Results 21 to 30 of about 20,303 (218)

Polyglutamine Disease: Acetyltransferases Awry [PDF]

Current Biology, 2002
Recent evidence indicates that inhibition of histone acetyltransferases may be a primary cause of cellular pathogenesis in polyglutamine diseases such as Huntington disease; the results raise the possibility that pharmacologic manipulation of protein acetylation levels could be of therapeutic benefit.
Hughes, Robert E., Robert E. Hughes
openaire   +4 more sources

Huntingtin Aggregate-Responsive Autophagy Gene Circuit Mitigates Disease Pathology in R6/2 Mice. [PDF]

Adv Sci (Weinh)
CD98‐mediated receptor‐mediated transcytosis enables LIP‐CD98 nanocarriers to cross the blood–brain barrier and deliver ARAA to neurons. mHTT aggregates activate the 11G–NarX sensor, initiating Auto‐P and Trans‐P signaling through the VP48–NarL relay.
Zhu J, Xie XX, Li L, Tian C, Wang HT, Wang XJ, Yu XL, Zhang GF, Liu RT.   +8 more
europepmc   +2 more sources

Polyglutamine-Specific Gold Nanoparticle Complex Alleviates Mutant Huntingtin-Induced Toxicity

, 2021
Huntington’s disease (HD) belongs to protein misfolding disorders associated with polyglutamine (polyQ)-rich mutant huntingtin (mHtt) protein inclusions. Currently, it is indicated that the aggregation of polyQ-rich mHtt participates in neuronal toxicity
Chun-Hong Kuo (1448776), Chia-Kang Tsao, Devi Wahyuningtyas, Joseph Jen-Tse Huang (416649), Wen-Hao Chen, Joseph Jen-Tse Huang, Y. Henry Sun (11846623), Pei-Kuen Wei, Ka Chon Ng, Yu-Jung He (11846614), Ruei-Yu He, Wen-Hao Chen (670976), Chu-Yi Yu, Ruei-Yu He (263959), Y. Henry Sun, Po-Chao Lu (11846617), Sheng-Hann Wang, Jiun-Jie Shie (1777837), Bryan Po-Wen Chen, Yung-An Huang (444988), Yu-Jung He, Chun-Hong Kuo, Yu-Cai Chen, Jiun-Jie Shie, Chu-Yi Yu (1357497), Yung-An Huang, Pei-Kuen Wei (525985), Chia-Kang Tsao (3185499), Devi Wahyuningtyas (11846611), Ka Chon Ng (1747456), Bryan Po-Wen Chen (608349), Yu-Cai Chen (8114170), Po-Chao Lu, Sheng-Hann Wang (11846620)   +33 more
core   +1 more source

Live axonal transport disruption by mutant huntingtin fragments in Drosophila motor neuron axons [PDF]

, 2009
Huntington's Disease is a neurodegenerative condition caused by a polyglutamine expansion in thehuntingtin (Htt) protein, which aggregates and also causes neuronal dysfunction. Pathogenic N-terminal httfragments perturb axonal transport in vitro.
Burbidge-King, T., Thompson, LM, Sinadinos, Christopher, Sinadinos, C, Marsh, J.L, Soh, D, Wyttenbach, Andreas, Mudher, Amritpal, Wyttenbach, A, Marsh, JL, Soh, D., Burbidge-King, T, Mudher, AK, Thompson, L.M.   +13 more
core   +1 more source

Polyglutamine pathogenesis

Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 1999
An increasing number of neurodegenerative disorders have been found to be caused by expanding CAG triplet repeats that code for polyglutamine. Huntington's disease (HD) is the most common of these disorders and dentato-rubral-pallidoluysian atrophy (DRPLA) is very similar to HD, but is caused by mutation in a different gene, making them good models to ...
C A, Ross, J D, Wood, G, Schilling, M F, Peters, F C, Nucifora, J K, Cooper, A H, Sharp, R L, Margolis, D R, Borchelt   +8 more
openaire   +3 more sources

Correlation of inter-locus polyglutamine toxicity with CAG•CTG triplet repeat expandability and flanking genomic DNA GC content [PDF]

, 2011
Dynamic expansions of toxic polyglutamine (polyQ)-encoding CAG repeats in ubiquitously expressed, but otherwise unrelated, genes cause a number of late-onset progressive neurodegenerative disorders, including Huntington disease and the spinocerebellar ...
Darren G. Monckton, Monckton, Darren G,, Monckton, D.G., Colm E. Nestor, Nestor, C.E., Nestor, Colm,, Darren G Monckton, Colm E Nestor   +7 more
core   +2 more sources

Oxidative Stress and Neurodegeneration: Interconnected Processes in PolyQ Diseases

Antioxidants, 2021
Neurodegenerative polyglutamine (polyQ) disorders are caused by trinucleotide repeat expansions within the coding region of disease-causing genes. PolyQ-expanded proteins undergo conformational changes leading to the formation of protein inclusions which
Ioannis Gkekas, Anna Gioran, Marina Kleopatra Boziki, Nikolaos Grigoriadis, Niki Chondrogianni, Spyros Petrakis   +5 more
doaj   +1 more source

Na+/H+ exchangers induce autophagy in neurons and inhibit polyglutamine-induced aggregate formation.

PLoS ONE, 2013
In polyglutamine diseases, an abnormally elongated polyglutamine results in protein misfolding and accumulation of intracellular aggregates. Autophagy is a major cellular degradative pathway responsible for eliminating unnecessary proteins, including ...
Kazuya Togashi, Shuji Wakatsuki, Akiko Furuno, Shinji Tokunaga, Yoshitaka Nagai, Toshiyuki Araki   +5 more
doaj   +1 more source

J Proteins Counteract Amyloid Propagation and Toxicity in Yeast

Biology, 2022
The accumulation of misfolded proteins as amyloids is associated with pathology in dozens of debilitating human disorders, including diabetes, Alzheimer’s, Parkinson’s, and Huntington’s diseases.
Daniel C. Masison, Michael Reidy, Jyotsna Kumar   +2 more
doaj   +1 more source

Solution structure of polyglutamine tracts in GST‐polyglutamine fusion proteins

FEBS Letters, 2002
Aggregation of expanded polyglutamine (polyQ) seems to be the cause of various genetic neurodegenerative diseases. Relatively little is known as yet about the polyQ structure and the mechanism that induces aggregation. We have characterised the solution structure of polyQ in a proteic context using a model system based on glutathione S‐transferase ...
Masino L, Kelly G, Leonard K, Trottier Y, Pastore A, RI Ebbinghaus Simon/F-2599-2012   +5 more
openaire   +4 more sources