Evidence map›Paper›PMID 25077809›Full record

ArticlePloS one2014

Real-time monitoring of protein conformational changes using a nano-mechanical sensor.

Livan Alonso-Sarduy, Paolo De Los Rios, Fabrizio Benedetti, Dusan Vobornik, Giovanni Dietler, Sandor Kasas, Giovanni Longo

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

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  13. Nanomotion detection based on atomic force microscopy cantilevers.Cell surface (Amsterdam, Netherlands) · 2019
    Review
  14. Article
  15. Precision ultrasound sensing on a chip.Nature communications · 2019
    Article
  16. Review
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  18. Article
  19. Detecting nanoscale vibrations as signature of life.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

7 authors at 2 institutions in 2 countries.

Livan Alonso-SarduyLaboratory of Physics of Living Matter, Institute of Physics of Biological Systems, School of Basic Sciences, École polytechnique fédérale de Lausanne, Lausanne, Switzerland.
Paolo De Los RiosLaboratory of Statistical Biophysics, Institute of Theoretical Physics, School of Basic Sciences, École polytechnique fédérale de Lausanne, Lausanne, Switzerland.
Fabrizio BenedettiLaboratory of Physics of Living Matter, Institute of Physics of Biological Systems, School of Basic Sciences, École polytechnique fédérale de Lausanne, Lausanne, Switzerland.
Dusan VobornikLaboratory of Physics of Living Matter, Institute of Physics of Biological Systems, School of Basic Sciences, École polytechnique fédérale de Lausanne, Lausanne, Switzerland.
Giovanni DietlerLaboratory of Physics of Living Matter, Institute of Physics of Biological Systems, School of Basic Sciences, École polytechnique fédérale de Lausanne, Lausanne, Switzerland.
Sandor KasasLaboratory of Physics of Living Matter, Institute of Physics of Biological Systems, School of Basic Sciences, École polytechnique fédérale de Lausanne, Lausanne, Switzerland; Faculty of Biology and Medicine, Department of Fundamental Neurosciences, Lausanne University, Lausanne, Switzerland.
Giovanni LongoLaboratory of Physics of Living Matter, Institute of Physics of Biological Systems, School of Basic Sciences, École polytechnique fédérale de Lausanne, Lausanne, Switzerland; Istituto Superiore di Sanità, Rome, Italy.
École Polytechnique Fédérale de Lausanne · CHIstituto Superiore di Sanità · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins can switch between different conformations in response to stimuli, such as pH or temperature variations, or to the binding of ligands. Such plasticity and its kinetics can have a crucial functional role, and their characterization has taken center stage in protein research. As an example, Topoisomerases are particularly interesting enzymes capable of managing tangled and supercoiled double-stranded DNA, thus facilitating many physiological processes. In this work, we describe the use of a cantilever-based nanomotion sensor to characterize the dynamics of human topoisomerase II (Topo II) enzymes and their response to different kinds of ligands, such as ATP, which enhance the conformational dynamics. The sensitivity and time resolution of this sensor allow determining quantitatively the correlation between the ATP concentration and the rate of Topo II conformational changes. Furthermore, we show how to rationalize the experimental results in a comprehensive model that takes into account both the physics of the cantilever and the dynamics of the ATPase cycle of the enzyme, shedding light on the kinetics of the process. Finally, we study the effect of aclarubicin, an anticancer drug, demonstrating that it affects directly the Topo II molecule inhibiting its conformational changes. These results pave the way to a new way of studying the intrinsic dynamics of proteins and of protein complexes allowing new applications ranging from fundamental proteomics to drug discovery and development and possibly to clinical practice.

Indexed as

Biosensing TechniquesAdenosine TriphosphateAntigens, NeoplasmDNA-Binding ProteinsDNA Topoisomerases, Type IIEnzymes, ImmobilizedHumansMicroscopy, Atomic ForceNanotechnologyProtein ConformationAdenosine TriphosphateAntigens, NeoplasmDNA-Binding ProteinsDNA Topoisomerases, Type IIEnzymes, Immobilized

Identifiers

PMID25077809
PMCPMC4117498
OpenAlexW2029901594

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.