Evidence map›Paper›PMID 7724562›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif.

A L Beddow, S A Richards, N R Orem, I G Macara

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. RanBPM, a scaffolding protein for gametogenesis.Current topics in developmental biology · 2013
    Review
  10. Article
  11. RanBPM is essential for mouse spermatogenesis and oogenesis.Development (Cambridge, England) · 2011
    Article
  12. The prospects for designer single-stranded RNA-binding proteins.Nature structural & molecular biology · 2011
    Article
  13. Review
  14. RanBPM, a scaffolding protein in the immune and nervous systems.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2007
    Review
  15. Article
  16. Review
  17. Article
  18. 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

4 authors at 1 institution in 1 country.

A L BeddowDepartment of Pathology, University of Vermont College of Medicine, Burlington 05405-0068, USA.
S A Richards
N R Orem
I G Macara
University of Vermont · US

Funding

The RAN GTPaseR01GM050526 · NIGMS · VANDERBILT UNIVERSITY · PI MACARA, IAN G · 1994 to 2014
$4.8M
NIGMS NIH HHS GM50526
6 · The paper itself

Abstract

Ran/TC4 is an essential, nuclear GTPase implicated in the initiation of DNA replication, entry into and exit from mitosis, and in nuclear RNA and protein transport through the nuclear pore complex. This diversity of functions suggests that Ran interacts with a large number of down-stream targets. Using an overlay assay, we detected a family of putative target proteins that associate with GTP-bound Ran. The sequence of only one such protein, HTF9a/RanBP1, is known. We have now cloned two additional Ran-binding proteins, allowing identification of a distinctive, highly conserved sequence motif of approximately 150 residues. This motif represents a minimal Ran-binding domain that stabilizes the GTP-bound state of Ran. The isolated domain also functions as a coactivator of Ran-GTPase-activating protein. Mutation of a conserved residue within the Ran-binding domain of HTF9a protein drastically reduced Ran binding. Ran-binding proteins coimmunoprecipitated with epitope-tagged Ran from cell lysates, suggesting that these proteins may associate in vivo. A previously uncharacterized Caenorhabditis elegans gene could encode a protein (96 kDa) possessing two Ran-binding domains. This open reading frame also contains similarities to nucleoporins, suggesting a functional link between Ran and nuclear pore complexes.

Indexed as

Amino Acid SequenceConserved SequenceDNA, ComplementaryGene LibraryGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateHippocampusHumansMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsProtein Bindingran GTP-Binding ProteinRNA-Binding ProteinsSequence Analysis, DNADNA, ComplementaryGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateNerve Tissue ProteinsNuclear Proteinsran-binding protein 1ran GTP-Binding ProteinRNA-Binding Proteins

Identifiers

PMID7724562
PMCPMC42159
OpenAlexW1995247882

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.