One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide - Wikidata - wikimedia - TriplyDB

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

http://www.wikidata.org/entity/Q34188910

about

Leu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experiment Glycosylation and specific deamidation of ribonuclease B affect the formation of three-dimensional domain-swapped oligomers.Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site-specific glycosylation in yeast.Protein multifunctionality: principles and mechanisms.A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.Prion protein glycosylation.Slow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein.Chemical approaches to study O-GlcNAcylation.How do amino acid substitutions affect the amyloidogenic properties and seeding efficiency of prion peptides Sperm DNA-mediated reduction of nonspecific fluorescence during cellular imaging with quantum dots.Excess APP O-glycosylation by GalNAc-T6 decreases Aβ production.OGlcNAcylation and phosphorylation have similar structural effects in α-helices: post-translational modifications as inducible start and stop signals in α-helices, with greater structural effects on threonine modification.Dissociation of recombinant prion autocatalysis from infectivity.Fate of pathological prion (PrP(sc)92-138) in soil and water: prion-clay nanoparticle molecular dynamics.Structural and functional studies of differentially O-glycosylated analogs of a thrombin inhibitory peptide - variegin.Sialylated and O-glycosidically linked glycans in prion protein deposits in a case of Gerstmann-Sträussler-Scheinker disease.A New Caged-Glutamine Derivative as a Tool To Control the Assembly of Glutamine-Containing Amyloidogenic Peptides.

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P2860

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

http://www.wikidata.org/entity/Q34188910

description

2002 nî lūn-bûn

@nan

2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@ast

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@en

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

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type

label

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@ast

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@en

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@nl

prefLabel

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@ast

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@en

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@nl

P1433

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P1433

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

P1476

One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide

@en

P2093

Chun-Cheng Lin

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

Su-Ching Lin

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

Sunney I Chan

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

Yin-Ting Chang

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

P2860

Prion Protein Biology

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

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

The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine

Glycosylation differences between the normal and pathogenic prion protein isoforms

Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform

Prion protein interconversions and the transmissible spongiform encephalopathies.

Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation

P304

12633-12638

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scholarly article

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10.1073/PNAS.192137799

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20

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99

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2002-09-16T00:00:00Z

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11156035

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12235358

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P921

Prion protein family

P932

130512

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