Evidence map›Paper›PMID 2550792›Full record

ArticleMolecular and cellular biology1989

Identification of four nuclear transport signal-binding proteins that interact with diverse transport signals.

L Yamasaki, P Kanda, R E Lanford

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

43 citing papers in PubMed, 101 citations in OpenAlex.

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  7. Nucleocytoplasmic transport.The Biochemical journal · 1994
    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 1 institution in 1 country.

L YamasakiDepartment of Virology and Immunology, Southwest Foundation for Biomedical Research, San Antonio, Texas.
P Kanda
R E Lanford
Texas Biomedical Research Institute · US

Funding

SV40 T ANTIGEN: MODEL FOR NUCLEAR TRANSPORT OF PROTIENSR01CA039390 · NCI · SOUTHWEST FOUNDATION FOR BIOMEDICAL RES · PI LANFORD, ROBERT E · 1985 to 1991
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NCI NIH HHS CA 39390
6 · The paper itself

Abstract

The transport of proteins into the nucleus requires not only the presence of a nuclear transport signal on the targeted protein but also the signal recognition proteins and the nuclear pore translocation apparatus. Complicating the search for the signal recognition proteins is the fact that the nuclear transport signals identified share little obvious homology. In this study, synthetic peptides homologous to the nuclear transport signals from the simian virus 40 large T antigen, Xenopus oocyte nucleoplasmin, adenovirus E1A, and Saccharomyces cerevisiae MAT alpha 2 proteins were coupled to a UV-photoactivable cross-linker and iodinated for use in an in vitro cross-linking reaction with cellular lysates. Four proteins, p140, p100, p70, and p55, which specifically interacted with the nuclear transport signal peptides were identified. Unique patterns of reactivity were observed with closely related pairs of nuclear transport signal peptides. Competition experiments with labeled and unlabeled peptides demonstrated that heterologous signals were able to bind the same protein and suggested that diverse signals use a common transport pathway. The subcellular distribution of the four nuclear transport signal-binding proteins suggested that nuclear transport involves both cytoplasmic and nuclear receptors. The four proteins were not bound by wheat germ agglutinin and were not associated tightly with the nuclear pore complex.

Indexed as

PhosphoproteinsSignal TransductionAdenovirus Early ProteinsAmino Acid SequenceAnimalsAntigens, Viral, TumorCell NucleusCross-Linking ReagentsMolecular Sequence DataMolecular WeightNuclear ProteinsNucleoplasminsOncogene Proteins, ViralProtein BindingProtein Sorting SignalsRatsAdenovirus Early ProteinsAntigens, Viral, TumorCross-Linking ReagentsNuclear ProteinsNucleoplasminsOncogene Proteins, ViralPhosphoproteinsProtein Sorting SignalsWheat Germ Agglutinins

Identifiers

PMID2550792
PMCPMC362771
OpenAlexW1804528610

What OpenQuestion holds

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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.