Evidence map›Paper›PMID 11320245›Full record

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

Controlling small guanine-nucleotide-exchange factor function through cytoplasmic RNA intramers.

G Mayer, M Blind, W Nagel, T Böhm, T Knorr, C L Jackson, W Kolanus, M Famulok

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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Targeting the Small GTPase Superfamily through Their Regulatory Proteins.Angewandte Chemie (International ed. in English) · 2020
    Review
  3. Review
  4. Article
  5. Selective aptamer-based control of intraneuronal signaling.Angewandte Chemie (International ed. in English) · 2015
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cell-specific aptamers as emerging therapeutics.Journal of nucleic acids · 2011
    Article
  11. Review
  12. Article
  13. Aptamers as therapeutics.Nature reviews. Drug discovery · 2010
    Review
  14. FRMD4A regulates epithelial polarity by connecting Arf6 activation with the PAR complex.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  15. Article
  16. Article
  17. Article
  18. Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein-protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  19. Article
  20. 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

8 authors at 3 institutions in 2 countries.

G MayerKekulé-Institut für Organische Chemie und Biochemie, Rheinische Friedrich-Wilhelms Universität Bonn, Gerhard-Domagk Strasse 1, D-53121 Bonn, Germany.
M Blind
W Nagel
T Böhm
T Knorr
C L Jackson
W Kolanus
M Famulok
Ludwig-Maximilians-Universität München · DECommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ADP-ribosylation factor (ARF) GTPases and their regulatory proteins have been implicated in the control of diverse biological functions. Two main classes of positive regulatory elements for ARF have been discovered so far: the large Sec7/Gea and the small cytohesin/ARNO families, respectively. These proteins harbor guanine-nucleotide-exchange factor (GEF) activity exerted by the common Sec7 domain. The availability of a specific inhibitor, the fungal metabolite brefeldin A, has enabled documentation of the involvement of the large GEFs in vesicle transport. However, because of the lack of such tools, the biological roles of the small GEFs have remained controversial. Here, we have selected a series of RNA aptamers that specifically recognize the Sec7 domain of cytohesin 1. Some aptamers inhibit guanine-nucleotide exchange on ARF1, thereby preventing ARF activation in vitro. Among them, aptamer M69 exhibited unexpected specificity for the small GEFs, because it does not interact with or inhibit the GEF activity of the related Gea2-Sec7 domain, a member of the class of large GEFs. The inhibitory effect demonstrated in vitro clearly is observed as well in vivo, based on the finding that M69 produces similar results as a dominant-negative, GEF-deficient mutant of cytohesin 1: when expressed in the cytoplasm of T-cells, M69 reduces stimulated adhesion to intercellular adhesion molecule-1 and results in a dramatic reorganization of F-actin distribution. These highly specific cellular effects suggest that the ARF-GEF activity of cytohesin 1 plays an important role in cytoskeletal remodeling events of lymphoid cells.

Indexed as

Saccharomyces cerevisiae ProteinsActinsADP-Ribosylation Factor 1Amino Acid SequenceBase SequenceCell AdhesionCell Adhesion MoleculesCell SizeCytoskeletonFungal ProteinsGuanine Nucleotide Exchange FactorsGuanosine DiphosphateGuanosine TriphosphateHumansIntercellular Adhesion Molecule-1Jurkat CellsActinsADP-Ribosylation Factor 1Cell Adhesion Moleculescytohesin-1Fungal ProteinsGEA2 protein, S cerevisiaeGuanine Nucleotide Exchange FactorsGuanosine DiphosphateGuanosine TriphosphateIntercellular Adhesion Molecule-1RNASaccharomyces cerevisiae ProteinsSec7 guanine nucleotide exchange factorsTetradecanoylphorbol Acetate

Identifiers

PMID11320245
PMCPMC33146
OpenAlexW1979454287

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.