Evidence map›Paper›PMID 32509800›Full record

ReviewFrontiers in molecular biosciences2020

Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.

Byeongseon Yang, Zhaowei Liu, Haipei Liu, Michael A Nash

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

50 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Article
  5. Silanes to Silatranes: Robust Functionalization for Single-Molecule Force Spectroscopy.Chembiochem : a European journal of chemical biology · 2026
    Article
  6. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  7. Physical Changes of Biomacromolecules upon Covalent Surface Immobilization.Langmuir : the ACS journal of surfaces and colloids · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
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  17. Article
  18. Review
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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

4 authors at 1 institution in 1 country.

Byeongseon YangDepartment of Chemistry, University of Basel, Basel, Switzerland.
Zhaowei LiuDepartment of Chemistry, University of Basel, Basel, Switzerland.
Haipei LiuDepartment of Chemistry, University of Basel, Basel, Switzerland.
Michael A NashDepartment of Chemistry, University of Basel, Basel, Switzerland.
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule force spectroscopy with the atomic force microscope provides molecular level insights into protein function, allowing researchers to reconstruct energy landscapes and understand functional mechanisms in biology. With steadily advancing methods, this technique has greatly accelerated our understanding of force transduction, mechanical deformation, and mechanostability within single- and multi-domain polyproteins, and receptor-ligand complexes. In this focused review, we summarize the state of the art in terms of methodology and highlight recent methodological improvements for AFM-SMFS experiments, including developments in surface chemistry, considerations for protein engineering, as well as theory and algorithms for data analysis. We hope that by condensing and disseminating these methods, they can assist the community in improving data yield, reliability, and throughput and thereby enhance the information that researchers can extract from such experiments. These leading edge methods for AFM-SMFS will serve as a groundwork for researchers cognizant of its current limitations who seek to improve the technique in the future for in-depth studies of molecular biomechanics.

Indexed as

AFMmolecular biomechanicsmolecular engineeringprotein stability and foldingsingle-molecule biophysics

Identifiers

PMID32509800
PMCPMC7248566
OpenAlexW3026365268

What OpenQuestion holds

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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.