Evidence map›Paper›PMID 33100165›Full record

ReviewPhilosophical transactions. Series A, Mathematical, physical, and engineering sciences2020

Biological physics by high-speed atomic force microscopy.

Ignacio Casuso, Lorena Redondo-Morata, Felix Rico

Open access · hybridAbstract readReview
In one paragraph

Review in Philosophical transactions. Series A, Mathematical, physical, and engineering sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.4field-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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Enhanced visualization of influenza A virus entry into living cells using virus-view atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  11. Review
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  19. DNA Manipulation and Single-Molecule Imaging.Molecules (Basel, Switzerland) · 2021
    Review
  20. 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

3 authors at 1 institution in 2 countries.

Ignacio CasusoAix-Marseile University, Inserm, CNRS, LAI, 163 Av. de Luminy, 13009 Marseille, France.
Lorena Redondo-MorataCenter for Infection and Immunity of Lille, INSERM U1019, CNRS UMR 8204, 59000 Lille, France.
Felix RicoAix-Marseile University, Inserm, CNRS, LAI, 163 Av. de Luminy, 13009 Marseille, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While many fields have contributed to biological physics, nanotechnology offers a new scale of observation. High-speed atomic force microscopy (HS-AFM) provides nanometre structural information and dynamics with subsecond resolution of biological systems. Moreover, HS-AFM allows us to measure piconewton forces within microseconds giving access to unexplored, fast biophysical processes. Thus, HS-AFM provides a tool to nourish biological physics through the observation of emergent physical phenomena in biological systems. In this review, we present an overview of the contribution of HS-AFM, both in imaging and force spectroscopy modes, to the field of biological physics. We focus on examples in which HS-AFM observations on membrane remodelling, molecular motors or the unfolding of proteins have stimulated the development of novel theories or the emergence of new concepts. We finally provide expected applications and developments of HS-AFM that we believe will continue contributing to our understanding of nature, by serving to the dialogue between biology and physics. This article is part of a discussion meeting issue 'Dynamic

Indexed as

Biophysical PhenomenaBiophysicsCell MembraneComputer SimulationIntrinsically Disordered ProteinsMembrane ProteinsMicroscopy, Atomic ForceModels, MolecularMolecular Motor ProteinsNanotechnologyProtein FoldingSingle Molecule ImagingSystems BiologyIntrinsically Disordered ProteinsMembrane ProteinsMolecular Motor Proteinsbiophysicscellshigh-speed force spectroscopymembranesproteinssingle molecules

Identifiers

PMID33100165
PMCPMC7661283
OpenAlexW3093943138

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.