Early-Onset Myopathy with Fatal Cardiomyopathy

Also Known As:

Myopathy, Early-Onset, with Fatal Cardiomyopathy; Salih Cmd; Salih Congenital Muscular Dystrophy; Salih Myopathy

Networked: 3 relevant articles (0 outcomes, 0 trials/studies)

1.	Limb-Girdle Muscular Dystrophies (Limb-Girdle Muscular Dystrophy)
2.	Distal Myopathies (Distal Muscular Dystrophy)
3.	Congenital Structural Myopathies (Centronuclear Myopathy)
4.	Central Core Myopathy (Central Core Disease)
5.	Emery-Dreifuss Muscular Dystrophy (Scapuloperoneal Muscular Dystrophy)

1.	Carmignac, Virginie: 2 articles (06/2008 - 04/2007)
2.	Ferreiro, Ana: 2 articles (06/2008 - 04/2007)
3.	Gautel, Mathias: 2 articles (06/2008 - 04/2007)
4.	Misaka, Tomofumi: 1 article (08/2019)
5.	Takeishi, Yasuchika: 1 article (08/2019)
6.	Yoshihisa, Akiomi: 1 article (08/2019)
7.	Fukuzawa, Atsushi: 1 article (06/2008)
8.	Holt, Mark: 1 article (06/2008)
9.	Lange, Stephan: 1 article (06/2008)
10.	Udd, Bjarne: 1 article (06/2008)

Drugs and Important Biological Agents (IBA) related to Early-Onset Myopathy with Fatal Cardiomyopathy:

1.	ConnectinIBA 04/01/2007 - "C-terminal titin deletions cause a novel early-onset myopathy with fatal cardiomyopathy." 08/01/2019 - "Titin-related muscular dystrophies include tibial muscular dystrophy, limb-girdle muscular dystrophy, Emery-Dreifuss muscular dystrophy, hereditary myopathy with early respiratory failure, central core myopathy, centronuclear myopathies, and Salih myopathy. " 06/01/2008 - "Furthermore, all titin mutations that have been linked to limb-girdle muscular dystrophy 2J (LGMD2J) or Salih myopathy weaken or abrogate titin-obscurin and titin-Obsl1 binding, and lead to obscurin mislocalization, suggesting that interference with the interaction of these proteins might be of pathogenic relevance for human disease."
2.	Proteins (Proteins, Gene)FDA Link 06/01/2008 - "Furthermore, all titin mutations that have been linked to limb-girdle muscular dystrophy 2J (LGMD2J) or Salih myopathy weaken or abrogate titin-obscurin and titin-Obsl1 binding, and lead to obscurin mislocalization, suggesting that interference with the interaction of these proteins might be of pathogenic relevance for human disease."