Evidence map›Paper›PMID 33847963›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Atomic Force Microscopy Reveals that the Drosophila Telomere-Capping Protein Verrocchio Is a Single-Stranded DNA-Binding Protein.

Alessandro Cicconi, Emanuela Micheli, Grazia Daniela Raffa, Stefano Cacchione

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 2 countries.

Alessandro CicconiDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, Rome, Italy. alessandro.cicconi@yale.edu.
Emanuela MicheliDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, Rome, Italy.
Grazia Daniela RaffaDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, Rome, Italy.
Stefano CacchioneDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, Rome, Italy. stefano.cacchione@uniroma1.it.
Sapienza University of Rome · ITYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atomic force microscopy (AFM) is a scanning probe technique that allows visualization of biological samples with a nanometric resolution. Determination of the physical properties of biological molecules at a single-molecule level is achieved through topographic analysis of the sample adsorbed on a flat and smooth surface. AFM has been widely used for the structural analysis of nucleic acid-protein interactions, providing insights on binding specificity and stoichiometry of proteins forming complexes with DNA substrates. Analysis of single-stranded DNA-binding proteins by AFM requires specific single-stranded/double-stranded hybrid DNA molecules as substrates for protein binding. In this chapter we describe the protocol for AFM characterization of binding properties of Drosophila telomeric protein Ver using DNA constructs that mimic the structure of chromosome ends. We provide details on the methodology used, including the procedures for the generation of DNA substrates, the preparation of samples for AFM visualization, and the data analysis of AFM images. The presented procedure can be adapted for the structural studies of any single-stranded DNA-binding protein.

Indexed as

AnimalsDNA, Single-StrandedDrosophila melanogasterDrosophila ProteinsMicroscopy, Atomic ForceProtein BindingSingle Molecule ImagingTelomereTelomere-Binding ProteinsDNA, Single-StrandedDrosophila ProteinsTelomere-Binding ProteinsVer protein, DrosophilaAtomic force microscopyBinding position analysisDNA-protein complexSingle-stranded DNATelomeric DNAVerVolume analysis

Identifiers

PMID33847963
OpenAlexW3155916981

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.