Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. - Wikidata - wikimedia - TriplyDB

Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform.

Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform.

http://www.wikidata.org/entity/Q36235271

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Glypican-1 mediates both prion protein lipid raft association and disease isoform formation The novel sorting nexin SNX33 interferes with cellular PrP formation by modulation of PrP shedding Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease Cholesterol, lipid rafts, and disease Prions Elimination of prions by branched polyamines and implications for therapeutics Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases Prion-induced neurotoxicity: Possible role for cell cycle activity and DNA damage response Cholesterol balance in prion diseases and Alzheimer's disease Cellular aspects of prion replication in vitro Prion protein accumulation in lipid rafts of mouse aging brain Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues Differential effects of glycosphingolipids on the detergent-insolubility of the glycosylphosphatidylinositol-anchored membrane dipeptidase Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment.Glycosylation influences cross-species formation of protease-resistant prion protein.The cellular prion protein interacts with the tissue non-specific alkaline phosphatase in membrane microdomains of bioaminergic neuronal cells The membrane environment of endogenous cellular prion protein in primary rat cerebellar neurons PrPC directly interacts with proteins involved in signaling pathways Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid rafts Effects of FlAsH/tetracysteine (TC) Tag on PrP proteolysis and PrPres formation by TC-scanning.Elastic membrane heterogeneity of living cells revealed by stiff nanoscale membrane domains Specific biarsenical labeling of cell surface proteins allows fluorescent- and biotin-tagging of amyloid precursor protein and prion proteins.Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Nonpolar substitution at the C-terminus of the prion protein, a mimic of the glycosylphosphatidylinositol anchor, partially impairs amyloid fibril formation.Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs The multivesicular body is the major internal site of prion conversion.Squalestatin alters the intracellular trafficking of a neurotoxic prion peptide.New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products.Docosahexaenoic and eicosapentaenoic acids increase prion formation in neuronal cells Paracrine diffusion of PrP(C) and propagation of prion infectivity by plasma membrane-derived microvesicles Pathologic prion protein infects cells by lipid-raft dependent macropinocytosis Activation of p53-regulated pro-apoptotic signaling pathways in PrP-mediated myopathy Lipid rafts and clathrin cooperate in the internalization of PrP in epithelial FRT cells Cellular biology of prion diseases.The role of the prion protein membrane anchor in prion infection.The intriguing prion disorders.Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review).

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P2860

Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform.

http://www.wikidata.org/entity/Q36235271

description

1995 nî lūn-bûn

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1995年の論文

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年學術文章

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1995年學術文章

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1995年學術文章

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Cholesterol depletion and modi ...... mation of the scrapie isoform.

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Cholesterol depletion and modi ...... mation of the scrapie isoform.

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Cholesterol depletion and modi ...... mation of the scrapie isoform.

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Cholesterol depletion and modi ...... mation of the scrapie isoform.

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Cholesterol depletion and modi ...... mation of the scrapie isoform.

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Cholesterol depletion and modi ...... mation of the scrapie isoform.

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Cholesterol depletion and modi ...... mation of the scrapie isoform.

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P2093

Avrahami D

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Laszlo L

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Scott M

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Semenov A

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Taraboulos A

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P2860

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

Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Mice devoid of PrP are resistant to scrapie

Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface

Molecular cloning of a candidate chicken prion protein.

A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity.

Attempts to convert the cellular prion protein into the scrapie isoform in cell-free systems.

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

Lipid sorting in epithelial cells.

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121-132

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1

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129

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Stanley B. Prusiner

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247533719

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7698979

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P921

Prion protein family

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2120366

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