Literature DB >> 15367857

Myopathies resulting from mutations in sarcomeric proteins.

Carsten G Bönnemann1, Nigel G Laing.   

Abstract

PURPOSE OF REVIEW: The past decade has seen the discovery of the major role that mutations in the protein components of the sarcomere plays as a cause of human muscle disease. An overview of the more precise molecular definitions of these diseases is timely. RECENT
FINDINGS: Recent findings include: the beginnings of an understanding of the role of the sarcomere in controlling muscle gene expression; the theoretical analysis of the increasing number of mutations identified in the skeletal muscle actin gene; the identification of mutations in myosin causing hereditary inclusion body myopathy and hyaline body myopathy and the identification of mutations in myotilin in myofibrillar myopathy.
SUMMARY: An increasing spectrum of human muscle diseases is being shown to be caused by mutations in proteins of all the major components of the sarcomere. Molecular analysis is providing a more accurate delineation of these diseases, but for the giant nebulin and titin genes, molecular diagnosis remains difficult. Treatment options for these disorders will only come through a deeper understanding of the sarcomere and of the pathogenesis of its disorders.

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Year:  2004        PMID: 15367857     DOI: 10.1097/00019052-200410000-00003

Source DB:  PubMed          Journal:  Curr Opin Neurol        ISSN: 1350-7540            Impact factor:   5.710


  14 in total

Review 1.  In vitro myoblast motility models: investigating migration dynamics for the study of skeletal muscle repair.

Authors:  K P Goetsch; K H Myburgh; Carola U Niesler
Journal:  J Muscle Res Cell Motil       Date:  2013-10-23       Impact factor: 2.698

Review 2.  Systems biology of skeletal muscle: fiber type as an organizing principle.

Authors:  Sarah M Greising; Heather M Gransee; Carlos B Mantilla; Gary C Sieck
Journal:  Wiley Interdiscip Rev Syst Biol Med       Date:  2012-07-18

Review 3.  Influence of exercise and aging on extracellular matrix composition in the skeletal muscle stem cell niche.

Authors:  Koyal Garg; Marni D Boppart
Journal:  J Appl Physiol (1985)       Date:  2016-08-18

4.  The Drosophila Z-disc protein Z(210) is an adult muscle isoform of Zasp52, which is required for normal myofibril organization in indirect flight muscles.

Authors:  Maria B Chechenova; Anton L Bryantsev; Richard M Cripps
Journal:  J Biol Chem       Date:  2012-12-27       Impact factor: 5.157

5.  Laing early onset distal myopathy: slow myosin defect with variable abnormalities on muscle biopsy.

Authors:  P J Lamont; B Udd; F L Mastaglia; M de Visser; P Hedera; T Voit; L R Bridges; V Fabian; A Rozemuller; N G Laing
Journal:  J Neurol Neurosurg Psychiatry       Date:  2005-08-15       Impact factor: 10.154

6.  New aspects of obscurin in human striated muscles.

Authors:  Lena Carlsson; Ji-Guo Yu; Lars-Eric Thornell
Journal:  Histochem Cell Biol       Date:  2008-03-19       Impact factor: 4.304

7.  Arginylation of myosin heavy chain regulates skeletal muscle strength.

Authors:  Anabelle S Cornachione; Felipe S Leite; Junling Wang; Nicolae A Leu; Albert Kalganov; Denys Volgin; Xuemei Han; Tao Xu; Yu-Shu Cheng; John R R Yates; Dilson E Rassier; Anna Kashina
Journal:  Cell Rep       Date:  2014-07-10       Impact factor: 9.423

8.  Myogenesis in Drosophila melanogaster: Dissection of Distinct Muscle Types for Molecular Analysis.

Authors:  Anton L Bryantsev; Lizzet Castillo; Sandy T Oas; Maria B Chechenova; Tracy E Dohn; TyAnna L Lovato
Journal:  Methods Mol Biol       Date:  2019

9.  At the Start of the Sarcomere: A Previously Unrecognized Role for Myosin Chaperones and Associated Proteins during Early Myofibrillogenesis.

Authors:  J Layne Myhre; David B Pilgrim
Journal:  Biochem Res Int       Date:  2012-01-30

10.  Myosin assembly, maintenance and degradation in muscle: Role of the chaperone UNC-45 in myosin thick filament dynamics.

Authors:  Torah M Kachur; David B Pilgrim
Journal:  Int J Mol Sci       Date:  2008-09-19       Impact factor: 6.208

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