Molecular basis and quantitative assessment of TRF1 and TRF2 protein interactions with TIN2 and Apollo peptides.

Umesh Kalathiya, Monikaben Padariya, Maciej Baginski

Abstract read

In one paragraph

Article in European biophysics journal : EBJ, 2017. 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

0.6field-weighted citation impact, top 28% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

TRF1 and TRF2: pioneering targets in telomere-based cancer therapy.Journal of cancer research and clinical oncology · 2024
Review

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.

Umesh KalathiyaDepartment of Pharmaceutical Technology and Biochemistry, Faculty of Chemistry, Gdansk University of Technology, Narutowicza St 11/12, 80-233, Gdansk, Poland. umekalat@gmail.com.

Monikaben PadariyaDepartment of Pharmaceutical Technology and Biochemistry, Faculty of Chemistry, Gdansk University of Technology, Narutowicza St 11/12, 80-233, Gdansk, Poland.

Maciej BaginskiDepartment of Pharmaceutical Technology and Biochemistry, Faculty of Chemistry, Gdansk University of Technology, Narutowicza St 11/12, 80-233, Gdansk, Poland.

Gdańsk University of Technology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Shelterin is a six-protein complex (TRF1, TRF2, POT1, RAP1, TIN2, and TPP1) that also functions in smaller subsets in regulation and protection of human telomeres. Two closely related proteins, TRF1 and TRF2, make high-affinity contact directly with double-stranded telomeric DNA and serve as a molecular platform. Protein TIN2 binds to TRF1 and TRF2 dimer-forming domains, whereas Apollo makes interaction only with TRF2. To elucidate the molecular basis of these interactions, we employed molecular dynamics (MD) simulations of TRF1

Indexed as

Molecular Dynamics SimulationDNA Repair EnzymesExodeoxyribonucleasesHumansNuclear ProteinsPeptidesProtein BindingShelterin ComplexTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2ACD protein, humanDCLRE1B protein, humanDNA Repair EnzymesExodeoxyribonucleasesNuclear ProteinsPeptidesShelterin ComplexTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2TERF2 protein, humanTINF2 protein, humanApolloMolecular dynamicsShelterin complexTIN2TRF1TRF2

Identifiers

PMID27450562

DOI10.1007/s00249-016-1157-7

OpenAlexW2499606276

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.