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UnknownDistinct TORC1 signalling branches regulate Adc17 proteasome assembly chaperone expression.
Not available
S-EPMC11298713 | biostudies-literature
UnknownProteasome assembly chaperone translation upon stress requires Ede1 phase separation at the plasma membrane.
Not available
S-EPMC10792233 | biostudies-literature
ProteomicsIdentification of proteins interacting with translating RPAC reporter mRNAs (FGH17)
To discover new regulators of Regulatory Particle Assembly Chaperone (RPAC) translation, we identified RNA-binding proteins (RBPs) with increased recruitment to translating WT FGH17 mRNAs compared to non-translatable FGH17-40ntΔ mRNAs in vivo. To this end, we first treated yeast cells with rapamycin...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-05-04 | PXD027655 | Pride
Proteasome assembly chaperone translation 
ProteomicsProteomic analysis demonstrated transcription factor gene YRR1 deletion in Saccharomyces cerevisiae enhances its resistance to vanillin through the upregulation of transcriptional activator Haa1, coactivator Mbf1, and proteasome assembly chaperone Tma17 expression
Vanillin is one of the major phenolic inhibitors of Saccharomyces cerevisiae in lignocellulosic hydrolysates. Deleting transcription factor gene YRR1 improves vanillin resistance by promoting some translation-related processes that were confirmed at the transcription level in our previous studies. I...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-09-09 | PXD017738 | Pride
Yrr1  quantitative proteomics  vanillin resistance  bioethanol  saccharomyces cerevisiae 
ProteomicsProteomic analysis demonstrated transcription factor gene YRR1 deletion in Saccharomyces cerevisiae enhances its resistance to vanillin through the upregulation of transcriptional activator Haa1, coactivator Mbf1, and proteasome assembly chaperone Tma17 expression
Vanillin is one of the major phenolic inhibitors of Saccharomyces cerevisiae in lignocellulosic hydrolysates. Deleting transcription factor gene YRR1 improves vanillin resistance by promoting some translation-related processes that were confirmed at the transcription level in our previous studies. I...
ORGANISM(S): Saccharomyces cf. cerevisiae 
2021-09-09 | PXD020951 | Pride
Yrr1  quantitative proteomics  vanillin resistance  bioethanol  saccharomyces cerevisiae 
UnknownProteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.
Not available
S-EPMC8128388 | biostudies-literature
TranscriptomicsExpression data from Saccharomyces cerevisiae WT, WT(hsf1), hac1delta and hac1delta(hsf1)
In the yeast Saccharomyces cerevisiae, accumulation of misfolded proteins in the endoplasmic reticulum (ER) causes ER stress and activates the unfolded protein response (UPR) mediated by Hac1p, whereas the heat shock response (HSR) mediated by Hsf1p mainly regulates cytosolic processes and protects ...
ORGANISM(S): Saccharomyces cerevisiae 
2014-07-01 | E-GEOD-39311 | biostudies-arrayexpress
TranscriptomicsGlobal regulation of mRNA translation and stability in the early Drosophila embryo by the Smaug RNA-binding protein- Polysome gradient/microarray study
To gain a panoramic view of Smaug function in the early embryo we identified mRNAs that are bound to Smaug using RNA co-immunoprecipitation followed by hybridization to DNA microarrays. We also identified the mRNAs that are translationally repressed by Smaug using polysome gradients and microarrays....
ORGANISM(S): Drosophila melanogaster 
2013-12-03 | E-GEOD-50026 | biostudies-arrayexpress
UnknownDiscovery of novel interacting partners of PSMD9, a proteasomal chaperone: Role of an Atypical and versatile PDZ-domain motif interaction and identification of putative functional modules.
Not available
S-EPMC4087146 | biostudies-literature
UnknownMolecular Mechanism of Adenovirus Late Protein L4-100K Chaperones the Trimerization of Hexon.
Not available
S-EPMC9888260 | biostudies-literature
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