Sort   by:  
 Page size 
ProteomicsProteome content of insoluble fraction of Httex1 transduced neurons
Investigate the protein content of the insoluble fraction of primary neurons transdusced with Httex1 (+/-GFP).The ultimate goal is to assess the protein contents of Httex1 transduced neurons depending on the polyQ length and the presence of a GFP tag.
ORGANISM(S): Mus musculus (Mouse) 
2021-10-08 | PXD028323 | Pride
Neurons Huntington disease Inclusions Httex1 
ProteomicsProteome content of insoluble fraction of Httex1 transfected cells
Investigate the protein content of the insoluble fraction of HEK cells transfected with Httex1 (+/-GFP).The ultimate goal is to assess the protein contents of Httex1 transfected cells depending on the polyQ length and the presence of a GFP tag.
ORGANISM(S): Homo sapiens (Human) 
2021-10-08 | PXD021742 | Pride
Httex1 inclusions hek cells urea fraction 
UnknownAmplification of neurotoxic HTTex1 assemblies in human neurons.
Not available
S-EPMC8943833 | biostudies-literature
ProteomicsTadpole-like conformations of polyglutamine-expanded soluble huntingtin exon 1 engenders novel interactions
Soluble huntingtin exon 1 (Httex1) with expanded polyglutamine (polyQ) engenders neurotoxicity in Huntington’s disease. To understand the structural basis of this toxicity, we characterized the structure of monomeric Httex1 for two polyQ lengths using hydrogen-deuterium exchange and nuclear magnetic...
ORGANISM(S): Mus musculus (Mouse) 
2019-11-08 | PXD006792 | Pride
Huntingtin Huntington's disease Polyq Neurodegeneration 
ProteomicsA Multiple Hit Model for the Diverse Pathogenic Effects Specific to Huntingtin Aggregate Stage in Cells
Huntington's disease is a fatal neurodegenerative disorder characterized by the aggregation of polyglutamine-expanded huntingtin into oligomers and fibrils. How protein aggregation leads to cellular dysfunction is not well understood. To address this question, we combined in-cell single molecule flu...
ORGANISM(S): Mus musculus (Mouse) 
2017-01-31 | PXD003446 | Pride
Interactions Huntington's disease Proteomics 
ProteomicsHuntingtin inclusions trigger cellular quiescence, deactivate apoptosis and lead to delayed necrosis
Two popular models for how mutant Huntingtin exon 1 (Httex1) aggregation into inclusions relates to pathogenesis involve seemingly contradictory mechanisms. In one model, inclusions are adaptive by sequestering the proteotoxicity of soluble Httex1. In the other, inclusions compromise cellular activi...
ORGANISM(S): Homo sapiens (Human) 
2017-05-04 | PXD005120 | Pride
Huntington's disease Huntingtin Mechanism of death Inclusion Apoptosis Aggregation 
UnknownFormation and Structure of Wild Type Huntingtin Exon-1 Fibrils.
Not available
S-EPMC5575822 | biostudies-literature
UnknownProtofibril Binding Peptides Recognize and Inhibit Huntingtin Amyloid Formation <i>in vitro</i> and <i>in vivo</i>.
Not available
S-EPMC12633338 | biostudies-literature
UnknownTDP43 and huntingtin Exon-1 undergo a conformationally specific interaction that strongly alters the fibril formation of both proteins.
Not available
S-EPMC11408864 | biostudies-literature
UnknownProbing the Interaction of Huntingtin Exon-1 Polypeptides with the Chaperonin Nanomachine GroEL.
Not available
S-EPMC8284913 | biostudies-literature
Sort   by:  
 Page size