Evidence map›Paper›PMID 11058104›Full record

ArticleNucleic acids research2000

The yeast CDP1 gene encodes a triple-helical DNA-binding protein.

M Musso, G Bianchi-Scarrà, M W Van Dyke

Abstract read
In one paragraph

Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 33 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

3 authors at 1 institution in 1 country.

M MussoDipartimento di Oncologia, Biologia e Genetica, Sezione di Biologia e Genetica, Università degli Studi di Genova, viale Benedetto XV, 6., 16132 Genova, Italy.
G Bianchi-Scarrà
M W Van Dyke
University of Genoa · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formation of triple-helical DNA has been implicated in several cellular processes, including transcription, replication and recombination. While there is no direct evidence for triplexes in vivo, cellular proteins that specifically recognize triplex DNA have been described. Using a purine-motif triplex probe and southwestern library screening, we isolated five independent clones expressing the same C-terminal 210 amino acids of the Saccharomyces cerevisiae protein Cdp1p fused with beta-galactosidase. In electrophoretic mobility shift assays, recombinant Cdp1pDelta1-867 bound Pu-motif triplex DNAs with high affinity (K:(d) approximately 5 nM) and bound Py-motif triplex, duplex and single-stranded DNAs with far lower affinity (0.5-5.0 microM). Genetic analyses revealed that the CDP1 gene product was required for proper chromosome segregation. The possible involvement of triplex DNA in this process is discussed.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid MotifsAmino Acid SequenceBase SequenceBinding, CompetitiveCell Cycle ProteinsCell DivisionChromosome SegregationCloning, MolecularDNADNA-Binding ProteinsDNA ProbesFungal ProteinsGenomic LibraryMolecular Sequence DataOligodeoxyribonucleotidesCell Cycle ProteinsCTR9 protein, S cerevisiaeDNADNA-Binding ProteinsDNA ProbesFungal ProteinsOligodeoxyribonucleotidesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscriptional Elongation Factorstriplex DNA

Identifiers

PMID11058104
PMCPMC113150
OpenAlexW2135400048

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.