The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors-Reference-Cited by-同舟云学术

The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors

Published:2005-06-21 Issue:26 Volume:102 Page:9323-9328
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Fusco D.,Forghieri C.,Campadelli-Fiume G.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference40 articles.

1. The novel receptors that mediate the entry of herpes simplex viruses and animal alphaherpesviruses into cells

2. Three Classes of Cell Surface Receptors for Alphaherpesvirus Entry

3. Entry of Alphaherpesviruses Mediated by Poliovirus Receptor-Related Protein 1 and Poliovirus Receptor

4. Herpes Simplex Virus-1 Entry into Cells Mediated by a Novel Member of the TNF/NGF Receptor Family

5. The Ectodomain of a Novel Member of the Immunoglobulin Subfamily Related to the Poliovirus Receptor Has the Attributes of a Bona Fide Receptor for Herpes Simplex Virus Types 1 and 2 in Human Cells

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