Evidence map›Paper›PMID 16174846›Full record

ArticleNucleic acids research2005

Phosphorylation of human DNA polymerase lambda by the cyclin-dependent kinase Cdk2/cyclin A complex is modulated by its association with proliferating cell nuclear antigen.

Isabelle Frouin, Magali Toueille, Elena Ferrari, Igor Shevelev, Ulrich Hübscher

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.0field-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

23 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  7. Protein phosphatases in chromatin structure and function.Biochimica et biophysica acta. Molecular cell research · 2019
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  17. Regulation of oxidative DNA damage repair by DNA polymerase λ and MutYH by cross-talk of phosphorylation and ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. Review
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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

5 authors at 1 institution in 1 country.

Isabelle FrouinInstitute of Veterinary Biochemistry and Molecular Biology, University of Zürich-Irchel Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
Magali Toueille
Elena Ferrari
Igor Shevelev
Ulrich Hübscher
University of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA polymerase (Pol) lambda is a member of the Pol X family and possesses four different enzymatic activities, being DNA polymerase, terminal transferase, deoxyribose phosphate lyase and polynucleotide synthetase, all localized in its C-terminal region. On the basis of its biochemical properties, Pol lambda has been implicated in various DNA repair pathways, such as abasic site translesion DNA synthesis, base excision repair and non-homologous end joining of double strand breaks. However, its role in vivo has not yet been elucidated. In addition, Pol lambda has been shown to interact with the replication clamp proliferating cell nuclear antigen (PCNA) in vitro and in vivo. In this work, we searched by affinity chromatography for novel partners and we identified the cyclin-dependent kinase Cdk2 as novel partner of Pol lambda. Pol lambda is phosphorylated in vitro by several Cdk/cyclin complexes, including Cdk2/cyclin A, in its proline-serine-rich domain. While the polymerase activity of Pol lambda was not affected by Cdk2/cyclin A phosphorylation, phosphorylation of Pol lambda was decreased by its interaction with PCNA. Finally, Pol lambda is also phosphorylated in vivo in human cells and this phosphorylation is modulated during the cell cycle.

Indexed as

Amino Acid SequenceCDC2-CDC28 KinasesCDC2 Protein KinaseCell CycleCyclin ACyclin-Dependent Kinase 2Cyclin EDNA Polymerase betaHeLa CellsHumansMolecular Sequence DataPhosphorylationProliferating Cell Nuclear AntigenProlineProtein Structure, TertiarySerineCDC2-CDC28 KinasesCDC2 Protein KinaseCDK2 protein, humanCyclin ACyclin-Dependent Kinase 2Cyclin EDNA Polymerase betaDNA polymerase beta2Proliferating Cell Nuclear AntigenProlineSerine

Identifiers

PMID16174846
PMCPMC1226315
OpenAlexW2147277852

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.