Evidence map›Paper›PMID 21112282›Full record

ArticleBiophysical journal2010

Deformation of dynamin helices damped by membrane friction.

Sandrine Morlot, Martin Lenz, Jacques Prost, Jean-François Joanny, Aurélien Roux

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Dynamic remodeling of the dynamin helix during membrane constriction.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  5. Article
  6. Review
  7. Article
  8. Optimized two-color super resolution imaging of Drp1 during mitochondrial fission with a slow-switching Dronpa variant.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Mechanics of dynamin-mediated membrane fission.Annual review of biophysics · 2013
    Review
  10. Article
  11. 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

5 authors at 3 institutions in 3 countries.

Sandrine MorlotLaboratoire Physico-Chimie Curie, Institut Curie, Centre de Recherche, Paris, France.
Martin Lenz
Jacques Prost
Jean-François Joanny
Aurélien Roux
Sorbonne Université · FRUniversity of Geneva · CHParisTech · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamin and other proteins of the dynamin superfamily are widely used by cells to sever lipid bilayers. During this process, a short helical dynamin polymer (one to three helical turns) assembles around a membrane tubule and reduces its radius and pitch upon guanosine triphosphate hydrolysis. This deformation is thought to be crucial for dynamin's severing action and results in an observable twisting of the helix. Here, we quantitatively characterize the dynamics of this deformation by studying long dynamin helices (many helical turns). We perform in vitro experiments where we attach small beads to the dynamin helix and track their rotation in real time, thus collecting information about the space and time dependence of the deformation. We develop a theoretical formalism to predict the dynamics of a mechanically continuous helix deforming on long timescales. Longer helices deform more slowly, as predicted by theory. This could account for the previously reported observation that they are less fission-competent. Comparison between experiments and our model indicates that the deformation dynamics is dominated by the draining of the membrane out of the helix, allowing quantification of helix-membrane interactions.

Indexed as

FrictionMembranes, ArtificialAnimalsBiomechanical PhenomenaDynaminsGuanosine TriphosphateHydrodynamicsHydrolysisMicrospheresMolecular WeightProtein Structure, SecondaryRatsReproducibility of ResultsRotationTime FactorsDynaminsGuanosine TriphosphateMembranes, Artificial

Identifiers

PMID21112282
PMCPMC2998610
OpenAlexW2125080444

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.