About: Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle.

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scientific article published on 27 May 2008

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 2008 (ast) наукова стаття, опублікована в травні 2008 (uk) مقالة علمية نشرت في 27 مايو 2008 (ar) scientific article published on 27 May 2008 (en)
publication date	wds:Q37173002-335B30DA-D214-4A67-927F-118671F96C71
publication date	2008-05-27 00:00:00Z (xsd:dateTime)
cites work	wds:Q37173002-E84D7839-652F-493F-91CE-F01AC705F57A
cites work	LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
author name string	wds:Q37173002-3E645465-B67D-4C62-9921-DF72685792A2 wds:Q37173002-3EFB98A9-2290-4E0B-918C-665391E07B20 wds:Q37173002-999508E2-745D-439C-BF72-A0598A14C152 wds:Q37173002-EBA26CAC-0E14-4C8E-9CCB-C2A883CAF9B9
author name string	Ikuya Nonaka Satoru Noguchi Paul Saftig May Christine Malicdan
rdfs:label	Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (en) Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (nl) Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (ast)
skos:prefLabel	Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (en) Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (nl) Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (ast)
name	Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (en) Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (nl) Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. (ast)
author	wds:Q37173002-3D78F927-12A3-4D59-AF72-7014005B22E5
author	Ichizo Nishino
title	wds:Q37173002-BE70C308-FF6C-4182-B089-B8EAD9A28E89
title	Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle (en)
page(s)	wds:Q37173002-446C8A2E-DB96-479F-8822-199A540DEF06
page(s)	521-529
instance of	wds:Q37173002-134328a5-a7cf-4e86-94df-8bd26b141826 wds:Q37173002-95D02156-0C96-4F16-8A93-F20A8F55D1AE
instance of	review article scholarly article
main subject	wds:Q37173002-FB3940EC-67C5-46F0-94A2-B18A890B4EC1
main subject	autophagosome
PubMed ID	wds:Q37173002-49C0476C-8897-4EAD-81A1-6294E2DE4E4A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18502640
PubMed ID	18502640
published in	wds:Q37173002-74AA115D-B88D-48E5-AF1D-D33A4F6A646B
published in	Neuromuscular Disorders
issue	wds:Q37173002-0E876AFD-AF74-40A6-91F6-06908C4AE0CA
volume	wds:Q37173002-0F05C309-0475-4C8D-B736-E781FB2B178D
issue	7
volume	18
DOI	wds:Q37173002-2EAB9685-8F40-4B5B-A21D-5274C4EF35D9
DOI	http://dx.doi.org/10.1016/J.NMD.2008.04.010
DOI	10.1016/J.NMD.2008.04.010
ResearchGate publication ID	wds:Q37173002-8C35CADB-66D6-4A41-830D-4A486D4AE66C
ResearchGate publication ID	5346927
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q37173002
is cites work of	Autophagy: for better or for worse Enhanced delivery of α-glucosidase for Pompe disease by ICAM-1-targeted nanocarriers: comparative performance of a strategy for three distinct lysosomal storage disorders Genetic screen in Drosophila muscle identifies autophagy-mediated T-tubule remodeling and a Rab2 role in autophagy Cathepsin-L ameliorates cardiac hypertrophy through activation of the autophagy-lysosomal dependent protein processing pathways Atrogin-1 deficiency promotes cardiomyopathy and premature death via impaired autophagy Inclusion body myopathy, Paget's disease of the bone and fronto-temporal dementia: a disorder of autophagy TRIM32 is an E3 ubiquitin ligase for dysbindin Autophagy in health and disease. 3. Involvement of autophagy in muscle atrophy Role and regulation of autophagy in cancer Autophagy as a therapeutic target in cancer. Impaired autophagy in sporadic inclusion-body myositis and in endoplasmic reticulum stress-provoked cultured human muscle fibers Valosin containing protein associated inclusion body myopathy: abnormal vacuolization, autophagy and cell fusion in myoblasts Autophagy is defective in collagen VI muscular dystrophies and its reactivation rescues myofiber degeneration Chaperone-assisted degradation: multiple paths to destruction Bone and skeletal muscle: neighbors with close ties VMA21 deficiency prevents vacuolar ATPase assembly and causes autophagic vacuolar myopathy Deleterious mutations in LRBA are associated with a syndrome of immune deficiency and autoimmunity Cellular and molecular mechanisms of muscle atrophy Skeletal muscle autophagy: a new metabolic regulator Four-week rapamycin treatment improves muscular dystrophy in a fukutin-deficient mouse model of dystroglycanopathy Prolonged mechanical ventilation alters diaphragmatic structure and function RETRACTED: VMA21 deficiency causes an autophagic myopathy by compromising V-ATPase activity and lysosomal acidification DHPR alpha1S subunit controls skeletal muscle mass and morphogenesis. Lysosomal-mediated waste clearance in retinal pigment epithelial cells is regulated by CRYBA1/βA3/A1-crystallin via V-ATPase-MTORC1 signaling Intensive expression of UNC-51-like kinase 1 is a novel biomarker of poor prognosis in patients with esophageal squamous cell carcinoma Defects of Vps15 in skeletal muscles lead to autophagic vacuolar myopathy and lysosomal disease Proteotoxicity: an underappreciated pathology in cardiac disease Clinical utility of LC3 and p62 immunohistochemistry in diagnosis of drug-induced autophagic vacuolar myopathies: a case-control study X-linked myopathy with excessive autophagy: a failure of self-eating Increased autophagy accelerates colchicine-induced muscle toxicity Effect of enzyme replacement therapy in late onset Pompe disease: open pilot study of 48 weeks follow-up. Progress and problems in muscle glycogenoses Molecular pathogenesis of a novel mutation, G108D, in short-chain acyl-CoA dehydrogenase identified in subjects with short-chain acyl-CoA dehydrogenase deficiency. Muscle biopsy in Pompe disease The beneficial role of proteolysis in skeletal muscle growth and stress adaptation

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