Evidence map›Paper›PMID 23807250›Full record

ReviewShock (Augusta, Ga.)2013

Extracellular heat shock proteins: a new location, a new function.

Antonio De Maio, Daniel Vazquez

Abstract readReview
In one paragraph

Review in Shock (Augusta, Ga.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

91 citing papers in PubMed, 169 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Does extracellular vesicle specificity truly exist?Cell communication and signaling : CCS · 2026
    Review
  6. Review
  7. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Exosome Mediated Cell-Cell Crosstalk in Tissue Injury and Repair.Results and problems in cell differentiation · 2024
    Review
  18. Review
  19. Article
  20. Article

31 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

2 authors at 2 institutions in 1 country.

Antonio De Maio*Center for Investigations of Health and Education Disparities; †Division of Trauma, Surgical Critical Care and Burns, Department of Surgery; and ‡Department of Neurosciences, School of Medicine University of California San Diego, La Jolla, California; and §Department of Surgery, South Florida University, Tampa, Florida.
Daniel Vazquez
University of California, San Diego · USUniversity of South Florida · US

Funding

Heat Shock Proteins and the Stress Observation SystemR01GM098455 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DE MAIO, ANTONIO · 2012 to 2015
$1.1M
NIGMS NIH HHS R01 GM098455
6 · The paper itself

Abstract

The expression of heat shock proteins (HSPs) is a basic and well-conserved cellular response to an array of stresses. These proteins are involved in the repair of cellular damage induced by the stress, which is necessary for the salutary resolution from the insult. Moreover, they confer protection from subsequent insults, which has been coined stress tolerance. Because these proteins are expressed in subcellular compartments, it was thought that their function during stress conditions was circumscribed to the intracellular environment. However, it is now well established that HSPs can also be present outside cells where they appear to display a function different than the well-understood chaperone role. Extracellular HSPs act as alert stress signals priming other cells, particularly of the immune system, to avoid the propagation of the insult and favor resolution. Because the majority of HSPs do not possess a secretory peptide signal, they are likely to be exported by a nonclassic secretory pathway. Different mechanisms have been proposed to explain the export of HSPs, including translocation across the plasma membrane and release associated with lipid vesicles, as well as the passive release after cell death by necrosis. Extracellular HSPs appear in various flavors, including membrane-bound and membrane-free forms. All of these variants of extracellular HSPs suggest that their interactions with cells may be quite diverse, both in target cell types and the activation signaling pathways. This review addresses some of our current knowledge about the release and relevance of extracellular HSPs.

Indexed as

Cell-Derived MicroparticlesExtracellular SpaceHeat-Shock ProteinsHumansNecrosisHeat-Shock Proteins

Identifiers

PMID23807250
PMCPMC4351735
OpenAlexW1984118541

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.