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TranscriptomicsDepletion of p62 reduces nuclear inclusions and paradoxically ameliorates disease phenotypes in Huntington's model mice
Huntington's disease (HD) is a dominantly inherited genetic disease caused by mutant huntingtin (htt) protein with expanded polyglutamine tracts. A neuropathological hallmark of HD is the presence of neuronal inclusions of mutant htt. p62 is an important regulatory protein in selective autophagy, ...
ORGANISM(S): Mus musculus 
2014-10-10 | E-GEOD-62210 | biostudies-arrayexpress
ProteomicsThe protein interactome of the polyG inclusions
The protein interactome of polyG inclusions was investigated in HEK293T cells by isolating polyG inclusions followed by mass spectrometry. Briefly, HEK293T cells expressing polyG–EGFP were lysed, and polyG inclusions were enriched by differential centrifugation and subsequent high-salt washes. The p...
ORGANISM(S): Homo sapiens (Human) 
2026-01-20 | PXD072293 | Pride
Polyg inlcusions Niid Ms 
ProteomicsMolecular Acclimation of Halobacterium salinarum to Halite Brine Inclusions
Halophilic microorganisms have long been known to survive within the brine inclusions of salt crystals, as evidenced by their pigmentation. However, the molecular mechanisms allowing this survival has remained an open question for decades. While protocols for the surface sterilization of halite (NaC...
ORGANISM(S): Halobacterium salinarum 
2023-03-10 | PXD037167 | Pride
Halobacterium Halophile Halite 
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 
ProteomicsSILAC proteomics on MG132-induced nuclear aggregates
H1299 cells were labelled either with light (Lys0/Arg0) or heavy (Lys8/Arg10) amino acids and were either unstressed (light), stressed (heavy) with MG132 (15hrs) or stressed with MG132 and allowed to recover for 8hrs (light). Equal number of unstressed and MG132 stressed cells or MG132 stressed cell...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD054637 | Pride
Nucleolus Nuclear inclusions Silac Proteasome Mg132 
ProteomicsDistinguishing post-translational modifications in dominantly inherited FTD: FTLD-TDP Type A (GRN) versus Type B (C9orf72)
Frontotemporal dementias are neuropathologically characterized by frontotemporal lobar degeneration (FTLD). Intraneuronal inclusions of transactive response DNA-binding protein 43 kDa (TDP-43) are the defining pathologic hallmark of approximately half of the FTLD cases, being referred to as FTLD-TDP...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-04-12 | MSV000089242 | MassIVE
ProteomicsPaleoproteomics characterization of fossil arthropod parasitiformes amber inclusions
In this study, we developed and applied a paleoproteomics approach to study inclusions of fossil arthropod parasitiformes in two Burmese amber (Cretaceous, ca. 124 - 99 mya) pieces. The results supported the identification of Cornupalpatum sp. and the first report of fossil Holothyrida, Neothyridae ...
ORGANISM(S): Holothyrida 
2025-11-06 | PXD055542 | Pride
Amber  arthropod  fossil  paleontology  paleoproteomics 
TranscriptomicsDepletion of p62 reduces nuclear inclusions and paradoxically ameliorates disease phenotypes in Huntington’s model mice
Huntington’s disease (HD) is a dominantly inherited genetic disease caused by mutant huntingtin (htt) protein with expanded polyglutamine tracts. A neuropathological hallmark of HD is the presence of neuronal inclusions of mutant htt. p62 is an important regulatory protein in selective autophagy, a ...
ORGANISM(S): Mus musculus 
2014-10-10 | GSE62210 | GEO
ProteomicsGel-like inclusions of C-terminal fragments of TDP-43 sequester and inhibit proteasomes
TDP-43 inclusions enriched in C-terminal terminal fragments of ~25 kDa ("TDP-25") are associated with neurodegeneration in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Here, we analyzed gain-of-function mechanisms of TDP-25 combining cryo-electron tomography, proteomics and...
ORGANISM(S): Rattus norvegicus (Rat) 
2022-04-14 | PXD024358 | Pride
Proteomics Proteasomes Tdp-43 Als Ftd 
ProteomicsProteomic characterization of synaptosomes and sarkosyl-insoluble protein inclusions from Alzheimer's disease patients
Alzheimer’s disease is characterized by neuropathological accumulation of amyloid plaques and neurofibrillary tangles composed of amyloid-beta peptides and hyperphosphorylated tau protein, respectively. These neuropathological changes alter the function of neurons, including synaptic contacts betwee...
ORGANISM(S): Homo sapiens (Human) 
2026-07-09 | PXD070075 | Pride
Human Synaptosomes Brain Alzheimer's disease Sarkosyl-insoluble fraction 
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