ArticleeLife2017
Ratiometric sensing of BiP-client versus BiP levels by the unfolded protein response determines its signaling amplitude.
Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
58 citing papers in PubMed, 94 citations in OpenAlex.
- Immunoglobulin binding protein (BiP) forms two types of dimers.Protein science : a publication of the Protein Society · 2026Article
- Targeting endoplasmic reticulum export disrupts metabolic resilience in multiple myeloma.Signal transduction and targeted therapy · 2026Article
- Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Quantitative Proteomics and CRISPR/Cas9 Editing Reveal UPR-Mediated Control of Immunoglobulin Homeostasis in Hybridomas.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- Two-Color Timestamping of Gene Expression with a Chemigenetic Reporter System.Chembiochem : a European journal of chemical biology · 2025Article
- A multichaperone condensate enhances protein folding in the endoplasmic reticulum.Nature cell biology · 2025Article
- Mechanism of ATP hydrolysis in the Hsp70 BiP nucleotide-binding domain.Nature communications · 2025Article
- PERK-dependent reciprocal crosstalk between ER and non-centrosomal microtubules coordinates ER architecture and cell shape.Cell reports · 2025Article
- p.Phe508del-CFTR Trafficking: A Protein Quality Control Perspective Through UPR, UPS, and Autophagy.International journal of molecular sciences · 2025Review
- Article
- Lysine p-nitroanilide impairs cellular energetics and potentiates statin-induced cytotoxicity in RD rhabdomyosarcoma cells.PloS one · 2025Article
- The stability of FKBP9 maintained by BiP is crucial for glioma progression.Genes & diseases · 2024Article
- The unfolded protein response regulates ER exit sites via SNRPB-dependent RNA splicing and contributes to bone development.The EMBO journal · 2024Article
- Congress of multiple dimers is needed for cross-phosphorylation of IRE1α and its RNase activity.Life science alliance · 2024Article
- HIV-protease inhibitors potentiate the activity of carfilzomib in triple-negative breast cancer.British journal of cancer · 2024Article
- The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis.Journal of molecular biology · 2024Review
- IRE1α recognizes a structural motif in cholera toxin to activate an unfolded protein response.The Journal of cell biology · 2024Article
- AMPylation and Endoplasmic Reticulum Protein Folding Homeostasis.Cold Spring Harbor perspectives in biology · 2023Review
- Chaperone-Dependent Mechanisms as a Pharmacological Target for Neuroprotection.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
Insufficient folding capacity of the endoplasmic reticulum (ER) activates the unfolded protein response (UPR) to restore homeostasis. Yet, how the UPR achieves ER homeostatic readjustment is poorly investigated, as in most studies the ER stress that is elicited cannot be overcome. Here we show that a proteostatic insult, provoked by persistent expression of the secretory heavy chain of immunoglobulin M (µ
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What OpenQuestion holds
Registered trials
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.