Evidence map›Paper›PMID 31514477›Full record

ReviewInternational journal of molecular sciences2019

Heat Shock Proteins Are Essential Components in Transformation and Tumor Progression: Cancer Cell Intrinsic Pathways and Beyond.

Benjamin J Lang, Martín Eduardo Guerrero-Giménez, Thomas L Prince, Andrew Ackerman, Cristina Bonorino, Stuart K Calderwood

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.6field-weighted citation impact, top 4% 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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 92 citations in OpenAlex.

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  13. The chaperone system in cancer therapies: Hsp90.Journal of molecular histology · 2023
    Review
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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

6 authors at 4 institutions in 3 countries.

Benjamin J LangDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA. bjlang@bidmc.harvard.edu.
Martín Eduardo Guerrero-GiménezLaboratory of Oncology, Institute of Medicine and Experimental Biology of Cuyo (IMBECU), National Scientific and Technical Research Council (CONICET), Buenos Aires B1657, Argentina. martiguerrerog89@gmail.com.
Thomas L PrinceDepartment of Functional Genomics, Geisinger Medical Center, Danville, PA 17822, USA. tprince@geisinger.org.
Andrew AckermanDepartment of Functional Genomics, Geisinger Medical Center, Danville, PA 17822, USA. aackerman@geisinger.org.
Cristina BonorinoDepartamento de Ciências Básicas da Saúde, Universidade Federal de Ciências da Saúde de Porto Alegre, Porto Alegre 90010, Brazil. cbonorino@ucsd.edu.
Stuart K CalderwoodDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA. scalderw@bidmc.harvard.edu.
Beth Israel Deaconess Medical Center · USGeisinger Medical Center · USConsejo Nacional de Investigaciones Científicas y Técnicas · ARUniversidade Federal de Ciências da Saúde de Porto Alegre · BR

Funding

TRANSMEMBRANE SIGNAL MODULATION BY HYPERTHERMIAR01CA047407 · NCI · DANA-FARBER CANCER INSTITUTE · PI CALDERWOOD, STUART KEITH · 1988 to 2014
$4.3M
Complex Role of HSF1 in Breast CancerR01CA176326 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CALDERWOOD, STUART KEITH, SHERMAN, MICHAEL Y · 2014 to 2018
$1.8M
Gene Repression by HSF1 during hyperthermia and stressesR01CA094397 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CALDERWOOD, STUART KEITH · 2002 to 2006
$1.5M
Gene repression by HSF1 during hyperthermia and other stresses.R01CA077465 · NCI · DANA-FARBER CANCER INSTITUTE · PI CALDERWOOD, STUART KEITH · 1998 to 2011
$1.5M
NCI NIH HHS R01 CA047407NCI NIH HHS R01 CA077465NCI NIH HHS R01 CA094397NCI NIH HHS R01 CA176326
6 · The paper itself

Abstract

Heat shock protein (HSP) synthesis is switched on in a remarkably wide range of tumor cells, in both experimental animal systems and in human cancer, in which these proteins accumulate in high levels. In each case, elevated HSP concentrations bode ill for the patient, and are associated with a poor outlook in terms of survival in most cancer types. The significance of elevated HSPs is underpinned by their essential roles in mediating tumor cell intrinsic traits such as unscheduled cell division, escape from programmed cell death and senescence, de novo angiogenesis, and increased invasion and metastasis. An increased HSP expression thus seems essential for tumorigenesis. Perhaps of equal significance is the pronounced interplay between cancer cells and the tumor milieu, with essential roles for intracellular HSPs in the properties of the stromal cells, and their roles in programming malignant cells and in the release of HSPs from cancer cells to influence the behavior of the adjacent tumor and infiltrating the normal cells. These findings of a triple role for elevated HSP expression in tumorigenesis strongly support the targeting of HSPs in cancer, especially given the role of such stress proteins in resistance to conventional therapies.

Indexed as

Disease ProgressionAnimalsCell Transformation, NeoplasticHeat-Shock ProteinsHumansModels, BiologicalNeoplasmsSignal TransductionHeat-Shock Proteinscancerchaperomeextracellular HSPsheat shock proteinsHsp70Hsp90molecular chaperonesproteotoxic stressstress proteins in cancertumor signaling

Identifiers

PMID31514477
PMCPMC6769451
OpenAlexW2972346906

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

None linked

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.