Evidence map›Paper›PMID 17278877›Full record

ReviewCell stress & chaperones2006

Heat shock protein 10 and signal transduction: a "capsula eburnea" of carcinogenesis?

Anna M Czarnecka, Claudia Campanella, Giovanni Zummo, Francesco Cappello

Open access · greenAbstract readReview
In one paragraph

Review in Cell stress & chaperones, 2006. 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
1.5field-weighted citation impact, top 19% 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, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Pediatric Brain Tumors: Signatures from the Intact Proteome.International journal of molecular sciences · 2022
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Therapeutic potential of heat shock protein induction for muscular dystrophy and other muscle wasting conditions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. The potential role of heat shock proteins in acute spinal cord injury.European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Heat shock protein 10 (Hsp10) in immune-related diseases: one coin, two sides.International journal of biochemistry and molecular biology · 2011
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Anna M CzarneckaDepartment of Genetics, University of Warsaw, ul. Pawinskiego 5a, 02-106, Warszawa, Poland.
Claudia Campanella
Giovanni Zummo
Francesco Cappello
University of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To date, little is known either about the physical interactions of heat shock protein 10 (Hsp10) with other proteins within the cell or its involvement in signal transduction pathways. Hsp10 has been considered mainly as a partner of Hsp60 in the Hsp60/10 protein folding machine. Only recently, Hsp10 was reported to interact with proteins involved in deoxyribonucleic acid checkpoint inactivation, termination of M-phase, messenger ribonucleic acid export, import of nuclear proteins, nucleocytoplasmic transport, and pheromone signaling pathways. At the same time, Hsp10 expression can be up-regulated in cancer cells, because it accumulates as the cell transformation progresses. Recent data suggest that Hsp10 may be not only a component of the folding machine but also an active player of the cell signaling network, influencing cell cycle, nucleocytoplasmic transport, and metabolism, with putative roles in the lack of cell differentiation and in the inhibition of apoptosis. In this review, we revise the involvement of Hsp10 in signal transduction pathways and its possible role in cancer etiology.

Indexed as

Signal TransductionApoptosisChaperonin 10Chaperonin 60ColonColonic NeoplasmsFungal ProteinsHumansNeoplasmsChaperonin 10Chaperonin 60Fungal Proteins

Identifiers

PMID17278877
PMCPMC1713189
OpenAlexW2181065268

What OpenQuestion holds

Textmetadata
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.