic, I. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1762 · Cited by 395

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53

Linares, L. K., Hengstermann, A., Ciechanover, A., Müller, S., & Scheffner, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2030930100 · Cited by 361

Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

Brzovic, P. S., Keeffe, J. R., Nishikawa, H., Miyamoto, K., Fox, D., Fukuda, M., Ohta, T., & Klevit, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0836054100 · Cited by 346

Ginkgolic Acid Inhibits Protein SUMOylation by Blocking Formation of the E1-SUMO Intermediate

Fukuda, I., Ito, A., Hirai, G., Nishimura, S., Kawasaki, H., Saitoh, H., Kimura, K.-I., Sodeoka, M., & Yoshida, M. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.01.009 · Cited by 355

Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget’s disease.

Hocking, L. J. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.22.2735 · Cited by 350

Post‐translational modification: nature's escape from genetic imprisonment and the basis for dynamic information encoding

Prabakaran, S., Lippens, G., Steen, H., & Gunawardena, J. (2012) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1185 · Cited by 335

Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation

Babu, J. R., Geetha, T., & Wooten, M. W. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03181.x · Cited by 315

Atypical mitogen-activated protein kinases: Structure, regulation and functions

Coulombe, P., & Meloche, S. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.11.001 · Cited by 298

Sleep and muscle recovery: Endocrinological and molecular basis for a new and promising hypothesis

Dattilo, M., Antunes, H. K. M., Medeiros, A., Mônico Neto, M., Souza, H. S., Tufik, S., & de Mello, M. T. (2011) · Medical Hypotheses · doi:10.1016/j.mehy.2011.04.017 · Cited by 290

Structure of the Cand1-Cul1-Roc1 Complex Reveals Regulatory Mechanisms for the Assembly of the Multisubunit Cullin-Dependent Ubiquitin Ligases

Goldenberg, S. J., Cascio, T. C., Shumway, S. D., Garbutt, K. C., Liu, J., Xiong, Y., & Zheng, N. (2004) · Cell · doi:10.1016/j.cell.2004.10.019 · Cited by 280

Recent advances in our understanding of neurodegeneration

Jellinger, K. A. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0240-y · Cited by 274

Homo-PROTACs: bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation

Maniaci, C., Hughes, S. J., Testa, A., Chen, W., Lamont, D. J., Rocha, S., Alessi, D. R., Romeo, R., & Ciulli, A. (2017) · Nature Communications · doi:10.1038/s41467-017-00954-1 · Cited by 245

Targeting Cullin–RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation

Bulatov, E., & Ciulli, A. (2015) · Biochemical Journal · doi:10.1042/bj20141450 · Cited by 237

Tyrosine-phosphorylation of AAV2 vectors and its consequences on viral intracellular trafficking and transgene expression

Zhong, L., Li, B., Jayandharan, G., Mah, C. S., Govindasamy, L., Agbandje-McKenna, M., Herzog, R. W., Weigel-Van Aken, K. A., Hobbs, J. A., Zolotukhin, S., et al. (2008) · Virology · doi:10.1016/j.virol.2008.08.027 · Cited by 232

Structural assembly of cullin-RING ubiquitin ligase complexes

Zimmerman, E. S., Schulman, B. A., & Zheng, N. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.010 · Cited by 227

C-terminal modifications regulate MDM2 dissociation and nuclear export of p53

Carter, S., Bischof, O., Dejean, A., & Vousden, K. H. (2007) · Nature Cell Biology · doi:10.1038/ncb1562 · Cited by 225

Ubiquitination of both adeno-associated virus type 2 and 5 capsid proteins affects the transduction efficiency of recombinant vectors

Yan, Z., Zak, R., Luxton, G. W. G., Ritchie, T. C., Bantel-Schaal, U., & Engelhardt, J. F. (2002) · Journal of Virology · doi:10.1128/jvi.76.5.2043-2053.2002 · Cited by 222

Suprafacial Orientation of the SCFCdc4 Dimer Accommodates Multiple Geometries for Substrate Ubiquitination

Tang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., & Tyers, M. (2007) · Cell · doi:10.1016/j.cell.2007.04.042 · 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

Essential Role of Ubiquitin-Specific Protease 8 for Receptor Tyrosine Kinase Stability and Endocytic Trafficking In Vivo

Niendorf, S., Oksche, A., Kisser, A., Löhler, J., Prinz, M., Schorle, H., Feller, S., Lewitzky, M., Horak, I., & Knobeloch, K.-P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01566-06 · Cited by 207

Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson’s disease

McNaught, K. S. P., & Olanow, C. W. (2003) · Annals of Neurology · doi:10.1002/ana.10512 · Cited by 203

Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms

Huseby, M. J., Kruse, A. C., Digre, J., Kohler, P. L., Vocke, J. A., Mann, E. E., Bayles, K. W., Bohach, G. A., Schlievert, P. M., Ohlendorf, D. H., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911032107 · Cited by 199

Ubiquitin ligase MKRN1 modulates telomere length homeostasis through a proteolysis of hTERT

Kim, J. H., Park, S.-M., Kang, M. R., Oh, S.-Y., Lee, T. H., Muller, M. T., & Chung, I. K. (2005) · Genes & Development · doi:10.1101/gad.1289405 · Cited by 197

p53 regulation by ubiquitin

Brooks, C. L., & Gu, W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.022 · Cited by 186

Identification of the ubiquitin–protein ligase that recognizes oxidized IRP2

Yamanaka, K., Ishikawa, H., Megumi, Y., Tokunaga, F., Kanie, M., Rouault, T. A., Morishima, I., Minato, N., Ishimori, K., & Iwai, K. (2003) · Nature Cell Biology · doi:10.1038/ncb952 · Cited by 181

Auxin Perception--Structural Insights

Calderon-Villalobos, L. I., Tan, X., Zheng, N., & Estelle, M. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005546 · Cited by 177

A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system

van Wijk, S. J. L., de Vries, S. J., Kemmeren, P., Huang, A., Boelens, R., Bonvin, A. M. J. J., & Timmers, H. T. M. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.55 · Cited by 164

The role of ubiquitin modification in the regulation of p53

Hock, A. K., & Vousden, K. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.022 · Cited by 168

Emerging insights into HAUSP (USP7) in physiology, cancer and other diseases.

Bhattacharya, S., Chakraborty, D., Basu, M., & Ghosh, M. K. (2018) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-018-0012-y · Cited by 162

Regulation of p53 by the Ubiquitin-conjugating Enzymes UbcH5B/C in Vivo

Saville, M. K., Sparks, A., Xirodimas, D. P., Wardrop, J., Stevenson, L. F., Bourdon, J.-C., Woods, Y. L., & Lane, D. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403362200 · Cited by 158

Feedback Regulation of Cholesterol Uptake by the LXR–IDOL–LDLR Axis

Zhang, L., Reue, K., Fong, L. G., Young, S. G., & Tontonoz, P. (2012) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.112.250571 · Cited by 137

Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53

Kostic, M., Matt, T., Martinez-Yamout, M. A., Dyson, H. J., & Wright, P. E. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.08.027 · Cited by 128

Priming and Extending: A UbcH5/Cdc34 E2 Handoff Mechanism for Polyubiquitination on a SCF Substrate

Wu, K., Kovacev, J., & Pan, Z.-Q. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.025 · Cited by 126

General aspects of neurodegeneration

Jellinger, K. A. (2003) · Journal of Neural Transmission. Supplementa · doi:10.1007/978-3-7091-0643-3_7 · Cited by 126

Altered responses in skeletal muscle protein turnover during aging in anabolic and catabolic periods

Attaix, D., Mosoni, L., Dardevet, D., Combaret, L., Mirand, P. P., & Grizard, J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.009 · Cited by 123

Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3

LeBron, C., Chen, L., Gilkes, D. M., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601032 · Cited by 122

Regulation of Epidermal Growth Factor Receptor Ubiquitination and Trafficking by the USP8·STAM Complex

Berlin, I., Schwartz, H., & Nash, P. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016287 · Cited by 121

Regulation of apoptosis by the ubiquitin and proteasome pathway

Wójcik, C. (2002) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2002.tb00309.x · Cited by 118

A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease‐relevant insults

Niikura, T., Hashimoto, Y., Tajima, H., Ishizaka, M., Yamagishi, Y., Kawasumi, M., Nawa, M., Terashita, K., Aiso, S., & Nishimoto, I. (2003) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2003.02553.x · Cited by 115

Control of biochemical reactions through supramolecular RING domain self-assembly

Kentsis, A., Gordon, R. E., & Borden, K. L. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202608799 · Cited by 112

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

An Atypical E3 Ligase Zinc Finger Protein 91 Stabilizes and Activates NF-κB-inducing Kinase via Lys63-linked Ubiquitination

Jin, X., Jin, H. R., Jung, H. S., Lee, S. J., Lee, J.-H., & Lee, J. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129551 · Cited by 94

Human Immunodeficiency Virus Type 1 Vpr-Binding Protein VprBP, a WD40 Protein Associated with the DDB1-CUL4 E3 Ubiquitin Ligase, Is Essential for DNA Replication and Embryonic Development

McCall, C. M., Miliani de Marval, P. L., Chastain, P. D., Jackson, S. C., He, Y. J., Kotake, Y., Cook, J. G., & Xiong, Y. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00232-08 · Cited by 83

UBE2G1 governs the destruction of cereblon neomorphic substrates

Lu, G., Weng, S., Matyskiela, M., Zheng, X., Fang, W., Wood, S., Surka, C., Mizukoshi, R., Lu, C.-C., Mendy, D., et al. (2018) · eLife · doi:10.7554/elife.40958 · Cited by 78

Cyclin dependent kinases and their role in regulation of plant cell cycle

Tank, J. G., & Thaker, V. S. (2011) · Biologia plantarum · doi:10.1007/s10535-011-0031-9 · Cited by 76

Alternative Effects of the Ubiquitin-Proteasome Pathway on Glucocorticoid Receptor Down-Regulation and Transactivation Are Mediated by CHIP, an E3 Ligase

Wang, X., & DeFranco, D. B. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0383 · Cited by 77

HDAC3 controls gap 2/mitosis progression in adult neural stem/progenitor cells by regulating CDK1 levels

Jiang, Y., & Hsieh, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411939111 · Cited by 71

Targeted Destruction of c-Myc by an Engineered Ubiquitin Ligase Suppresses Cell Transformation and Tumor Formation

Hatakeyama, S., Watanabe, M., Fujii, Y., & Nakayama, K. I. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1581 · Cited by 67

RING-Domain E3 Ligase-Mediated Host–Virus Interactions: Orchestrating Immune Responses by the Host and Antagonizing Immune Defense by Viruses

Zhang, Y., Li, L.-F., Munir, M., & Qiu, H.-J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01083 · Cited by 62

Targeted Degradation of KRAS by an Engineered Ubiquitin Ligase Suppresses Pancreatic Cancer Cell Growth In Vitro and In Vivo

Ma, Y., Gu, Y., Zhang, Q., Han, Y., Yu, S., Lu, Z., & Chen, J. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0650 · Cited by 55

Dual inhibition of AKT-mTOR and AR signaling by targeting HDAC3 in PTEN- or SPOP-mutated prostate cancer

Yan, Y., An, J., Yang, Y., Wu, D., Bai, Y., Cao, W., Ma, L., Chen, J., Yu, Z., He, Y., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708478 · Cited by 53

Stabilization of MCRS1 by BAP1 Prevents Chromosome Instability in Renal Cell Carcinoma

Peng, J., Ma, J., Li, W., Mo, R., Zhang, P., Gao, K., Jin, X., Xiao, J., Wang, C., & Fan, J. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.08.013 · Cited by 46

Endotoxin reduces CD95-induced neutrophil apoptosis by cIAP-2-mediated caspase-3 degradation

Mica, L., Härter, L., Trentz, O., & Keel, M. (2004) · Journal of the American College of Surgeons · doi:10.1016/j.jamcollsurg.2004.05.272 · Cited by 40

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

The Structural Differences between a Glycoprotein Specific F-Box Protein Fbs1 and Its Homologous Protein FBG3

Kumanomidou, T., Nishio, K., Takagi, K., Nakagawa, T., Suzuki, A., Yamane, T., Tokunaga, F., Iwai, K., Murakami, A., Yoshida, Y., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0140366 · Cited by 21

Comparison of native and non-native ubiquitin oligomers reveals analogous structures and reactivities

Pham, G. H., Rana, A. S. J. B., Korkmaz, E. N., Trang, V. H., Cui, Q., & Strieter, E. R. (2016) · Protein Science · doi:10.1002/pro.2834 · Cited by 21

Inhibition of Proteasome Activity Upregulates IL-6 Expression in RPE Cells through the Activation of P38 MAPKs

Qin, T., & Gao, S. (2018) · Journal of Ophthalmology · doi:10.1155/2018/5392432 · Cited by 13

USP7 protects TFEB from proteasome-mediated degradation

Keshri, S., Vicinanza, M., Takla, M., & Rubinsztein, D. C. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114872 · Cited by 8

Top‐down analysis of novel synthetic branched proteins

Gomes, F., Lemma, B., Abeykoon, D., Chen, D., Wang, Y., Fushman, D., & Fenselau, C. (2019) · Journal of Mass Spectrometry · doi:10.1002/jms.4303 · Cited by 7