Evidence map›Paper›PMID 28853973›Full record

ReviewCell cycle (Georgetown, Tex.)2017

Decoding telomere protein Rap1: Its telomeric and nontelomeric functions and potential implications in diabetic cardiomyopathy.

Yin Cai, Vidya Kandula, Ramoji Kosuru, Xiaodong Ye, Michael G Irwin, Zhengyuan Xia

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Trial
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  3. Fu-Fang-Qi-Di-Hua-Yu-Tang Improves Diabetic Macrovascular Disease via PI3K/AKT Pathway Regulation.Diabetes, metabolic syndrome and obesity : targets and therapy · 2025
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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

6 authors at 1 institution in 1 country.

Yin Caia Department of Anaesthesiology , The University of Hong Kong , Hong Kong SAR , China.
Vidya Kandulaa Department of Anaesthesiology , The University of Hong Kong , Hong Kong SAR , China.
Ramoji Kosurua Department of Anaesthesiology , The University of Hong Kong , Hong Kong SAR , China.
Xiaodong Yea Department of Anaesthesiology , The University of Hong Kong , Hong Kong SAR , China.
Michael G Irwina Department of Anaesthesiology , The University of Hong Kong , Hong Kong SAR , China.
Zhengyuan Xiaa Department of Anaesthesiology , The University of Hong Kong , Hong Kong SAR , China.
University of Hong Kong · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian Rap1, the most conserved telomere-interacting protein, beyond its role within nucleus for the maintenance of telomeric functions, is also well known for its pleiotropic functions in various physiological and pathological conditions associated with metabolism, inflammation and oxidative stress. For all these, nowadays Rap1 is the subject of critical investigations aimed to unveil its molecular signaling pathways and to scrutinize the applicability of its modulation as a promising therapeutic strategy with clinical relevance. However, the underlying intimate mechanisms of Rap1 are not extensively studied, but any modulation of this protein level has been associated with pathologies like inflammation, oxidative stress and deregulated metabolism. This is considerably important in light of the recent discovery of Rap1 modulation in diseases like cancer and cardiac metabolic disorders. In this review, we focus on both the telomeric and nontelomeric functions of Rap1 and its modulation in various health risks, especially on the heart.

Indexed as

DNA RepairTelomere HomeostasisAnimalsDiabetic CardiomyopathiesDNAGene Expression RegulationHumansMetabolic Networks and PathwaysMiceOxidative StressProtein BindingShelterin ComplexSignal TransductionTelomereTelomere-Binding ProteinsDNAShelterin ComplexTelomere-Binding ProteinsTERF2IP protein, humandiabetic cardiomyopathyinflammationmetabolismoxidative stressRap1

Identifiers

PMID28853973
PMCPMC5628636
OpenAlexW2752080178

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.