Making Contact: VAP Targeting by Intracellular Pathogens

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Making Contact: VAP Targeting by Intracellular Pathogens

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Making Contact: VAP Targeting by Intracellular Pathogens

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Making Contact: VAP Targeting by Intracellular Pathogens

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Making Contact: VAP Targeting by Intracellular Pathogens

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Making Contact: VAP Targeting by Intracellular Pathogens

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Making Contact: VAP Targeting by Intracellular Pathogens

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Making Contact: VAP Targeting by Intracellular Pathogens

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P1476

Making Contact: VAP Targeting by Intracellular Pathogens

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P2093

Isabelle Derré

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Rebecca Stanhope

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P2860

The lipid transfer protein CERT interacts with the Chlamydia inclusion protein IncD and participates to ER-Chlamydia inclusion membrane contact sites

Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies

Chlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular development

Building Viral Replication Organelles: Close Encounters of the Membrane Types

Reconceptualizing the chlamydial inclusion as a pathogen-specified parasitic organelle: an expanded role for Inc proteins.

Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning.

VAP, a Versatile Access Point for the Endoplasmic Reticulum: Review and analysis of FFAT-like motifs in the VAPome.

Interactions between the Coxiella burnetii parasitophorous vacuole and the endoplasmic reticulum involve the host protein ORP1L.

Noroviruses Co-opt the Function of Host Proteins VAPA and VAPB for Replication via a Phenylalanine-Phenylalanine-Acidic-Tract-Motif Mimic in Nonstructural Viral Protein NS1/2.

Rhinovirus uses a phosphatidylinositol 4-phosphate/cholesterol counter-current for the formation of replication compartments at the ER-Golgi interface.

P31

scholarly article

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10.1177/2515256418775512

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English

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P577

2018-01-01T00:00:00Z

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30101212

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6083021

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