Evidence map›Paper›PMID 32784992›Full record

ArticleMolecules (Basel, Switzerland)2020

Generation and Characterization of a DNA-GCN4 Oligonucleotide-Peptide Conjugate: The Impact DNA/Protein Interactions on the Sensitization of DNA.

Paweł Wityk, Rafał Piątek, Robert Nowak, Dorota Kostrzewa-Nowak

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. 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
0.3field-weighted citation impact, top 43% 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, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. X-ray and UV Radiation Damage of dsDNA/Protein Complexes.Molecules (Basel, Switzerland) · 2021
    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 at 2 institutions in 1 country.

Paweł WitykFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland.ORCID 0000-0001-8612-727X
Rafał PiątekFaculty of Chemistry, Gdańsk University of Technology, Narutowicza 11/12, 80-233 Gdańsk, Poland.
Robert NowakCentre for Human Structural and Functional Research, University of Szczecin, 17C Narutowicza St., 70-240 Szczecin, Poland.ORCID 0000-0003-3037-644X
Dorota Kostrzewa-NowakCentre for Human Structural and Functional Research, University of Szczecin, 17C Narutowicza St., 70-240 Szczecin, Poland.ORCID 0000-0001-7025-3087
Gdańsk University of Technology · PLUniversity of Szczecin · PL

Funding

Ministry of Science and Higher Education 0138/DIA/2014/43Ministry of Science and Higher Education 775/FNiTP/127/2013
6 · The paper itself

Abstract

Radiotherapy, the most common therapy for the treatment of solid tumors, exerts its effects by inducing DNA damage. To fully understand the extent and nature of this damage, DNA models that mimic the in vivo situation should be utilized. In a cellular context, genomic DNA constantly interacts with proteins and these interactions could influence both the primary radical processes (triggered by ionizing radiation) and secondary reactions, ultimately leading to DNA damage. However, this is seldom addressed in the literature. In this work, we propose a general approach to tackle these shortcomings. We synthesized a protein-DNA complex that more closely represents DNA in the physiological environment than oligonucleotides solution itself, while being sufficiently simple to permit further chemical analyses. Using click chemistry, we obtained an oligonucleotide-peptide conjugate, which, if annealed with the complementary oligonucleotide strand, forms a complex that mimics the specific interactions between the GCN4 protein and DNA. The covalent bond connecting the oligonucleotide and peptide constitutes a part of substituted triazole, which forms due to the click reaction between the short peptide corresponding to the specific amino acid sequence of GCN4 protein (yeast transcription factor) and a DNA fragment that is recognized by the protein. DNAse footprinting demonstrated that the part of the DNA fragment that specifically interacts with the peptide in the complex is protected from DNAse activity. Moreover, the thermodynamic characteristics obtained using differential scanning calorimetry (DSC) are consistent with the interaction energies calculated at the level of metadynamics. Thus, we present an efficient approach to generate a well-defined DNA-peptide conjugate that mimics a real DNA-peptide complex. These complexes can be used to investigate DNA damage under conditions very similar to those present in the cell.

Indexed as

Amino Acid SequenceBasic-Leucine Zipper Transcription FactorsBinding SitesCalorimetry, Differential ScanningCatalysisChromatography, High Pressure LiquidClick ChemistryCopperDNADNA DamageDNA, Single-StrandedMolecular Dynamics SimulationNucleic Acid ConformationPeptidesProtein DomainsSaccharomyces cerevisiae ProteinsBasic-Leucine Zipper Transcription FactorsCopperDNADNA, Single-StrandedGCN4 protein, S cerevisiaePeptidesSaccharomyces cerevisiae ProteinsDNA-protein interactionsradiotherapysensitizers

Identifiers

PMID32784992
PMCPMC7466028
OpenAlexW3047777854

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.