Database : MEDLINE
Search on : Sarcoglycanopathies [Words]
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[PMID]: 29360879
[Au] Autor:Henriques SF; Patissier C; Bourg N; Fecchio C; Sandona D; Marsolier J; Richard I
[Ad] Address:INTEGRARE, Genethon, Inserm, Univ Evry, Université Paris-Saclay, Evry, France.
[Ti] Title:Different outcome of sarcoglycan missense mutation between human and mouse.
[So] Source:PLoS One;13(1):e0191274, 2018.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Sarcoglycanopathies are rare autosomic limb girdle muscular dystrophies caused by mutations in one of the genes coding for sarcoglycan (α, ß, δ, and γ-sarcoglycans). Sarcoglycans form a complex, which is an important part of the dystrophin-associated glycoprotein complex that protects sarcolemma against muscle contraction-induced damages. Absence of one of the sarcoglycan at the plasma membrane induces the disappearance of the whole complex and perturbs muscle fiber membrane integrity. We previously demonstrated that point mutations in the human sarcoglycan genes affects the folding of the corresponding protein, which is then retained in the endoplasmic reticulum by the protein quality control and prematurely degraded by the proteasome. Interestingly, modulation of the quality control using pharmacological compounds allowed the rescue of the membrane localization of the mutated sarcoglycan. Two previously generated mouse models, knock-in for the most common sarcoglycan mutant, R77C α-sarcoglycan, failed in reproducing the dystrophic phenotype observed in human patients. Based on these results and the need to test therapies for these fatal diseases, we decided to generate a new knock-in mouse model carrying the missense mutation T151R in the ß-sarcoglycan gene since this is the second sarcoglycan protein with the most frequently reported missense mutations. Muscle analysis, performed at the age of 4 and 9-months, showed the presence of the mutated ß-sarcoglycan protein and of the other components of the dystrophin-associated glycoprotein complex at the muscle membrane. In addition, these mice did not develop a dystrophic phenotype, even at a late stage or in condition of stress-inducing exercise. We can speculate that the absence of phenotype in mouse may be due to a higher tolerance of the endoplasmic reticulum quality control for amino-acid changes in mice compared to human.
[Mh] MeSH terms primary: Muscular Dystrophies, Limb-Girdle/genetics
Mutation, Missense
Sarcoglycans/genetics
[Mh] MeSH terms secundary: Amino Acid Sequence
Amino Acid Substitution
Animals
Disease Models, Animal
Female
Humans
Male
Mice
Mice, 129 Strain
Mice, Inbred C57BL
Mice, Transgenic
Muscle, Skeletal/metabolism
Muscle, Skeletal/pathology
Muscular Dystrophies, Limb-Girdle/metabolism
Muscular Dystrophies, Limb-Girdle/pathology
Proteolysis
Sarcoglycans/metabolism
Species Specificity
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (SGCB protein, human); 0 (Sarcoglycans)
[Em] Entry month:1802
[Cu] Class update date: 180226
[Lr] Last revision date:180226
[Js] Journal subset:IM
[Da] Date of entry for processing:180124
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191274

  2 / 139 MEDLINE  
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[PMID]: 29350766
[Au] Autor:Liewluck T; Milone M
[Ad] Address:Department of Neurology, Mayo Clinic, 200 First Street SW Rochester, Minnesota, 55905, USA.
[Ti] Title:Untangling the complexity of limb-girdle muscular dystrophies.
[So] Source:Muscle Nerve;, 2018 Jan 19.
[Is] ISSN:1097-4598
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The limb-girdle muscular dystrophies (LGMDs) are a group of genetically heterogeneous, autosomal inherited muscular dystrophies with a childhood to adult onset, manifesting with hip- and shoulder-girdle muscle weakness. When the term LGMD was first conceptualized in 1954, it was thought to be a single entity. Currently, there are 8 autosomal dominant (LGMD1A-1H) and 26 autosomal recessive (LGMD2A-2Z) variants according to the Online Mendelian Inheritance in Man database. In addition, there are other genetically identified muscular dystrophies with an LGMD phenotype not yet classified as LGMD. This highlights the entanglement of LGMDs, which represents an area in continuous expansion. Herein we aim to simplify the complexity of LGMDs by subgrouping them on the basis of the underlying defective protein and impaired function. Muscle Nerve, 2018.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1801
[Cu] Class update date: 180207
[Lr] Last revision date:180207
[St] Status:Publisher
[do] DOI:10.1002/mus.26077

  3 / 139 MEDLINE  
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[PMID]: 28889091
[Au] Autor:Tasca G; Monforte M; Díaz-Manera J; Brisca G; Semplicini C; D'Amico A; Fattori F; Pichiecchio A; Berardinelli A; Maggi L; Maccagnano E; Løkken N; Marini-Bettolo C; Munell F; Sanchez A; Alshaikh N; Voermans NC; Dastgir J; Vlodavets D; Haberlová J; Magnano G; Walter MC; Quijano-Roy S; Carlier RY; van Engelen BGM; Vissing J; Straub V; Bönnemann CG; Mercuri E; Muntoni F; Pegoraro E; Bertini E; Udd B; Ricci E; Bruno C
[Ad] Address:Istituto di Neurologia, Università Cattolica del Sacro Cuore, Fondazione Policlinico Universitario 'A Gemelli', Rome, Italy.
[Ti] Title:MRI in sarcoglycanopathies: a large international cohort study.
[So] Source:J Neurol Neurosurg Psychiatry;, 2017 Sep 09.
[Is] ISSN:1468-330X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:OBJECTIVES: To characterise the pattern and spectrum of involvement on muscle MRI in a large cohort of patients with sarcoglycanopathies, which are limb-girdle muscular dystrophies (LGMD2C-2F) caused by mutations in one of the four genes coding for muscle sarcoglycans. METHODS: Lower limb MRI scans of patients with LGMD2C-2F, ranging from severe childhood variants to milder adult-onset forms, were collected in 17 neuromuscular referral centres in Europe and USA. Muscle involvement was evaluated semiquantitatively on T1-weighted images according to a visual score, and the global pattern was assessed as well. RESULTS: Scans from 69 patients were examined (38 LGMD2D, 18 LGMD2C, 12 LGMD2E and 1 LGMD2F). A common pattern of involvement was found in all the analysed scans irrespective of the mutated gene. The most and earliest affected muscles were the thigh adductors, glutei and posterior thigh groups, while lower leg muscles were relatively spared even in advanced disease. A proximodistal gradient of involvement of vasti muscles was a consistent finding in these patients, including the most severe ones. CONCLUSIONS: Muscle involvement on MRI is consistent in patients with LGMD2C-F and can be helpful in distinguishing sarcoglycanopathies from other LGMDs or dystrophinopathies, which represent the most common differential diagnoses. Our data provide evidence about selective susceptibility or resistance to degeneration of specific muscles when one of the sarcoglycans is deficient, as well as preliminary information about progressive involvement of the different muscles over time.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1709
[Cu] Class update date: 171114
[Lr] Last revision date:171114
[St] Status:Publisher

  4 / 139 MEDLINE  
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[PMID]: 28883879
[Au] Autor:Ghafouri-Fard S; Hashemi-Gorji F; Fardaei M; Miryounesi M
[Ad] Address:Department of Medical Genetics, Shahid Beheshti University of Medical sciences, Tehran, Iran.
[Ti] Title:Limb Girdle Muscular Dystrophy Type 2E Due to a Novel Large Deletion in SGCB Gene.
[So] Source:Iran J Child Neurol;11(3):57-60, 2017.
[Is] ISSN:1735-4668
[Cp] Country of publication:Iran
[La] Language:eng
[Ab] Abstract:Autosomal recessive limb-girdle muscular dystrophies (LGMD type 2) are a group of clinically and genetically heterogeneous diseases with the main characteristics of weakness and wasting of the pelvic and shoulder girdle muscles. Among them are sarcoglycanopathies caused by mutations in at least four genes named SGCA, SGCB, SGCG and SGCD. Here we report a consanguineous Iranian family with two children affected with LGMD type 2E. Mutation analysis revealed a novel homozygous exon 2 deletion of SGCB gene in the patients with the parents being heterozygous for this deletion. This result presents a novel underlying genetic mechanism for LGMD type 2E.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1709
[Cu] Class update date: 171001
[Lr] Last revision date:171001
[St] Status:PubMed-not-MEDLINE

  5 / 139 MEDLINE  
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[PMID]: 28821434
[Au] Autor:Fukai Y; Ohsawa Y; Ohtsubo H; Nishimatsu SI; Hagiwara H; Noda M; Sasaoka T; Murakami T; Sunada Y
[Ad] Address:Department of Neurology, Kawasaki Medical School, 577 Matsushima, Kurashiki, Okayama 701-0192, Japan.
[Ti] Title:Cleavage of ß-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9.
[So] Source:Biochem Biophys Res Commun;492(2):199-205, 2017 Oct 14.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND: The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning ß-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa ß-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved ß-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of ß-dystroglycan. However, this has remained uninvestigated in vivo. METHODS: We generated triple-knockout (TKO) mice targeting MMP-2, MMP-9 and γ-sarcoglycan to examine the status of ß-dystroglycan cleavage in the absence of the candidate matrix metalloproteinases in sarcoglycan-deficient muscles. RESULTS: Unexpectedly, ß-dystroglycan was cleaved in muscles from TKO mice. Muscle pathology was not ameliorated but worsened in TKO mice compared with γ-sarcoglycan single-knockout mice. The gene expression of MMP-14 was up-regulated in TKO mice as well as in γ-sarcoglycan knockout mice. In vitro assay showed MMP-14 is capable to cleave ß-dystroglycan. CONCLUSIONS: Double-targeting of MMP-2 and MMP-9 cannot prevent cleavage of ß-dystroglycan in sarcoglycanopathy. Thus, matrix metalloproteinases contributing to ß-dystroglycan cleavage are redundant, and MMP-14 could participate in the pathogenesis of sarcoglycanopathy.
[Mh] MeSH terms primary: Dystroglycans/metabolism
Matrix Metalloproteinase 2/genetics
Matrix Metalloproteinase 9/genetics
Muscle, Skeletal/metabolism
Sarcoglycanopathies/genetics
Sarcoglycans/genetics
[Mh] MeSH terms secundary: Animals
Gene Deletion
Humans
Matrix Metalloproteinase 14/genetics
Matrix Metalloproteinase 14/metabolism
Matrix Metalloproteinase 2/metabolism
Matrix Metalloproteinase 9/metabolism
Mice, Knockout
Muscle, Skeletal/pathology
Proteolysis
Sarcoglycanopathies/metabolism
Sarcoglycanopathies/pathology
Sarcoglycans/metabolism
Up-Regulation
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Sarcoglycans); 146888-27-9 (Dystroglycans); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 3.4.24.80 (Matrix Metalloproteinase 14)
[Em] Entry month:1709
[Cu] Class update date: 170925
[Lr] Last revision date:170925
[Js] Journal subset:IM
[Da] Date of entry for processing:170820
[St] Status:MEDLINE

  6 / 139 MEDLINE  
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[PMID]: 28687063
[Au] Autor:Alavi A; Esmaeili S; Nilipour Y; Nafissi S; Tonekaboni SH; Zamani G; Ashrafi MR; Kahrizi K; Najmabadi H; Jazayeri F
[Ad] Address:a Genetics Research Center , University of Social Welfare and Rehabilitation Sciences , Tehran , Iran.
[Ti] Title:LGMD2E is the most common type of sarcoglycanopathies in the Iranian population.
[So] Source:J Neurogenet;31(3):161-169, 2017 Sep.
[Is] ISSN:1563-5260
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Sarcoglycanopathies (SGCs) which are caused by mutations in SGCA, SGCB, SGCG or SGCD genes are a subgroup of autosomal-recessive limb-girdle-muscular-dystrophies (LGMD2). Although frequencies of mutations in these genes are different among populations, mutations in SGCA and SGCD, respectively, have the highest and lowest frequencies in most populations. Here, we report the proportion of mutations in SGC genes among a group of Iranian SGCs patients. Clinical features and results of SGC genes screening of 25 SGCs probands are presented. Large deletion mutations are confirmed with MLPA assays. In total, 15 candidate disease causing mutations were observed in the SGCA, SGCB, SGCG and SGCD genes; ten were novel. Fourteen (56%), seven (28%), three (12%) and one (4%) patient, respectively, carried mutations in SGCB, SGCG, SGCD and SGCA. The findings suggest that LGMD2E is the most common form of SGCs in the Iranian population and that LGMD2D is the rarest. Twelve LGMD2E cases carried the same mutation. To the best of knowledge, the mutation spectrum in SGCs is being reported for the first time in Iranian population. The finding will be beneficial for screening and genetic-counseling of SGCs patients in Iran.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1707
[Cu] Class update date: 170904
[Lr] Last revision date:170904
[St] Status:In-Process
[do] DOI:10.1080/01677063.2017.1346093

  7 / 139 MEDLINE  
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[PMID]: 28615891
[Au] Autor:Khadilkar SV; Faldu HD; Patil SB; Singh R
[Ad] Address:Department of Neurology, Bombay Hospital, Mumbai, Maharashtra, India.
[Ti] Title:Limb-girdle Muscular Dystrophies in India: A Review.
[So] Source:Ann Indian Acad Neurol;20(2):87-95, 2017 Apr-Jun.
[Is] ISSN:0972-2327
[Cp] Country of publication:India
[La] Language:eng
[Ab] Abstract:Limb-girdle muscular dystrophies (LGMDs) are common in India. Information on LGMDs has been gradually evolving in the recent years. This information is scattered in case series and case studies. The aim of this study is to collate available Indian information on LGMDs and put it in perspective. PubMed search using keywords such as limb-girdle muscular dystrophies in India, sarcoglycanopathies, dysferlinopathy, calpainopathy, and GNE myopathy was carried out. The published information on LGMDs in Indian context suggests that dysferlinopathy, calpainopathy, sarcoglycanopathies, and other myopathies such as GNE myopathy are frequently seen in India. Besides these, anecdotal reports of many other forms are available, some with genetic support and others showing immunocytochemical defects. The genotypic information on LGMDs is gradually evolving and founder mutations have been detected in selected populations. Further multicenter studies are necessary to document the incidence and prevalence of these common conditions in India.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1706
[Cu] Class update date: 170619
[Lr] Last revision date:170619
[St] Status:PubMed-not-MEDLINE
[do] DOI:10.4103/aian.AIAN_81_17

  8 / 139 MEDLINE  
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[PMID]: 28521973
[Au] Autor:Marsolier J; Laforet P; Pegoraro E; Vissing J; Richard I; Sarcoglycanopathies Working Group
[Ad] Address:Généthon, INSERM, U951, INTEGRARE Research Unit, Evry F-91002, France.
[Ti] Title:1st International Workshop on Clinical trial readiness for sarcoglycanopathies 15-16 November 2016, Evry, France.
[So] Source:Neuromuscul Disord;27(7):683-692, 2017 Jul.
[Is] ISSN:1873-2364
[Cp] Country of publication:England
[La] Language:eng
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1705
[Cu] Class update date: 170606
[Lr] Last revision date:170606
[St] Status:In-Data-Review

  9 / 139 MEDLINE  
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[PMID]: 28284983
[Au] Autor:Pozsgai ER; Griffin DA; Heller KN; Mendell JR; Rodino-Klapac LR
[Ad] Address:Biomedical Sciences Graduate Program, The Ohio State University, Columbus, OH 43210, USA; Center for Gene Therapy, The Research Institute at Nationwide Children's Hospital, Columbus, OH 43205, USA.
[Ti] Title:Systemic AAV-Mediated ß-Sarcoglycan Delivery Targeting Cardiac and Skeletal Muscle Ameliorates Histological and Functional Deficits in LGMD2E Mice.
[So] Source:Mol Ther;25(4):855-869, 2017 Apr 05.
[Is] ISSN:1525-0024
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Limb-girdle muscular dystrophy type 2E (LGMD2E), resulting from mutations in ß-sarcoglycan (SGCB), is a progressive dystrophy with deteriorating muscle function, respiratory failure, and cardiomyopathy in 50% or more of LGMD2E patients. SGCB knockout mice share many of the phenotypic deficiencies of LGMD2E patients. To investigate systemic SGCB gene transfer to treat skeletal and cardiac muscle deficits, we designed a self-complementary AAVrh74 vector containing a codon-optimized human SGCB transgene driven by a muscle-specific promoter. We delivered scAAV.MHCK7.hSGCB through the tail vein of SGCB mice to provide a rationale for a clinical trial that would lead to clinically meaningful results. This led to 98.1% transgene expression across all muscles that was accompanied by improvements in histopathology. Serum creatine kinase (CK) levels were reduced following treatment by 85.5%. Diaphragm force production increased by 94.4%, kyphoscoliosis of the spine was significantly reduced by 48.1%, overall ambulation increased by 57%, and vertical rearing increased dramatically by 132% following treatment. Importantly, no adverse effects were seen in muscle of wild-type mice injected systemically with scAAV.hSGCB. In this well-defined model of LGMD2E, we have demonstrated the efficacy and safety of systemic scAAV.hSGCB delivery, and these findings have established a path for clinically beneficial AAV-mediated gene therapy for LGMD2E.
[Mh] MeSH terms primary: Dependovirus/genetics
Genetic Vectors/genetics
Muscle, Skeletal/metabolism
Myocardium/metabolism
Sarcoglycanopathies/diagnosis
Sarcoglycanopathies/genetics
Sarcoglycans/genetics
[Mh] MeSH terms secundary: Animals
Biopsy
Cardiomyopathies/diagnosis
Cardiomyopathies/genetics
Disease Models, Animal
Gene Order
Gene Transfer Techniques
Genetic Vectors/administration & dosage
Genetic Vectors/pharmacokinetics
Humans
Kyphosis/diagnosis
Kyphosis/genetics
Kyphosis/therapy
Mice
Mice, Knockout
Motor Activity
Muscle, Skeletal/pathology
Muscle, Skeletal/physiopathology
Myocardium/pathology
Recovery of Function
Sarcoglycanopathies/therapy
Scoliosis/diagnosis
Scoliosis/genetics
Scoliosis/therapy
Tissue Distribution
Transduction, Genetic
X-Ray Microtomography
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (SGCB protein, human); 0 (Sarcoglycans)
[Em] Entry month:1706
[Cu] Class update date: 170606
[Lr] Last revision date:170606
[Js] Journal subset:IM
[Da] Date of entry for processing:170313
[St] Status:MEDLINE

  10 / 139 MEDLINE  
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[PMID]: 28219397
[Au] Autor:Suriyonplengsaeng C; Dejthevaporn C; Khongkhatithum C; Sanpapant S; Tubthong N; Pinpradap K; Srinark N; Waisayarat J
[Ad] Address:Department of Pathology, Faculty of Medicine Ramathibodi Hospital, Mahidol University, Bangkok, 10400, Thailand.
[Ti] Title:Immunohistochemistry of sarcolemmal membrane-associated proteins in formalin-fixed and paraffin-embedded skeletal muscle tissue: a promising tool for the diagnostic evaluation of common muscular dystrophies.
[So] Source:Diagn Pathol;12(1):19, 2017 Feb 20.
[Is] ISSN:1746-1596
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: The analysis of fresh frozen muscle specimens is standard following routine muscle biopsy, but this service is not widely available in countries with limited medical facilities, such as Thailand. Nevertheless, immunohistochemistry (IHC) analysis is essential for the diagnosis of patients with a strong clinical suspicion of muscular dystrophy, in the absence of mutations detected by molecular genetics. As the successful labelling of sarcolemmal membrane-associated proteins in formalin-fixed and paraffin-embedded (FFPE) muscle sections using IHC staining has rarely been described, this study aimed to develop a reproducible IHC method for such an analysis. METHODS: Thirteen cases were studied from the files of the Department of Pathology, Mahidol University. Diagnoses included three Duchenne muscular dystrophy (DMD), one Becker muscular dystrophy (BMD), one dysferlinopathy, and several not-specified muscular dystrophies. IHC was performed on FFPE sections at different thicknesses (3 µm, 5 µm, and 8 µm) using the heat-mediated antigen retrieval method with citrate/EDTA buffer, followed by an overnight incubation with primary antibodies at room temperature. Antibodies against spectrin, dystrophin (rod domain, C-terminus, and N-terminus), dysferlin, sarcoglycans (α, ß, and γ), and ß-dystroglycan were used. Frozen sections were tested in parallel for comparative analysis. RESULTS: Antibodies labelling spectrin, dystrophin (rod domain and C-terminus), dysferlin, sarcoglycans (α, ß, and γ), and ß-dystroglycan clearly exhibited sarcolemmal staining in FFPE sections. However, staining of FFPE sections using the antibody directed against the N-terminus of dystrophin was unsuccessful. The absence of labeling for dystrophins and dysferlin in FFPE sections was documented in all three DMD patients and the dysferlinopathy patient. The BMD diagnosis could not be made using IHC in FFPE sections alone because of a lack of staining for the dystrophin N-terminus, indicating a limitation of this method. CONCLUSIONS: We developed a reliable and reproducible IHC technique using FFPE muscle. This could become a valuable tool for the diagnosis of some muscular dystrophies, dystrophinopathies, sarcoglycanopathies (LGMD2D, LGMD2E, and LGMD2C), and dysferlinopathy, especially in situations where the analysis of fresh frozen muscle samples is not routinely available.
[Mh] MeSH terms primary: Dystroglycans/metabolism
Dystrophin/metabolism
Membrane Proteins/metabolism
Muscle Proteins/metabolism
Muscular Dystrophies, Limb-Girdle/diagnosis
Muscular Dystrophies/diagnosis
Sarcoglycans/metabolism
[Mh] MeSH terms secundary: Adolescent
Adult
Child
Child, Preschool
Dysferlin
Female
Humans
Immunohistochemistry
Infant
Male
Middle Aged
Muscle, Skeletal/metabolism
Muscle, Skeletal/pathology
Muscular Dystrophies/metabolism
Muscular Dystrophies, Limb-Girdle/metabolism
Muscular Dystrophy, Duchenne/diagnosis
Muscular Dystrophy, Duchenne/metabolism
Paraffin Embedding
Reproducibility of Results
Sarcoglycanopathies/diagnosis
Sarcoglycanopathies/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (DAG1 protein, human); 0 (DYSF protein, human); 0 (Dysferlin); 0 (Dystrophin); 0 (Membrane Proteins); 0 (Muscle Proteins); 0 (Sarcoglycans); 146888-27-9 (Dystroglycans)
[Em] Entry month:1702
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:170222
[St] Status:MEDLINE
[do] DOI:10.1186/s13000-017-0610-y


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