Evidence map›Paper›PMID 18238776›Full record

ArticleThe Journal of biological chemistry2008

Two DNA-binding and nick recognition modules in human DNA ligase III.

Elizabeth Cotner-Gohara, In-Kwon Kim, Alan E Tomkinson, Tom Ellenberger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

46 citing papers in PubMed, 61 citations in OpenAlex.

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  15. Biomolecular NMR assignments · 2019
    Article
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  20. Enzyme-guided DNA Sewing Architecture.Scientific reports · 2015
    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

4 authors at 2 institutions in 1 country.

Elizabeth Cotner-GoharaBiological and Biomedical Sciences Program, Harvard Medical School, Boston, Massachusetts 02115, USA.
In-Kwon Kim
Alan E Tomkinson
Tom Ellenberger
Washington University in St. Louis · USUniversity of Maryland, Baltimore · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Gregory L Hura · 2001 to 2026
$89.6M
Roles of LIG3 and XRCC1 genes in genome stability.R01ES012512 · NIEHS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Alan E Tomkinson · 2004 to 2026
$6.3M
NCI NIH HHS P01 CA092584NIEHS NIH HHS ES12512NIGMS NIH HHS GM52504
6 · The paper itself

Abstract

Human DNA ligase III contains an N-terminal zinc finger domain that binds to nicks and gaps in DNA. This small domain has been described as a DNA nick sensor, but it is not required for DNA nick joining activity in vitro. In light of new structural information for mammalian ligases, we measured the DNA binding affinity and specificity of each domain of DNA ligase III. These studies identified two separate, independent DNA-binding modules in DNA ligase III that each bind specifically to nicked DNA over intact duplex DNA. One of these modules comprises the zinc finger domain and DNA-binding domain, which function together as a single DNA binding unit. The catalytic core of ligase III is the second DNA nick-binding module. Both binding modules are required for ligation of blunt ended DNA substrates. Although the zinc finger increases the catalytic efficiency of nick ligation, it appears to occupy the same binding site as the DNA ligase III catalytic core. We present a jackknife model for ligase III that posits conformational changes during nick sensing and ligation to extend the versatility of the enzyme.

Indexed as

Amino Acid SequenceBiochemistryCatalytic DomainCloning, MolecularDNADNA Ligase ATPDNA LigasesGene DeletionHumansKineticsModels, MolecularMolecular Sequence DataPoly-ADP-Ribose Binding ProteinsProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidDNADNA Ligase ATPDNA ligase III alpha protein, XenopusDNA LigasesLIG3 protein, humanPoly-ADP-Ribose Binding ProteinsXenopus Proteins

Identifiers

PMID18238776
PMCPMC2447648
OpenAlexW2089568056

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.