Evidence map›Paper›PMID 19396626›Full record

ArticleCell stress & chaperones2009

Novel Hsp90 partners discovered using complementary proteomic approaches.

Pavel A Tsaytler, Jeroen Krijgsveld, Soenita S Goerdayal, Stefan Rüdiger, Maarten R Egmond

Open access · bronzeAbstract read
In one paragraph

Article in Cell stress & chaperones, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
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  5. A Chemical Biology Approach to the Chaperome in Cancer-HSP90 and Beyond.Cold Spring Harbor perspectives in biology · 2020
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  20. Approaches for defining the Hsp90-dependent proteome.Biochimica et biophysica acta · 2012
    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

5 authors at 1 institution in 1 country.

Pavel A TsaytlerDepartment of Membrane Enzymology, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, Utrecht 3584 CH, The Netherlands. p.a.tsaytler@uu.nl
Jeroen Krijgsveld
Soenita S Goerdayal
Stefan Rüdiger
Maarten R Egmond
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hsp90 is an essential eukaryotic molecular chaperone that stabilizes a large set of client proteins, many of which are involved in various cellular signaling pathways. The current list of Hsp90 interactors comprises about 200 proteins and this number is growing steadily. In this paper, we report on the application of three complementary proteomic approaches directed towards identification of novel proteins that interact with Hsp90. These methods are coimmunoprecipitation, pull down with biotinylated geldanamycin, and immobilization of Hsp90beta on sepharose. In all, this study led to the identification of 42 proteins, including 18 proteins that had not been previously characterized as Hsp90 interactors. These novel Hsp90 partners not only represent abundant protein species, but several proteins were identified at low levels, among which signaling kinase Cdk3 and putative transcription factor tripartite motif-containing protein 29. Identification of tetratricopeptide-repeat-containing mitochondrial import receptor protein Tom34 suggests the involvement of Hsp90 in the early steps of translocation of mitochondrial preproteins. Taken together, our data expand the knowledge of the Hsp90 interactome and provide a further step in our understanding of the Hsp90 chaperone system.

Indexed as

Amino Acid MotifsCell Line, TumorConsensus SequenceCyclin-Dependent Kinase 3DNA-Binding ProteinsHSP90 Heat-Shock ProteinsHumansImmunoprecipitationMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProtein BindingProteomicsTranscription FactorsCyclin-Dependent Kinase 3DNA-Binding ProteinsHSP90AB1 protein, humanHSP90 Heat-Shock ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsTOMM34 protein, humanTranscription FactorsTRIM29 protein, human

Identifiers

PMID19396626
PMCPMC2866955
OpenAlexW1970847499

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.