Evidence map›Paper›PMID 26881084›Full record

ReviewBiotechnology research international2015

Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi.

Shraddha Tiwari, Raman Thakur, Jata Shankar

Open access · diamondAbstract readReview
In one paragraph

Review in Biotechnology research international, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

115 citing papers in PubMed, 252 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Glutathione Peroxidase fromInternational journal of molecular sciences · 2026
    Article
  6. Article
  7. Combined Transcriptomic and Metabolomic Analyses of the Response ofJournal of fungi (Basel, Switzerland) · 2025
    Article
  8. Article
  9. Cold adaptation mechanisms of the psychrotolerant filamentous ascomycete Psychrophilomyces antarcticus.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025
    Article
  10. Article
  11. Membrane Lipids and Osmolytes Rearrangements Under Cell Wall Stress inInternational journal of molecular sciences · 2025
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

55 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

3 authors at 1 institution in 1 country.

Shraddha TiwariDepartment of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Solan, Himachal Pradesh 173234, India.
Raman ThakurDepartment of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Solan, Himachal Pradesh 173234, India.
Jata ShankarDepartment of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Solan, Himachal Pradesh 173234, India.
Jaypee University of Information Technology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stress (biotic or abiotic) is an unfavourable condition for an organism including fungus. To overcome stress, organism expresses heat-shock proteins (Hsps) or chaperons to perform biological function. Hsps are involved in various routine biological processes such as transcription, translation and posttranslational modifications, protein folding, and aggregation and disaggregation of proteins. Thus, it is important to understand holistic role of Hsps in response to stress and other biological conditions in fungi. Hsp104, Hsp70, and Hsp40 are found predominant in replication and Hsp90 is found in transcriptional and posttranscriptional process. Hsp90 and Hsp70 in combination or alone play a major role in morphogenesis and dimorphism. Heat stress in fungi expresses Hsp60, Hsp90, Hsp104, Hsp30, and Hsp10 proteins, whereas expression of Hsp12 protein was observed in response to cold stress. Hsp30, Hsp70, and Hsp90 proteins showed expression in response to pH stress. Osmotic stress is controlled by small heat-shock proteins and Hsp60. Expression of Hsp104 is observed under high pressure conditions. Out of these heat-shock proteins, Hsp90 has been predicted as a potential antifungal target due to its role in morphogenesis. Thus, current review focuses on role of Hsps in fungi during morphogenesis and various stress conditions (temperature, pH, and osmotic pressure) and in antifungal drug tolerance.

Identifiers

PMID26881084
PMCPMC4736001
OpenAlexW2228816633

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.