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ProteomicsSurveyance of apparent proteome unfolding curves via thiol labelling
Census of apparent proteome unfolding curves following urea denaturation in cell lysate using thiol reactivity probe tetraphenylethene maleimide (TPE-MI).
ORGANISM(S): Mus musculus (Mouse) 
2022-05-19 | PXD022640 | Pride
Denaturation curve Tetraphenylethene maleimide (tpe-mi) Cm Protein folding 
ProteomicsASAP-ID: Proximity labelling with small tags
Biotinylation-based proximity labelling methods are valuable for discovering protein-protein interactions within cellular systems. However, one limitation of these approaches is that most require fusing the target protein with the enzyme that biotinylates nearby proteins (i.e., TurboID or APEX2), wh...
ORGANISM(S): Homo sapiens (Human) 
2026-09-07 | PXD066625 | Pride
Human Lc-ms/ms 
ProteomicsSurveyance of chaperone-client interactions via thiol labelling
Census of apparent chaperone-client interaction using thiol reactivity probe tetraphenylethene maleimide (TPE-MI).
ORGANISM(S): Homo sapiens (Human) Sus scrofa domesticus (domestic pig) 
2022-05-19 | PXD022587 | Pride
Molecular chaperone Tetraphenylethene maleimide (tpe-mi) Denaturation Protein folding 
ProteomicsSurveyance of apparent proteome unfolding curves via thiol labelling under HSP70 inhibition
Census of apparent proteome unfolding curves following urea denaturation in cell lysate derived from control of VER155008-treated N2a cells using thiol reactivity probe tetraphenylethene maleimide (TPE-MI).
ORGANISM(S): Mus musculus (Mouse) 
2022-05-20 | PXD030567 | Pride
Denaturation Protein folding 
ProteomicsArginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that transmits multiple modes of toxicity
Motor Neuron Disease patients with the C9ORF72 hexanucleotide expansion mutations feature abnormal expression of 5 different dipeptide repeat polymers (DPRs). Two of these, poly-GR and poly-PR, have proven highly toxic to cell and animal models. To investigate the mechanisms, we defined the interact...
ORGANISM(S): Mus musculus (Mouse) 
2020-02-25 | PXD015177 | Pride
Ran-translation  amyotrophic lateral sclerosis (als)  proteotoxicity  protein aggregation  abce1  methylosome  prmt1  prmt5 
ProteomicsArginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that transmits multiple modes of toxicity
C9ORF72-associated Motor Neuron Disease patients feature abnormal expression of 5 dipeptide repeat (DPR) polymers. Here we used quantitative proteomics in a mouse neuronal-like cell line (Neuro2a) to demonstrate that the valency of Arg in the most toxic DPRS, PR and GR, drives promiscuous binding to...
ORGANISM(S): Mus musculus (Mouse) 
2020-02-25 | PXD015180 | Pride
Ran-translation  amyotrophic lateral sclerosis (als)  proteotoxicity  protein aggregation  abce1  methylosome  prmt1  prmt5 
ProteomicsInclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation
Poly(glycine-alanine) (polyGA) is one of the dipolypeptides expressed in Motor Neuron Disease caused by C9ORF72 mutations and accumulates as inclusion bodies in the brain of patients. Superficially these inclusions are similar to those formed by polyglutamine (polyQ) in Huntington’s disease and bot...
ORGANISM(S): Mus musculus (Mouse) 
2020-08-18 | PXD018505 | Pride
Huntington C9orf72 Chaperones Proteosome Inclusions 
ProteomicsInclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation
Poly(glycine-alanine) (polyGA) is one of the dipolypeptides expressed in Motor Neuron Disease caused by C9ORF72 mutations and accumulates as inclusion bodies in the brain of patients. Superficially these inclusions are similar to those formed by polyglutamine (polyQ) in Huntington’s disease and both...
ORGANISM(S): Mus musculus (Mouse) 
2020-08-18 | PXD018824 | Pride
Huntington Aggregates C9prf72 Polyga 
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 
ProteomicsA thiol probe for measuring unfolded protein load and proteostasis in cells
When proteostasis becomes unbalanced, unfolded proteins accumulate and can aggregate. However, probes quantifying proteostasis imbalance are lacking. We report a dye, tetraphenylethene maleimide (TPE-MI) that can measure unfolded protein load.TPE-MI fluorescence is enhanced upon reaction with cellul...
ORGANISM(S): Mus musculus (Mouse) 
2018-10-24 | PXD006527 | Pride
Neuro2a Mouse Tpe-mi Silac Lc/msms Orbitrap fusion lumos 
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