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Classical Swine Fever Virus p7 Protein Interacts with Host Protein CAMLG and Regulates Calcium Perme...

Classical Swine Fever Virus p7 Protein Interacts with Host Protein CAMLG and Regulates Calcium Perme...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_0224ea974d694f75b6761246635b39d0

Classical Swine Fever Virus p7 Protein Interacts with Host Protein CAMLG and Regulates Calcium Permeability at the Endoplasmic Reticulum

About this item

Full title

Classical Swine Fever Virus p7 Protein Interacts with Host Protein CAMLG and Regulates Calcium Permeability at the Endoplasmic Reticulum

Publisher

Switzerland: MDPI AG

Journal title

Viruses, 2018-08, Vol.10 (9), p.460

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

We have previously shown that Classical Swine Fever Virus (CSFV) p7 is an essential nonstructural protein with a viroporin activity, a critical function in the progression of virus infection. We also identified p7 domains and amino acid residues critical for pore formation. Here, we describe how p7 specifically interacts with host protein CAMLG, an...

Alternative Titles

Full title

Classical Swine Fever Virus p7 Protein Interacts with Host Protein CAMLG and Regulates Calcium Permeability at the Endoplasmic Reticulum

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_0224ea974d694f75b6761246635b39d0

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_0224ea974d694f75b6761246635b39d0

Other Identifiers

ISSN

1999-4915

E-ISSN

1999-4915

DOI

10.3390/v10090460

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