Evidence map›Paper›PMID 18589007›Full record

ArticleBiochimica et biophysica acta2008

Stability of dystrophin STR fragments in relation to junction helicity.

Ahmed Mirza, Nick Menhart

Abstract read
In one paragraph

Article in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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.

Ahmed MirzaDepartment of Biological, Chemical and Physical Sciences, Illinois Institute of Technology, 3101 South Dearborn, Chicago, IL 60616, USA.
Nick Menhart

Funding

Structure of the dystrophin rod in relation to exon boundaries and exon skippingR01AR053970 · NIAMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI MENHART, NICK · 2006 to 2009
$416k
NIAMS NIH HHS 5R01AR053970NIAMS NIH HHS R01 AR053970
6 · The paper itself

Abstract

Dystrophin is a rod shaped protein consisting of amino- and carboxy-terminal binding domains linked by a large central rod composed of 24 homologous copies of the STR motif and 4 non-homologous regions termed hinges. These hinges are proposed to confer local flexibility; conversely, the tacit implication is that the STR regions away from the hinges are comparatively rigid. This, and the repeating nature of this rod, has contributed to the view that the STR region of the rod is uniform and monolithic. However, we have produced various 2 STR fragments, chosen to have high and low alpha-helix content at their junctions with each other, and show that they exhibit markedly different stabilities. In contrast to a related protein, spectrin, these differences are not correlated with the calculated helicity, but appear to be an intrinsic property of the motifs themselves. A full understanding of how these properties vary along the length of the rod has implications for the engineering of these rods regions in exon skipping and minidystrophin therapies.

Indexed as

Amino Acid SequenceCircular DichroismDrug StabilityDystrophinEndopeptidase KHumansLightModels, MolecularPeptide FragmentsProtein DenaturationProtein Structure, SecondaryRecombinant ProteinsScattering, RadiationSpectrometry, FluorescenceThermodynamicsDMD protein, humanDystrophinEndopeptidase KPeptide FragmentsRecombinant Proteins

Identifiers

PMID18589007
PMCPMC2579755

What OpenQuestion holds

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Registered trials

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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.