Evidence map›Paper›PMID 1464327›Full record

ArticleThe EMBO journal1992

A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1.

C Wimmer, V Doye, P Grandi, U Nehrbass, E C Hurt

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

99 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
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  7. YeastThe Journal of biological chemistry · 2017
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39 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 2 countries.

C WimmerEMBL, Heidelberg, Germany.
V Doye
P Grandi
U Nehrbass
E C Hurt
European Bioinformatics Institute · GBEuropean Molecular Biology Organization · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NSP1 is a nuclear pore protein (nucleoporin) essential for cell growth. To identify the components that functionally interact with NSP1 in the living cell, we developed a genetic screen for mutants that are lethal in a genetic background of mutated, but not wild type NSP1. Fourteen synthetic lethal mutants were obtained, belonging to at least four different complementation groups. The genes of two complementation groups, NSP116 and NSP49, were cloned. Like the previously described nucleoporins, these genes encode proteins with many repeat sequences. NSP116 and NSP49, however, contain a new repetitive sequence motif 'GLFG', which classifies them as a subclass of nucleoporins. NSP116 and NSP49, tagged with the IgG binding domain of protein A and expressed in yeast, are located at the nuclear envelope. These data provide in vivo evidence that distinct subclasses of nucleoporins physically interact or share overlapping function in nuclear pore complexes.

Indexed as

Calcium-Binding ProteinsNuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceDNA, FungalFungal ProteinsGenetic Complementation TestMembrane GlycoproteinsMolecular Sequence DataNuclear EnvelopeNuclear ProteinsPlasmidsRestriction MappingSaccharomyces cerevisiaeSequence Homology, Amino AcidCalcium-Binding ProteinsDNA, FungalFungal ProteinsMembrane GlycoproteinsNSP1 protein, S cerevisiaeNuclear Pore Complex Proteinsnuclear pore protein p62Nuclear ProteinsNUP116 protein, S cerevisiaeNUP49 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsStaphylococcal Protein A

Identifiers

PMID1464327
PMCPMC556983
OpenAlexW1490035592

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.