Evidence map›Paper›PMID 39028512›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Atomic Force Microscopy Characterization of Reconstituted Protein-DNA Complexes.

Marc Kenneth M Cajili, Eloise I Prieto

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. 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. 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

2 authors.

Marc Kenneth M CajiliLeiden Institute of Chemistry, Leiden University, Leiden, Netherlands.
Eloise I PrietoNational Institute of Molecular Biology and Biotechnology, University of the Philippines, Quezon City, Philippines. eiprieto@up.edu.ph.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atomic force microscopy is a high-resolution imaging technique useful for observing the structures of biomolecular complexes. This approach provides a straightforward method to characterize the binding behavior of different chromatin architectural proteins and to analyze the increasingly complex structural units assembled on the DNA. The protocol describes the preparation, AFM imaging, and structural analysis of chromatin that is reconstituted in vitro using purified proteins and DNA. Here, we describe the successful application of the method on the chromatin architectural proteins of the archaeon Sulfolobus solfataricus.

Indexed as

DNAMicroscopy, Atomic ForceSulfolobus solfataricusArchaeal ProteinsChromatinDNA-Binding ProteinsProtein BindingArchaeal ProteinsChromatinDNADNA-Binding ProteinsArchaeaAtomic force microscopyChromatinChromatin reconstitutionNucleoidNucleoid-associated protein (NAP)

Identifiers

PMID39028512

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.