Evidence map›Paper›PMID 15277685›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Discriminatory aptamer reveals serum response element transcription regulated by cytohesin-2.

Mirko G Theis, Alexander Knorre, Bettina Kellersch, Jörg Moelleken, Felix Wieland, Waldemar Kolanus, Michael Famulok

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 63 citations in OpenAlex.

  1. Therapeutic Potential of Aptamer-Protein Interactions.ACS pharmacology & translational science · 2022
    Review
  2. An overview and future prospects on aptamers for food safety.Applied microbiology and biotechnology · 2020
    Review
  3. Aptamers as Valuable Molecular Tools in Neurosciences.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Review
  4. Selective aptamer-based control of intraneuronal signaling.Angewandte Chemie (International ed. in English) · 2015
    Article
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  8. Cell-specific aptamers as emerging therapeutics.Journal of nucleic acids · 2011
    Article
  9. Aptamers as therapeutics.Nature reviews. Drug discovery · 2010
    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

7 authors at 2 institutions in 1 country.

Mirko G TheisKekulé Institut für Organische Chemie und Biochemie, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany.
Alexander Knorre
Bettina Kellersch
Jörg Moelleken
Felix Wieland
Waldemar Kolanus
Michael Famulok
Heidelberg University · DEUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytohesins are a family of highly homologous guanine nucleotide exchange factors (GEFs) that act on ADP-ribosylation factors (ARFs). The small ARF-GEFs are involved in integrin signaling, actin cytoskeleton remodeling, and vesicle transport. Here, we selected and applied a specific inhibitor for ARF nucleotide-binding site opener (ARNO)/cytohesin-2, an RNA aptamer that clearly discriminates between cytohesin-1 and cytohesin-2. This reagent bound to an N-terminal segment of cytohesin-2 and did not inhibit ARF-GEF function in vitro. When transfected into HeLa cells, it persisted for at least 6 h without requiring stabilization. Its effect in vivo was to down-regulate gene expression mediated through the serum-response element and knockdown mitogen-activated protein kinase activation, indicating that cytohesin-2 acts by means of mitogen-activated protein kinase signaling. We conclude that the N-terminal coiled-coil and parts of the Sec7 domain of cytohesin-2 are required for serum-mediated transcriptional activation in nonimmune cells, whereas cytohesin-1 is not. Our results indicate that intramer technology can be used not only for assigning novel biological functions to proteins or protein domains but also to prove nonredundancy of highly homologous proteins.

Indexed as

ADP-Ribosylation FactorsBase SequenceCell Adhesion MoleculesGene ExpressionGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsHeLa CellsHumansMAP Kinase Signaling SystemMolecular Sequence DataProtein Structure, TertiaryRNASerum Response ElementTranscriptional ActivationTranscription, GeneticADP-Ribosylation FactorsCell Adhesion Moleculescytohesin-1cytohesin-2GTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsRNASec7 guanine nucleotide exchange factors

Identifiers

PMID15277685
PMCPMC509187
OpenAlexW2018872864

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.