ReviewNeuro-oncology2005
Chaperone proteins and brain tumors: potential targets and possible therapeutics.
Review in Neuro-oncology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 58 citations in OpenAlex.
- Review
- The function of chaperones in the radioresistance of glioblastoma: a new insight into the current knowledge.Brain tumor pathology · 2025Review
- Novel Immunotherapeutic Approaches for the Treatment of Glioblastoma.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Review
- Natural Products Targeting Hsp90 for a Concurrent Strategy in Glioblastoma and Neurodegeneration.Metabolites · 2022Review
- Immunotherapy and radiation for high-grade glioma: a narrative review.Translational cancer research · 2021Review
- Immunotherapy for Neuro-oncology.Advances in experimental medicine and biology · 2021Review
- T-Cell based therapies for overcoming neuroanatomical and immunosuppressive challenges within the glioma microenvironment.Journal of neuro-oncology · 2020Review
- Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells.International journal of molecular sciences · 2020Article
- HSP90 inhibitors in the context of heat shock and the unfolded protein response: effects on a primary canine pulmonary adenocarcinoma cell line.International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group · 2017Article
- Tumor Vaccines for Malignant Gliomas.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2017Review
- Induction of anti-EGFR immune response with mimotopes identified from a phage display peptide library by panitumumab.Oncotarget · 2016Article
- Review
- The unfolded protein response in glioblastomas: targetable or trouble?Future science OA · 2015Review
- Heat shock protein vaccines against glioblastoma: from bench to bedside.Journal of neuro-oncology · 2015Review
- Targeted therapy in gliomas.Current oncology reports · 2014Review
- Vaccine strategies for glioblastoma: progress and future directions.Immunotherapy · 2013Review
- Hsp27 (HSPB1): a possible surrogate molecular marker for loss of heterozygosity (LOH) of chromosome 1p in oligodendrogliomas but not in astrocytomas.Cell stress & chaperones · 2012Article
- Medulloblastoma exosome proteomics yield functional roles for extracellular vesicles.PloS one · 2012Article
- A novel therapeutic strategy for the treatment of glioma, combining chemical and molecular targeting of hsp90a.Cancers · 2011Article
- Serum autoantibody profiling using a natural glycoprotein microarray for the prognosis of early melanoma.Journal of proteome research · 2010Article
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
Chaperone proteins are most notable for the proteo- and cyotoprotective capacities they afford during cellular stress. Under conditions of cellular normalcy, chaperones still play integral roles in the folding of nascent polypeptides into functional entities, in assisting in intracellular/intraorganellar transport, in assembly and maintenance of multi-subunit protein complexes, and in aiding and abetting the degradation of senescent proteins. Tumors frequently have relatively enhanced needs for chaperone number and activity because of the stresses of rapid proliferation, increased metabolism, and overall genetic instability. Thus, it may be possible to take advantage of this reliance that tumor cells have on chaperones by pharmacologic and biologic means. Certain chaperones are abundant in the brain, which implies important roles for them. While it is presumed that the requirements of brain tumors for chaperone proteins are similar to those of any other cell type, tumor or otherwise, very little inquiry has been directed at the possibility of using chaperone proteins as therapeutic targets or even as therapeutic agents against central nervous system malignancies. This review highlights some of the research on the functions of chaperone proteins, on what can be done to modify those functions, and on the physiological responses that tumors and organisms can have to chaperone-targeted or chaperone-based therapies. In particular, this review will also underscore areas of research where brain tumors have been part of the field, although in general those instances are few and far between. This relative dearth of research devoted to chaperone protein targets and therapeutics in brain tumors reveals much untrodden turf to explore for potential treatments of these dreadfully refractive diseases.
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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.