Evidence map›Paper›PMID 10688657›Full record

ArticleMolecular and cellular biology2000

Cloning of a mammalian transcriptional activator that binds unmethylated CpG motifs and shares a CXXC domain with DNA methyltransferase, human trithorax, and methyl-CpG binding domain protein 1.

K S Voo, D L Carlone, B M Jacobsen, A Flodin, D G Skalnik

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
2.6field-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

102 citing papers in PubMed, 201 citations in OpenAlex.

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  19. Domain Structure of the Dnmt1, Dnmt3a, and Dnmt3b DNA Methyltransferases.Advances in experimental medicine and biology · 2022
    Article
  20. Review

42 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

K S VooHerman B. Wells Center for Pediatric Research, Section of Pediatric Hematology/Oncology, Department of Pediatrics, Indianapolis, Indiana 46202, USA.
D L Carlone
B M Jacobsen
A Flodin
D G Skalnik
Indiana University School of MedicineIndiana University – Purdue University Indianapolis · US

Funding

TRANSCRIPTIONAL REPRESSION AND ACTIVATION BY YY1R01CA058997 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI SHI, YANG · 1993 to 1995
–
NCI NIH HHS CA58997
6 · The paper itself

Abstract

Ligand screening was utilized to isolate a human cDNA that encodes a novel CpG binding protein, human CpG binding protein (hCGBP). This factor contains three cysteine-rich domains, two of which exhibit homology to the plant homeodomain finger domain. A third cysteine-rich domain conforms to the CXXC motif identified in DNA methyltransferase, human trithorax, and methyl-CpG binding domain protein 1. A fragment of hCGBP that contains the CXXC domain binds to an oligonucleotide probe containing a single CpG site, and this complex is disrupted by distinct oligonucleotide competitors that also contain a CpG motif(s). However, hCGBP fails to bind oligonucleotides in which the CpG motif is either mutated or methylated, and it does not bind to single-stranded DNA or RNA probes. Furthermore, the introduction of a CpG dinucleotide into an unrelated oligonucleotide sequence is sufficient to produce a binding site for hCGBP. Native hCGBP is detected as an 88-kDa protein by Western analysis and is ubiquitously expressed. The DNA-binding activity of native hCGBP is apparent in electrophoretic mobility shift assays, and hCGBP trans-activates promoters that contain CpG motifs but not promoters in which the CpG is ablated. These data indicate that hCGBP is a transcriptional activator that recognizes unmethylated CpG dinucleotides, suggesting a role in modulating the expression of genes located within CpG islands.

Indexed as

Drosophila ProteinsGenome, HumanTranscription FactorsAmino Acid SequenceBase SequenceCloning, MolecularDNA-Binding ProteinsDNA, ComplementaryHumansMethyltransferasesMolecular Sequence DataRepressor ProteinsSequence AlignmentSequence AnalysisTrans-ActivatorsDNA-Binding ProteinsDNA, ComplementaryDrosophila ProteinsMBD1 protein, humanMethyltransferasesRepressor ProteinsTrans-ActivatorsTranscription FactorsTrl protein, Drosophila

Identifiers

PMID10688657
PMCPMC110827
OpenAlexW2118916005

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.