Evidence map›Paper›PMID 36009419›Full record

ArticleBiomedicines2022

G-Quadruplex Formed by the Promoter Region of the

Anzhela V Pavlova, Victoria Yu Savitskaya, Nina G Dolinnaya, Mayya V Monakhova, Anastasia V Litvinova, Elena A Kubareva, Maria I Zvereva

Open access · goldAbstract read
In one paragraph

Article in Biomedicines, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Position-Dependent Effects of AP Sites Within anInternational journal of molecular sciences · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. International journal of molecular sciences · 2023
    Article
  12. Article
  13. Review
  14. 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

7 authors at 1 institution in 1 country.

Anzhela V PavlovaDepartment of Chemistry, Lomonosov Moscow State University, Leninskye Gory 1, 119991 Moscow, Russia.ORCID 0000-0002-5961-2277
Victoria Yu SavitskayaDepartment of Chemistry, Lomonosov Moscow State University, Leninskye Gory 1, 119991 Moscow, Russia.
Nina G DolinnayaDepartment of Chemistry, Lomonosov Moscow State University, Leninskye Gory 1, 119991 Moscow, Russia.ORCID 0000-0003-1780-813X
Mayya V MonakhovaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskye Gory 1, 119991 Moscow, Russia.ORCID 0000-0002-2582-6226
Anastasia V LitvinovaDepartment of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Leninskye Gory 1, 119991 Moscow, Russia.
Elena A KubarevaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskye Gory 1, 119991 Moscow, Russia.
Maria I ZverevaDepartment of Chemistry, Lomonosov Moscow State University, Leninskye Gory 1, 119991 Moscow, Russia.ORCID 0000-0002-7432-1574
Lomonosov Moscow State University · RU

Funding

Russian Science Foundation 21-14-00161
6 · The paper itself

Abstract

G-quadruplexes (G4s) are a unique class of noncanonical DNAs that play a key role in cellular processes and neoplastic transformation. Herein, we focused on the promoter region of human TERT oncogene, whose product is responsible for the immortality of cancer cells. It has been shown by chemical probing and spectroscopic methods that synthetic 96-nt DNAs modeling the wild-type G-rich strand of the hTERT promoter and its variants with G>A point substitutions corresponding to somatic driver mutations fold into three stacked parallel G4s with sites of local G4 destabilization caused by G>A substitutions in the G4 motif. These models were used to elucidate how the hTERT multiG4 affects the binding affinity and functional responses of two key proteins, MutS and MutL, involved in the initial stage of DNA mismatch repair (MMR) in Escherichiacoli and Neisseriagonorrhoeae with different MMR mechanisms. We have shown for the first time that (i) point substitutions do not affect the effective binding of these proteins to the hTERT G4 structure, and (ii) the endonuclease activity of MutL from N. gonorrhoeae is significantly suppressed by the stable G4 scaffold. It is likely that some of the genomic instability associated with G4 may be related to the blockage of human intrinsic methyl-independent MMR attempting to operate near G4 structures.

Indexed as

DNA mismatch repairG-quadruplexhTERT promoterMutLMutS

Identifiers

PMID36009419
PMCPMC9405553
OpenAlexW4289704646

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.