Evidence map›Paper›PMID 33723041›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Modulation of a protein-folding landscape revealed by AFM-based force spectroscopy notwithstanding instrumental limitations.

Devin T Edwards, Marc-Andre LeBlanc, Thomas T Perkins

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. 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
3.2field-weighted citation impact, top 8% 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, 29 citations in OpenAlex.

  1. Article
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  4. Enhancing glucaric acid production fromApplied and environmental microbiology · 2024
    Article
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  6. Review
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  10. Review
  11. Energy landscapes of fast-folding proteins pushing the limits of atomic force microscope (AFM) pulling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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 1 country.

Devin T EdwardsJILA, National Institute of Standards and Technology and University of Colorado Boulder, Boulder, CO 80309.ORCID 0000-0002-2612-9561
Marc-Andre LeBlancJILA, National Institute of Standards and Technology and University of Colorado Boulder, Boulder, CO 80309.ORCID 0000-0002-5520-7389
Thomas T PerkinsJILA, National Institute of Standards and Technology and University of Colorado Boulder, Boulder, CO 80309; tperkins@jila.colorado.edu.ORCID 0000-0003-4826-9490
National Institute of Standards and Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule force spectroscopy is a powerful tool for studying protein folding. Over the last decade, a key question has emerged: how are changes in intrinsic biomolecular dynamics altered by attachment to μm-scale force probes via flexible linkers? Here, we studied the folding/unfolding of α

Indexed as

Models, MolecularProtein FoldingHydrogen-Ion ConcentrationMechanical PhenomenaMicroscopy, Atomic ForceProteinsSingle Molecule ImagingProteinsatomic force microscopyenergy landscapefolding dynamicsforce spectroscopysingle molecule

Identifiers

PMID33723041
PMCPMC8000363
OpenAlexW3136074695

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.