Evidence map›Paper›PMID 1955455›Full record

ArticleThe Journal of cell biology1991

Radixin is a novel member of the band 4.1 family.

N Funayama, A Nagafuchi, N Sato, S Tsukita, S Tsukita

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 166 citations in OpenAlex.

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  10. Gephyrin, the enigmatic organizer at GABAergic synapses.Frontiers in cellular neuroscience · 2012
    Article
  11. Review
  12. Review
  13. Novel insights of the gastric gland organization revealed by chief cell specific expression of moesin.American journal of physiology. Gastrointestinal and liver physiology · 2009
    Article
  14. ERM proteins regulate growth cone responses to Sema3A.The Journal of comparative neurology · 2008
    Article
  15. Article
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  17. Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007
    Article
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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 1 institution in 1 country.

N FunayamaDepartment of Information Physiology, National Institute for Physiological Sciences, Okazaki, Aichi, Japan.
A Nagafuchi
N Sato
S Tsukita
S Tsukita
National Institute for Physiological Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Radixin is an actin barbed-end capping protein which is highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively (Tsukita, Sa., Y. Hieda, and Sh. Tsukita. 1989 a.J. Cell Biol. 108:2369-2382; Sato, N., S. Yonemura, T. Obinata, Sa. Tsukita, and Sh. Tsukita. 1991. J. Cell Biol. 113:321-330). To further understand the structure and functions of the radixin molecule, we isolated and sequenced the cDNA clones encoding mouse radixin. Direct peptide sequencing of radixin and immunological analysis with antiserum to a fusion protein were performed to confirm that the protein encoded by these clones is identical to radixin. The composite cDNA is 4,241 nucleotides long and codes for a 583-amino acid polypeptide with a calculated molecular mass of 68.5 kD. Sequence analysis has demonstrated that mouse radixin shares 75.3% identity with human ezrin, which was reported to be a member of the band 4.1 family. We then isolated the cDNA encoding mouse ezrin. Sequence analysis and Northern blot analysis revealed that radixin and ezrin are similar but distinct (74.9% identity), leading us to conclude that radixin is a novel member of the band 4.1 family. In erythrocytes the band 4.1 protein acts as a key protein in the association of short actin filaments with a plasma membrane protein (glycophorin), together with spectrin. Therefore, the sequence similarity between radixin and band 4.1 protein described in this study favors the idea that radixin plays a crucial role in the association of the barbed ends of actin filaments with the plasma membrane in the cell-to-cell adherens junction and the cleavage furrow.

Indexed as

Cytoskeletal ProteinsNeuropeptidesAmino Acid SequenceAnimalsBase SequenceBlood ProteinsDNAEzrinFluorescent Antibody TechniqueHumansImmunoblottingMembrane ProteinsMiceMolecular Sequence DataPhosphoproteinsRestriction MappingBlood ProteinsCytoskeletal ProteinsDNAerythrocyte membrane band 4.1 proteinerythrocyte membrane protein band 4.1-like 1EzrinMembrane ProteinsNeuropeptidesPhosphoproteinsradixin

Identifiers

PMID1955455
PMCPMC2289953
OpenAlexW2107151898

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.