Results 101 to 110 of about 22,723 (239)

Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila. [PDF]

PLoS Biology, 2008
The expansion of polyglutamine tracts in a variety of proteins causes devastating, dominantly inherited neurodegenerative diseases, including six forms of spinal cerebellar ataxia (SCA).
Derek Lessing, Nancy M Bonini
doaj   +1 more source

Technologies for engineering repetitive DNA

Quantitative Biology, Volume 14, Issue 3, September 2026.
Abstract Repetitive DNA, a fundamental architectural element of genomes, is widespread across organisms and comprises about 54% of the human genome. With advances in long‐read sequencing and bioinformatics approaches, highly repetitive sequences can now be characterized in depth.
Shuting Ma, Yali Cui, Yi Wu
wiley   +1 more source

Exploring and Targeting the Connection of Iron and Copper Homeostasis to Neurodegenerative Diseases

MedComm, Volume 7, Issue 6, June 2026.
Iron and copper dyshomeostasis, along with their interactions with key intrinsically disordered proteins (e.g., Aβ, tau, α‐synuclein) have a strong implication in the onset and progression of neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), Prion diseases (PrDs), Huntington's disease (HD), Wilson's disease (WD),
Xin Liu, Lin Jia, Kerong Wu, Mo Chen, Jichao Sun, Chuanbin Yang, Chengchao Xu, Jie Sun, Jigang Wang, Lingyun Dai   +9 more
wiley   +1 more source

Autophagy is dysregulated in spinocerebellar ataxia type 2

Autophagy Reports, 2022
The accumulation of misfolded proteins and fibrillar aggregates inside neurons is a hallmark of several neurodegenerative diseases. While the exact role of these aggregates is still controversial, they are part of a cascade of molecular events that ...
Adriana Marcelo, Carlos A. Matos, Clévio Nóbrega   +2 more
doaj   +1 more source

The Unfolded Protein Response and its potential role in Huntington's disease [PDF]

, 2012
Huntington's disease (HD) is a progressive, neurodegenerative disease with fatal outcome. Although the disease-causing gene (huntingtin) has been known for some time, the exact cause of neuronal cell death is still unknown.
Kamesh Ayasolla, Matthias E. Futschik, Ravi K. R. Kalathur   +2 more
core   +2 more sources

Huntingtin as an Actin Organizer: Structural and Functional Insights

Cytoskeleton, EarlyView.
M. Capizzi, S. Humbert
wiley   +1 more source

Lipid composition controls the huntingtin exon 1 membrane‐association and differentially modulates its flanking regions' dynamics

Protein Science, Volume 35, Issue 6, June 2026.
Abstract The pathological expansion of the polyglutamine (polyQ) repeat within the first exon of huntingtin (Httex1) protein is a defining hallmark of Huntington's disease (HD). Multiple evidence supports that the membrane recruitment of Httex1 is critical for its self‐assembly and related toxicity in HD.
Tânia Sousa, Gonçalo Damas, Ana Coutinho, Nuno Bernardes, Ana Azevedo, Manuel Prieto, Ana M. Melo   +6 more
wiley   +1 more source

Discovery and Targeted Proteomic Studies Reveal Striatal Markers Validated for Huntington's Disease

Annals of Clinical and Translational Neurology, Volume 13, Issue 5, Page 911-923, May 2026.
ABSTRACT Objective Clinical trials for Huntington's disease (HD) enrolling persons before clinical motor diagnosis (CMD) lack validated biomarkers. This study aimed to conduct an unbiased discovery analysis and a targeted examination of proteomic biomarkers scrutinized by clinical validation. Methods Cerebrospinal fluid was obtained from PREDICT‐HD and
Daniel Chelsky, Cara Joyce, H. Jeremy Bockholt, Paul A. Rudnick, William H. Adams, Fiona McAllister, Justin W. Smock, Michael A. Newton, Jane S. Paulsen   +8 more
wiley   +1 more source

Polyglutamine Aggregation in Huntington and Related Diseases [PDF]

, 2012
Polyglutamine (polyQ)-expansions in different proteins cause nine neurodegenerative diseases. While polyQ aggregation is a key pathological hallmark of these diseases, how aggregation relates to pathogenesis remains contentious. In this chapter, we review what is known about the aggregation process and how cells respond and interact with the polyQ ...
Polling, S, Hill, AF, Hatters, DM
openaire   +3 more sources

IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome [PDF]

, 2009
Expansion of the polyglutamine repeat within the protein Huntingtin (Htt) causes Huntington's disease, a neurodegenerative disease associated with aging and the accumulation of mutant Htt in diseased neurons.
Aiken, Ali Khoshnan, Alice L. Lau, Ana Maria Cuervo, Anne, Apostol, Arrasate, Arrasate, Ashish Massey, Atwal, Atwal, Björkqvist, Brown, Charity T. Aiken, Chen, Chondrogianni, Cornett, Cuervo, Cuervo, Cuervo, D'Orazi, Dan, Donald C. Lo, Fang, Finkbeiner, Frank M. LaFerla, Gillian Bates, Graham, Grossman, Gu, Guerrero, Gutekunst, Hasan Khashwji, Henn, Hernandez-Hernandez, Hietakangas, Hofmann, Hu, Huang, Humbert, Hunter, J. Lawrence Marsh, Jacqueline Gire O'Rourke, Jeong, Jiang, Joan S. Steffan, Karin, Karin, Katalin Illes, Kaushik, Kazantsev, Khoshnan, Khoshnan, Kim N. Green, Komatsu, Lan Huang, Leslie Michels Thompson, Linda S. Kaltenbach, Liu, Lo, Luo, Mangiarini, Marta Martinez-Vincente, Martinez-Vicente, Massey, Massey, Michael R. Hayden, Michels, Mizushima, Montserrat Arrasate, Namita Agrawal, Orr, Paul H. Patterson, Peters-Libeu, Rockabrand, Saudou, Schilling, Scott O. Zeitlin, Shao, Southwell, Steffan, Steffan, Steffan, Steven Finkbeiner, Tagwerker, Tamas Lukacsovich, Tonoki, Verma, Walker, Warby, Warby, Warby, Wu, Xia, Ya-Zhen Zhu, Yanai, Zhang, Zuccato   +97 more
core   +3 more sources