Evidence map›Paper›PMID 9636166›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export.

T Taura, H Krebber, P A Silver

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Capturing the Asc1p/Molecular & cellular proteomics : MCP · 2017
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  19. The human T-cell leukemia virus Rex protein.Frontiers in bioscience : a journal and virtual library · 2005
    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

3 authors at 2 institutions in 1 country.

T TauraDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and The Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA.
H Krebber
P A Silver
Harvard University · USDana-Farber Cancer Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast cells mutated in YRB2, which encodes a nuclear protein with similarity to other Ran-binding proteins, fail to export nuclear export signal (NES)-containing proteins including HIV Rev out of the nucleus. Unlike Xpo1p/Crm1p/exportin, an NES receptor, Yrb2p does not shuttle between the nucleus and the cytoplasm but instead remains inside the nucleus. However, by both biochemical and genetic criteria, Yrb2p interacts with Xpo1p and not with other members of the importin/karyopherin beta superfamily. Moreover, the Yrb2p region containing nucleoporin-like FG repeats is important for NES-mediated protein export. Taken together, these data suggest that Yrb2p acts inside the nucleus to mediate the action of Xpo1p in at least one of several nuclear export pathways.

Indexed as

KaryopherinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsBiological TransportCarrier ProteinsCell NucleusExportin 1 ProteinFungal ProteinsGTPase-Activating ProteinsNuclear ProteinsProtein BindingSaccharomyces cerevisiaeTranscription FactorsCarrier ProteinsExportin 1 ProteinFungal ProteinsGTPase-Activating ProteinsKaryopherinsNuclear ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsTranscription FactorsYRB2 protein, S cerevisiae

Identifiers

PMID9636166
PMCPMC22639
OpenAlexW2109495138

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.