Two different neurodegenerative diseases caused by proteins with similar structures - Wikidata - wikimedia - TriplyDB

Two different neurodegenerative diseases caused by proteins with similar structures

Two different neurodegenerative diseases caused by proteins with similar structures

http://www.wikidata.org/entity/Q27630179

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Doppel-induced cerebellar degeneration in transgenic mice Prion-like protein Doppel expression is not modified in scrapie-infected cells and in the brains of patients with Creutzfeldt-Jakob disease The human "prion-like" protein Doppel is expressed in both Sertoli cells and spermatozoa Prion protein paralog doppel protein interacts with alpha-2-macroglobulin: a plausible mechanism for doppel-mediated neurodegeneration Evolutionary descent of prion genes from the ZIP family of metal ion transporters The PrP-like protein Doppel binds copper Comparative genomic analysis of prion genes The prion protein modulates A-type K+ currents mediated by Kv4.2 complexes through dipeptidyl aminopeptidase-like protein 6 Enhanced stability of human prion proteins with two disulfide bridges.Copper(II) binding to the human Doppel protein may mark its functional diversity from the prion protein.Similar folds with different stabilization mechanisms: the cases of Prion and Doppel proteins.Doppel and PrPC co-immunoprecipitate in detergent-resistant membrane domains of epithelial FRT cells Normal neurogenesis and scrapie pathogenesis in neural grafts lacking the prion protein homologue Doppel The N-terminal, polybasic region is critical for prion protein neuroprotective activity.Absence of the prion protein homologue Doppel causes male sterility.Protease-resistant prions selectively decrease Shadoo protein.Biochemical signatures of doppel protein in human astrocytomas to support prediction in tumor malignancy.Prion and doppel proteins bind to granule cells of the cerebellum Age-dependent impairment of eyeblink conditioning in prion protein-deficient mice.A strategy for synthesis of pathogenic human immunoglobulin free light chains in E. coli.Prion protein misfolding.Male infertility and DNA damage in Doppel knockout and prion protein/Doppel double-knockout mice Structural defects and the diagnosis of amyloidogenic propensity Did the prion protein become vulnerable to misfolding after an evolutionary divide and conquer event?Cellular prion protein: from physiology to pathology.Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations.Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil.Molecular basis of cerebral neurodegeneration in prion diseases.Prion neurotoxicity: insights from prion protein mutants Transgene-driven expression of the Doppel protein in Purkinje cells causes Purkinje cell degeneration and motor impairment Antagonistic roles of the N-terminal domain of prion protein to doppel.A structural overview of the vertebrate prion proteins.Disruption of Doppel prevents neurodegeneration in mice with extensive Prnp deletions.Prion proteins with pathogenic and protective mutations show similar structure and dynamics.Disruption of glycosylation enhances ubiquitin-mediated proteasomal degradation of Shadoo in Scrapie-infected rodents and cultured cells.Endoproteolytic processing of the mammalian prion glycoprotein family.Expression of truncated PrP targeted to Purkinje cells of PrP knockout mice causes Purkinje cell death and ataxia.alpha-Helical domains promote translocation of intrinsically disordered polypeptides into the endoplasmic reticulum The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections.Folding pathways of prion and doppel.

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P2860

Two different neurodegenerative diseases caused by proteins with similar structures

http://www.wikidata.org/entity/Q27630179

description

2001 nî lūn-bûn

@nan

2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Two different neurodegenerative diseases caused by proteins with similar structures

@ast

Two different neurodegenerative diseases caused by proteins with similar structures

@en

Two different neurodegenerative diseases caused by proteins with similar structures

@nl

type

label

Two different neurodegenerative diseases caused by proteins with similar structures

@ast

Two different neurodegenerative diseases caused by proteins with similar structures

@en

Two different neurodegenerative diseases caused by proteins with similar structures

@nl

prefLabel

Two different neurodegenerative diseases caused by proteins with similar structures

@ast

Two different neurodegenerative diseases caused by proteins with similar structures

@en

Two different neurodegenerative diseases caused by proteins with similar structures

@nl

P1433

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

P1476

Two different neurodegenerative diseases caused by proteins with similar structures

@en

P2093

D Westaway

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

H J Dyson

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

H Mo

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

P E Wright

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

R C Moore

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P2860

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

NMR solution structure of the human prion protein

NMR structure of the bovine prion protein

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

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

1H, 13C and 15N chemical shift referencing in biomolecular NMR

Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

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2352-7

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scholarly article

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10.1073/PNAS.051627998

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5

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98

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Stanley B. Prusiner

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2001-02-27T00:00:00Z

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12105722

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11226243

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neurodegeneration

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30142

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