The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein. - Wikidata - awgldk - TriplyDB

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

http://www.wikidata.org/entity/Q39790846

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The novel sorting nexin SNX33 interferes with cellular PrP formation by modulation of PrP shedding Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal Is tau ready for admission to the prion club?The role of the cellular prion protein in the immune system Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases Cellular aspects of prion replication in vitro Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1 The membrane environment of endogenous cellular prion protein in primary rat cerebellar neurons The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP.Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs Clearance and prevention of prion infection in cell culture by anti-PrP antibodies.Pathologic prion protein infects cells by lipid-raft dependent macropinocytosis Alternative translation initiation generates cytoplasmic sheep prion protein.Lipid rafts and clathrin cooperate in the internalization of PrP in epithelial FRT cells The intriguing prion disorders.The N-terminal, polybasic region is critical for prion protein neuroprotective activity.Protease-resistant prions selectively decrease Shadoo protein.Functional mechanisms of the cellular prion protein (PrP(C)) associated anti-HIV-1 properties.Prion infection of epithelial Rov cells is a polarized event.Influence of pH on the human prion protein: insights into the early steps of misfolding.An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity.Arf6-independent GPI-anchored protein-enriched early endosomal compartments fuse with sorting endosomes via a Rab5/phosphatidylinositol-3'-kinase-dependent machinery.Bovine prion is endocytosed by human enterocytes via the 37 kDa/67 kDa laminin receptor.Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation Characterization of four new monoclonal antibodies against the distal N-terminal region of PrP(c).Prion diseases: from molecular biology to intervention strategies.A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation.Spontaneous generation of anchorless prions in transgenic mice.Lipids as targeting signals: lipid rafts and intracellular trafficking.Prion protein at the crossroads of physiology and disease.Exosomes: a bubble ride for prions?The cellular prion protein (PrP(C)): its physiological function and role in disease Modulation of Glycosaminoglycans Affects PrPSc Metabolism but Does Not Block PrPSc Uptake.Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1.The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc).Prion strain- and species-dependent effects of antiprion molecules in primary neuronal cultures Cellular prion protein: from physiology to pathology.Mutated but Not Deleted Ovine PrP(C) N-Terminal Polybasic Region Strongly Interferes with Prion Propagation in Transgenic Mice Disease-associated mutations in the prion protein impair laminin-induced process outgrowth and survival Traffic of prion protein between different compartments on the neuronal surface, and the propagation of prion disease.

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P2860

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

http://www.wikidata.org/entity/Q39790846

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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name

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

@en

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

@nl

type

label

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

@en

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

@nl

prefLabel

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

@en

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

@nl

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P1433

The EMBO Journal

P1476

The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein.

@en

P2093

Angela Jen

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

Claire Sunyach

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

Jacques Grassi

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

Juelin Deng

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Kathleen T Fitzgerald

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Mary W McCaffrey

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Roger Morris

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Yveline Frobert

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P2860

Direct binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activity

Functional rafts in cell membranes

Mice devoid of PrP are resistant to scrapie

GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment.

Functionally different GPI proteins are organized in different domains on the neuronal surface.

The mode of anchorage to the cell surface determines both the function and the membrane location of Thy-1 glycoprotein

Copper stimulates endocytosis of the prion protein

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

Mapping the early steps in the pH-induced conformational conversion of the prion protein.

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3591-3601

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10.1093/EMBOJ/CDG344

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14

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22

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2003-07-01T00:00:00Z

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6630623

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12853474

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Prion protein family

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165614

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