Results 111 to 120 of about 9,929 (238)

Chemical Chaperones Reduce Aggregate Formation and Cell Death Caused by the Truncated Machado–Joseph Disease Gene Product with an Expanded Polyglutamine Stretch

Neurobiology of Disease, 2002
Machado–Joseph disease/spinocerebellar ataxia-3 (MJD/SCA-3) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in the MJD gene-encoded protein ataxin-3.
Hideaki Yoshida, Toshihiro Yoshizawa, Futoshi Shibasaki, Shin'ichi Shoji, Ichiro Kanazawa   +4 more
doaj   +1 more source

CHARACTERIZATION OF THE UBIQUITIN LIGASE, UBE4B, IN ENDOCYTIC TRAFFICKING [PDF]

, 2017
Endocytosis is a process by which cells internalize membrane proteins to remove them from the plasma membrane, allowing cells to regulate the cell surface expression of transmembrane proteins.
Sirisaengtaksin, Natalie, Sirisaengtaksin, Natalie   +1 more
core   +1 more source

Chronic treatment with 17-DMAG improves balance and coordination in a new mouse model of Machado-Joseph disease [PDF]

, 2014
Machado-Joseph disease (MJD) or spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disease currently with no treatment. We describe a novel mouse model of MJD which expresses mutant human ataxin-3 at near endogenous levels and manifests MJD-like
A Ferro, A Silva-Fernandes, A Sittler, A Teixeira-Castro, A Teixeira-Castro, AH Chou, AJ Williams, Anabela Silva-Fernandes, Andreia Neves-Carvalho, Andreia Teixeira-Castro, C Costa Mdo, C Palacios, Carina Soares-Cunha, CK Cemal, D Goti, DG Hay, EA Ronnen, GM Harris, H Yoshida, HJ Curtis, HJ Gundersen, HL Paulson, HR Kim, J Boy, J Labbadia, J Zou, JH Feder, JJ Cerqueira, JM Warrick, K Seidel, K Tokui, Kenneth Thirstrup, KK Chadman, M Akerfelt, M Herbst, M Hollingshead, M Katsuno, M Riedel, M Waza, Marina Amorim, MJ Egorin, MJ West, MP Zijlstra, P Coutinho, P Maciel, P Rusmini, Patrícia Maciel, Pedro Oliveira, R Morris, RJ Carter, RK Ramanathan, S Huang, S Kaushik, Sara Duarte-Silva, T Lamark, U Bichelmeier, U Rub, V Smith, W Nicklas, Y Chai   +59 more
core   +1 more source

ORMDL Proteins Turnover via Proteasome and Autophagy Is Cell‐Type Dependent and Tied to Ceramide Homeostasis

The FASEB Journal, Volume 40, Issue 6, 31 March 2026.
ORMDL proteins in the endoplasmic reticulum (ER) negatively regulate serine palmitoyltransferase (SPT) activity in response to the rate of de novo sphingolipid synthesis. Disruption of ceramide homeostasis by myriocin or fumonisin B1 (FB1) appears to destabilize the ORMDL‐SPT complex, leading to ORMDL degradation as a feedback mechanism.
Michal Mrkacek, Magda Tumova, Alex Puskasu, Pavol Utekal, Marek Vrbacky, Ladislav Kuchar, Petr Draber, Viktor Bugajev   +7 more
wiley   +1 more source

Understanding the role of the Josephin domain in the PolyUb binding and cleavage properties of ataxin-3.

PLoS ONE, 2010
Ataxin-3, the disease protein in the neurodegenerative disorder Spinocerebellar Ataxia Type 3 or Machado Joseph disease, is a cysteine protease implicated in the ubiquitin proteasome pathway.
Giuseppe Nicastro, Sokol V Todi, Ezgi Karaca, Alexandre M J J Bonvin, Henry L Paulson, Annalisa Pastore   +5 more
doaj   +1 more source

Promoter Variation and Expression Levels of Inflammatory Genes IL1A, IL1B, IL6 and TNF in Blood of Spinocerebellar Ataxia Type 3 (SCA3) Patients [PDF]

, 2016
Age at onset in spinocerebellar ataxia type 3 (SCA3/MJD) is incompletely explained by the size of the CAG tract at the ATXN3 gene, implying the existence of genetic modifiers.
Bettencourt, C, Bruges-Armas, J, Kay, T, Kazachkova, N, Lima, M, Ramos, A, Raposo, M, Vasconcelos, J   +7 more
core   +1 more source

Beclin 1 mitigates motor and neuropathological deficits in genetic mouse models of Machado-Joseph disease [PDF]

, 2017
Machado-Joseph disease or spinocerebellar ataxia type 3, the most common dominantly-inherited spinocerebellar ataxia, results from translation of the polyglutamine-expanded and aggregation prone ataxin 3 protein.
Albuquerque, David, Aveleira, Célia, Déglon, Nicole, Hirai, Hirokazu, Nascimento-Ferreira, Isabel, Nóbrega, Clévio, Onofre, Isabel, Pereira de Almeida, Luís, Vasconcelos-Ferreira, Ana   +8 more
core  

Discovery of Therapeutic Approaches for Polyglutamine Diseases: A Summary of Recent Efforts [PDF]

, 2017
Polyglutamine (PolyQ) diseases are a group of neurodegenerative disorders caused by the expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats in the coding region of specific genes.
Acquatella-Tran Van Ba, Adachi, Aiken, Al-Ramahi, Allison, Anderson, Andreassen, Andreassen, Apostol, Appleby, Arrasate, Arribat, Arribat, Auluck, Bailey, Baldo, Bauer, Bauer, Bauer, Becher, Beglinger, Beglinger, Berger, Berger, Berger, Blackwell, Blum, Bodner, Bourdenx, Boy, Brundin, Burg, Butler, Calamini, Calignon, Caplen, Carmichael, Casarosa, Castel, Cemal, Cepeda, Chai, Chatterjee, Chen, Chen, Chen, Chintawar, Chong, Chou, Colomer Gould, Como, Cortes, Costa, Costa, Coufal, Crespo-Barreto, Crowe, Cubo, Cuervo, Cummings, Cummings, Cunha-Santos, Curtis, D'Eletto, Dandage, David, David, Davies, Dedeoglu, DeMarch, Deroover, Desai, DiFiglia, Dragatsis, Duarte-Silva, Duarte-Silva, Duyao, Ebert, Ehrlich, Ehrnhoefer, Ellerby, Esteves, Everett, Evers, Evers, Feng, Feo, Fernández-Rhodes, Ferrante, Ferrante, Ferrante, Ferrante, Fraczek, Frank, Friedman, Fuentealba, Fujikake, Fujimoto, Gafni, Gammoh, Garden, Gardian, Geary, Ghiglieri, Giampà, Gispert, Goldberg, Goti, Graham, Grote, Guo, Gusella, Gutekunst, Haacke, Harper, Harrison, Haussecker, Hay, Heiser, Heiser, Hersch, Hockly, Hoffstrom, Holmberg, Holmes, HORIZON Investigators of the Huntington Study Group and European Huntington's Disease Network, Huang, Huang, Hubbert, Huntington Study Group, Huntington Study Group, Huntington Study Group, Huntington Study Group Reach2HD Investigators, Huntington Study Group TREND-HD Investigators, Huynh, Hyman, Hübener, Ibrahim, Igarashi, Ikeda, Imbert, Jia, Jimenez-Sanchez, Jimonet, Jin, Johnson, Johri, Jung, Kalmar, Kaltenbach, Katsuno, Katsuno, Katsuno, Kawaguchi, Keene, Kieburtz, Kieburtz, Kim, Kim, Klement, Kobayashi, Kodali, Koide, Kordasiewicz, Kovacs, Kremer, Kubodera, Kvam, Kwak, Kwak, Labbadia, Landwehrmeyer, Latouche, Lazzeroni, Lee, Lee, Lee, Lei, Lesort, Levine, Li, Li, Li, Lim, Lim, Lin, Lin, Liu, Lo, Lopes-Cendes, Lundin, Machida, Maciel, Maciel, Maday, Maeda, Malik, Maltecca, Margulis, Marsicano, Martin, Martorana, Matilla-Dueñas, Mealer, Meijer, Menzies, Menzies, Menzies, Mielcarek, Mihm, Miller, Miller, Minamiyama, Mishra, Miyai, Moffitt, Morimoto, Morishima, Moskowitz, Murphy, Murphy, Nagafuchi, Nagai, Nagai, Nagai, Naia, Naito, Nakamura, Nakano, Nascimento-Ferreira, Nechiporuk, Neef, Neves-Carvalho, Nollen, Nucifora, Nóbrega, Nóbrega, O'Suilleabhain, Ona, Ono, Orr, Orr, Paganetti, Palazzolo, Pandey, Parker, Paulson, Pawate, Perutz, Phillips, Piccioni, Pollitt, Popiel, Popiel, Pruss, Puri, Qadri, Raamsdonk, Ramachandran, Rand, Ratovitski, Ravikumar, Redmann, Reilmann, Reinhart, Ren, Ren, Rimoldi, Rocher, Rodriguez-Lebron, Rodríguez-Lebrón, Rolfs, Romano, Roos, Rosas, Rose, Ross, Rubinsztein, Rubinsztein, Rujano, Régulier, Saccà, Sanchez Mejia, Sancho, Sanpei, Sarkar, Sarkar, Sarkar, Sarkar, Sarkar, Saute, Schiefer, Schiefer, Schilling, Schmidt, Schulte, Schulte, Schöls, Selvi, Shao, Shao, Shibata, Shim, Shoulson, Silva-Fernandes, Simoes, Simões, Siska, Sittler, Smith, Smith, Smith, Snyder-Keller, Spada, Spada, Stack, Stack, Stack, Stanek, Stefani, Strand, Subramaniam, Subramaniam, Swami, Takahashi, Takano, Tanaka, Tanaka, Teixeira-Castro, Teixeira-Castro, Telenius, The Huntington's Disease Collaborative Research Group, Thomas, Thoreen, Thornberry, Tokui, Travers, Tsai, Tsai, Varma, Varma, Verbessem, Verhaar, Verhagen Metman, Violante, Voisine, Vugt, Waldron-Roby, Walter, Wang, Wang, Wang, Wang, Wang, Warrick, Watase, Waza, Weber, Wellington, Weydt, Williams, Wong, Wood, Wood, Wu, Xia, Xiong, Yamamoto, Yang, Yang, Yang, Yi, Ying, Yu, Yvert, Zesiewicz, Zhang, Zhang, Zhao, Zhuchenko, Zijlstra, Zoghbi, Zu, Zuccato, Zuccato, Zádori   +385 more
core   +1 more source

Conditional deletion of the multiple sclerosis susceptibility gene ATXN1 identifies cell‐autonomous effects in the B‐cell compartment

The FEBS Journal, Volume 293, Issue 5, Page 1459-1477, March 2026.
Ataxin‐1 is a polyglutamine protein associated with the etiology of spinocerebellar ataxia type 1 (SCA1) that has been recently found implicated in the risk of developing the autoimmune disorder multiple sclerosis (MS). Here, we took a conditional knockout approach to ablate ataxin‐1 exclusively in the B‐cell compartment and we found that this protein ...
Jonathan Jacob Carver, Rachael Riley Denbrock, Cindy Carolina Martines, Alessandro Didonna   +3 more
wiley   +1 more source

Ataxin-3 phosphorylation protects neurons [PDF]

J Cell Biol, 2016
![Figure][1] Expanded ataxin-3 causes an extensive loss of neurons (brown) in rat brains (left). But the amount of neurodegeneration is reduced when serine 12 is mutated to aspartate (right).
europepmc   +3 more sources