Evidence map›Paper›PMID 26676145›Full record

ReviewPhysiological reviews2016

Absence of Dystrophin Disrupts Skeletal Muscle Signaling: Roles of Ca2+, Reactive Oxygen Species, and Nitric Oxide in the Development of Muscular Dystrophy.

David G Allen, Nicholas P Whitehead, Stanley C Froehner

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Physiological reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 262 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
262citing papers in PubMed, 1 pooled it
12.5field-weighted citation impact, top 1% 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

262 citing papers in PubMed, 1 synthesis or guideline pooled it, 413 citations in OpenAlex.

  1. Pooled it
  2. Trial
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  6. Review
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  9. Ryanodine Receptor CaActa physiologica (Oxford, England) · 2026
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  17. Twisting Paths: The Paradox of Fiber Branching in Muscle Regeneration.International journal of molecular sciences · 2026
    Review
  18. Article
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  20. Article

202 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 2 countries.

David G AllenSydney Medical School & Bosch Institute, University of Sydney, New South Wales, Australia; and Department of Physiology & Biophysics, University of Washington, Seattle, Washington.
Nicholas P WhiteheadSydney Medical School & Bosch Institute, University of Sydney, New South Wales, Australia; and Department of Physiology & Biophysics, University of Washington, Seattle, Washington.
Stanley C FroehnerSydney Medical School & Bosch Institute, University of Sydney, New South Wales, Australia; and Department of Physiology & Biophysics, University of Washington, Seattle, Washington.
University of Washington · US

Funding

Regulation of Syntrophin FunctionR01NS033145 · NINDS · UNIVERSITY OF WASHINGTON · PI FROEHNER, STANLEY C · 1995 to 2013
$5.2M
Golgi-associated NO-cGMP Signaling Defect in Muscular DystrophyR01AR056221 · NIAMS · UNIVERSITY OF WASHINGTON · PI BEAVO, JOSEPH A, FROEHNER, STANLEY C · 2009 to 2013
$2.9M
Evaluating a novel pathway for treatment of Duchenne muscular dystrophyR21NS088691 · NINDS · UNIVERSITY OF WASHINGTON · PI FROEHNER, STANLEY C, WHITEHEAD, NICHOLAS · 2014 to 2015
$773k
NIAMS NIH HHS R01AR056221NINDS NIH HHS P01 NS04678NINDS NIH HHS R01 NS033145NINDS NIH HHS R01 NS33145NINDS NIH HHS R21 NS088691
6 · The paper itself

Abstract

Dystrophin is a long rod-shaped protein that connects the subsarcolemmal cytoskeleton to a complex of proteins in the surface membrane (dystrophin protein complex, DPC), with further connections via laminin to other extracellular matrix proteins. Initially considered a structural complex that protected the sarcolemma from mechanical damage, the DPC is now known to serve as a scaffold for numerous signaling proteins. Absence or reduced expression of dystrophin or many of the DPC components cause the muscular dystrophies, a group of inherited diseases in which repeated bouts of muscle damage lead to atrophy and fibrosis, and eventually muscle degeneration. The normal function of dystrophin is poorly defined. In its absence a complex series of changes occur with multiple muscle proteins showing reduced or increased expression or being modified in various ways. In this review, we will consider the various proteins whose expression and function is changed in muscular dystrophies, focusing on Ca(2+)-permeable channels, nitric oxide synthase, NADPH oxidase, and caveolins. Excessive Ca(2+) entry, increased membrane permeability, disordered caveolar function, and increased levels of reactive oxygen species are early changes in the disease, and the hypotheses for these phenomena will be critically considered. The aim of the review is to define the early damage pathways in muscular dystrophy which might be appropriate targets for therapy designed to minimize the muscle degeneration and slow the progression of the disease.

Indexed as

Signal TransductionAnimalsCalciumCalcium SignalingDystrophinGene Expression RegulationHumansMuscle DevelopmentMuscle, SkeletalMuscular DystrophiesNitric OxideReactive Oxygen SpeciesRegenerationCalciumDystrophinNitric OxideReactive Oxygen Species

Identifiers

PMID26676145
PMCPMC4698395
OpenAlexW2206766868

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.