Global changes to the ubiquitin system in Huntington's disease

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes

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Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice

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Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain

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Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

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Polyubiquitin chains: polymeric protein signals

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Neurological abnormalities in a knock-in mouse model of Huntington's disease

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Parkin Protects against the Toxicity Associated with Mutant α-Synuclein

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Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease

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Global Impairment of the Ubiquitin-Proteasome System by Nuclear or Cytoplasmic Protein Aggregates Precedes Inclusion Body Formation

Bennett, E. J., Bence, N., Rajadas, J., & Kopito, R. R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.021 · Cited by 511

Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release

Jana, N. R. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.10.1049 · Cited by 453

The E3 Ubiquitin Ligase MID1 Catalyzes Ubiquitination and Cleavage of Fu

Schweiger, S., Dorn, S., Fuchs, M., Köhler, A., Matthes, F., Müller, E., Wanker, E. E., Schneider, R., & Krauß, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.541219 · Cited by 28

Diverse polyubiquitin chains accumulate following 26S proteasomal dysfunction in mammalian neurones

Bedford, L., Layfield, R., Mayer, R. J., Peng, J., & Xu, P. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2010.12.064 · Cited by 29

Local TrkB signaling: themes in development and neural plasticity

Johnstone, A. D., & Mobley, W. C. (2020) · Cell and Tissue Research · doi:10.1007/s00441-020-03278-7 · Cited by 28

Dysregulation of system xc− expression induced by mutant huntingtin in a striatal neuronal cell line and in R6/2 mice

Frederick, N. M., Bertho, J., Patel, K. K., Petr, G. T., Bakradze, E., Smith, S. B., & Rosenberg, P. A. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.06.017 · Cited by 27

Selective autophagy: The new player in the fight against neurodegenerative diseases?

Wu, M.-Y., Song, J., Wang, S.-F., Cai, C.-Z., Li, M., & Lu, J. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.11.009 · Cited by 27

Induction of chemokines, MCP‐1, and KC in the mutant huntingtin expressing neuronal cells because of proteasomal dysfunction

Godavarthi, S. K., Narender, D., Mishra, A., Goswami, A., Rao, S. N. R., Nukina, N., & Jana, N. R. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05823.x · Cited by 27

Mitochondrial accumulation of polyubiquitinated proteins and differential regulation of apoptosis by polyubiquitination sites Lys‐48 and ‐63

Sun, F., Kanthasamy, A., Anantharam, V., & Kanthasamy, A. G. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00775.x · Cited by 29

The UPS and autophagy in chronic neurodegenerative disease: Six of one and half a dozen of the other—Or not?

Bedford, L., Paine, S., Rezvani, N., Mee, M., Lowe, J. S., & Mayer, R. J. (2009) · Autophagy · doi:10.4161/auto.5.2.7389 · Cited by 29

Rapamycin prevents the mutant huntingtin-suppressed GLT-1 expression in cultured astrocytes

Chen, L.-L., Wu, J.-C., Wang, L.-H., Wang, J., Qin, Z.-H., Difiglia, M., & Lin, F. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2011.162 · Cited by 26

Aqueous Extract ofPaeonia lactifloraand Paeoniflorin as Aggregation Reducers Targeting Chaperones in Cell Models of Spinocerebellar Ataxia 3

Chang, K., Chen, W.-L., Lee, L.-C., Lin, C., Kung, P., Lin, T., Wu, Y.-C., Wu, Y., Chen, Y., Lee‐Chen, G., et al. (2013) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2013/471659 · Cited by 26

Mutant Huntingtin Alters Cell Fate in Response to Microtubule Depolymerization via the GEF-H1-RhoA-ERK Pathway

Varma, H., Yamamoto, A., Sarantos, M. R., Hughes, R. E., & Stockwell, B. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125542 · Cited by 26

Strategies to Investigate Ubiquitination in Huntington's Disease

Sap, K. A., & Reits, E. A. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00485 · Cited by 25

BimEL as a possible molecular link between proteasome dysfunction and cell death induced by mutant huntingtin

Leon, R., Bhagavatula, N., Ulukpo, O., McCollum, M. H., & Wei, J. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07215.x · Cited by 25

Mechanisms of ubiquitin-independent proteasomal degradation and their roles in age-related neurodegenerative disease

Church, T. R., & Margolis, S. S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1531797 · Cited by 25

Phosphodiesterase-4 Inhibition in Parkinson’s Disease: Molecular Insights and Therapeutic Potential

Roy, D., Balasubramanian, S., Krishnamurthy, P. T., Sola, P., & Rymbai, E. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01349-1 · Cited by 24

Polyglutamine-Rich Suppressors of Huntingtin Toxicity Act Upstream of Hsp70 and Sti1 in Spatial Quality Control of Amyloid-Like Proteins

Wolfe, K. J., Ren, H. Y., Trepte, P., & Cyr, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095914 · Cited by 25

Conjugation of Complex Polyubiquitin Chains to WRNIP1

Bish, R. A., Fregoso, O. I., Piccini, A., & Myers, M. P. (2008) · Journal of Proteome Research · doi:10.1021/pr800217q · Cited by 24

Methods to measure ubiquitin chain length and linkage

Ohtake, F., Tsuchiya, H., Tanaka, K., & Saeki, Y. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.12.019 · Cited by 24

Therapeutic gene silencing strategies for polyglutamine disorders

Scholefield, J., & Wood, M. J. A. (2009) · Trends in Genetics · doi:10.1016/j.tig.2009.11.005 · Cited by 26

The Cyclophilin-like Domain of Ran-binding Protein-2 Modulates Selectively the Activity of the Ubiquitin-Proteasome System and Protein Biogenesis

Yi, H., Friedman, J. L., & Ferreira, P. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706903200 · Cited by 24

Mitochondrial quality control: Epigenetic signatures and therapeutic strategies

Ambekar, T., Pawar, J., Rathod, R., Patel, M., Fernandes, V., Kumar, R., Singh, S. B., & Khatri, D. K. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105095 · Cited by 23

Aging Is Not Associated with Proteasome Impairment in UPS Reporter Mice

Cook, C. N., Gass, J. M., Dunmore, J., Tong, J., Taylor, J. P., Eriksen, J. L., McGowan, E. M., Lewis, J. M., Johnston, J. A., & Petrucelli, L. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005888 · Cited by 25

Ubiquitin: a potential cerebrospinal fluid progression marker in Huntington's disease

Vinther‐Jensen, T., Simonsen, A. H., Budtz–Jørgensen, E., Hjermind, L. E., & Nielsen, J. E. (2015) · European Journal of Neurology · doi:10.1111/ene.12750 · Cited by 23

Modifiers of mutant huntingtin aggregationfunctional conservation of C. elegans-modifiers of polyglutamine aggregation

Teuling, E., Bourgonje, A. M., Veenje, S., Thijssen, K. L., de Boer, J., van der Velde, K. J., Swertz, M. A., & Nollen, E. A. A. (2011) · PLoS Currents · doi:10.1371/currents.rrn1255 · Cited by 24

The polyubiquitin Ubc gene modulates histone H2A monoubiquitylation in the R6/2 mouse model of Huntington's disease

Bett, J. S., Benn, C., Ryu, K., Kopito, R. R., & Bates, G. P. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00543.x · Cited by 26

scyllo-Inositol Promotes Robust Mutant Huntingtin Protein Degradation

Lai, A. Y., Lan, C. P., Hasan, S., Brown, M. E., & McLaurin, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.501635 · Cited by 22

Niclosamide Prevents the Formation of Large Ubiquitin-Containing Aggregates Caused by Proteasome Inhibition

Gies, E., Wilde, I., Winget, J. M., Brack, M., Rotblat, B., Novoa, C. A., Balgi, A. D., Sorensen, P. H. B., Roberge, M., & Mayor, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014410 · Cited by 23

UPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review

Papaevgeniou, N., & Chondrogianni, N. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_1 · Cited by 23

Quantification of Huntington’s Disease Related Markers in the R6/2 Mouse Model

Etxeberria-Rekalde, E., Alzola-Aldamizetxebarria, S., Flunkert, S., Isabella, H., Daurer, M., Neddens, J., & Hutter‐Paier, B. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.617229 · Cited by 22

Overexpression of F0F1-ATP synthase α suppresses mutant huntingtin aggregation and toxicity in vitro

Wang, H., Xu, Y.-X., Zhao, X.-Y., Zhao, H., Yan, J., Sun, X.-B., Guo, J.-C., & Zhu, C.-Q. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.139 · Cited by 22

Induced Pluripotent Stem Cells in Huntington’s Disease: Disease Modeling and the Potential for Cell-Based Therapy

Liu, L., Huang, J., Han, C., Zhang, G., Xu, X., Shen, Y., Li, J., Jiang, H., Lin, Z., Xiong, N., et al. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9601-8 · Cited by 23

A Bystander Mechanism Explains the Specific Phenotype of a Broadly Expressed Misfolded Protein

Klabonski, L. A., Zha, J., Senthilkumar, L., & Gidalevitz, T. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006450 · Cited by 23

Targeting Ubiquitin Proteasome Pathway with Traditional Chinese Medicine for Treatment of Spinocerebellar Ataxia Type 3

Chen, I., Chang, C.-N., Chen, W.-L., Lin, T., Chao, C., Lin, C., Lin, H.-Y., Cheng, M., Chiang, M.-C., Lin, J., et al. (2019) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x19500046 · Cited by 21

Molecular biology of Huntington's disease

McFarland, K. N., & Cha, J.-H. J. (2011) · Handbook of clinical neurology · doi:10.1016/b978-0-444-52014-2.00003-3 · Cited by 21

Quantitative proteomics to decipher ubiquitin signaling

Chen, P., Na, C. H., & Peng, J. (2012) · Amino Acids · doi:10.1007/s00726-012-1286-y · Cited by 21

A clinical study and future prospects for bioactive compounds and semi-synthetic molecules in the therapies for Huntington's disease

Islam, M. R., Jony, M. H., Thufa, G. K., Akash, S., Dhar, P. S., Rahman, M. M., Afroz, T., Ahmed, M., Hemeg, H. A., Rauf, A., et al. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03604-4 · Cited by 20

Differential Degradation of Full-length and Cleaved Ataxin-7 Fragments in a Novel Stable Inducible SCA7 Model

Yu, X., Ajayi, A., Boga, N. R., & Ström, A. (2012) · Journal of Molecular Neuroscience · doi:10.1007/s12031-012-9722-8 · Cited by 20

HSF1 and Its Role in Huntington’s Disease Pathology

Kim, H., & Gómez‐Pastor, R. (2022) · Advances in experimental medicine and biology · doi:10.1007/5584_2022_742 · Cited by 21

Aggregation of Human S100A8 and S100A9 Amyloidogenic Proteins Perturbs Proteostasis in a Yeast Model

Eremenko, E., Ben‐Zvi, A., Morozova‐Roche, L. A., & Raveh, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058218 · Cited by 19

Fluorescent Tools for In Vivo Studies on the Ubiquitin-Proteasome System

Matilainen, O., Jha, S., & Holmberg, C. I. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_12 · Cited by 19

ESI-IM-MS and Collision-Induced Unfolding That Provide Insight into the Linkage-Dependent Interfacial Interactions of Covalently Linked Diubiquitin

Wagner, N. D., Clemmer, D. E., & Russell, D. H. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b02932 · Cited by 19

Deciphering the ubiquitin proteome: Limits and advantages of high throughput global affinity purification-mass spectrometry approaches

Polge, C., Uttenweiler‐Joseph, S., Leulmi, R., Heng, A.-É., Burlet‐Schiltz, O., Attaix, D., & Taillandier, D. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.031 · Cited by 18

Putting Huntingtin “Aggregation” in View with Windows into the Cellular Milieu

Hatters, D. M. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026611212220013 · Cited by 18

Dysregulation of long non‐coding RNAs and their mechanisms in Huntington's disease

Tan, X., Liu, Y., Liu, Y., Zhang, T., & Cong, S. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24825 · Cited by 19

Ubiquitin-Proteasome-Mediated Protein Degradation and Disorders of the Central Nervous System

Hegde, A. N., Timm, L. E., Sivley, C. J., Ramiyaramcharankarthic, S., Lowrimore, O. J., Hendrix, B. J., Grozdanov, T. G., & Anderson, W. J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26030966 · Cited by 19

Caspase-2 is a condensate-mediated deubiquitinase in protein quality control

Ge, Y., Zhou, L., Fu, Y., He, L., Chen, Y., Li, D., Xie, Y., Yang, J., Wu, H., Dai, H., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01522-8 · Cited by 18

Regulation of cellular protein quality control networks in a multicellular organism

Bar‐Lavan, Y., Kosolapov, L., Frumkin, A., & Ben‐Zvi, A. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08455.x · Cited by 17

Ubiquitin-like modifiers

Taherbhoy, A. M., Schulman, B. A., & Kaiser, S. E. (2012) · Essays in Biochemistry · doi:10.1042/bse0520051 · Cited by 17

Increased E4 Activity in Mice Leads to Ubiquitin-containing Aggregates and Degeneration of Hypothalamic Neurons Resulting in Obesity

Susaki, E. A., Kaneko-Oshikawa, C., Miyata, K., Tabata, M., Yamada, T., Oike, Y., Katagiri, H., & Nakayama, K. I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105841 · Cited by 17

Global ubiquitination analysis reveals extensive modification and proteasomal degradation of cowpox virus proteins, but preservation of viral cores

Grossegesse, M., Doellinger, J., Fritsch, A., Laue, M. M., Piesker, J., Schaade, L., & Nitsche, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-20130-9 · Cited by 18

Inhibition of p38 Mitogen–Activated Protein Kinase Ameliorates HAP40 Depletion–Induced Toxicity and Proteasomal Defect in Huntington’s Disease Model

Huang, Z.-N., Chen, J.-M., Huang, L.-C., Fang, Y.-H., & Her, L. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02280-y · Cited by 17

Modest proteasomal inhibition by aberrant ubiquitin exacerbates aggregate formation in a Huntington disease mouse model

de Pril, R., Hobo, B., van Tijn, P., Roos, R. A. C., van Leeuwen, F. W., & Fischer, D. F. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.12.001 · Cited by 17

Polyglutamine expansion disturbs the endoplasmic reticulum formation, leading to caspase-7 activation through Bax

Ueda, M., Li, S., Itoh, M., Hayakawa‐Yano, Y., Wang, M.-X., Hayakawa, M., Hasebe-Matsubara, R., Ohta, K., Ohta, E., Mizuno, A., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.12.114 · Cited by 16

Assembly of K11-Linked Ubiquitin Chains by the Anaphase-Promoting Complex

Rapé, M. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4419-6676-6_9 · Cited by 17

Orthogonal approaches required to measure proteasome composition and activity in mammalian brain tissue

Türker, F., Bharadwaj, R. A., Kleinman, J. E., Weinberger, D. R., Hyde, T. M., White, C. J., Williams, D. W., & Margolis, S. S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104811 · Cited by 16

The Differential Profiling of Ubiquitin‐Proteasome and Autophagy Systems in Different Tissues before the Onset of H untington's Disease Models

Her, L., Lin, J., Fu, M., Chang, Y., Li, C., Tang, T., Jhang, Y.-L., Chang, C., Shih, M., Cheng, P., et al. (2014) · Brain Pathology · doi:10.1111/bpa.12191 · Cited by 16

Analysis of alpha hemoglobin stabilizing protein overexpression in murine β‐thalassemia

Nasimuzzaman, M., Khandros, E., Wang, X., Kong, Y., Zhao, H., Weiss, D., Rivella, S., Weiss, M. J., & Persons, D. A. (2010) · American Journal of Hematology · doi:10.1002/ajh.21829 · Cited by 16

The Ubiquitin Receptor ADRM1 Modulates HAP40-Induced Proteasome Activity

Huang, Z.-N., & Her, L. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0247-y · Cited by 16

Induced neural stem cells as a means of treatment in Huntington’s disease

Choi, K., & Hong, S. (2017) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2017.1365133 · Cited by 16

Neuronal Proteomic Analysis of the Ubiquitinated Substrates of the Disease-Linked E3 Ligases Parkin and Ube3a

Martinez, A., Ramírez, J., Osinalde, N., Arizmendi, J. M., & Mayor, U. (2018) · BioMed Research International · doi:10.1155/2018/3180413 · Cited by 16

Pathobiology of the autophagy-lysosomal pathway in the Huntington’s disease brain

Berg, M. J., Veeranna, Rosa, C. M., Kumar, A. R., Mohan, P. S., Stavrides, P. H., Darji, S., Marchionini, D. M., Yang, D., & Nixon, R. A. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02131-8 · Cited by 15

Chronic over‐expression of ubiquitin impairs learning, reduces synaptic plasticity, and enhances GRIA receptor turnover in mice

Vaden, J. H., Tian, T. M., Golf, S. R., McLean, J. W., Wilson, J. A., & Wilson, S. M. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14630 · Cited by 16

Current understanding on the pathogenesis of polyglutamine diseases

He, X., Lin, F., & Qin, Z. (2010) · Neuroscience Bulletin · doi:10.1007/s12264-010-0113-2 · Cited by 16

Therapeutic approaches to spinal and bulbar muscular atrophy

Ranganathan, S., & Fischbeck, K. H. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.08.005 · Cited by 15

Effect of p62/SQSTM1 polyubiquitination on its autophagic adaptor function and cellular survival under oxidative stress induced by arsenite

Lee, H., Kim, M.-N., & Ryu, K. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.03.146 · Cited by 15

A role of cellular translation regulation associated with toxic Huntingtin protein

Joag, H., Ghatpande, V., Desai, M., Sarkar, M., Raina, A., Shinde, M., Chitale, R., Deo, A., Bose, T., & Majumdar, A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03392-y · Cited by 15

Structural Propensities of Human Ubiquitination Sites: Accessibility, Centrality and Local Conformation

Zhou, Y., Liu, S., Song, J., & Zhang, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083167 · Cited by 14

Investigation of cerebrocortical and cerebellar pathology in canine fucosidosis and comparison to aged brain

Kondagari, G. S., Yang, J. L., & Taylor, R. M. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.10.026 · Cited by 14

Huntington's and other polyglutamine diseases: many effects of single gene mutations

Luthi‐Carter, R. (2007) · Drug Discovery Today Disease Mechanisms · doi:10.1016/j.ddmec.2007.10.002 · Cited by 14

Bortezomib paradigm shift in myeloma

McConkey, D. J. (2009) · Blood · doi:10.1182/blood-2009-06-223230 · Cited by 14

Mechanisms underlying neurodegeneration in Huntington disease: applications to novel disease-modifying therapies

Ross, C. A., Kronenbuerger, M., Duan, W., & Margolis, R. L. (2017) · Handbook of clinical neurology · doi:10.1016/b978-0-12-801893-4.00002-x · Cited by 14

Spatial sequestration of misfolded proteins in neurodegenerative diseases

Rolli, S., & Sontag, E. M. (2022) · Biochemical Society Transactions · doi:10.1042/bst20210862 · Cited by 14

Using the Ubiquitin-modified Proteome to Monitor Protein Homeostasis Function

Carrano, A. C., & Bennett, E. J. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r113.029744 · Cited by 13

RNA therapy for polyglutamine neurodegenerative diseases

Watson, L. M., & Wood, M. J. A. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2011.1 · Cited by 12

Role of circRNA in E3 Modification under Human Disease

Chen, Z., Song, M., Wang, T., Gao, J.-W., Lin, F., Dai, H., & Zhang, C. (2022) · Biomolecules · doi:10.3390/biom12091320 · Cited by 12

Isolated RING2 Domain of Parkin Is Sufficient for E2-Dependent E3 Ligase Activity

Rankin, C. A., Galeva, N. A., Bae, K., Ahmad, M. N., Witte, T. M., & Richter, M. L. (2013) · Biochemistry · doi:10.1021/bi401378p · Cited by 12

Atypical ubiquitination of proteins

Бунеева, О. А., & Medvedev, A. E. (2016) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20166205496 · Cited by 12

Analysis of Ubiquitinated Proteome by Quantitative Mass Spectrometry

Na, C. H., & Peng, J. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-885-6_26 · Cited by 12

Targeting New Candidate Genes by Small Molecules Approaching Neurodegenerative Diseases

Fan, H., Chi, C.-S., Cheng, S.-N., Lee, H.-F., Tsai, J., Lin, S., & Harn, H. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms17010026 · Cited by 12

Identification of substrates for human deubiquitinating enzymes (DUBs): An up-to-date review and a case study for neurodevelopmental disorders

Elu, N., Osinalde, N., Ramírez, J., Presa, N., Rodríguez, J. A., Prieto, G., & Mayor, U. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.01.001 · Cited by 15

Uncoupling the Trade-Off between Somatic Proteostasis and Reproduction in Caenorhabditis elegans Models of Polyglutamine Diseases

Shemesh, N., Shai, N., Meshnik, L., Katalan, R., & Ben‐Zvi, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00101 · Cited by 12

Selective Autophagy Pathway of Nanoparticles and Nanodrugs: Drug Delivery and Pathophysiological Effects

Raj, E. N., Lin, Y., Chen, C., Liu, K., & Chao, J. (2020) · Advanced Therapeutics · doi:10.1002/adtp.202000085 · Cited by 10

Deciphering Tissue-Specific Ubiquitylation by Mass Spectrometry

Mayor, U., & Peng, J. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-474-2_3 · Cited by 10

Cellular Models: HD Patient-Derived Pluripotent Stem Cells

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Salvage NAD+ biosynthetic pathway enzymes moonlight as molecular chaperones to protect against proteotoxicity

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