Aberrant trafficking of hepatitis B virus glycoproteins in cells in which N-glycan processing is inhibited - Wikidata - awgldk - TriplyDB

Aberrant trafficking of hepatitis B virus glycoproteins in cells in which N-glycan processing is inhibited

Aberrant trafficking of hepatitis B virus glycoproteins in cells in which N-glycan processing is inhibited

http://www.wikidata.org/entity/Q36042105

about

Alpha-glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum Study of the mechanism of antiviral action of iminosugar derivatives against bovine viral diarrhea virus α-Glucosidase inhibitors as potential broad based anti-viral agents Phosphorothioate di- and trinucleotides as a novel class of anti-hepatitis B virus agents.O-glycan sialylation and the structure of the stalk-like region of the T cell co-receptor CD8.Hepatitis B virus large and middle glycoproteins are degraded by a proteasome pathway in glucosidase-inhibited cells but not in cells with functional glucosidase enzyme.Structure-activity relationship of a new class of anti-hepatitis B virus agents.Evolving therapies for the treatment of chronic hepatitis B virus infection.Enhanced Aromatic Sequons Increase Oligosaccharyltransferase Glycosylation Efficiency and Glycan Homogeneity.The alkylated imino sugar, n-(n-Nonyl)-deoxygalactonojirimycin, reduces the amount of hepatitis B virus nucleocapsid in tissue culture.Clathrin mediates infectious hepatitis C virus particle egress.Structure and glycosylation patterns of surface proteins from woodchuck hepatitis virus.alpha-Glucosidase inhibitors have a prolonged antiviral effect against hepatitis B virus through the sustained inhibition of the large and middle envelope glycoproteins.Fine mapping of hepatitis B virus pre-S deletion and its association with hepatocellular carcinoma.Treatment of chronic hepadnavirus infection in a woodchuck animal model with an inhibitor of protein folding and trafficking.

P2860

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P2860

Aberrant trafficking of hepatitis B virus glycoproteins in cells in which N-glycan processing is inhibited

http://www.wikidata.org/entity/Q36042105

description

1997 nî lūn-bûn

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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1997年论文

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1997年论文

@zh-cn

name

Aberrant trafficking of hepati ...... glycan processing is inhibited

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Aberrant trafficking of hepati ...... glycan processing is inhibited

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type

label

Aberrant trafficking of hepati ...... glycan processing is inhibited

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Aberrant trafficking of hepati ...... glycan processing is inhibited

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prefLabel

Aberrant trafficking of hepati ...... glycan processing is inhibited

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Aberrant trafficking of hepati ...... glycan processing is inhibited

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Aberrant trafficking of hepati ...... glycan processing is inhibited

@en

P2093

A Mehta

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

B S Blumberg

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M Dadmarz

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R Dwek

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

T M Block

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X Lu

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P2860

Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control

Demonstration that Golgi endo-alpha-D-mannosidase provides a glucosidase-independent pathway for the formation of complex N-linked oligosaccharides of glycoproteins

Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum.

How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.

Production of hepatitis B virus particles in Hep G2 cells transfected with cloned hepatitis B virus DNA.

Secretion of human hepatitis B virus is inhibited by the imino sugar N-butyldeoxynojirimycin

Protease-induced infectivity of hepatitis B virus for a human hepatoblastoma cell line.

Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex.

Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus

Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment.

P304

2380-2385

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scholarly article

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10.1073/PNAS.94.6.2380

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6

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94

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1997-03-01T00:00:00Z

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14096529

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9122203

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20096

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