Evidence map›Paper›PMID 36101505›Full record

ArticleBiophysical journal2022

Dual-wavelength stopped-flow analysis of the lateral and longitudinal assembly kinetics of vimentin.

Lovis Schween, Norbert Mücke, Stéphanie Portet, Wolfgang H Goldmann, Harald Herrmann, Ben Fabry

Abstract read
In one paragraph

Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Continuous self-repair protects vimentin intermediate filaments from fragmentation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. 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.

Lovis SchweenDepartment of Physics, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany; Muscle Research Center Erlangen (MURCE), Friedrich-Alexander-Universität of Erlangen-Nürnberg, Erlangen, Germany.
Norbert MückeDivision of Chromatin Networks, German Cancer Research Center, Heidelberg, Germany.
Stéphanie PortetDepartment of Mathematics, University of Manitoba, Winnipeg, Manitoba, Canada.
Wolfgang H GoldmannDepartment of Physics, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany; Muscle Research Center Erlangen (MURCE), Friedrich-Alexander-Universität of Erlangen-Nürnberg, Erlangen, Germany.
Harald HerrmannInstitute of Neuropathology, University Hospital Erlangen, Erlangen, Germany; Muscle Research Center Erlangen (MURCE), Friedrich-Alexander-Universität of Erlangen-Nürnberg, Erlangen, Germany.
Ben FabryDepartment of Physics, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany; Muscle Research Center Erlangen (MURCE), Friedrich-Alexander-Universität of Erlangen-Nürnberg, Erlangen, Germany. Electronic address: ben.fabry@fau.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vimentin is a highly charged intermediate filament protein that inherently forms extended dimeric coiled coils, which serve as the basic building blocks of intermediate filaments. Under low ionic strength conditions, vimentin filaments dissociate into uniform tetrameric complexes of two anti-parallel-oriented, half-staggered coiled-coil dimers. By addition of salt, vimentin tetramers spontaneously reassemble into filaments in a time-dependent process: 1) lateral assembly of tetramers into unit-length filaments, 2) longitudinal annealing of unit-length filaments, and 3) longitudinal assembly of filaments coupled with subsequent radial compaction. To independently determine the lateral and longitudinal assembly kinetics, we measure with a stopped-flow instrument the static light scattering signal at two different wavelengths (405 and 594 nm) with a temporal resolution of 3 ms and analyze the signals based on Rayleigh-Gans theory. This theory considers that the intensity of the scattered light depends not only on the molecular weight of the scattering object but also on its shape. This shape dependence is more pronounced at shorter wavelengths, allowing us to decompose the scattered light signal into its components arising from lateral and longitudinal filament assembly. We demonstrate that both the lateral and longitudinal filament assembly kinetics increase with salt concentration.

Indexed as

CytoskeletonIntermediate FilamentsKineticsOsmolar ConcentrationVimentinVimentin

Identifiers

PMID36101505
PMCPMC9674981

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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.