Evidence map›Paper›PMID 15077153›Full record

ArticleOncogene2004

Molecular chaperones and the stress of oncogenesis.

Dick D Mosser, Richard I Morimoto

Registry-linked trialAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT01168752 (Phase I Dose-escalation, Pharmacokinetic and Pharmacodynamic Study of Debio 0932, a Novel Hsp90-inhibitor, Administered Orally, in Patients With Advanced Solid Tumours or Lymphoma), which is not on this map. Cited by 174 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
174citing papers in PubMed, 1 pooled it
13.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

NCT01168752 phase1completednot on this mapstarted 2010, after this paper: background citation

Phase I Dose-escalation, Pharmacokinetic and Pharmacodynamic Study of Debio 0932, a Novel Hsp90-inhibitor, Administered Orally, in Patients With Advanced Solid Tumours or Lymphoma

TypeinterventionalSponsorDebiopharm International SARan2010 to 2013Enrolled81ConditionsCancer, Neoplasms, Solid Tumors, LymphomaArmsDebio 0932
3 · Its place in the literature

Who cites it

174 citing papers in PubMed, 1 synthesis or guideline pooled it, 501 citations in OpenAlex.

  1. Pooled it
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  11. The roles of HSP40/DNAJ protein family in neurodegenerative diseases.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2022
    Review
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114 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Dick D MosserDepartment of Molecular Biology and Genetics, University of Guelph, Guelph, Ontario, Canada N1G 2W1. rmosser@uoguelph.ca
Richard I Morimoto
Northwestern University · USUniversity of Guelph · CA

Funding

REGULATION AND EXPRESSION OF THE HSP70 GENE FAMILYR37GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2000 to 2009
$5.6M
NIGMS NIH HHS R37 GM038109PHS HHS 38109
6 · The paper itself

Abstract

Protein-damaging stresses induce the expression of 'heat-shock proteins', which have essential roles in protecting cells from the potentially lethal effects of stress and proteotoxicity. These stress-protective heat-shock proteins are often overexpressed in cells of various cancers and have been suggested to be contributing factors in tumorigenesis. An underlying basis of oncogenesis is the acquisition and accumulation of mutations that provide the transformed cell with the combined characteristics of deregulated cell proliferation and suppressed cell death. Heat-shock proteins with dual roles as regulators of protein conformation and stress sensors may therefore have intriguing and central roles in both cell proliferation and apoptosis. It has been established that heat-shock proteins exhibit specificity to particular classes of polypeptide substrates and client proteins in vivo, and that chaperones can stabilize mutations that affect the folded conformation. Likewise, overexpression of chaperones has also been shown to protect cells against apoptotic cell death. The involvement of chaperones, therefore, in such diverse roles might suggest novel anticancer therapeutic approaches targeting heat-shock protein function for a broad spectrum of tumor types.

Indexed as

ApoptosisHeat-Shock ProteinsMAP Kinase Kinase 4AnimalsHSP27 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesMolecular ChaperonesNeoplasm ProteinsNeoplasmsProtein FoldingSignal TransductionHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHSPB1 protein, humanMAP2K4 protein, humanMAP Kinase Kinase 4Mitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesMolecular ChaperonesNeoplasm Proteins

Identifiers

PMID15077153
OpenAlexW1995486038

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.