Evidence map›Paper›PMID 1332978›Full record

ArticleThe Journal of cell biology1992

Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins.

N Imamoto, Y Matsuoka, T Kurihara, K Kohno, M Miyagi, F Sakiyama, Y Okada, S Tsunasawa, Y Yoneda

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
9.2field-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

44 citing papers in PubMed, 177 citations in OpenAlex.

  1. Article
  2. Identification of HSPA8 as an interacting partner of MAB21L2 and an important factor in eye development.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
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  14. Review
  15. Nucleocytoplasmic transport of macromolecules.Microbiology and molecular biology reviews : MMBR · 1997
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

9 authors at 1 institution in 1 country.

N ImamotoInstitute for Molecular and Cellular Biology, Osaka University, Japan.
Y Matsuoka
T Kurihara
K Kohno
M Miyagi
F Sakiyama
Y Okada
S Tsunasawa
Y Yoneda
Osaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previously, we found that anti-DDDED antibodies strongly inhibited in vivo nuclear transport of nuclear proteins and that these antibodies recognized a protein of 69 kD (p69) from rat liver nuclear envelopes that showed specific binding activities to the nuclear location sequences (NLSs) of nucleoplasmin and SV-40 large T-antigen. Here we identified this protein as the 70-kD heat shock cognate protein (hsc70) based on its mass, isoelectric point, cellular localization, and partial amino acid sequences. Competition studies indicated that the recombinant hsc70 expressed in Escherichia coli binds to transport competent SV-40 T-antigen NLS more strongly than to the point mutated transport incompetent mutant NLS. To investigate the possible involvement of hsc70 in nuclear transport, we examined the effect of anti-hsc70 rabbit antibodies on the nuclear accumulation of karyophilic proteins. When injected into the cytoplasm of tissue culture cells, anti-hsc70 strongly inhibited the nuclear import of nucleoplasmin, SV-40 T-antigen NLS bearing BSA and histone H1. In contrast, anti-hsc70 IgG did not prevent the diffusion of lysozyme or 17.4-kD FITC-dextran into the nuclei. After injection of these antibodies, cells continued RNA synthesis and were viable. These results indicate that hsc70 interacts with NLS-containing proteins in the cytoplasm before their nuclear import.

Indexed as

HSP70 Heat-Shock ProteinsPhosphoproteinsAmino Acid SequenceAntigens, Viral, TumorBinding, CompetitiveBiological TransportCarrier ProteinsCell CompartmentationCell LineCell NucleusFluorescent Antibody TechniqueHistonesHSC70 Heat-Shock ProteinsHumansIsoelectric PointMolecular Sequence DataAntigens, Viral, TumorCarrier ProteinsHistonesHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPA8 protein, humanHspa8 protein, ratNuclear ProteinsNucleoplasminsPhosphoproteinsProtein Sorting SignalsRecombinant Proteins

Identifiers

PMID1332978
PMCPMC2289726
OpenAlexW2029306713

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LicenceCC BY-NC-SA
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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.