Evidence map›Paper›PMID 26921193›Full record

ArticleOncotarget2016

PARP activation promotes nuclear AID accumulation in lymphoma cells.

Sandra Tepper, Julia Jeschke, Katrin Böttcher, Angelika Schmidt, Kathrin Davari, Peter Müller, Elisabeth Kremmer, Peter Hemmerich, Ines Pfeil, Berit Jungnickel

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Oncotarget, 2016. 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
0.8field-weighted citation impact, top 25% 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. Review
  2. Article
  3. Article
  4. 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

10 authors at 3 institutions in 1 country.

Sandra TepperDepartment of Cell Biology, Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine, Friedrich-Schiller University, 07745 Jena, Germany.
Julia JeschkeDepartment of Cell Biology, Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine, Friedrich-Schiller University, 07745 Jena, Germany.
Katrin BöttcherDepartment of Cell Biology, Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine, Friedrich-Schiller University, 07745 Jena, Germany.
Angelika SchmidtDepartment of Cell Biology, Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine, Friedrich-Schiller University, 07745 Jena, Germany.
Kathrin DavariDepartment of Cell Biology, Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine, Friedrich-Schiller University, 07745 Jena, Germany.
Peter MüllerDepartment of Cell Biology, Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine, Friedrich-Schiller University, 07745 Jena, Germany.
Elisabeth KremmerInstitute of Molecular Immunology, Helmholtz Center Munich, 81377 Munich, Germany.
Peter HemmerichImaging Facility, Leibniz- Institute on Aging - Fritz Lipmann Institute, 07745 Jena, Germany.
Ines PfeilInstitute of Clinical and Molecular Biology, Helmholtz Center Munich, 81377 Munich, Germany.
Berit JungnickelDepartment of Cell Biology, Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine, Friedrich-Schiller University, 07745 Jena, Germany.
Friedrich Schiller University Jena · DEHelmholtz Zentrum München · DELeibniz Institute on Aging - Fritz Lipmann Institute (FLI) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation-induced cytidine deaminase (AID) initiates immunoglobulin diversification in germinal center B cells by targeted introduction of DNA damage. As aberrant nuclear AID action contributes to the generation of B cell lymphoma, the protein's activity is tightly regulated, e.g. by nuclear/cytoplasmic shuttling and nuclear degradation. In the present study, we asked whether DNA damage may affect regulation of the AID protein. We show that exogenous DNA damage that mainly activates base excision repair leads to prevention of proteasomal degradation of AID and hence its nuclear accumulation. Inhibitor as well as knockout studies indicate that activation of poly (ADP-ribose) polymerase (PARP) by DNA damaging agents promotes both phenomena. These findings suggest that PARP inhibitors influence DNA damage dependent AID regulation, with interesting implications for the regulation of AID function and chemotherapy of lymphoma.

Indexed as

AICDA (Activation-Induced Cytidine Deaminase)AnimalsCell Line, TumorCell NucleusCytidine DeaminaseDNA DamageDNA RepairEnzyme ActivationHumansLymphomaPoly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesAICDA (Activation-Induced Cytidine Deaminase)Cytidine DeaminasePoly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) Polymerasesactivation-induced cytidine deaminaseDNA damagelymphomapoly (ADP-ribose) polymeraseprotein stability

Identifiers

PMID26921193
PMCPMC4914351
OpenAlexW2301095947

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.