Evidence map›Paper›PMID 19275675›Full record

ReviewCurrent protein & peptide science2009

Heat shock proteins in diabetes and wound healing.

Mustafa Atalay, Niku Oksala, Jani Lappalainen, David E Laaksonen, Chandan K Sen, Sashwati Roy

Open access · greenAbstract readReview
In one paragraph

Review in Current protein & peptide science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
3.9field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 1 synthesis or guideline pooled it, 142 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Recent advances toward the development of Hsp90 C-terminal inhibitors.Bioorganic & medicinal chemistry letters · 2023
    Review
  10. Article
  11. Neurobiological Opportunities in Diabetic Polyneuropathy.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article
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

6 authors at 1 institution in 1 country.

Mustafa AtalayInstitute of Biomedicine, Physiology, University of Kuopio, Finland. mustafa.atalay@uku.fi
Niku Oksala
Jani Lappalainen
David E Laaksonen
Chandan K Sen
Sashwati Roy
University of Eastern Finland · FI

Funding

Redox Control of Wound HealingR01GM069589 · NIGMS · OHIO STATE UNIVERSITY · PI SEN, CHANDAN K · 2004 to 2013
$2.3M
Tissue Oxygenation and Wound HealingR01GM077185 · NIGMS · OHIO STATE UNIVERSITY · PI SEN, CHANDAN K · 2007 to 2016
$2.3M
Mechanisms underlying impaired diabetic wound healingR01DK076566 · NIDDK · OHIO STATE UNIVERSITY · PI ROY, SASHWATI · 2008 to 2011
$1.2M
Mechanisms underlying impaired diabetic wound healingR56DK076566 · NIDDK · OHIO STATE UNIVERSITY · PI ROY, SASHWATI · 2016 to 2016
$347k
NIDDK NIH HHS DK 76566NIDDK NIH HHS R01 DK076566NIDDK NIH HHS R56 DK076566NIGMS NIH HHS GM 069589NIGMS NIH HHS GM 077185NIGMS NIH HHS R01 GM069589NIGMS NIH HHS R01 GM077185
6 · The paper itself

Abstract

The heat shock proteins (HSPs), originally identified as heat-inducible gene products, are a highly conserved family of proteins that respond to a wide variety of stress. Although HSPs are among the most abundant intracellular proteins, they are expressed at low levels under normal physiological conditions, and show marked induction in response to various stressors. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific pathways for degradation. By modulating inflammation, wound debris clearance, cell proliferation, migration and collagen synthesis, HSPs are essential for normal wound healing of the skin. In this review, our goal is to discuss the role and clinical implications of HSP with respect to skin wound healing and diabetes. The numerous defects in the function of HSPs associated with diabetes could contribute to the commonly observed complications and delayed wound healing in diabetics. Several physical, pharmacological and genetic approaches may be considered to address HSP-directed therapies both in the laboratory and in the clinics.

Indexed as

AnimalsDiabetes ComplicationsDiabetes MellitusGene Expression RegulationHeat-Shock ProteinsHumansWound HealingHeat-Shock Proteins

Identifiers

PMID19275675
PMCPMC2743605
OpenAlexW2140007927

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.