Evidence map›Paper›PMID 26973652›Full record

ReviewFrontiers in immunology2016

Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic Implications.

Daming Zuo, John Subjeck, Xiang-Yang Wang

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed, 2 pooled it
5.6field-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

56 citing papers in PubMed, 2 syntheses or guidelines pooled it, 116 citations in OpenAlex.

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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

3 authors at 3 institutions in 2 countries.

Daming ZuoDepartment of Immunology, Southern Medical University, Guangzhou, China; State Key Laboratory of Organ Failure Research, Department of Infectious Diseases, Nanfang Hospital, Southern Medical University, Guangzhou, China; Guangdong Provincial Key Laboratory of Viral Hepatitis Research, Department of Infectious Diseases, Nanfang Hospital, Southern Medical University, Guangzhou, China.
John SubjeckDepartment of Cellular Stress Biology, Roswell Park Cancer Institute , Buffalo, NY , USA.
Xiang-Yang WangDepartment of Human and Molecular Genetics, Virginia Commonwealth University, Richmond, VA, USA; VCU Massey Cancer Center, Virginia Commonwealth University, Richmond, VA, USA; VCU Institute of Molecular Medicine, Virginia Commonwealth University, Richmond, VA, USA.
Nanfang Hospital · CNRoswell Park Comprehensive Cancer Center · USVirginia Commonwealth University · US

Funding

Virus Vector Shared ResourceP30CA016059 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Kim Felder Rhoads · 1985 to 2026
$51.0M
Large heat shock proteins and their role in cancer therapyR01CA099326 · NCI · ROSWELL PARK CANCER INSTITUTE CORP · PI REPASKY, ELIZABETH A, WANG, XIANG-YANG SHAWN · 2003 to 2020
$5.7M
Host-tumor interactions and cancer relapse after radiation therapyR01CA175033 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI WANG, XIANG-YANG SHAWN · 2014 to 2018
$1.6M
Large Stress Proteins in Biology and MedicineR01CA154708 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI WANG, XIANG-YANG SHAWN · 2011 to 2015
$1.5M
Scavenger Receptor-A and Immune RegulationR01CA129111 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI WANG, XIANG-YANG SHAWN · 2007 to 2011
$1.2M
NCI NIH HHS P30 CA016059NCI NIH HHS R01 CA099326NCI NIH HHS R01 CA129111NCI NIH HHS R01 CA154708NCI NIH HHS R01 CA175033
6 · The paper itself

Abstract

Heat shock proteins (HSPs) of eukaryotes are evolutionarily conserved molecules present in all the major intracellular organelles. They mainly function as molecular chaperones and participate in maintenance of protein homeostasis in physiological state and under stressful conditions. Despite their relative abundance, the large HSPs, i.e., Hsp110 and glucose-regulated protein 170 (Grp170), have received less attention compared to other conventional HSPs. These proteins are distantly related to the Hsp70 and belong to Hsp70 superfamily. Increased sizes of Hsp110 and Grp170, due to the presence of a loop structure, result in their exceptional capability in binding to polypeptide substrates or non-protein ligands, such as pathogen-associated molecules. These interactions that occur in the extracellular environment during tissue injury or microbial infection may lead to amplification of an immune response engaging both innate and adaptive immune components. Here, we review the current advances in understanding these large HSPs as molecular chaperones in proteostasis control and immune modulation as well as their therapeutic implications in treatment of cancer and neurodegeneration. Given their unique immunoregulatory activities, we also discuss the emerging evidence of their potential involvement in inflammatory and immune-related diseases.

Indexed as

antigen cross-presentationcytoprotectionglucose-regulated protein 170heat shock protein 110inflammatory diseaseinnate immunity

Identifiers

PMID26973652
PMCPMC4771732
OpenAlexW2308345772

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.