Evidence map›Paper›PMID 24138853›Full record

ArticleBiophysical journal2013

The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks.

Jona Kayser, Martin Haslbeck, Lisa Dempfle, Maike Krause, Carsten Grashoff, Johannes Buchner, Harald Herrmann, Andreas R Bausch

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 53 citations in OpenAlex.

  1. Trial
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  4. The J Domain of Sacsin Disrupts Intermediate Filament Assembly.International journal of molecular sciences · 2022
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  20. Intermediate Filaments: Structure and Assembly.Cold Spring Harbor perspectives in biology · 2016
    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

8 authors at 4 institutions in 1 country.

Jona KayserLehrstuhl für Zellbiophysik, Technische Universität München, Garching, Germany.
Martin Haslbeck
Lisa Dempfle
Maike Krause
Carsten Grashoff
Johannes Buchner
Harald Herrmann
Andreas R Bausch
Technical University of Munich · DECenter for Integrated Protein Science Munich · DEHeidelberg University · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanical properties of living cells are essential for many processes. They are defined by the cytoskeleton, a composite network of protein fibers. Thus, the precise control of its architecture is of paramount importance. Our knowledge about the molecular and physical mechanisms defining the network structure remains scarce, especially for the intermediate filament cytoskeleton. Here, we investigate the effect of small heat shock proteins on the keratin 8/18 intermediate filament cytoskeleton using a well-controlled model system of reconstituted keratin networks. We demonstrate that Hsp27 severely alters the structure of such networks by changing their assembly dynamics. Furthermore, the C-terminal tail domain of keratin 8 is shown to be essential for this effect. Combining results from fluorescence and electron microscopy with data from analytical ultracentrifugation reveals the crucial role of kinetic trapping in keratin network formation.

Indexed as

Cluster AnalysisHSP27 Heat-Shock ProteinsIntermediate FilamentsKeratinsKineticsMutant ProteinsProtein BindingProtein MultimerizationSolubilityStructure-Activity RelationshipHSP27 Heat-Shock ProteinsKeratinsMutant Proteins

Identifiers

PMID24138853
PMCPMC3797587
OpenAlexW2017718238

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.