Evidence map›Paper›PMID 10747020›Full record

ArticleThe EMBO journal2000

Hsp90 is required for c-Mos activation and biphasic MAP kinase activation in Xenopus oocytes.

D L Fisher, E Mandart, M Dorée

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 66 citations in OpenAlex.

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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.

D L FisherCNRS-CRBM, 1919 Route de Mende, 34293 Montpellier, Cedex 05, France.
E Mandart
M Dorée
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During Xenopus oocyte maturation, the Mos protein kinase is synthesized and activates the MAP kinase cascade. In this report, we demonstrate that the synthesis and activation of Mos are two separable processes. We find that Hsp90 function is required for activation and phosphorylation of Mos and full activation of the MAP kinase cascade. Once Mos is activated, Hsp90 function is no longer required. We show that Mos interacts with both Hsp90 and Hsp70, and that there is an inverse relationship between association of Mos with these two chaperones. We propose that Mos protein kinase is activated by a novel mechanism involving sequential association with Hsp70 and Hsp90 as well as phosphorylation. We also present evidence for a two-phase activation of MAP kinase in Xenopus oocytes.

Indexed as

AnimalsBase SequenceEnzyme ActivationFemaleHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsIn Vitro TechniquesMitogen-Activated Protein KinasesOligodeoxyribonucleotides, AntisenseOocytesPhosphorylationProtein BiosynthesisProto-Oncogene Proteins c-mosRecombinant ProteinsXenopusHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMitogen-Activated Protein KinasesOligodeoxyribonucleotides, AntisenseProto-Oncogene Proteins c-mosRecombinant Proteins

Identifiers

PMID10747020
PMCPMC310221
OpenAlexW2162995156

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.