Signal Peptide Peptidase-catalyzed Cleavage of Hepatitis C Virus Core Protein Is Dispensable for Virus Budding but Destabilizes the Viral Capsid-Reference-Cited by-同舟云学术

Signal Peptide Peptidase-catalyzed Cleavage of Hepatitis C Virus Core Protein Is Dispensable for Virus Budding but Destabilizes the Viral Capsid

Published:2006-09 Issue:38 Volume:281 Page:27679-27692
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Vauloup-Fellous Christelle,Pène Véronique,Garaud-Aunis Julie,Harper Francis,Bardin Sabine,Suire Yannick,Pichard Evelyne,Schmitt Alain,Sogni Philippe,Pierron Gérard,Briand Pascale,Rosenberg Arielle R.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference72 articles.

1. Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs

2. Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease

3. Drosophila Signal Peptide Peptidase Is an Essential Protease for Larval Development

4. Expression of the presenilin-like signal peptide peptidase (SPP) in mouse adult brain and during development

5. Consensus Analysis of Signal Peptide Peptidase and Homologous Human Aspartic Proteases Reveals Opposite Topology of Catalytic Domains Compared with Presenilins

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1. BmSPP is a virus resistance gene in Bombyx mori;Frontiers in Immunology;2024-03-22

2. Signal peptide peptidase: a potential therapeutic target for parasitic and viral infections;Expert Opinion on Therapeutic Targets;2022-03-04

3. Very-long-chain fatty acid metabolic capacity of 17-beta-hydroxysteroid dehydrogenase type 12 (HSD17B12) promotes replication of hepatitis C virus and related flaviviruses;Scientific Reports;2020-03-04

4. The potential of signal peptide peptidase as a therapeutic target for hepatitis C;Expert Opinion on Therapeutic Targets;2017-08-22

5. Role of cleavage at the core-E1 junction of hepatitis C virus polyprotein in viral morphogenesis;PLOS ONE;2017-04-24