Evidence map›Paper›PMID 26898980›Full record

ReviewCancer letters2016

Targeting Hsp70: A possible therapy for cancer.

Sanjay Kumar, James Stokes, Udai P Singh, Karyn Scissum Gunn, Arbind Acharya, Upender Manne, Manoj Mishra

Open access · greenAbstract readReview
In one paragraph

Review in Cancer letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
9.7field-weighted citation impact, top 2% 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

108 citing papers in PubMed, 224 citations in OpenAlex.

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48 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

7 authors at 4 institutions in 2 countries.

Sanjay KumarCancer Biology Research and Training Program, Department of Biological Sciences, Alabama State University, AL 36101, USA.
James StokesCancer Biology Research and Training Program, Department of Biological Sciences, Alabama State University, AL 36101, USA.
Udai P SinghDepartment of Pathology, Microbiology and Immunology, University of South Carolina School of Medicine, Columbia, SC 29208, USA.
Karyn Scissum GunnCancer Biology Research and Training Program, Department of Biological Sciences, Alabama State University, AL 36101, USA.
Arbind AcharyaCentre of Advance Study in Zoology, Faculty of Science, Banaras Hindu University, Varanasi 221 005, India.
Upender ManneDepartment of Pathology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Manoj MishraCancer Biology Research and Training Program, Department of Biological Sciences, Alabama State University, AL 36101, USA. Electronic address: mmishra@alasu.edu.
Alabama State University · USBanaras Hindu University · INUniversity of Alabama at Birmingham · USUniversity of South Carolina · US

Funding

Training and Education ProgramP20CA192973 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MANNE, UPENDER · 2014 to 2017
$767k
Project 2: 2/2 The Alabama State University/UAB Comprehensive Cancer Center PartnershipP20CA192976 · NCI · ALABAMA STATE UNIVERSITY · PI MISHRA, MANOJ K. · 2014 to 2017
$598k
NCI NIH HHS P20 CA192973NCI NIH HHS P20CA192973NCI NIH HHS P20 CA192976NCI NIH HHS P20CA192976
6 · The paper itself

Abstract

In all organisms, heat-shock proteins (HSPs) provide an ancient defense system. These proteins act as molecular chaperones by assisting proper folding and refolding of misfolded proteins and aid in the elimination of old and damaged cells. HSPs include Hsp100, Hsp90, Hsp70, Hsp40, and small HSPs. Through its substrate-binding domains, Hsp70 interacts with wide spectrum of molecules, ranging from unfolded to natively folded and aggregated proteins, and provides cytoprotective role against various cellular stresses. Under pathophysiological conditions, the high expression of Hsp70 allows cells to survive with lethal injuries. Increased Hsp70, by interacting at several points on apoptotic signaling pathways, leads to inhibition of apoptosis. Elevated expression of Hsp70 in cancer cells may be responsible for tumorigenesis and for tumor progression by providing resistance to chemotherapy. In contrast, inhibition or knockdown of Hsp70 reduces the size of tumors and can cause their complete regression. Moreover, extracellular Hsp70 acts as an immunogen that participates in cross presentation of MHC-I molecules. The goals of this review are to examine the roles of Hsp70 in cancer and to present strategies targeting Hsp70 in the development of cancer therapeutics.

Indexed as

AnimalsGene Knockdown TechniquesHSP70 Heat-Shock ProteinsHumansMolecular Targeted TherapyNeoplasmsHSP70 Heat-Shock ProteinsApoptosisCancer therapeuticsHsp70Immunogenicity

Identifiers

PMID26898980
PMCPMC5553548
OpenAlexW2274711011

What OpenQuestion holds

Textmetadata
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Read underepoch 390

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.