Evidence map›Paper›PMID 31998315›Full record

ReviewFrontiers in immunology2019

Immunological Outcomes Mediated Upon Binding of Heat Shock Proteins to Scavenger Receptors SCARF1 and LOX-1, and Endocytosis by Mononuclear Phagocytes.

Ayesha Murshid, Thiago J Borges, Cristina Bonorino, Benjamin J Lang, Stuart K Calderwood

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

20 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Structural and molecular principles of DAMP biology.Nature structural & molecular biology · 2026
    Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. The Role of SREC-Ⅰ in Innate Immunity to Aspergillus fumigatus Keratitis.Investigative ophthalmology & visual science · 2021
    Article
  17. Review
  18. Article
  19. The Role of Heat Shock Protein 70 kDa in Asthma.Journal of asthma and allergy · 2020
    Review
  20. Vaccine-Induced CD8Frontiers in immunology · 2020
    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

5 authors at 3 institutions in 2 countries.

Ayesha MurshidDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA, United States.
Thiago J BorgesDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA, United States.
Cristina BonorinoLaboratório de Immunoterapia, Departmento de Ciências Básicas da Saúde, Universidade Federal de Ciências da Saúde de Porto Alegre, Porto Alegre, Brazil.
Benjamin J LangDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA, United States.
Stuart K CalderwoodDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA, United States.
Beth Israel Deaconess Medical Center · USBrigham and Women's Hospital · USUniversidade 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
Extracellular Hsp70 and hyperthermia in tumor therapyR01CA119045 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CALDERWOOD, STUART KEITH · 2007 to 2016
$3.1M
NCI NIH HHS R01 CA047407NCI NIH HHS R01 CA119045
6 · The paper itself

Abstract

Heat shock proteins (HSP) are a highly abundant class of molecular chaperones that can be released into the extracellular milieu and influence the immune response. HSP release can occur when cells undergo necrosis and exude their contents. However, HSPs are also secreted from intact cells, either in free form or in lipid vesicles including exosomes to react with receptors on adjacent cells. Target cells are able recognize extracellular HSPs through cell surface receptors. These include scavenger receptors (SR) such as class E member oxidized low-density lipoprotein receptor-1 (LOX-1, aka OLR1, Clec8A, and SR-E1) and scavenger receptor class F member 1 (SCARF1, aka SREC1). Both receptors are expressed by dendritic cells (DC) and macrophages. These receptors can bind HSPs coupled to client binding proteins and deliver the chaperone substrate to the pathways of antigen processing in cells. SR are able to facilitate the delivery of client proteins to the proteasome, leading to antigen processing and presentation, and stimulation of adaptive immunity. HSPs may also may be involved in innate immunity through activation of inflammatory signaling pathways in a mechanism dependent on SR and toll-like receptor 4 (TLR4) on DC and macrophages. We will discuss the pathways by which HSPs can facilitate uptake of protein antigens and the receptors that regulate the ensuing immune response.

Indexed as

AnimalsEndocytosisHeat-Shock ProteinsHumansPhagocytesReceptors, ScavengerScavenger Receptors, Class EScavenger Receptors, Class FHeat-Shock ProteinsReceptors, ScavengerScavenger Receptors, Class EScavenger Receptors, Class Fdendriticheat shock proteinsimmunitymacrophagescavenger receptor

Identifiers

PMID31998315
PMCPMC6968791
OpenAlexW2999276947

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.