Evidence map›Paper›PMID 35023106›Full record

ReviewAdvances in experimental medicine and biology2021

Force Spectroscopy in Mechanical Protein Domains Unfolding.

Dionysios G Cheirdaris

Abstract readReview
PubMed Publisher
In one paragraph

Review in Advances in experimental medicine and biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

1 author.

Dionysios G CheirdarisDepartment of Informatics, Ionian University, Kerkira, Greece. hirdarisd@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single molecule force spectroscopy (SMFS) has emerged since the past few years as a prominent set of techniques, within the broader field of atomic force microscopy (AFM), for the study of interactions and binding forces of individual protein molecules. Since force spectroscopy measures the behavior of a molecule when stretching or torsional mechanical force is applied, it can be an excellent tool in the hands of researchers who study protein folding and misfolding mechanisms, by reverse engineering the forced unfolding. Such studies could be of crucial importance in the field of protein-related diseases. In this review we wish to provide a glimpse at SMFS concept and recent advances, paired with the protein misfolding issue in neurodegenerative diseases.

Indexed as

Protein FoldingSingle Molecule ImagingMicroscopy, Atomic ForceProtein DomainsProtein UnfoldingSpectrum AnalysisForce spectroscopyMechanical protein unfoldingNeurodegenerative diseases

Identifiers

PMID35023106

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.