Evidence map›Paper›PMID 24586428›Full record

ArticlePloS one2014

Importin 7 and Nup358 promote nuclear import of the protein component of human telomerase.

Cornelia Frohnert, Saskia Hutten, Sarah Wälde, Annegret Nath, Ralph H Kehlenbach

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

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  4. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
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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

5 authors at 2 institutions in 1 country.

Cornelia FrohnertInstitute of Molecular Biology, Faculty of Medicine, University of Göttingen, Göttingen, Germany.
Saskia HuttenInstitute of Molecular Biology, Faculty of Medicine, University of Göttingen, Göttingen, Germany.
Sarah WäldeInstitute of Molecular Biology, Faculty of Medicine, University of Göttingen, Göttingen, Germany.
Annegret NathInstitute of Molecular Biology, Faculty of Medicine, University of Göttingen, Göttingen, Germany.
Ralph H KehlenbachInstitute of Molecular Biology, Faculty of Medicine, University of Göttingen, Göttingen, Germany.
University of Göttingen · DEInstitute of Molecular Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In actively dividing eukaryotic cells, chromosome ends (telomeres) are subject to progressive shortening, unless they are maintained by the action of telomerase, a dedicated enzyme that adds DNA sequence repeats to chromosomal 3'end. For its enzymatic function on telomeres, telomerase requires nuclear import of its protein component (hTERT in human cells) and assembly with the RNA component, TERC. We now confirm a major nuclear localization signal (NLS) in the N-terminal region of hTERT and describe a novel one in the C-terminal part. Using an siRNA approach to deplete several import receptors, we identify importin 7 as a soluble nuclear transport factor that is required for efficient import. At the level of the nuclear pore complex (NPC), Nup358, a nucleoporin that forms the cytoplasmic filaments of the NPC, plays an important role in nuclear import of hTERT. A structure-function analysis of Nup358 revealed that the zinc finger region of the nucleoporin is of particular importance for transport of hTERT. Together, our study sheds light on the nuclear import pathway of hTERT.

Indexed as

Active Transport, Cell NucleusFluorescent Antibody TechniqueHeLa CellsHumansImmunoprecipitationKaryopherinsMolecular ChaperonesNuclear Localization SignalsNuclear Pore Complex ProteinsReceptors, Cytoplasmic and NuclearRNA InterferenceRNA, Small InterferingTelomeraseIPO7 protein, humanKaryopherinsMolecular ChaperonesNuclear Localization SignalsNuclear Pore Complex Proteinsran-binding protein 2Receptors, Cytoplasmic and NuclearRNA, Small InterferingTelomerase

Identifiers

PMID24586428
PMCPMC3930611
OpenAlexW1979247529

What OpenQuestion holds

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LicenceCC BY
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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.