Evidence map›Paper›PMID 29240668›Full record

ReviewInternational journal of molecular sciences2017

Heat Shock Proteins in Vascular Diabetic Complications: Review and Future Perspective.

Stefania Bellini, Federica Barutta, Raffaella Mastrocola, Luigi Imperatore, Graziella Bruno, Gabriella Gruden

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.7field-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

44 citing papers in PubMed, 85 citations in OpenAlex.

  1. Trial
  2. Review
  3. Diabetes, Protein Misfolding, and Heat Stress: Molecular Insights and Translational Perspectives.TH open : companion journal to thrombosis and haemostasis · 2026
    Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. LRG1 loss effectively restrains glomerular TGF-β signaling to attenuate diabetic kidney disease.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Multi-organ single-cell RNA sequencing in mice reveals early hyperglycemia responses that converge on fibroblast dysregulation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  16. Article
  17. Article
  18. Anserine and Carnosine Induce HSP70-Dependent HAntioxidants (Basel, Switzerland) · 2022
    Article
  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.

Stefania BelliniLaboratory of Diabetic Nephropathy, Department of Medical Sciences, University of Turin, Corso Dogliotti 14, 10126 Turin, Italy. stefania.bellini@unito.it.
Federica BaruttaLaboratory of Diabetic Nephropathy, Department of Medical Sciences, University of Turin, Corso Dogliotti 14, 10126 Turin, Italy. federica.barutta@unito.it.
Raffaella MastrocolaDepartment of Clinical and Biological Sciences, University of Turin, Corso Raffaello 30, 10125 Turin, Italy. raffaella.mastrocola@unito.it.ORCID 0000-0002-0104-6129
Luigi ImperatoreLaboratory of Diabetic Nephropathy, Department of Medical Sciences, University of Turin, Corso Dogliotti 14, 10126 Turin, Italy. limperat@unito.it.
Graziella BrunoLaboratory of Diabetic Nephropathy, Department of Medical Sciences, University of Turin, Corso Dogliotti 14, 10126 Turin, Italy. graziella.bruno@unito.it.
Gabriella GrudenLaboratory of Diabetic Nephropathy, Department of Medical Sciences, University of Turin, Corso Dogliotti 14, 10126 Turin, Italy. gabriella.gruden@unito.it.
University of Turin · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock proteins (HSPs) are a large family of proteins highly conserved throughout evolution because of their unique cytoprotective properties. Besides assisting protein refolding and regulating proteostasis under stressful conditions, HSPs also play an important role in protecting cells from oxidative stress, inflammation, and apoptosis. Therefore, HSPs are crucial in counteracting the deleterious effects of hyperglycemia in target organs of diabetes vascular complications. Changes in HSP expression have been demonstrated in diabetic complications and functionally related to hyperglycemia-induced cell injury. Moreover, associations between diabetic complications and altered circulating levels of both HSPs and anti-HSPs have been shown in clinical studies. HSPs thus represent an exciting therapeutic opportunity and might also be valuable as clinical biomarkers. However, this field of research is still in its infancy and further studies in both experimental diabetes and humans are required to gain a full understanding of HSP relevance. In this review, we summarize current knowledge and discuss future perspective.

Indexed as

AnimalsApoptosisBiomarkersDiabetic AngiopathiesHeat-Shock ProteinsHumansInflammationModels, BiologicalProtein IsoformsBiomarkersHeat-Shock ProteinsProtein Isoformsalbuminuriabiomarkersdiabetesdiabetes complicationsdiabetic nephropathydiabetic neuropathydiabetic retinopathyHeat shock protein (HSP) 27heat shock proteinsHSP47HSP60HSP70HSP90

Identifiers

PMID29240668
PMCPMC5751310
OpenAlexW2772134117

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.