Glycosylation differences between the normal and pathogenic prion protein isoforms - Wikidata - awgldk - TriplyDB

Glycosylation differences between the normal and pathogenic prion protein isoforms

Glycosylation differences between the normal and pathogenic prion protein isoforms

http://www.wikidata.org/entity/Q30810971

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Large-scale approaches for glycobiology.Multifaceted Role of Sialylation in Prion Diseases Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1 PK-sensitive PrP is infectious and shares basic structural features with PK-resistant PrP Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo Acquisition of drug resistance and dependence by prions Attachment of pathogenic prion protein to model oxide surfaces.Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor.Brain glycogen re-awakened.Species and strain glycosylation patterns of PrPSc The intriguing prion disorders.Genes contributing to prion pathogenesis Novel antibody-lectin enzyme-linked immunosorbent assay that distinguishes prion proteins in sporadic and variant cases of Creutzfeldt-Jakob disease.Deletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform.N-glycosylation and biological activity of recombinant human alpha1-antitrypsin expressed in a novel human neuronal cell line.One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide Confident assignment of site-specific glycosylation in complex glycoproteins in a single step Propagation of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strain Lipopolysaccharide induced conversion of recombinant prion protein.The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1-->2 mannose residues on the outer face of gp120.Searching for reliable premortem protein biomarkers for prion diseases: progress and challenges to date.Prion and doppel proteins bind to granule cells of the cerebellum Altered functionality of anti-bacterial antibodies in patients with chronic hepatitis C virus infection A quantitative proteomic approach to prion disease biomarker research: delving into the glycoproteome.Revisiting the Role of Acetylcholinesterase in Alzheimer's Disease: Cross-Talk with P-tau and β-Amyloid Characterization of spontaneously generated prion-like conformers in cultured cells.Glycosylation of prion strains in transmissible spongiform encephalopathies.The systems biology of glycosylation.Prion protein glycosylation.Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio Post-conversion sialylation of prions in lymphoid tissues.Stressing out the ER: a role of the unfolded protein response in prion-related disorders Chemoenzymatic method for glycomics: Isolation, identification, and quantitation.Synthetic prions.Prion strain discrimination in cell culture: the cell panel assay A structural overview of the vertebrate prion proteins.Prions: Beyond a Single Protein.

P2860

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P2860

Glycosylation differences between the normal and pathogenic prion protein isoforms

http://www.wikidata.org/entity/Q30810971

description

1999 nî lūn-bûn

@nan

1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի նոյեմբերին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Glycosylation differences between the normal and pathogenic prion protein isoforms

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Glycosylation differences between the normal and pathogenic prion protein isoforms

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type

label

Glycosylation differences between the normal and pathogenic prion protein isoforms

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Glycosylation differences between the normal and pathogenic prion protein isoforms

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Glycosylation differences between the normal and pathogenic prion protein isoforms

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Glycosylation differences between the normal and pathogenic prion protein isoforms

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PNAS.96.23.13044

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

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Glycosylation differences between the normal and pathogenic prion protein isoforms

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Colominas C

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Dwek RA

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Endo T

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Groth D

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Harvey DJ

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Wheeler SF

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Wormald MR

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P2860

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

NMR structure of the mouse prion protein domain PrP(121-231)

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform

Eight prion strains have PrP(Sc) molecules with different conformations

Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies expressed in Chinese hamster ovary cells.

A statistical analysis of N- and O-glycan linkage conformations from crystallographic data.

Sialylated N-glycans in adult rat brain tissue--a widespread distribution of disialylated antennae in complex and hybrid structures.

Prion protein conformation in a patient with sporadic fatal insomnia.

Human N-acetylglucosaminyltransferase III gene is transcribed from multiple promoters.

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13044-13049

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scholarly article

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23

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Stanley B. Prusiner

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235610750

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10557270

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Prion protein family

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