ReviewCancer science2007
Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis.
Review in Cancer science, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 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
137 citing papers in PubMed, 239 citations in OpenAlex.
- The Amyloid State of Mutant p53 in Cancer.JMA journal · 2026Review
- Article
- Development of a chaperone-mediated protein degrader targeting ERK5 that efficaciously reduces tumor growth.Cell communication and signaling : CCS · 2026Article
- Hsa_circ_0000520 Promotes Invasion and Metastasis of Breast Cancer Cells by Targeting HSP90AA1.Breast cancer (Dove Medical Press) · 2026Article
- Mendelian Randomization in Conjunction with WGCNA Was Employed to Investigate the Potential Role of the Liver-Brain Axis in the Pathogenesis of Hepatocellular Carcinoma and Alzheimer's Disease.Molecular neurobiology · 2025Article
- The Hsp90β Isoform: An Attractive Target for Drug Development.Medicinal research reviews · 2025Review
- Design, Synthesis, and Biological Evaluation of Chiral-Proline Derivatives as Novel HSP90 Inhibitors.ACS medicinal chemistry letters · 2025Article
- Synthesis, Anticancer Screening, and In Silico Evaluations of Thieno[2,3-Pharmaceuticals (Basel, Switzerland) · 2025Article
- The Interplay between Heat Shock Proteins and Cancer Pathogenesis: A Novel Strategy for Cancer Therapeutics.Cancers · 2024Review
- Hsp90 is a potential risk factor for ovarian cancer prognosis: an evidence of a Chinese clinical center.BMC cancer · 2023Article
- The Role of Extracellular Heat Shock Proteins in Cardiovascular Diseases.Biomedicines · 2023Review
- Extracellular vesicle-microRNAs mediated response of bovine ovaries to seasonal environmental changes.Journal of ovarian research · 2023Article
- Review
- Expression Levels of GHRH-Receptor, pAkt and Hsp90 Predict 10-Year Overall Survival in Patients with Locally Advanced Rectal Cancer.Biomedicines · 2023Article
- Smart Nanofiber Mesh with Locally Sustained Drug Release Enabled Synergistic Combination Therapy for Glioblastoma.Nanomaterials (Basel, Switzerland) · 2023Article
- HSP90 inhibitors and cancer: Prospects for use in targeted therapies (Review).Oncology reports · 2023Review
- BAG2 drives chemoresistance of breast cancer by exacerbating mutant p53 aggregate.Theranostics · 2023Article
- Learn from antibody-drug conjugates: consideration in the future construction of peptide-drug conjugates for cancer therapy.Experimental hematology & oncology · 2022Review
- Expression of membrane Hsp90 is a molecular signature of T cell activation.Scientific reports · 2022Article
- Targeting HSP90 as a Novel Therapy for Cancer: Mechanistic Insights and Translational Relevance.Cells · 2022Review
77 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is required for the stability and function of multiple mutated, chimeric and over-expressed signaling proteins that promote the growth and/or survival of cancer cells. Hsp90 client proteins include mutated p53, Bcr-Abl, Raf-1, Akt, HER2/Neu (ErbB2) and HIF-1alpha. Hsp90 inhibitors, by interacting specifically with a single molecular target, cause the destabilization and eventual degradation of Hsp90 client proteins, and the first-in-class Hsp90 inhibitor, 17-allylamino-17 demethoxygeldanamycin (17AAG), is currently in phase II clinical trials. A fraction of Hsp90 has been identified at the cell surface and its presence has recently been shown to correlate with melanoma progression. Inhibition of cell-surface Hsp90 with antibodies or cell-impermeable Hsp90 inhibitors blocks cell motility and invasion in vitro and cancer metastasis in vivo. Thus, cell-surface Hsp90 may play a unique role in tumor metastasis, distinct from but perhaps overlapping with its intracellular function. In addition, because cell-surface Hsp90 may be the point of contact between some viruses and host cells, this pool of the chaperone may play a distinct role in initiation of infectious disease.
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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.