ArticlePloS one2012
A peptidic unconjugated GRP78/BiP ligand modulates the unfolded protein response and induces prostate cancer cell death.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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.
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
- GRP78 dysregulation: A proposed molecular mechanism linking the tumor microenvironment to sepsis susceptibility in patients with cancer (Review).International journal of molecular medicine · 2026Review
- GRP78 in human diseases: From molecular chaperone to therapeutic target.Theranostics · 2026Review
- A BAG-1-inhibitory peptide, GO-Pep, suppresses c-Raf activity in cancer.Communications biology · 2025Article
- Pyroptosis in urinary malignancies: a literature review.Discover oncology · 2023Review
- Relationship between pyroptosis-mediated inflammation and the pathogenesis of prostate disease.Frontiers in medicine · 2023Review
- The endoplasmic reticulum stress response in prostate cancer.Nature reviews. Urology · 2022Review
- GRP78 in lung cancer.Journal of translational medicine · 2021Review
- Interactome analysis of Bag-1 isoforms reveals novel interaction partners in endoplasmic reticulum-associated degradation.PloS one · 2021Article
- Endoplasmic Reticulum Stress Pathway, the Unfolded Protein Response, Modulates Immune Function in the Tumor Microenvironment to Impact Tumor Progression and Therapeutic Response.International journal of molecular sciences · 2019Review
- Effect of binding immunoglobulin protein on induction of regulatory B cells with killer phenotype during inflammation and disease.Future science OA · 2019Review
- Unfolded Protein Response as a Therapeutic Target in Cardiovascular Disease.Current topics in medicinal chemistry · 2019Review
- Development of Bag-1L as a therapeutic target in androgen receptor-dependent prostate cancer.eLife · 2017Article
- Tumor-Specific Binding of Radiolabeled PEGylated GIRLRG Peptide: A Novel Agent for Targeting Cancers.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2016Article
- Prostate cancer and the unfolded protein response.Oncotarget · 2016Review
- GRP78 and α2-macroglobulin are new promising targets for metastatic castrate-resistant prostate cancer treatment.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2015Article
- Cell type-specific transcriptomics of hypothalamic energy-sensing neuron responses to weight-loss.eLife · 2015Article
- Glucose-regulated protein 78 and heparanase expression in oral squamous cell carcinoma: correlations and prognostic significance.World journal of surgical oncology · 2014Article
- Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential.Nature reviews. Cancer · 2014Review
- Coregulator control of androgen receptor action by a novel nuclear receptor-binding motif.The Journal of biological chemistry · 2014Article
- Endoplasmic reticulum chaperones and oxidoreductases: critical regulators of tumor cell survival and immunorecognition.Frontiers in oncology · 2014Review
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
The molecular chaperone GRP78/BiP is a key regulator of protein folding in the endoplasmic reticulum, and it plays a pivotal role in cancer cell survival and chemoresistance. Inhibition of its function has therefore been an important strategy for inhibiting tumor cell growth in cancer therapy. Previous efforts to achieve this goal have used peptides that bind to GRP78/BiP conjugated to pro-drugs or cell-death-inducing sequences. Here, we describe a peptide that induces prostate tumor cell death without the need of any conjugating sequences. This peptide is a sequence derived from the cochaperone Bag-1. We have shown that this sequence interacts with and inhibits the refolding activity of GRP78/BiP. Furthermore, we have demonstrated that it modulates the unfolded protein response in ER stress resulting in PARP and caspase-4 cleavage. Prostate cancer cells stably expressing this peptide showed reduced growth and increased apoptosis in in vivo xenograft tumor models. Amino acid substitutions that destroyed binding of the Bag-1 peptide to GRP78/BiP or downregulation of the expression of GRP78 compromised the inhibitory effect of this peptide. This sequence therefore represents a candidate lead peptide for anti-tumor therapy.
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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.