Evidence map›Paper›PMID 7988666›Full record

ReviewExperientia1994

Hsp70 in parasites: as an inducible protective protein and as an antigen.

B Maresca, G S Kobayashi

Abstract readReview
PubMed Publisher
In one paragraph

Review in Experientia, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Proteomic Analysis ofPathogens (Basel, Switzerland) · 2022
    Article
  5. A Biological and Immunological Characterization ofInternational journal of molecular sciences · 2020
    Article
  6. Comparative Transcriptome Analyses ofFrontiers in microbiology · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum.Protein science : a publication of the Protein Society · 2007
    Review
  17. Article
  18. Article
  19. Heat shock proteins in immune reactions.Folia microbiologica · 1999
    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

2 authors at 2 institutions in 2 countries.

B MarescaInternational Institute of Genetics and Biophysics, CNR, Naples, Italy.
G S Kobayashi
Institute of Genetics and Biophysics · ITWashington University in St. Louis · US

Funding

DIMORPHISM AND VIRULENCE IN HISTOPLASMA CAPSULATUMR01AI029609 · NIAID · WASHINGTON UNIVERSITY · PI KOBAYASHI, GEORGE S · 1990 to 1994
–
NIAID NIH HHS AI 29609
6 · The paper itself

Abstract

The heat shock (HS) response is a general homeostatic mechanism that protects cells and the entire organism from the deleterious effects of environmental stresses. It has been demonstrated that heat shock proteins (HSP) play major roles in many cellular processes, and have a unique role in several areas of cell biology, from chronic degenerative diseases to immunology, from cancer research to interaction between host and parasites. This review deals with the hsp70 gene family and with its protein product, hsp70, as an antigen when pathogens infect humans. Members of HSP have been shown to be major antigens of many pathogenic organisms when they experience a major temperature shift upwards at the onset of infection and become targets for host B and T cells.

Indexed as

AnimalsAntigensHSP70 Heat-Shock ProteinsHumansParasitic DiseasesRNA, MessengerAntigensHSP70 Heat-Shock ProteinsRNA, Messenger

Identifiers

PMID7988666
OpenAlexW1973518711

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.