Evidence map›Paper›PMID 20411297›Full record

ReviewCellular and molecular life sciences : CMLS2010

Do we already know how spectrin attracts ankyrin?

Aleksander Czogalla, Aleksander F Sikorski

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Article
  2. Article
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  5. Article
  6. Review
  7. 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

2 authors.

Aleksander CzogallaResearch and Development Centre Novasome Sp. z o.o., 51-423 Wrocław, Poland. aleksander.czogalla@cbr.novasome.pl
Aleksander F Sikorski

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction of ankyrin and spectrin yields the major anchor between the membrane skeleton and the lipid bilayer. It is critical for red cell deformability and stability, and it is also involved in the cellular localization of several proteins, in cell differentiation, and in neuron activity. Therefore, its nature is of great interest, and recently, several researchers have had varying degrees of success in elucidating the structural basis of ankyrin-spectrin recognition. In this short paper, we briefly summarize the data obtained and compare the resulting conclusions.

Indexed as

AnkyrinsErythrocyte DeformabilityErythrocytesGlucose Transporter Type 1GlycophorinsHumansIntracellular Signaling Peptides and ProteinsKineticsLipid BilayersModels, BiologicalSpectrinAnkyrinsGlucose Transporter Type 1GlycophorinsIntracellular Signaling Peptides and ProteinsLipid BilayersSpectrinUNC5CL protein, human

Identifiers

PMID20411297
PMCPMC11115695

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.