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Cytoplasmic redox imbalance in the thioredoxin system activates Hsf1 and results in hyperaccumulation of the sequestrase Hsp42 with misfolded proteins

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.06.26.546610Source: DataRank Database

Cytoplasmic redox imbalance in the thioredoxin system activates Hsf1 and results in hyperaccumulation of the sequestrase Hsp42 with misfolded proteins is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2023). On theSindex it has a DataRank of 0. It has been cited 2 times.

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Open Access2 citations

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Enrichment:Funding (4 grants)OA: greenTopics (28)IDs (PubMed, OpenAlex)SDGs (1)

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Authors (3)

Sara Peffer ORCID,Kevin A. Morano ORCID,Davi Gonçalves ORCID

Live enrichment

PubMed:37425817 OpenAlex:https://openalex.org/W4382284181

National Institutes of Health

Grant: 5R01GM127287-04

Mechanisms of cytosolic proteostasis in yeast

National Institutes of Health

Grant: 5R35GM149196-02

Chaperone-mediated mechanisms of cellular proteostasis

NIGMS NIH HHS

Grant: R01 GM127287

NIGMS NIH HHS

Grant: R35 GM149196

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2023/06/26/2023.06.26.546610.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2023.06.26.546610

repositoryhttps://doi.org/10.1101/2023.06.26.546610

repositoryhttps://pubmed.ncbi.nlm.nih.gov/37425817

Fields of Study

Heat shock proteins researchEndoplasmic Reticulum Stress and DiseaseRedox biology and oxidative stress0301 basic medicine03 medical and health sciences

Keywords

ThioredoxinThioredoxin reductaseCytosolCell biologyProtein foldingCytoplasmHeat shock proteinProteostasisOxidative phosphorylationChaperoninBiochemistryBiologyOxidative stressChemistryEnzymeGeneArticleaggregaseheat shockredoxsHSPsequestraseyeast

Sustainable Development Goals

SDG 0: Life in Land