ArticleNature chemical biology2014
Targeted protein destabilization reveals an estrogen-mediated ER stress response.
Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 85 citations in OpenAlex.
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- Pooled tagging and hydrophobic targeting of endogenous proteins for unbiased mapping of unfolded protein responses.Molecular cell · 2025Article
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- Female sex hormones exacerbate retinal neurodegeneration.Science advances · 2025Article
- Utilizing small molecules to probe and harness the proteome by pooled protein tagging with ligandable domains.Frontiers in pharmacology · 2025Review
- miRNA-378 Is Downregulated by XBP1 and Inhibits Growth and Migration of Luminal Breast Cancer Cells.International journal of molecular sciences · 2023Article
- Downregulation of EphA2 stability by RNF5 limits its tumor-suppressive function in HER2-negative breast cancers.Cell death & disease · 2023Article
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- RRM2 and CDC6 are novel effectors of XBP1-mediated endocrine resistance and predictive markers of tamoxifen sensitivity.BMC cancer · 2023Article
- CDNF Interacts with ER Chaperones and Requires UPR Sensors to Promote Neuronal Survival.International journal of molecular sciences · 2022Article
- ER-phagy: mechanisms, regulation, and diseases connected to the lysosomal clearance of the endoplasmic reticulum.Physiological reviews · 2022Review
- Recent biomedical advances enabled by HaloTag technology.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2022Article
- Synthesis and evaluation of bifunctional PTP4A3 phosphatase inhibitors activating the ER stress pathway.Bioorganic & medicinal chemistry letters · 2021Article
- Hypoxia-induced SETX links replication stress with the unfolded protein response.Nature communications · 2021Article
- Vaginal Aging-What We Know and What We Do Not Know.International journal of environmental research and public health · 2021Review
- Mechanisms of Hypercapnia-Induced Endoplasmic Reticulum Dysfunction.Frontiers in physiology · 2021Review
- Prey for the Proteasome: Targeted Protein Degradation-A Medicinal Chemist's Perspective.Angewandte Chemie (International ed. in English) · 2020Review
- Targeted protein degradation as a powerful research tool in basic biology and drug target discovery.Nature structural & molecular biology · 2020Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Accumulation of unfolded proteins within the endoplasmic reticulum (ER) of eukaryotic cells leads to an unfolded protein response (UPR) that either restores homeostasis or commits the cells to apoptosis. Tools traditionally used to study the UPR are proapoptotic and thus confound analysis of long-term cellular responses to ER stress. Here, we describe an ER-localized HaloTag (ERHT) protein that can be conditionally destabilized using a small-molecule hydrophobic tag (HyT36). Treatment of ERHT-expressing cells with HyT36 induces acute, resolvable ER stress that results in transient UPR activation without induction of apoptosis. Transcriptome analysis of late-stage responses to this UPR stimulus reveals a link between UPR activity and estrogen signaling.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.