Evidence map›Paper›PMID 7798308›Full record

ArticleThe Journal of cell biology1994

Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex.

D A Byrd, D J Sweet, N Panté, K N Konstantinov, T Guan, A C Saphire, P J Mitchell, C S Cooper, U Aebi, L Gerace

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1994. 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
5.2field-weighted citation impact, top 3% 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, 114 citations in OpenAlex.

  1. Article
  2. Article
  3. Distinct roles of nuclear basket proteins in directing the passage of mRNA through the nuclear pore.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  6. Article
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  9. Article
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  11. Review
  12. Nuclear transport and the mitotic apparatus: an evolving relationship.Cellular and molecular life sciences : CMLS · 2010
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Nuclear pore proteins and cancer.Seminars in cell & developmental biology · 2009
    Review
  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

10 authors at 1 institution in 1 country.

D A ByrdDepartment of Cell Biology, Scripps Research Institute, La Jolla, California 92037.
D J Sweet
N Panté
K N Konstantinov
T Guan
A C Saphire
P J Mitchell
C S Cooper
U Aebi
L Gerace
Scripps Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

From a panel of monoclonal antibodies raised against fractions of rat liver nuclear envelopes (NEs), we have identified an antibody, RL30, which reacts with novel nuclear pore complex (NPC) antigens that are not O-glycosylated. By immunofluorescence staining of cultured cells, RL30 reacts exclusively with the NE in a punctate pattern that largely coincides with that of identified NPC proteins. RL30 labels only the cytoplasmic surface of the NPC in immunogold electron microscopy, predominantly in peripheral regions nearby the cytoplasmic ring. In immunoblots of isolated rat liver NEs and cultured rat cells, RL30 recognizes a 265-kD band, as well as a series of 175-265-kD bands in rat liver NEs that are likely to be proteolytic products of p265. Sequencing of peptides from the 175- and 265-kD RL30 antigens of rat liver revealed that they are both closely related to human Tpr, a protein whose amino-terminal 150-250 amino acids appear in oncogenic fusions with the kinase domains of the met, trk, and raf protooncogenes. We found that in vitro translation of human Tpr mRNA yields a major 265-kD band. Considered together, these data indicate that the 265-kD RL30 antigen in the NPC is the rat homologue of Tpr. Interestingly, Tpr contains an exceptionally long predicted coiled coil domain (approximately 1600 amino acids). The localization and predicted structure of Tpr suggest that it is a component of the cytoplasmic fibrils of the NPC implicated in nuclear protein import. Immunofluorescence microscopy shows that during NPC reassembly at the end of mitosis, Tpr becomes concentrated at the NE significantly later than O-linked glycoproteins, including p62. This indicates that reassembly of the NPC after mitosis is a stepwise process, and that the Tpr-containing peripheral structures are assembled later than p62.

Indexed as

Cell CompartmentationCell PolarityAmino Acid SequenceAnimalsArtifactsBase SequenceEnzyme ActivationFluorescent Antibody TechniqueHumansLiverMembrane GlycoproteinsMicroscopy, ImmunoelectronMitosisMolecular Sequence DataNuclear EnvelopeNuclear Pore Complex ProteinsMembrane GlycoproteinsNuclear Pore Complex Proteinsnuclear pore protein p62Protein KinasesProto-Oncogene ProteinsTPR protein, human

Identifiers

PMID7798308
PMCPMC2120283
OpenAlexW2091265469

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.