Evidence map›Paper›PMID 29177670›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2018

Molecular Chaperone Receptors.

Ayesha Murshid, Jimmy Theriault, Jianlin Gong, Stuart K Calderwood

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review
  3. Effect of Benzyl Alcohol on Main Defense System Components ofInternational journal of molecular sciences · 2024
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
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

4 authors at 3 institutions in 1 country.

Ayesha MurshidMolecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA, 02215, USA.
Jimmy TheriaultMolecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA, 02215, USA.
Jianlin GongDepartment of Medicine, Boston University School of Medicine, Boston, MA, 02118, USA.
Stuart K CalderwoodDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA, 02215, USA. scalderw@bidmc.harvard.edu.
Harvard University · USBeth Israel Deaconess Medical Center · USBoston University · US

Funding

TRANSMEMBRANE SIGNAL MODULATION BY HYPERTHERMIAR01CA047407 · NCI · DANA-FARBER CANCER INSTITUTE · PI CALDERWOOD, STUART KEITH · 1988 to 2014
$4.3M
Extracellular Hsp70 and hyperthermia in tumor therapyR01CA119045 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CALDERWOOD, STUART KEITH · 2007 to 2016
$3.1M
Gene Repression by HSF1 during hyperthermia and stressesR01CA094397 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CALDERWOOD, STUART KEITH · 2002 to 2006
$1.5M
NCI NIH HHS R01 CA047407NCI NIH HHS R01 CA094397NCI NIH HHS R01 CA119045
6 · The paper itself

Abstract

Extracellular heat shock proteins (HSP) play important roles in cell signaling and immunity. Many of these effects are mediated by surface receptors expressed on a wide range of cell types. We have investigated the nature of such proteins by cloning candidate receptors into cells (CHO-K1) with the rare property of being null for HSP binding. Using this approach we have discovered that Hsp70 binds avidly to at least two classes of receptors including: (1) c-type lectin receptors (CLR) and (2) scavenger receptors (SR). However, the structural nature of the receptor-ligand interactions is not clear at this time. Hsp70 can bind to LOX-1 (a member of both the CLR and SR), with the c-type lectin binding domain (CTLD) as well as the SR family members SREC-I and FEEL-1/CLEVER-1/STABILIN-1, which by contrast have arrays of EGF-like repeats in their extracellular domains. In this chapter we will discuss: (1) methods for discovery of HSP receptors, (2) approaches to the study of individual receptors in cells that contain multiple such receptors, and (3) methods for investigating HSP receptor function in vivo.

Indexed as

AnimalsCell Line, TumorCHO CellsChromatography, Ion ExchangeCloning, MolecularCricetulusHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansLectins, C-TypeMiceMice, Inbred C57BLMice, KnockoutReceptors, ScavengerSf9 CellsSpodopteraHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsLectins, C-TypeReceptors, ScavengerExtracellularHeatImmunityProteinReceptorScavengerShock

Identifiers

PMID29177670
PMCPMC6777869
OpenAlexW2770187636

What OpenQuestion holds

Textmetadata
LicenceTDM
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.