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ProteomicsThe Aged Neuronal Aggregome Identified by BONCAT
Aggregating neuronal proteins. The identification of neuronal proteins contributing to aged protein aggregates was enabled by labeling the neuronal proteome with BONCAT technology, enrichment of insoluble protein aggregates, and affinity enrichment for the tagged proteins.
ORGANISM(S): Mus musculus (Mouse) 
2025-11-07 | PXD066053 | Pride
Boncat Aggregates Neurons Aggregome 
UnknownAgeing promotes microglial accumulation of slow-degrading synaptic proteins.
Not available
S-EPMC12935553 | biostudies-literature
UnknownAmyloid domains in the cell nucleus controlled by nucleoskeletal protein lamin B1 reveal a new pathway of mercury neurotoxicity.
Not available
S-EPMC4327309 | biostudies-literature
TranscriptomicsAnalysis of lacking Nα-terminal acetylation of proteins by NatA and NatB in Saccharomyces cerevisiae on mRNA levels and protein synthesis
N-terminal (Nt)-acetylation is a highly prevalent co-translational protein modification in eukaryotes, catalyzed by at least five Nt-acetyltransferases (Nat) with differing specificities. Nt-acetylation has been implicated in protein quality control but its broad biological significance remains elus...
ORGANISM(S): Saccharomyces cerevisiae 
2020-07-27 | GSE140255 | GEO
UnknownBacterial mimetics of endocrine secretory granules as immobilized in vivo depots for functional protein drugs.
Not available
S-EPMC5075894 | biostudies-literature
UnknownAnti-amyloid compounds protect from silica nanoparticle-induced neurotoxicity in the nematode C. elegans.
Not available
S-EPMC4819850 | biostudies-literature
GenomicsAnalysis of lacking Nα-terminal acetylation of proteins by NatA and NatB in Saccharomyces cerevisiae on mRNA levels and protein synthesis
Analysis of lacking Nα-terminal acetylation of proteins by NatA and NatB in Saccharomyces cerevisiae on mRNA levels and protein synthesis
PRJNA589056 | ENA
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