Structural basis of agrin-LRP4-MuSK signaling - Wikidata - awgldk - TriplyDB

Structural basis of agrin-LRP4-MuSK signaling

Structural basis of agrin-LRP4-MuSK signaling

http://www.wikidata.org/entity/Q27677019

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Animal models of myasthenia gravis: utility and limitations Alterations of cAMP-dependent signaling in dystrophic skeletal muscle The role of muscle-specific tyrosine kinase (MuSK) and mystery of MuSK myasthenia gravis Crosstalk between Agrin and Wnt signaling pathways in development of vertebrate neuromuscular junction The role of WNT signaling in adult ovarian folliculogenesis LRP4 third β-propeller domain mutations cause novel congenital myasthenia by compromising agrin-mediated MuSK signaling in a position-specific manner.Building a synapse: a complex matter.LRP4 is critical for neuromuscular junction maintenance A mutation causes MuSK reduced sensitivity to agrin and congenital myasthenia.β-Catenin gain of function in muscles impairs neuromuscular junction formation.Distinct roles of muscle and motoneuron LRP4 in neuromuscular junction formation.Cholesterol: its regulation and role in central nervous system disorders.Muscle autoantibodies in myasthenia gravis: beyond diagnosis?Laminins in basement membrane assembly Agrin mediates chondrocyte homeostasis and requires both LRP4 and α-dystroglycan to enhance cartilage formation in vitro and in vivo APP interacts with LRP4 and agrin to coordinate the development of the neuromuscular junction in mice.CuZnSOD gene deletion targeted to skeletal muscle leads to loss of contractile force but does not cause muscle atrophy in adult mice Lrp4 in astrocytes modulates glutamatergic transmission Schwann Cells in Neuromuscular Junction Formation and Maintenance Antibodies against low-density lipoprotein receptor-related protein 4 induce myasthenia gravis.Structure and activation of MuSK, a receptor tyrosine kinase central to neuromuscular junction formation.Computational design of an epitope-specific Keap1 binding antibody using hotspot residues grafting and CDR loop swapping.Structural mechanisms of the agrin-LRP4-MuSK signaling pathway in neuromuscular junction differentiation.Structure of the neuromuscular junction: function and cooperative mechanisms in the synapse.The role of MuSK in synapse formation and neuromuscular disease.Pathogenic immune mechanisms at the neuromuscular synapse: the role of specific antibody-binding epitopes in myasthenia gravis.Osteoblastic Lrp4 promotes osteoclastogenesis by regulating ATP release and adenosine-A2AR signaling.Screening for lipoprotein receptor-related protein 4-, agrin-, and titin-antibodies and exploring the autoimmune spectrum in myasthenia gravis.β-Catenin regulates membrane potential in muscle cells by regulating the α2 subunit of Na,K-ATPase.Musk Kinase Activity is Modulated By A Serine Phosphorylation Site in The Kinase Loop Functional Roles of the Interaction of APP and Lipoprotein Receptors.Matrix metalloproteinase 3 deletion preserves denervated motor endplates after traumatic nerve injury.Synaptic Homeostasis and Its Immunological Disturbance in Neuromuscular Junction Disorders.Salbutamol-responsive limb-girdle congenital myasthenic syndrome due to a novel missense mutation and heteroallelic deletion in MUSK.New horizons for lipoprotein receptors: communication by β-propellers.How multi-scale structural biology elucidated context-dependent variability in ectodomain conformation along with the ligand capture and release cycle for LDLR family members.Agrin-LRP4-MuSK signaling as a therapeutic target for myasthenia gravis and other neuromuscular disorders.Increasing Agrin Function Antagonizes Muscle Atrophy and Motor Impairment in Spinal Muscular Atrophy.Induction of Anti-agrin Antibodies Causes Myasthenia Gravis in Mice.Linking Extracellular Matrix Agrin to the Hippo Pathway in Liver Cancer and Beyond.

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Structural basis of agrin-LRP4-MuSK signaling

http://www.wikidata.org/entity/Q27677019

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2012 nî lūn-bûn

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2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2012 թվականի փետրվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Structural basis of agrin-LRP4-MuSK signaling

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Structural basis of agrin-LRP4-MuSK signaling

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Structural basis of agrin-LRP4-MuSK signaling

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Structural basis of agrin-LRP4-MuSK signaling

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Structural basis of agrin-LRP4-MuSK signaling

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Structural basis of agrin-LRP4-MuSK signaling

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Structural basis of agrin-LRP4-MuSK signaling

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Structural basis of agrin-LRP4-MuSK signaling

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Structural basis of agrin-LRP4-MuSK signaling

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Genes & Development

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Structural basis of agrin-LRP4-MuSK signaling

@en

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Bin Zhang

http://www.w3.org/2001/XMLSchema#string

Dwight Figueiredo

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Guorui Yao

http://www.w3.org/2001/XMLSchema#string

Jie Zhou

http://www.w3.org/2001/XMLSchema#string

Kay Perry

http://www.w3.org/2001/XMLSchema#string

Kwangkook Lee

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Lin Mei

http://www.w3.org/2001/XMLSchema#string

Rongsheng Jin

http://www.w3.org/2001/XMLSchema#string

Shenyan Gu

http://www.w3.org/2001/XMLSchema#string

Yinong Zong

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P2860

Neuroligins and neurexins link synaptic function to cognitive disease

Cell signaling by receptor tyrosine kinases

To build a synapse: signaling pathways in neuromuscular junction assembly

MolProbity: all-atom structure validation for macromolecular crystallography

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Distinct domains of MuSK mediate its abilities to induce and to associate with postsynaptic specializations

Structure of the LDL receptor extracellular domain at endosomal pH

Complex between nidogen and laminin fragments reveals a paradigmatic beta-propeller interface

The Structure of the Glial Cell Line-derived Neurotrophic Factor-Coreceptor Complex: INSIGHTS INTO RET SIGNALING AND HEPARIN BINDING

Wnt antagonists bind through a short peptide to the first β-propeller domain of LRP5/6

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247-58

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3349135

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10.1101/GAD.180885.111

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3

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26

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2012-02-01T00:00:00Z

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22302937

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3278892

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