Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.
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Structural basis of laminin binding to the LARGE glycans on dystroglycan.The functional O-mannose glycan on α-dystroglycan contains a phospho-ribitol primed for matriglycan additionWhoa man! Unexpected protein O-mannosylation pathways in mammalsProtein O-Mannosylation in the Murine Brain: Occurrence of Mono-O-Mannosyl Glycans and Identification of New SubstratesISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol phosphate onto α-dystroglycan.Expression pattern in retinal photoreceptors of POMGnT1, a protein involved in muscle-eye-brain disease.Lassa Virus Cell Entry via Dystroglycan Involves an Unusual Pathway of Macropinocytosis.Role of dystroglycan in limiting contraction-induced injury to the sarcomeric cytoskeleton of mature skeletal muscle.Structure of protein O-mannose kinase reveals a unique active site architecture.Whole-blood RNA transcript-based models can predict clinical response in two large independent clinical studies of patients with advanced melanoma treated with the checkpoint inhibitor, tremelimumab.Reverse Nearest Neighbor Search on a Protein-Protein Interaction Network to Infer Protein-Disease AssociationsWhat Have We Learned from Glycosyltransferase Knockouts in Mice?Glycan susceptibility factors in autism spectrum disorders.Biological roles of glycans.Can Human Pluripotent Stem Cell-Derived Cardiomyocytes Advance Understanding of Muscular Dystrophies?Lassa Virus Cell Entry Reveals New Aspects of Virus-Host Cell InteractionB4GALNT2 (GALGT2) Gene Therapy Reduces Skeletal Muscle Pathology in the FKRP P448L Mouse Model of Limb Girdle Muscular Dystrophy 2I.Structural basis for antibody-mediated neutralization of Lassa virus.Recent advancements in understanding mammalian O-mannosylation.Structural flexibility of human α-dystroglycan.Studies of Lassa Virus Cell Entry.O-mannosylation and N-glycosylation: two coordinated mechanisms regulating the tumour suppressor functions of E-cadherin in cancer.Direct Mapping of Additional Modifications on Phosphorylated O-glycans of α-Dystroglycan by Mass Spectrometry Analysis in Conjunction with Knocking Out of Causative Genes for Dystroglycanopathy.The effect of the pathological V72I, D109N and T190M missense mutations on the molecular structure of α-dystroglycanDeletion of Pofut1 in Mouse Skeletal Myofibers Induces Muscle Aging-Related Phenotypes in cis and in trans.Lectin-binding characterizes the healthy human skeletal muscle glycophenotype and identifies disease-specific changes in dystrophic muscle.Protein O-Linked Mannose β-1,4-N-Acetylglucosaminyl-transferase 2 (POMGNT2) Is a Gatekeeper Enzyme for Functional Glycosylation of α-Dystroglycan.Muscular Dystrophy with Ribitol-Phosphate Deficiency: A Novel Post-Translational Mechanism in Dystroglycanopathy.Axl can serve as entry factor for Lassa virus depending on the functional glycosylation of dystroglycan.Protein O-mannosyltransferases affect sensory axon wiring and dynamic chirality of body posture in the Drosophila embryo.A dystroglycan mutation (p.Cys667Phe) associated to muscle-eye-brain disease with multicystic leucodystrophy results in ER-retention of the mutant protein.Deep-intronic variant of fukutin is the most prevalent point mutation of Fukuyama congenital muscular dystrophy in Japan.Expression in retinal neurons of fukutin and FKRP, the protein products of two dystroglycanopathy-causative genes.Rapid screening of sugar-nucleotide donor specificities of putative glycosyltransferases.Non-Glycanated Biglycan and LTBP4: Leveraging the extracellular matrix for Duchenne Muscular Dystrophy therapeutics.Impairment of photoreceptor ribbon synapses in a novel Pomt1 conditional knockout mouse model of dystroglycanopathy.Overexpression of Mutant FKRP Restores Functional Glycosylation and Improves Dystrophic Phenotype in FKRP Mutant Mice.Structure of the Lassa virus glycan shield provides a model for immunological resistanceRibitol restores functionally glycosylated α-dystroglycan and improves muscle function in dystrophic FKRP-mutant mice
P2860
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P2860
Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.
@en
type
label
Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.
@en
prefLabel
Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.
@en
P2860
P921
P356
P1433
P1476
Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane
@en
P2093
Takako Yoshida-Moriguchi
P2860
P304
P356
10.1093/GLYCOB/CWV021
P577
2015-04-16T00:00:00Z