Evidence map›Paper›PMID 1656223›Full record

ArticleMolecular and cellular biology1991

A hydrophobic protein sequence can override a nuclear localization signal independently of protein context.

K van Zee, F Appel, E Fanning

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026
    Article
  2. Article
  3. Article
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  5. Nucleocytoplasmic transport and snRNP assembly.Molecular biology reports · 1993
    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.

K van ZeeInstitute for Biochemistry, Munich, Germany.
F Appel
E Fanning

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Simian virus 40 T antigen is specifically targeted to the nucleus by the signal Pro-Lys-Lys-128-Lys-Arg-Lys-Val. We have previously described the isolation of a simian virus 40 T-antigen mutant, 676FS, which retains a wild-type nuclear localization signal but fails to accumulate properly in the nucleus and interferes with the nuclear localization of heterologous proteins. Here we report that the hydrophobic carboxy-terminal sequence novel to 676FS T antigen overrides the nuclear localization signal if fused to other proteins, thereby anchoring the proteins in the cytoplasm. We discuss possible mechanisms by which missorting of such a fusion protein could interfere with the nuclear transport of heterologous proteins.

Indexed as

Amino Acid SequenceAntigens, Polyomavirus Transformingbeta-GalactosidaseCell LineCell NucleusFluorescent Antibody TechniqueMolecular Sequence DataMutationNuclear ProteinsProtein Sorting SignalsRecombinant Fusion ProteinsSimian virus 40Antigens, Polyomavirus Transformingbeta-GalactosidaseNuclear ProteinsProtein Sorting SignalsRecombinant Fusion Proteins

Identifiers

PMID1656223
PMCPMC361531
OpenAlexW2138240173

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.