Terminal N-linked galactose is the primary receptor for adeno-associated virus 9. - Wikidata - awgldk - TriplyDB

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

http://www.wikidata.org/entity/Q34787342

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Biology of adeno-associated viral vectors in the central nervous system Adeno-associated Virus as a Mammalian DNA Vector Parvovirus glycan interactions Axonal transport of AAV9 in nonhuman primate brain.Predictors of hepatitis B cure using gene therapy to deliver DNA cleavage enzymes: a mathematical modeling approach Structural Insight into the Unique Properties of Adeno-Associated Virus Serotype 9 Structural Insights into Adeno-Associated Virus Serotype 5 Electron microscopy analysis of a disaccharide analog complex reveals receptor interactions of adeno-associated virus Gene delivery to the spinal cord using MRI-guided focused ultrasound Adeno-associated virus serotype 9 efficiently targets ischemic skeletal muscle following systemic delivery.Adeno-associated virus serotype 9 administered systemically after reperfusion preferentially targets cardiomyocytes in the infarct border zone with pharmacodynamics suitable for the attenuation of left ventricular remodeling.Quantitative 3D tracing of gene-delivery viral vectors in human cells and animal tissues.Sialic acid deposition impairs the utility of AAV9, but not peptide-modified AAVs for brain gene therapy in a mouse model of lysosomal storage disease Comparative analysis of adeno-associated virus capsid stability and dynamics Association analyses of large-scale glycan microarray data reveal novel host-specific substructures in influenza A virus binding glycans Systemic gene delivery to the central nervous system using Adeno-associated virus.Biodistribution of adeno-associated virus serotype 9 (AAV9) vector after intrathecal and intravenous delivery in mouse Peptide ligands incorporated into the threefold spike capsid domain to re-direct gene transduction of AAV8 and AAV9 in vivo Gene transfer to the CNS using recombinant adeno-associated virus Adeno-associated virus serotypes 1, 8, and 9 share conserved mechanisms for anterograde and retrograde axonal transport.Adeno-associated virus: fit to serve Intravenous AAV9 efficiently transduces myenteric neurons in neonate and juvenile mice.AAV9 targets cone photoreceptors in the nonhuman primate retina.Multiple roles for sialylated glycans in determining the cardiopulmonary tropism of adeno-associated virus 4 Analysis of transduction efficiency, tropism and axonal transport of AAV serotypes 1, 2, 5, 6, 8 and 9 in the mouse brain.The AAV9 receptor and its modification to improve in vivo lung gene transfer in mice Functional analysis of the putative integrin recognition motif on adeno-associated virus 9.Gene transfer properties and structural modeling of human stem cell-derived AAV.The expression pattern of systemically injected AAV9 in the developing mouse retina is determined by age Effectiveness of gene delivery systems for pluripotent and differentiated cells.Hybrid- and complex-type N-glycans are not essential for Newcastle disease virus infection and fusion of host cells.Intracellular transport of recombinant adeno-associated virus vectors.Controlling AAV Tropism in the Nervous System with Natural and Engineered Capsids.The AAV vector toolkit: poised at the clinical crossroads Methods for gene transfer to the central nervous system.In Vivo Selection Yields AAV-B1 Capsid for Central Nervous System and Muscle Gene Therapy Robust Lentiviral Gene Delivery But Limited Transduction Capacity of Commonly Used Adeno-Associated Viral Serotypes in Xenotransplanted Human Skin.Advances in cell and gene-based therapies for cystic fibrosis lung disease Systemic gene delivery following intravenous administration of AAV9 to fetal and neonatal mice and late-gestation nonhuman primates.Genome-wide RNAi screening identifies host restriction factors critical for in vivo AAV transduction

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P2860

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

http://www.wikidata.org/entity/Q34787342

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

@zh-tw

2011年论文

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name

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@ast

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@en

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@nl

type

label

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@ast

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@en

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@nl

prefLabel

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@ast

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@en

Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@nl

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JBC.M110.210922

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Journal of Biological Chemistry

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Terminal N-linked galactose is the primary receptor for adeno-associated virus 9.

@en

P2093

Aravind Asokan

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

Kelli D Bryant

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Sarah M Brown

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Scott H Randell

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Shen Shen

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

P2860

Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity

Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions

Sialidase enhances recovery from spinal cord contusion injury

Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry

Structural Characterization of the Dual Glycan Binding Adeno-Associated Virus Serotype 6

Attachment and cell entry of mammalian orthoreovirus

Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor

Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation

Sialidase fusion protein as a novel broad-spectrum inhibitor of influenza virus infection.

Novel pandemic influenza A(H1N1) viruses are potently inhibited by DAS181, a sialidase fusion protein.

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15

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286

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2011-02-17T00:00:00Z

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21330365

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3075699

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