SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
about
Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of α-dystroglycan in cells and tissuesB4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycanThe glucuronyltransferase B4GAT1 is required for initiation of LARGE-mediated α-dystroglycan functional glycosylationA Single Kinase Generates the Majority of the Secreted PhosphoproteomeGlycan Engineering for Cell and Developmental BiologyHunting Viral Receptors Using Haploid CellsThe secretory pathway kinasesXylose phosphorylation functions as a molecular switch to regulate proteoglycan biosynthesisAGO61-dependent GlcNAc modification primes the formation of functional glycans on α-dystroglycanThe Structure of the T190M Mutant of Murine α-Dystroglycan at High Resolution: Insight into the Molecular Basis of a Primary DystroglycanopathyA POGLUT1 mutation causes a muscular dystrophy with reduced Notch signaling and satellite cell loss.POMK mutations disrupt muscle development leading to a spectrum of neuromuscular presentationsStructural basis of laminin binding to the LARGE glycans on dystroglycan.The Muscular Dystrophy Gene TMEM5 Encodes a Ribitol β1,4-Xylosyltransferase Required for the Functional Glycosylation of Dystroglycan.The functional O-mannose glycan on α-dystroglycan contains a phospho-ribitol primed for matriglycan additionMammalian O-mannosylation of cadherins and plexins is independent of protein O-mannosyltransferases 1 and 2.Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans.Contribution of dysferlin deficiency to skeletal muscle pathology in asymptomatic and severe dystroglycanopathy models: generation of a new model for Fukuyama congenital muscular dystrophyA robust methodology to subclassify pseudokinases based on their nucleotide-binding properties.Secretome analysis identifies novel signal Peptide peptidase-like 3 (Sppl3) substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways.Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome.Fukutin is prerequisite to ameliorate muscular dystrophic phenotype by myofiber-selective LARGE expression.Intrafamilial variability in GMPPB-associated dystroglycanopathy: Broadening of the phenotypeProtein glycosylation in cancer.Neurons and glia modify receptor protein-tyrosine phosphatase ζ (RPTPζ)/phosphacan with cell-specific O-mannosyl glycans in the developing brain.Ectopic clustering of Cajal-Retzius and subplate cells is an initial pathological feature in Pomgnt2-knockout mice, a model of dystroglycanopathy.Downregulation of dystroglycan glycosyltransferases LARGE2 and ISPD associate with increased mortality in clear cell renal cell carcinoma.Comprehensive target capture/next-generation sequencing as a second-tier diagnostic approach for congenital muscular dystrophy in Taiwan.Milder forms of muscular dystrophy associated with POMGNT2 mutations.Global serum glycoform profiling for the investigation of dystroglycanopathies & Congenital Disorders of Glycosylation.ISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol phosphate onto α-dystroglycan.Phosphorylation of spore coat proteins by a family of atypical protein kinases.Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of α-dystroglycanMining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins.LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.Structure of protein O-mannose kinase reveals a unique active site architecture.Evolution of protein N-glycosylation process in Golgi apparatus which shapes diversity of protein N-glycan structures in plants, animals and fungiDissecting the molecular basis of the role of the O-mannosylation pathway in disease: α-dystroglycan and forms of muscular dystrophy.A novel missense mutation in POMT1 modulates the severe congenital muscular dystrophy phenotype associated with POMT1 nonsense mutations.Protein O-mannosylation in metazoan organisms.
P2860
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P248
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P2860
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
description
2013 nî lūn-bûn
@nan
2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@ast
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@en
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@en-gb
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@nl
type
label
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@ast
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@en
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@en-gb
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@nl
prefLabel
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@ast
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@en
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@en-gb
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@nl
P2093
P2860
P921
P3181
P356
P1433
P1476
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
@en
P2093
David Venzke
Francesco Muntoni
Mary E Anderson
Stanley F Nelson
Takako Yoshida-Moriguchi
Tamieka Whyte
Tobias Willer
P2860
P304
P3181
P356
10.1126/SCIENCE.1239951
P407
P577
2013-08-08T00:00:00Z