Evidence map›Paper›PMID 2677025›Full record

ArticleThe Journal of cell biology1989

Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.

T J Byers, A Husain-Chishti, R R Dubreuil, D Branton, L S Goldstein

Abstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1989. 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
–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

57 citing papers in PubMed.

  1. Review
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  17. Golgi localization of Syne-1.Molecular biology of the cell · 2003
    Article
  18. Article
  19. Drosophila alpha- and beta-spectrin mutations disrupt presynaptic neurotransmitter release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    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

5 authors.

T J ByersDepartment of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.
A Husain-Chishti
R R Dubreuil
D Branton
L S Goldstein

Funding

GENETIC STUDIES OF NON-ERYTHROID SPECTRINR01GM039686 · NIGMS · HARVARD UNIVERSITY · PI BRANTON, DANIEL · 1988 to 1996
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NIGMS NIH HHS GM39686
6 · The paper itself

Abstract

We used chicken alpha spectrin as a ligand probe to isolate Drosophila beta spectrin cDNA sequences from a lambda gt11 expression library. Analysis of 800 residues of deduced amino acid sequence at the amino-terminal end revealed a strikingly conserved domain of integral of 230 residues that shows a high degree of sequence similarity to the amino-terminal domains of alpha actinin and dystrophin. This conserved domain constitutes a new diagnostic criterion for spectrin-related proteins and allows the known properties of one of these proteins to predict functional properties of the others. The conservation of the amino-terminal domain, and other regions in spectrin, alpha actinin, and dystrophin, demonstrates that a common set of domains were linked in different combinations through evolution to generate the distinctive members of the spectrin superfamily.

Indexed as

ActininAmino Acid SequenceAnimalsBase SequenceChickensCloning, MolecularDNADrosophilaDystrophinErythrocyte MembraneMacromolecular SubstancesMolecular Sequence DataMuscle ProteinsNucleic Acid HybridizationProtein ConformationRestriction MappingActininDNADystrophinMacromolecular SubstancesMuscle ProteinsRNA, MessengerSpectrin

Identifiers

PMID2677025
PMCPMC2115807

What OpenQuestion holds

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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.