Evidence map›Paper›PMID 27508268›Full record

ArticleData in brief2016

Single molecule force spectroscopy data and BD- and MD simulations on the blood protein von Willebrand factor.

Sandra Posch, Camilo Aponte-Santamaría, Richard Schwarzl, Andreas Karner, Matthias Radtke, Frauke Gräter, Tobias Obser, Gesa König, Maria A Brehm, Hermann J Gruber and 5 more

Open access · goldAbstract read
In one paragraph

Article in Data in brief, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

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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

15 authors at 7 institutions in 2 countries.

Sandra PoschDepartment of Applied Experimental Biophysics, Institute of Biophysics, Johannes Kepler University, Linz, Austria.
Camilo Aponte-SantamaríaMolecular Biomechanics Group, Heidelberg Institute for Theoretical Studies, Heidelberg, Germany.
Richard SchwarzlDepartment of Physics, FU Berlin, Berlin, Germany.
Andreas KarnerCenter for Advanced Bioanalysis GmbH (CBL), Linz, Austria.
Matthias RadtkeDepartment of Physics, FU Berlin, Berlin, Germany.
Frauke GräterMolecular Biomechanics Group, Heidelberg Institute for Theoretical Studies, Heidelberg, Germany.
Tobias ObserDepartment of Pediatric Hematology and Oncology, University Medical Center Hamburg -Eppendorf, Hamburg, Germany.
Gesa KönigDepartment of Pediatric Hematology and Oncology, University Medical Center Hamburg -Eppendorf, Hamburg, Germany.
Maria A BrehmDepartment of Pediatric Hematology and Oncology, University Medical Center Hamburg -Eppendorf, Hamburg, Germany.
Hermann J GruberDepartment of Applied Experimental Biophysics, Institute of Biophysics, Johannes Kepler University, Linz, Austria.
Roland R NetzDepartment of Physics, FU Berlin, Berlin, Germany.
Carsten BaldaufTheory Department, Fritz-Haber-Institut der Max-Planck-Gesellschaft, Berlin, Germany.
Reinhard SchneppenheimDepartment of Pediatric Hematology and Oncology, University Medical Center Hamburg -Eppendorf, Hamburg, Germany.
Robert TampéInstitute of Biochemistry, Biocenter, Goethe-University Frankfurt, Frankfurt/Main, Germany.
Peter HinterdorferDepartment of Applied Experimental Biophysics, Institute of Biophysics, Johannes Kepler University, Linz, Austria; Center for Advanced Bioanalysis GmbH (CBL), Linz, Austria.
Freie Universität Berlin · DEJohannes Kepler University of Linz · ATHeidelberg Institute for Theoretical Studies · DEUniversität Hamburg · DEUniversity Medical Center Hamburg-Eppendorf · DEFritz Haber Institute of the Max Planck Society · DEGoethe University Frankfurt · DE

Funding

Austrian Science Fund FWF I 2083Austrian Science Fund FWF I 767Austrian Science Fund FWF P 25844
6 · The paper itself

Abstract

We here give information for a deeper understanding of single molecule force spectroscopy (SMFS) data through the example of the blood protein von Willebrand factor (VWF). It is also shown, how fitting of rupture forces versus loading rate profiles in the molecular dynamics (MD) loading-rate range can be used to demonstrate the qualitative agreement between SMFS and MD simulations. The recently developed model by Bullerjahn, Sturm, and Kroy (BSK) was used for this demonstration. Further, Brownian dynamics (BD) simulations, which can be utilized to estimate the lifetimes of intramolecular VWF interactions under physiological shear, are described. For interpretation and discussion of the methods and data presented here, we would like to directly point the reader to the related research paper, "Mutual A domain interactions in the force sensing protein von Willebrand Factor" (Posch et al., 2016) [1].

Indexed as

Atomic force microscopyBrownian dynamics simulationMolecular dynamics simulationSingle molecule force spectroscopyvon Willebrand factor

Identifiers

PMID27508268
PMCPMC4970544
OpenAlexW2489774550

What OpenQuestion holds

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LicenceCC BY
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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.