Evidence map›Paper›PMID 34390111›Full record

ArticleChembiochem : a European journal of chemical biology2021

Fluorine NMR Spectroscopy Enables to Quantify the Affinity Between DNA and Proteins in Cell Lysate.

Hannah Welte, Pia Sinn, Michael Kovermann

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Quantifying Ligand-to-Protein Distances in Complex Environments Using IntermolecularChembiochem : a European journal of chemical biology · 2026
    Article
  2. 2'-Frontiers in molecular biosciences · 2024
    Article
  3. What remains from living cells in bacterial lysate-based cell-free systems.Computational and structural biotechnology journal · 2023
    Review
  4. 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.

Hannah WelteDepartment of Chemistry, University of Konstanz, Universitätsstrasse 10, 78467, Konstanz, Germany.
Pia SinnDepartment of Chemistry, University of Konstanz, Universitätsstrasse 10, 78467, Konstanz, Germany.
Michael KovermannDepartment of Chemistry, University of Konstanz, Universitätsstrasse 10, 78467, Konstanz, Germany.
University of Konstanz · DE

Funding

Deutsche Forschungsgemeinschaft KO4687/4-1
6 · The paper itself

Abstract

The determination of the binding affinity quantifying the interaction between proteins and nucleic acids is of crucial interest in biological and chemical research. Here, we have made use of site-specific fluorine labeling of the cold shock protein from Bacillus subtilis, BsCspB, enabling to directly monitor the interaction with single stranded DNA molecules in cell lysate. High-resolution

Indexed as

Bacillus subtilisBacterial ProteinsDNAFluorine-19 Magnetic Resonance ImagingHeat-Shock ProteinsModels, MolecularSpectrometry, FluorescenceBacterial Proteinscold shock protein, BacillusDNAHeat-Shock Proteinscell lysateNMR spectroscopyprotein folding

Identifiers

PMID34390111
PMCPMC8596521
OpenAlexW3187169536

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.