Evidence map›Paper›PMID 35454182›Full record

ArticleBiomolecules2022

Molecular Recognition of Proteins through Quantitative Force Maps at Single Molecule Level.

Carlos Marcuello, Rocío de Miguel, Anabel Lostao

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
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  13. Visualizing Intramolecular Dynamics of Membrane Proteins.International journal of molecular sciences · 2022
    Review
  14. Imaging the Infection Cycle of T7 at the Single Virion Level.International journal of molecular sciences · 2022
    Article
  15. Article
  16. Protein-Protein Interaction Prediction for Targeted Protein Degradation.International journal of molecular sciences · 2022
    Article
  17. 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.

Carlos MarcuelloInstituto de Nanociencia y Materiales de Aragón (INMA), CSIC-Universidad de Zaragoza, 50018 Zaragoza, Spain.ORCID 0000-0003-3459-8605
Rocío de MiguelInstituto de Nanociencia y Materiales de Aragón (INMA), CSIC-Universidad de Zaragoza, 50018 Zaragoza, Spain.
Anabel LostaoInstituto de Nanociencia y Materiales de Aragón (INMA), CSIC-Universidad de Zaragoza, 50018 Zaragoza, Spain.ORCID 0000-0001-7460-5916
Universidad de Zaragoza · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intermittent jumping force is an operational atomic-force microscopy mode that produces simultaneous topography and tip-sample maximum-adhesion images based on force spectroscopy. In this work, the operation conditions have been implemented scanning in a repulsive regime and applying very low forces, thus avoiding unspecific tip-sample forces. Remarkably, adhesion images give only specific rupture events, becoming qualitative and quantitative molecular recognition maps obtained at reasonably fast rates, which is a great advantage compared to the force-volume modes. This procedure has been used to go further in discriminating between two similar protein molecules, avidin and streptavidin, in hybrid samples. The adhesion maps generated scanning with biotinylated probes showed features identified as avidin molecules, in the range of 40-80 pN; meanwhile, streptavidin molecules rendered 120-170 pN at the selected working conditions. The gathered results evidence that repulsive jumping force mode applying very small forces allows the identification of biomolecules through the specific rupture forces of the complexes and could serve to identify receptors on membranes or samples or be applied to design ultrasensitive detection technologies.

Indexed as

AvidinMicroscopy, Atomic ForceStreptavidinAvidinStreptavidinadhesion mapsatomic force microscopyjumping modemolecular recognition imagingprotein detectionprotein:ligand interactionsrupture forcesingle molecule

Identifiers

PMID35454182
PMCPMC9024611
OpenAlexW4224273580

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.