Evidence map›Paper›PMID 14535848›Full record

ArticleThe Biochemical journal2004

A membrane proximal region of the integrin alpha5 subunit is important for its interaction with nischarin.

Suresh K Alahari, Hani Nasrallah

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
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  6. Article
  7. Effect of ITGA5 down-regulation on the migration capacity of human dental pulp stem cells.International journal of clinical and experimental pathology · 2015
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  11. Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

2 authors at 1 institution in 1 country.

Suresh K AlahariDepartment of Pharmacology, University of North Carolina School of Medicine, Chapel Hill, NC 27599-7365, USA. alahari@med.unc.edu
Hani Nasrallah
University of North Carolina at Chapel Hill · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In a previous study [Alahari, Lee and Juliano (2000) J. Cell Biol. 151, 1141-1154], we have identified a novel protein, nischarin, that specifically interacts with the cytoplasmic tail of the alpha5 integrin subunit. Overexpression of this protein profoundly affects cell migration. To examine the nischarin-alpha5 interaction in detail, and to find the minimal region required for the interaction, several mutants of nischarin and alpha5 were created. The results obtained for the yeast two-hybrid system indicate that a 99-aminoacid region of nischarin (from residues 464 to 562) is indispensable for the interaction. Also, we demonstrate that the membrane proximal region (from residues 1017 to 1030) of the alpha5 cytoplasmic tail is essential for the interaction. To characterize more directly the properties of the interaction between nischarin and alpha5, we performed surface-plasmon resonance studies in which peptides were immobilized on the surface of a sensor chip, and the recombinant nischarin protein fragments were injected. Consistent with the two-hybrid results, recombinant nischarin binds well to immobilized alpha5 peptides. In addition, mutational analysis revealed that residues Tyr(1018) and Lys(1022) are crucial for alpha5-nischarin interactions. These results provide evidence that nischarin is capable of directly and selectively binding to a portion of the alpha5 cytoplasmic domain. Further studies demonstrated that the minimal alpha5 binding region of nischarin does not affect cell migration.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalorimetryCell MovementCHO CellsCricetinaeIntegrin alpha5Intracellular Signaling Peptides and ProteinsMembrane ProteinsMolecular Sequence DataProteinsProtein Structure, TertiaryProtein SubunitsSequence AlignmentSequence DeletionIntegrin alpha5Intracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsProtein Subunits

Identifiers

PMID14535848
PMCPMC1223876
OpenAlexW1997487584

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.