Evidence map›Paper›PMID 31485633›Full record

ArticleMolecular medicine reports2019

DNA‑PKcs PARylation regulates DNA‑PK kinase activity in the DNA damage response.

Yang Han, Feng Jin, Ying Xie, Yike Liu, Sai Hu, Xiao-Dan Liu, Hua Guan, Yongqing Gu, Teng Ma, Ping-Kun Zhou

Open access · hybridAbstract read
In one paragraph

Article in Molecular medicine reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

24 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  14. Targeting DNA-PK.Cancer treatment and research · 2023
    Article
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  16. Review
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  19. Characterization of the interactome profiling ofFrontiers in microbiology · 2022
    Article
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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

10 authors at 2 institutions in 1 country.

Yang HanInstitute for Environmental Medicine and Radiation Hygiene, School of Public Health, University of South China, Hengyang, Hunan 421001, P.R. China.
Feng JinDepartment of Radiation Biology, Beijing Key Laboratory for Radiobiology, Beijing Institute of Radiation Medicine, Beijing 100850, P.R. China.
Ying XieDepartment of Radiation Biology, Beijing Key Laboratory for Radiobiology, Beijing Institute of Radiation Medicine, Beijing 100850, P.R. China.
Yike LiuDepartment of Radiation Biology, Beijing Key Laboratory for Radiobiology, Beijing Institute of Radiation Medicine, Beijing 100850, P.R. China.
Sai HuInstitute for Environmental Medicine and Radiation Hygiene, School of Public Health, University of South China, Hengyang, Hunan 421001, P.R. China.
Xiao-Dan LiuDepartment of Radiation Biology, Beijing Key Laboratory for Radiobiology, Beijing Institute of Radiation Medicine, Beijing 100850, P.R. China.
Hua GuanDepartment of Radiation Biology, Beijing Key Laboratory for Radiobiology, Beijing Institute of Radiation Medicine, Beijing 100850, P.R. China.
Yongqing GuDepartment of Radiation Biology, Beijing Key Laboratory for Radiobiology, Beijing Institute of Radiation Medicine, Beijing 100850, P.R. China.
Teng MaDepartment of Radiation Biology, Beijing Key Laboratory for Radiobiology, Beijing Institute of Radiation Medicine, Beijing 100850, P.R. China.
Ping-Kun ZhouDepartment of Radiation Biology, Beijing Key Laboratory for Radiobiology, Beijing Institute of Radiation Medicine, Beijing 100850, P.R. China.
Beijing Radiation Center · CNUniversity of South China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA‑dependent protein kinase catalytic subunit (‑PKcs) is the core protein involved in the non‑homologous end‑joining repair of double‑strand breaks. In addition, it can form a complex with poly(ADP‑ribose) polymerase 1 (PARP1), which catalyzes protein PARylation. However, it is unclear how DNA‑PKcs interacts with PARP1 in the DNA damage response and how PARylation affects DNA‑PK kinase activity. Using immunoprecipitation, immunofluorescence and flow cytometry the present study found that DNA‑PKcs was PARylated after DNA damage, and the PARP1/2 inhibitor olaparib completely abolished DNA‑PKcs PARylation. Olaparib treatment prevented DNA‑PKcs protein detachment from chromatin after DNA damage and maintained DNA‑PK activation, as evidenced by DNA‑PKcs Ser2056 phosphorylation. Furthermore, olaparib treatment synergized with DNA‑PK inhibition to suppress cell survival. All of the above results are suggestive of the important role of DNA‑PKcs PARylation in regulating DNA‑PK activity.

Indexed as

DNA DamagePoly ADP RibosylationDNA-Activated Protein KinaseDNA RepairHeLa CellsHumansNeoplasmsPoly (ADP-Ribose) Polymerase-1DNA-Activated Protein KinasePARP1 protein, humanPoly (ADP-Ribose) Polymerase-1PRKDC protein, human

Identifiers

PMID31485633
PMCPMC6755157
OpenAlexW2971836713

What OpenQuestion holds

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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.