Evidence map›Paper›PMID 23671687›Full record

ArticlePloS one2013

Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteins.

Flavia Autore, Mark Pfuhl, Xueping Quan, Aisling Williams, Roland G Roberts, Catherine M Shanahan, Franca Fraternali

Abstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

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3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

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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

7 authors.

Flavia AutoreRandall Division of Cell and Molecular Biophysics, School of Physical Sciences and Engineering, King's College London, London, United Kingdom.
Mark Pfuhl
Xueping Quan
Aisling Williams
Roland G Roberts
Catherine M Shanahan
Franca Fraternali

Funding

British Heart Foundation NH/12/2/29427British Heart Foundation RG/11/14/29056
6 · The paper itself

Abstract

Nesprin-1 and nesprin-2 are nuclear envelope (NE) proteins characterized by a common structure of an SR (spectrin repeat) rod domain and a C-terminal transmembrane KASH [Klarsicht-ANC-Syne-homology] domain and display N-terminal actin-binding CH (calponin homology) domains. Mutations in these proteins have been described in Emery-Dreifuss muscular dystrophy and attributed to disruptions of interactions at the NE with nesprins binding partners, lamin A/C and emerin. Evolutionary analysis of the rod domains of the nesprins has shown that they are almost entirely composed of unbroken SR-like structures. We present a bioinformatical approach to accurate definition of the boundaries of each SR by comparison with canonical SR structures, allowing for a large-scale homology modelling of the 74 nesprin-1 and 56 nesprin-2 SRs. The exposed and evolutionary conserved residues identify important pbs for protein-protein interactions that can guide tailored binding experiments. Most importantly, the bioinformatics analyses and the 3D models have been central to the design of selected constructs for protein expression. 1D NMR and CD spectra have been performed of the expressed SRs, showing a folded, stable, high content α-helical structure, typical of SRs. Molecular Dynamics simulations have been performed to study the structural and elastic properties of consecutive SRs, revealing insights in the mechanical properties adopted by these modules in the cell.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceConsensus SequenceCytoskeletal ProteinsEvolution, MolecularHumansMicrofilament ProteinsMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsPrincipal Component AnalysisProtein Structure, SecondaryProtein Structure, TertiaryRepetitive Sequences, Amino AcidSequence Analysis, ProteinSpectrinCytoskeletal ProteinsMicrofilament ProteinsNerve Tissue ProteinsNuclear ProteinsSpectrinSYNE1 protein, humanSYNE2 protein, human

Identifiers

PMID23671687
PMCPMC3646009

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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.