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

MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366

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

Mangiarini, L., Sathasivam, K., Seller, M., Cozens, B., Harper, A., Hetherington, C., Lawton, M., Trottier, Y., Lehrach, H., Davies, S. W., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81369-0 · Cited by 3,073

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

DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., & Aronin, N. (1997) · Science · doi:10.1126/science.277.5334.1990 · Cited by 2,439

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,209

Polyubiquitin chains: polymeric protein signals

Pickart, C. M., & Fushman, D. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.09.009 · Cited by 1,075

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

Lin, C. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.2.137 · Cited by 592

Parkin Protects against the Toxicity Associated with Mutant α-Synuclein

Petrucelli, L., O’Farrell, C., Lockhart, P. J., Baptista, M. J., Kehoe, K. J., Vink, L., Choi, P., Wolozin, B. L., Farrer, M. J., Hardy, J., et al. (2002) · Neuron · doi:10.1016/s0896-6273(02)01125-x · Cited by 561

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

Lowe, J., Blanchard, A., Morrell, K., Lennox, G., Reynolds, L., Billett, M., Landon, M., & Mayer, R. J. (1988) · The Journal of Pathology · doi:10.1002/path.1711550105 · Cited by 539

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 molecular mechanisms of spinocerebellar ataxias for DNA repeat expansion in disease

Kumar, M., Tyagi, N., & Faruq, M. (2023) · Emerging Topics in Life Sciences · doi:10.1042/etls20230013 · Cited by 8

Effect of the overexpression of mutant ubiquitin (K48R) on the cellular response induced by 4-hydroxy-2,3-trans-nonenal, an end-product of lipid peroxidation

Hyun, D. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.04.045 · Cited by 6

Huntington's Disease: Can Mice Lead the Way to Treatment?

Crook, Z. R., & Housman, D. E. (2011) · Neuron · doi:10.1016/j.neuron.2011.02.029 · Cited by 6

Particle radiation-induced dysregulation of protein homeostasis in primary human and mouse neuronal cells

Shaler, T., Lin, H., Bakke, J. P., Chen, S., Grover, A., & Chang, P. Y. (2020) · Life Sciences in Space Research · doi:10.1016/j.lssr.2020.02.003 · Cited by 6

Modulation of Huntingtin Toxicity by BAG1 is Dependent on an Intact BAG Domain

Liman, J., Sroka, K., Dohm, C. P., Deeg, S., Bähr, M., & Kermer, P. (2010) · Molecules · doi:10.3390/molecules15106678 · Cited by 6

Translating protein phosphatase research into treatments for neurodegenerative diseases

Sundaram, J. R., Lee, I. C. J., & Shenolikar, S. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160157 · Cited by 5

Advances in human brain proteomics analysis of neurodegenerative diseases

Chen, Y., Wang, X., & Xu, B. (2022) · Human Brain · doi:10.37819/hb.001.001.0197 · Cited by 5

Brain-Derived 11S Regulator (PA28αβ) Promotes Proteasomal Hydrolysis of Elongated Oligoglutamine-Containing Peptides

Kriachkov, V. A., Gotmanova, N. N., Tashlitsky, V. N., & Bacheva, A. V. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713275 · Cited by 5

Genesis of ER stress in Huntington’s Disease

Shenkman, M., Eiger, H., & Lederkremer, G. Z. (2015) · Endoplasmic Reticulum Stress in Diseases · doi:10.1515/ersc-2015-0007 · Cited by 5

The Ubiquitin–Proteasome System in Brain Disorders: Pathogenic Pathways, Post-Translational Tweaks, and Therapeutic Frontiers

Gupta, R. V., Begum, M. Y., Kumar, R., Gupta, J., Nagraik, R., Panda, S. P., Abomughaid, M. M., Lakhanpal, S., Avinash, D., Osmani, R. A. M., et al. (2025) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-025-10258-7 · Cited by 4

Saroglitazar, a PPAR α/γ agonist alleviates 3-Nitropropionic acid induced neurotoxicity in rats: Unveiling the underlying mechanisms

Jakkamsetti, M. S., Kolusu, A. S., Rongala, S., Arakareddy, B. P., Nori, L. P., & Samudrala, P. K. (2024) · NeuroToxicology · doi:10.1016/j.neuro.2024.09.004 · Cited by 4

Regenerative Medicine of Neural Tissues

Stocum, D. L. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-384860-4.00011-3 · Cited by 4

The Potential of Small Molecules in Preventing Tau Oligomer Formation and Toxicity

Gerson, J. E., Cascio, F. L., & Kayed, R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00006-5 · Cited by 4

Examination of genetic and pharmacological tools to study the proteasomal deubiquitinating enzyme ubiquitin‐specific protease 14 in the nervous system

Tian, T. M., McLean, J. W., Wilson, J. A., & Wilson, S. M. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15180 · Cited by 4

Dynamic Role of Ubiquitination in the Management of Misfolded Proteins Associated with Neurodegenerative Diseases

Wong, E. S. P., Tan, J. M. M., & Lim, K. (2008) · Focus on structural biology · doi:10.1007/978-1-4020-9434-7_3 · Cited by 4

Les maladies neurodégénératives par expansion de polyglutamine : physiopathologie et stratégies thérapeutiques

Ravache, M., Sleymane, G. A., & Trottier, Y. (2010) · Pathologie Biologie · doi:10.1016/j.patbio.2009.12.004 · Cited by 5

Aggregation-Prone Proteins Modulate Huntingtin Inclusion Body Formation in Yeast

Kantcheva, R., Mason, R. P., & Giorgini, F. (2014) · PLoS Currents · doi:10.1371/currents.hd.501008f3051342c9a5c0cd0f3a5bf3a4 · Cited by 4

Correction: Ku70 Alleviates Neurodegeneration in Drosophila Models of Huntington's Disease

Tamura, T., Sone, M., Iwatsubo, T., Tagawa, K., Wanker, E. E., & Okazawa, H. (2012) · PLoS ONE · doi:10.1371/annotation/e436994f-3b22-4b35-bd29-49992f64a584 · Cited by 4

Inhibition of UBE2N promotes the clearance of mutant HTT (huntingtin) in HD knock-in mice

Ou, K., Wang, X., Guo, M., Li, D., Zhang, C., Chen, L., Hou, J., Jia, Q., Zhu, L., Yang, S., et al. (2025) · Autophagy · doi:10.1080/15548627.2025.2549109 · Cited by 3

The Ubiquitin Script: writing protein fates in chains

Gupta, D., & Maddika, S. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253031 · Cited by 3

Treatment with Tau fibrils impact Huntington's disease-related phenotypes in cell and mouse models

Salem, S., Alpaugh, M., Saint‐Pierre, M., Borba, F. N., Cerquera‐Cleves, C., Lemieux, M., Ngonza-Nito, S. B., Koninck, P. D., Melki, R., & Cicchetti, F. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106696 · Cited by 3

What Is the Role of Adenosine Tone and Adenosine Receptors in Huntington’s Disease?

Blum, D. L., Chern, E. C., Domenici, M. R., Buée, L., Lin, C. Y., Ferré, S., & Popoli, P. (2018) · Springer eBooks · doi:10.1007/978-3-319-90808-3_12 · Cited by 3

Therapeutic Prospects for Polyglutamine Disease

Pennuto, M., & Fischbeck, K. H. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch40 · Cited by 3

Advances in Research on Endoplasmic Reticulum-Associated Degradation Mechanisms in Neurodegenerative Diseases

Kong, B. Z., Huang, W., Zhong, Y., Liu, Y., Wang, H., Shen, Y., Xu, J., Xiang, M., & Ye, B. (2026) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-026-01687-w · Cited by 2

Exploring the pleiotropic effects of lncRNA in different repeat expansion disorders

Das, S., Khandelwal, S., Shukla, S., & Kumar, A. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.168089 · Cited by 2

Role of the ubiquitin–proteasome system and autophagy in polyglutamine neurodegenerative diseases

Jana, N. R. (2009) · Future Neurology · doi:10.2217/fnl.09.69 · Cited by 2

In Vivo Strategies to Isolate and Characterize the Neuronal Ubiquitinated Proteome

Ramírez, J., Elu, N., Martinez, A., Lectez, B. L. P., & Mayor, U. (2017) · Neuromethods · doi:10.1007/978-1-4939-7119-0_11 · Cited by 2

Ubiquitin Mediated Posttranslational Modification of Proteins Involved in Various Signaling Diseases

LAVANYA, V. A., Jamal, S., & Ahmed, N. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811913-6.00005-9 · Cited by 2

Regenerative Medicine of Neural Tissues

Stocum, D. L. (2006) · Elsevier eBooks · doi:10.1016/b978-012369371-6/50023-x · Cited by 2

Amyloid fibrils are nanoparticles that target lysosomes.

Jakhria, T. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University) · Cited by 2

The Ubiquitin–Proteasome System in Neurodegenerative Diseases: More than the Usual Suspects

Bertolotti, A. (2011) · Wiley eBooks · doi:10.1002/9781118063903.ch5 · Cited by 2

Huntington's Disease and Other Choreas

Salman, H., Wild, E. J., & Tabrizi, S. J. (2017) · Neurodegeneration · doi:10.1002/9781118661895.ch21 · Cited by 2

Proteotoxic stresses stimulate dissociation of UBL4A from the tail-anchored protein recognition complex

Hagiwara, T., Minami, R., Ushio, C., Yokota, N., & Kawahara, H. (2023) · Biochemical Journal · doi:10.1042/bcj20230267 · Cited by 1

Nosological structure and frequency of autosomal dominant spinocerebellar ataxias associated with nucleotide repeat expansions in Russia

Vuta, E. V., Nazarov, V. D., Sidorenko, D. V., Банина, Д. Ю., Lapin, S. V., & Маzing, A. V. (2025) · Neuromuscular Diseases · doi:10.17650/2222-8721-2025-15-3-10-21 · Cited by 1

Ubiquitin signatures on aggregating proteins in neurodegeneration

Sahoo, S., Padhy, A. A., Shivani, K., Misra, A., & Mishra, P. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253046 · Cited by 1

INVESTIGATING THE MECHANISM OF PROMOTER-SPECIFIC N-TERMINAL MUTANT HUNTINGTIN-MEDIATED TRANSCRIPTIONAL DYSREGULATION

Hogel, M. (2012) · Library and Archives Canada (Government of Canada) · Cited by 1

Regulation of Endocytic Trafficking of Receptors and Transporters by Ubiquitination: Possible Role in Neurodegenerative Disease

Sorkin, A. D. (2009) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-540-87941-1_11 · Cited by 1

Regulation of Gene Expression by the Ubiquitin–Proteasome System and Implications for Neurological Disease

Lukaesko, L., & Meller, R. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_12 · Cited by 1

Huntington Disease

Kim, E. H., Mehrabi, N. F., Tippett, L. J., Waldvogel, H. J., & Faull, R. L. M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801942-9.00008-2 · Cited by 1

The Ubiquitin–Proteasome System in Synapses

Tydlacka, S., Li, S., & Li, X. (2010) · Springer eBooks · doi:10.1007/978-1-4419-7061-9_10 · Cited by 1

Huntingtin toxicity is ameliorated by BAG1 through modulation of its aggregation, degradation and subcellular distribution

Sroka, K. (2009) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3273 · Cited by 1

The Role of Mitochondrial Dysfunction in Neurodegenerative Proteinopathies and Aging.

Ocampo, A. (2012) · Cited by 1

Degradative proteomics and disease mechanisms

Lanucara, F., Brownridge, P., Young, I. S., Whitfield, P. D., & Doherty, M. K. (2010) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200900159 · Cited by 1

Endoplasmic Reticulum Stress, Regulation of Autophagy and Ubiquitin-proteasome System in Cellular Models of Huntington s Disease

Hyrskyluoto, A. (2014) · Työväentutkimus Vuosikirja · Cited by 1

Global Analysis of Ubiquitination

Meierhofer, D., & Kaiser, P. (2011) · Neuromethods · doi:10.1007/978-1-61779-111-6_15 · Cited by 1

Proteomics of the endoplasmic reticulum to determine cellular organization and protein function

Jain, M. D. (2009) · doi:10.82308/15158 · Cited by 1

EasyAb: A High-Throughput Workflow for Antibody-Based PTM Peptide Enrichment Method Coupled to Mass SpectrometryPreprint

Jayavelu, A. K., Liu, J. J., Schriever, S. C., Pfluger, P. T., Schwarzer, C., Krahmer, N., & Mann, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.29.620939 · Cited by 1

Peripheral and cerebral metabolic features in an animal model of huntington's disease expressing full-length mutant huntingtin

Lopes, C. (2010) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

Characterization of Proteins Involved in Neurodegeneration

Xu, Z. (2012)

STUDIES OF FACTORS AFFECTING INTRACELLULAR TOXICITY OF THE SCA7 DISEASE PROTEIN ATAXIN - 7 : FOCUS ON ATAXIN-7 DEGRADATION AND OXIDATIVE STRESS

Yu, X. (2011) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Inhibition of specific histone deacetylases suppresses pathogenesis in a Drosophila model of Huntington’s disease

Pallos, J. (2012) · SZTE Repository of Dissertations (University of Szeged) · doi:10.14232/phd.1071

Polyglutamine Neuropathies: Animal Models to Molecular Mechanisms

Hui, K. K., & Henderson, J. T. (2009) · Wiley eBooks · doi:10.1002/9783527628100.ch17

Protein Degradation in Neurodegeneration: The Ubiquitin Pathway

Bedford, L., Layfield, R., Rezvani, N., Paine, S., Lowe, J. S., & Mayer, R. J. (2011) · Wiley eBooks · doi:10.1002/9781444341256.ch5

Innovative approaches to monitor mutant huntingtin and to facilitate its degradation in Huntington's disease models

Baldo, B. (2011) · edoc (University of Basel) · doi:10.5451/unibas-005705769

Cell Adaptation, Injury, and Death: Ubiquitin–Proteasome System

Holler, D. A., & Dikic, I. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-386456-7.01404-0

Simply quantifying ubiquitin complexity

Bennett, E. J., & Harper, J. W. (2011) · Nature Methods · doi:10.1038/nmeth.1651

Studies of polyglutamine expanded Ataxin-7 toxicity

Yu, X. (2015) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

A Genome-Wide RNAi Screen for Modifiers of Polyglutamine-Induced Neurotoxicity in Drosophila

Voßfeldt, H. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3767

The Hunt in Huntington: What Causes Toxicity?

Cass, D. K. (2009) · Eukaryon

Ppd Biomarker Discovery Sciences

Schulman, H. (2008) · Biomarkers in Medicine · doi:10.2217/17520363.2.6.549

Hypericum perforatum phenolic compounds : protective role in the toxicity induced by heterologous expression of α-synuclein and huntingtin in yeast cells

Vieira, P. M. D. S. (2011) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

IL RUOLO DELL�HUNTINGTINA NELLA FISIOLOGIA DEL DIFFERENZIAMENTO NEURONALE E NELLA PATOLOGIA

Camnasio, S. (2014) · Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) · doi:10.13130/camnasio-stefano_phd2014-01-16

Maladies par expansion de polyglutamine: Avancées récentes et perspectives thérapeutiques Polyglutamine expansion diseases: Recent advances and therapeutic perspectives Revue de la littérature

Sleymane, G. A., & Trottier, Y. (2010) · HAL

Hypericum perforatum phenolic compounds: Protective role in the toxicity induced by heterologous expression of -synuclein and huntingtin in yeast cells !

de Ciências, E. (2011)

The ubiquitin proteasome system in Huntington disease : impairment of the proteolytic machinery aggravates huntingtin aggregation and toxicity

de Pril, R. (2011)

The role of autophagy in clearance of protein aggregates

Isakson, P. (2011) · NORA - Norwegian Open Research Archives

Proteasomal Degradation of Soluble, Misfolded Proteins

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00003-1

Cargo Recognition Failure Underlies Macroautophagy Defects in Huntington’s Disease

Tang, G., & Sulzer, D. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405529-2.00010-x

Ubiquitin Localization Changes as C. elegans Undergo Stress

Sanders, J. T. (2016)

Assembly and Disassembly of Protein Aggregates

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00006-7

Identification of non-essential host genes required for PrP106-126 mediated neurotoxicity

Stobart, M. J. (2011) · Mspace (University of Manitoba)

A Transgenic Monkey Model of Huntington’s Disease

Cho, I. K., & Chan, A. W. S. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811353-0.00045-2

A Proteomic Analysis of Mitochondrial Complex III Inhibition in SH-SY5Y Human Neuroblastoma Cell Line

Acıoğlu, Ç., Tüzüner, M. B., Serhatlı, M., Açılan, C., Şahin, B., Akgün, E., Adıgüzel, Z., Gürel, B., & Baykal, A. T. (2018) · Current Proteomics · doi:10.2174/1570164615666180713110139

The impact of proteostasis imbalance on proteome solubility

Sui, X. (2019) · Minerva Access (University of Melbourne)

Polyglutamine (PolyQ) Diseases: Molecular pathology to treatment

Fawzy, A. (2015) · Biochemistry Letters · doi:10.21608/blj.2015.63845

Adaptor protein WDFY3 is neuroprotective by counteracting age-dependent decline in proteostasis

Fun, X. H. (2020) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/139649

Faculty Opinions recommendation of Identification of a physiological E2 module for the human anaphase-promoting complex.

Wilkinson, K. D. (2011) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.13371038.14741163

Huntington’s Chorea

Lewis, P. A., & Spillane, J. E. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811069-0.00006-9

Intrinsically disordered proteins share a common molecular mechanism in membranes damages: Lipid-chaperone hypothesis

Rosa, C. L. (2020) · doi:10.1021/scimeetings.0c00244

Molecular Insights into the Role of ER Stress in Neurodegenerative Diseases

Kabir, M. T. (2022) · Springer eBooks · doi:10.1007/978-981-16-7606-2_9

Proteomics in Huntington’s Disease Biomarker Discovery

Červenka, J., Budkova, K., Suchá, R., Vodička, P., & Voukali, E. (2023) · Contemporary clinical neuroscience · doi:10.1007/978-3-031-32815-2_9

Caracterização de CNVS patogênicas em quatro indivíduos do sexo masculino com deficiência intelectual ligada ao X

Henrique, P. P. (2019) · doi:10.47749/t/unicamp.2019.1149394

Crystal structure of the RNA-recognition motif of Drosophila melanogaster tRNA (uracil-5-)-methyltransferase homolog A

Witzenberger, M., Janowski, R., & Niessing, D. (2024) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x24000645

Recent aspects in the molecular genetics of Huntington's disease

Mostafa, O. A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15702-8.00022-1

Insights into Proteostasis System in Ageing and Neurodegenerative Disorders

Mishra, Y., Kumar, R., & Netam, R. K. (2025) · Springer eBooks · doi:10.1007/978-981-96-6202-9_9

Bortezomib and Osteoclasts and Osteoblasts

Krauze, M. T., & Roodman, G. D. (2010) · Springer eBooks · doi:10.1007/978-3-7643-8948-2_3

Additional file 1 of Composition of the Intranuclear Inclusions of Fragile X-associated Tremor/Ataxia Syndrome

Ma, L., Herren, A. W., Espinal, G. M., Randol, J. L., McLaughlin, B. E., Martinez-Cerdeño, V., Pessah, I. N., Hagerman, R. J., & Hagerman, P. J. (2019) · Figshare · doi:10.6084/m9.figshare.9766562

Systems-Wide Analysis of Protein Ubiquitylation: We Finally Have the Tiger by the Tail

Fang, N. N., Albu, R. F., & Mayor, T. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1130-1_14

Utilisation des cellules souches embryonnaires humaines porteuses de la mutation causale de la maladie de Huntington en tant que nouveau modèle pathologique

Feyeux, M. (2011) · theses.fr (ABES) · doi:10.70675/d3786477zc560z42e3za489z601932156212

Role of the cholesterol hydroxylase enzyme CYP46A1 in cholesterol metabolism and neuroprotection in Huntington's disease

Kacher, R. (2019) · theses.fr (ABES) · doi:10.70675/2e6ac10bz0700z4936z81f8z18565a62aaf5

Les astrocytes réactifs, des partenaires anti-agrégants dans la maladie de Huntington : identification des mécanismes impliqués dans le dialogue neurone-astrocyte

Abjean, L. (2019) · theses.fr (ABES) · doi:10.70675/f664e003zf93fz467eza6a3z3d953eaffe4e

Décryptage des mécanismes d’ubiquitylation régulant l’histone centromérique CenH3 chez Saccharomyces cerevisiae

Boulch, M. L. (2019) · theses.fr (ABES) · doi:10.70675/801dbbc1z6df7z4b22z996bz353e41479c93

Recherche de médicaments à partir de dérivés neuronaux issus de cellules souches pluripotentes humaines porteuses de la mutation causale de la maladie de Huntington

Bigarreau, J. (2019) · theses.fr (ABES) · doi:10.70675/100830e2z15daz4b0az801ez4e0feeab3078

Functional impacts of Huntingtin lowering on the synaptic maturation and activity of neuronal networks derived from human induced pluripotent stem cells

Louçã, M. (2024) · theses.fr (ABES) · doi:10.70675/f5800d08zd8f4z4fbdz9043za4bde4fa031a

Revisiting the clastosome: a stress-induced nuclear proteolytic compartment of mammalian cells

Lafarga, M., Berciano, M. T., Rueda, N., Cardona-Cortés, S., & Tapia, O. (2026) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2026.1839944

Mouse models targeted for the tissue inhibitor of metalloproteinases-3 (TIMP3) - molecular and functional dissection of Sorsby fundus dystrophy (SFD)

Fogarasi, M. (2010) · University of Regensburg Publication Server (University of Regensburg) · doi:10.5283/epub.12390

Role of ER Stress in Dysfunction of the Nervous System

Kanekura, K., Lu, S., Lipson, K. L., & Urano, F. (2012) · Springer eBooks · doi:10.1007/978-94-007-4351-9_13

Ubiquitin–proteasome system involvement in Huntington’s disease

Ortega, Z., & Lucas, J. J. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00077 · Cited by 117

The Ubiquitin-Proteasome System in Huntington’s Disease

Valera, A., Dı́az-Hernández, M., Hernández, F., Ortega, Z., & Lucas, J. J. (2005) · The Neuroscientist · doi:10.1177/1073858405280639 · Cited by 55

The ubiquitin proteasome system in Huntington disease : impairment of the proteolytic machinery aggravates huntingtin aggregation and toxicity

de Pril, R. (2011) · Leiden Repository (Leiden University)

The Ubiquitin-Proteasome Pathway in Huntington's Disease

Mitra, S. S., & Finkbeiner, S. M. (2008) · The Scientific World JOURNAL · doi:10.1100/tsw.2008.60 · Cited by 76

The ubiquitin-proteasome system in Huntington's disease and other polyglutamine diseases

Kelly, L., & Storey, E. (2007)