Evidence map›Paper›PMID 10793148›Full record

ArticleMolecular biology of the cell2000

Complex regulation of the yeast heat shock transcription factor.

J J Bonner, T Carlson, D L Fackenthal, D Paddock, K Storey, K Lea

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.

  1. Clinical practice guidelines for the management of cryptococcal disease: 2010 update by the infectious diseases society of america.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2010
    Guideline
  2. Genetic inactivation of essentialMolecular biology of the cell · 2023
    Article
  3. Article
  4. The life and death of RNA across temperatures.Computational and structural biotechnology journal · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Induced metastable memory in heat shock response.Journal of biological physics · 2006
    Article
  18. Article
  19. Article
  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.

J J BonnerDepartment of Biology, Indiana University, Bloomington, Indiana 47405-3700, USA. jbonner@bio.indiana.edu
T Carlson
D L Fackenthal
D Paddock
K Storey
K Lea
Indiana University Bloomington · US

Funding

POSTTRANSLATIONAL REGULATION OF HSF ACTIVITYR01GM051853 · NIGMS · INDIANA UNIVERSITY BLOOMINGTON · PI BONNER, JAMES J · 1996 to 2002
$362k
NIGMS NIH HHS GM51853
6 · The paper itself

Abstract

The yeast heat shock transcription factor (HSF) is regulated by posttranslational modification. Heat and superoxide can induce the conformational change associated with the heat shock response. Interaction between HSF and the chaperone hsp70 is also thought to play a role in HSF regulation. Here, we show that the Ssb1/2p member of the hsp70 family can form a stable, ATP-sensitive complex with HSF-a surprising finding because Ssb1/2p is not induced by heat shock. Phosphorylation and the assembly of HSF into larger, ATP-sensitive complexes both occur when HSF activity decreases, whether during adaptation to a raised temperature or during growth at low glucose concentrations. These larger HSF complexes also form during recovery from heat shock. However, if HSF is assembled into ATP-sensitive complexes (during growth at a low glucose concentration), heat shock does not stimulate the dissociation of the complexes. Nor does induction of the conformational change induce their dissociation. Modulation of the in vivo concentrations of the SSA and SSB proteins by deletion or overexpression affects HSF activity in a manner that is consistent with these findings and suggests the model that the SSA and SSB proteins perform distinct roles in the regulation of HSF activity.

Indexed as

Saccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsDNA-Binding ProteinsFungal ProteinsGene DeletionGene Expression Regulation, FungalHeat-Shock ProteinsHeat-Shock ResponseHSP70 Heat-Shock ProteinsPhosphorylationProtein Processing, Post-TranslationalSuperoxidesTranscription FactorsYeastsDNA-Binding ProteinsFungal ProteinsHeat-Shock ProteinsHSF1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSSB1 protein, S cerevisiaeSSB2 protein, S pombeSuperoxidesTranscription Factors

Identifiers

PMID10793148
PMCPMC14880
OpenAlexW2116837564

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.