Evidence map›Paper›PMID 11481441›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Activation and autoregulation of DNA-PK from structured single-stranded DNA and coding end hairpins.

S Soubeyrand, H Torrance, W Giffin, W Gong, C Schild-Poulter, R J Haché

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

6 citing papers in PubMed, 26 citations in OpenAlex.

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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.

S SoubeyrandDepartment of Medicine, University of Ottawa, Ottawa Health Research Institute, ON, Canada.
H Torrance
W Giffin
W Gong
C Schild-Poulter
R J Haché
University of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA-dependent protein kinase (DNA-PK) acts through an essential relationship with DNA to participate in the regulation of multiple cellular processes. Yet the role of DNA as a cofactor in kinase activity remains to be completely elucidated. For example, although DNA-PK activity appears to be required for the resolution of hairpin coding ends in variable diversity joining recombination, kinase activity remains to be demonstrated from hairpin ends or other DNA structures. In the present study we report that DNA-PK is strongly activated from hairpin ends and structured single-stranded DNA, but that the phosphorylation of many heterologous substrates is blocked efficiently by inactivation of the kinase through autophosphorylation. However, substrates that bound efficiently to single-stranded DNA such as p53 and replication protein A were efficiently phosphorylated by DNA-PK from structured DNA. DNA-PK also was found to be active toward heterologous substrates from hairpin ends on double-stranded DNA under conditions where autophosphorylation was minimized. These results suggest that the role of DNA-PK in resolving coding end hairpins is likely to be enzymatic rather than structural, expand understanding of how DNA-PK binding to structured DNA relates to enzyme activity, and suggest a mechanism for autoregulatory control of its kinase activity in the cell.

Indexed as

DNA-Binding ProteinsNucleic Acid ConformationBase SequenceDNA-Activated Protein KinaseDNA NucleotidyltransferasesDNA, Single-StrandedEnzyme ActivationHumansMolecular Sequence DataNuclear ProteinsPeptide FragmentsPhosphorylationProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesRecombinant Fusion ProteinsStructure-Activity RelationshipDNA-Activated Protein KinaseDNA-Binding ProteinsDNA NucleotidyltransferasesDNA, Single-StrandedNuclear ProteinsPeptide FragmentsPRKDC protein, humanProtein Serine-Threonine KinasesRecombinant Fusion ProteinsTumor Suppressor Protein p53VDJ Recombinases

Identifiers

PMID11481441
PMCPMC55499
OpenAlexW2103491663

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.