The Fate of PrP GPI-Anchor Signal Peptide is Modulated by P238S Pathogenic Mutation-Reference-Cited by-同舟云学术

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The Fate of PrP GPI-Anchor Signal Peptide is Modulated by P238S Pathogenic Mutation

Published:2013-10-31 Issue:1 Volume:15 Page:78-93
ISSN:1398-9219
Container-title:Traffic
language:en
Short-container-title:Traffic

Author:

Guizzunti Gianni¹,Zurzolo Chiara¹

Affiliation:

1. Institut Pasteur; Unité de Trafic Membranaire et Pathogenèse; 25-28 rue du Docteur Roux 75015 Paris France

Funder

Federation of European Biochemical Societies (FEBS)

Fondation pour la Recherche Médicale (FRM)

European Union

Agence Nationale de la Recherche

Pasteur-Weizmann Foundation

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/tra.12126/fullpdf

Reference56 articles.

1. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids;Orlean;J Lipid Res,2007

2. The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes;McConville;Biochem J,1993

3. Protein translocation across the endoplasmic reticulum;Walter;Cell,1984

4. PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8;Ohishi;EMBO J,2001

5. Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase;Eisenhaber;Protein Eng,1998

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