Dynamic Force Spectroscopy for Analysis of Multiple Disulfide-Bonded Protein States.

Laura Moldovan, Lining Arnold Ju

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in

0citing 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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Laura MoldovanSchool of Biomedical Engineering, The University of Sydney, Darlington, NSW, Australia.

Lining Arnold JuSchool of Biomedical Engineering, The University of Sydney, Darlington, NSW, Australia. arnold.ju@sydney.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An emerging concept in chemical biology is that protein function can be regulated by the redox state of disulfide bonds. This chapter describes the dynamic force spectroscopy method for analyzing the redox regulation of distinct disulfide-bonded protein conformations. The main method described in this chapter is the biomembrane force probe (BFP), in which an ultrasoft human red blood cell is used as an ultrasensitive mechanical force probe. The BFP uses a high-speed camera and real-time imaging tracking techniques to characterize a single molecular bond with ~1 pN (10

Indexed as

DisulfidesMicroscopy, Atomic ForceProteinsSpectrum AnalysisAntithrombinsHeparinHumansKineticsOxidation-ReductionProtein BindingProtein ConformationAntithrombinsDisulfidesHeparinProteinsAntithrombinDisulfide bondDynamic force spectroscopyHeparinMass spectrometryMicropipette

Identifiers

PMID42681369

DOI10.1016/j.bpj.2017.10.013

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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.