Results 31 to 40 of about 22,598 (233)

ER stress-induced eIF2-alpha phosphorylation underlies sensitivity of striatal neurons to pathogenic huntingtin.

PLoS ONE, 2014
A hallmark of Huntington's disease is the pronounced sensitivity of striatal neurons to polyglutamine-expanded huntingtin expression. Here we show that cultured striatal cells and murine brain striatum have remarkably low levels of phosphorylation of ...
Julia Leitman, Boaz Barak, Ron Benyair, Marina Shenkman, Uri Ashery, F Ulrich Hartl, Gerardo Z Lederkremer   +6 more
doaj   +1 more source

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

Molecules, 2010
Huntington´s disease, one of the so-called poly-glutamine diseases, is a dominantly inherited movement disorder characterized by formation of cytosolic and nuclear inclusion bodies and progressive neurodegeneration.
Mathias Bähr, Pawel Kermer, Sebastian Deeg, Christoph P. Dohm, Kamila Sroka, Jan Liman   +5 more
doaj   +1 more source

Forms and Phases in Huntingtin Protein Aggregation [PDF]

Molecular Cell, 2018
Using a combination of fluorescence microscopy and electron tomography, Peskett et al. (2018), in this issue of Molecular Cell, explore the nucleation of amyloid-like filaments from liquid-like condensates of huntingtin protein exon1 with disease-related polyQ extensions.
openaire   +2 more sources

Huntingtin interacts with a family of WW domain proteins [PDF]

Human Molecular Genetics, 1998
The hallmark neuropathology of Huntington's disease (HD) is due to elongation of a polyglutamine segment in huntingtin, a novel approximately 350 kDa protein of unknown function. We used a yeast two-hybrid interactor screen to identify proteins whose association with huntingtin might be altered in the pathogenic process.
P W, Faber, G T, Barnes, J, Srinidhi, J, Chen, J F, Gusella, M E, MacDonald   +5 more
openaire   +2 more sources

Huntingtin Subcellular Localisation Is Regulated by Kinase Signalling Activity in the StHdhQ111 Model of HD.

PLoS ONE, 2015
Huntington's disease is a neurodegenerative disorder characterised primarily by motor abnormalities, and is caused by an expanded polyglutamine repeat in the huntingtin protein.
Kathryn R Bowles, Simon P Brooks, Stephen B Dunnett, Lesley Jones   +3 more
doaj   +1 more source

The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-kB/Rel/dorsal family transcription factor

BMC Neuroscience, 2002
Background Huntington's disease (HD) pathogenesis is due to an expanded polyglutamine tract in huntingtin, but the specificity of neuronal loss compared with other polyglutamine disorders also implies a role for the protein's unknown inherent function ...
Gusella James F, Takano Hiroki
doaj   +1 more source

The interaction between RE1-silencing transcription factor (REST) and heat shock protein 90 as new therapeutic target against Huntington's disease.

PLoS ONE, 2019
The wild type huntingtin protein (Htt), supports the production of brain-derived neurotrophic factor (BDNF), a survival factor for striatal neurons, through cytoplasmic sequestering of RE-1silencing transcription factor (REST). In Huntington´s Disease an
Raúl Orozco-Díaz, Angélica Sánchez-Álvarez, José Manuel Hernández-Hernández, José Tapia-Ramírez   +3 more
doaj   +1 more source

Inhibition of mitochondrial protein import by mutant huntingtin [PDF]

Nature Neuroscience, 2014
Mitochondrial dysfunction is associated with neuronal loss in Huntington's disease (HD), a neurodegenerative disease caused by an abnormal polyglutamine expansion in huntingtin (Htt). However, the mechanisms linking mutant Htt and mitochondrial dysfunction in HD remain unknown.
Hiroko, Yano, Sergei V, Baranov, Oxana V, Baranova, Jinho, Kim, Yanchun, Pan, Svitlana, Yablonska, Diane L, Carlisle, Robert J, Ferrante, Albert H, Kim, Robert M, Friedlander   +9 more
openaire   +2 more sources

Alterations in mRNA 3′ UTR Isoform Abundance Accompany Gene Expression Changes in Human Huntington’s Disease Brains

Cell Reports, 2017
The huntingtin gene has two mRNA isoforms that differ in their 3′ UTR length. The relationship of these isoforms with Huntington’s disease is not established.
Lindsay Romo, Ami Ashar-Patel, Edith Pfister, Neil Aronin   +3 more
doaj   +1 more source

Robust Cell-Free Expression of Sub-Pathological and Pathological Huntingtin Exon-1 for NMR Studies. General Approaches for the Isotopic Labeling of Low-Complexity Proteins

Biomolecules, 2020
The high-resolution structural study of huntingtin exon-1 (HttEx1) has long been hampered by its intrinsic properties. In addition to being prone to aggregate, HttEx1 contains low-complexity regions (LCRs) and is intrinsically disordered, ruling out ...
Anna Morató, Carlos A. Elena-Real, Matija Popovic, Aurélie Fournet, Karen Zhang, Frédéric Allemand, Nathalie Sibille, Annika Urbanek, Pau Bernadó   +8 more
doaj   +1 more source