Evidence map›Paper›PMID 11809804›Full record

ArticleMolecular and cellular biology2002

Unique motif for nucleolar retention and nuclear export regulated by phosphorylation.

Frédéric Catez, Monique Erard, Nathalie Schaerer-Uthurralt, Karine Kindbeiter, Jean-Jacques Madjar, Jean-Jacques Diaz

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Article
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  9. The nucleolus and viral infection.Virologica Sinica · 2010
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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

6 authors.

Frédéric CatezINSERM U369, Faculté de Médecine Lyon-René Théophile Hyacinthe Laennec, 69372 Lyon Cedex 08, France.
Monique Erard
Nathalie Schaerer-Uthurralt
Karine Kindbeiter
Jean-Jacques Madjar
Jean-Jacques Diaz

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By microinjecting purified glutathione S-transferase linked to all or parts of herpes simplex virus type 1 US11 protein into either the nucleus or the cytoplasm, we have demonstrated that this nucleolar protein exhibits a new type of localization signal controlling both retention in nucleoli and export to the cytoplasm. Saturated mutagenesis combined with computer modeling allowed us to draw the fine-structure map of this domain, revealing a new proline-rich motif harboring both activities, which are temperature dependent and regulated by phosphorylation. Finally, crossing the nuclear pore complex from the cytoplasm to the nucleus is an energy-dependent process for US11 protein, while getting to nucleoli through the nucleoplasm is energy independent.

Indexed as

Protein Sorting SignalsActive Transport, Cell NucleusAmino Acid MotifsAmino Acid SequenceCell NucleolusGlutathione TransferaseHeLa CellsHumansMicroinjectionsMicroscopy, FluorescenceModels, MolecularMolecular Sequence DataPhosphorylationProtein Structure, TertiaryRecombinant Fusion ProteinsRNA-Binding ProteinsGlutathione TransferaseProtein Sorting SignalsRecombinant Fusion ProteinsRNA-Binding ProteinsSerum Albumin, BovineUS11 protein, herpesvirusViral Proteins

Identifiers

PMID11809804
PMCPMC134639

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.