Evidence map›Paper›PMID 38094082›Full record

ArticleFrontiers in molecular biosciences2023

Predicting the placement of biomolecular structures on AFM substrates based on electrostatic interactions.

Romain Amyot, Kaho Nakamoto, Noriyuki Kodera, Holger Flechsig

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

Romain AmyotJSPS International Research Fellow, Kanazawa, Ishikawa, Japan.
Kaho NakamotoNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa, Japan.
Noriyuki KoderaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa, Japan.
Holger FlechsigNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atomic force microscopy (AFM) and high-speed AFM allow direct observation of biomolecular structures and their functional dynamics. Based on scanning the molecular surface of a sample deposited on a supporting substrate by a probing tip, topographic images of its dynamic shape are obtained. Critical to successful AFM observations is a balance between immobilization of the sample while avoiding too strong perturbations of its functional conformational dynamics. Since the sample placement on the supporting substrate cannot be directly controlled in experiments, the relative orientation is

Indexed as

AFM (atomic force microscope)electrostatic interactionimage analysisprotein dynamics analysissample placementsoftware application

Identifiers

PMID38094082
PMCPMC10717842

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.