Zhou G.; Avitabile E.; Campadelli-Fiume G.; Roizman B., The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectin1, «JOURNAL OF VIROLOGY», 2003, 77, pp. 3759 - 3767 [articolo]
Menotti L.; Avitabile E.; Dubreuil P.; Lopez M.; Campadelli-Fiume G., Comparison of murine and human nectin1 binding to herpes simplex virus glycoprotein D (gD) reveals a weak interaction of murine nectin1 to gD and a gD-dependent pathway of entry, «VIROLOGY», 2001, 282, pp. 256 - 266 [articolo]
Lopez M.; Cocchi F.; Avitabile E.; Leclerc A.; Adelaide J.; Campadelli-Fiume G.; Dubreuil P., Novel, soluble isoform of the herpes simplex virus (HSV) receptor nectin1 (or PRR1-HIgR-HveC) modulates positively and negatively susceptibility to HSV infection, «JOURNAL OF VIROLOGY», 2001, 75, pp. 5684 - 5691 [articolo]
Lopez M.; Cocchi F.; Menotti L.; Avitabile E.; Dubreuil P.; Campadelli-Fiume G., Nectin2α (PRR2α or HveB) and nectin2δ are low-efficiency mediators for entry of herpes simplex virus mutants carrying the Leu25Pro substitution in glycoprotein D, «JOURNAL OF VIROLOGY», 2000, 74, pp. 1267 - 1274 [articolo]
Menotti L.; Lopez M.; Avitabile E.; Stefan A.; Cocchi F.; Adelaide J.; Lecocq E.; Dubreuil P.; Campadelli-Fiume G., The murine homolog of human Nectin1δ serves as a species nonspecific mediator for entry of human and animal αherpesviruses in a pathway independent of a detectable binding to gD, «PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA», 2000, 97, pp. 4867 - 4872 [articolo]
Ward P.L.; Avitabile E.; Campadelli-Fiume G.; Roizman B., Conservation of the architecture of the Golgi apparatus related to a differential organization of microtubules in polykaryocytes induced by syn- mutants of herpes simplex virus 1, «VIROLOGY», 1998, 241, pp. 189 - 199 [articolo]
Kempf W.; Adams V.; Wey N.; Moos R.; Schmid M.; Avitabile E.; Campadelli-Fiume G., CD68+ cells of monocyte/macrophage lineage in the environment of AIDS-associated and classic-sporadic Kaposi sarcoma are singly or doubly infected with human herpesviruses 7 and 6B, «PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA», 1997, 94, pp. 7600 - 7605 [articolo]
Foa-Tomasi L.; Fiorilli M.P.; Avitabile E.; Campadelli-Fiume G., Identification of an 85 kDa phosphoprotein as an immunodominant protein specific for human herpesvirus 7-infected cells, «JOURNAL OF GENERAL VIROLOGY», 1996, 77, pp. 511 - 518 [articolo]
Avitabile E.; Di Gaeta S.; Torrisi M.R.; Ward P.L.; Roizman B.; Campadelli-Fiume G., Redistribution of microtubules and Golgi apparatus in herpes simplex virus-infected cells and their role in viral exocytosis, «JOURNAL OF VIROLOGY», 1995, 69, pp. 7472 - 7482 [articolo]
Foa-tomasi L.; Avitabile E.; Campadelli-fiume G., Selection of a monoclonal antibody specific for variant B human herpesvirus 6-infected mononuclear cells, «JOURNAL OF VIROLOGICAL METHODS», 1995, 51, pp. 289 - 296 [articolo]
Ward P.L.; Campadelli-Fiume G.; Avitabile E.; Roizman B., Localization and putative function of the U(L)20 membrane protein in cells infected with herpes simplex virus 1, «JOURNAL OF VIROLOGY», 1994, 68, pp. 7406 - 7417 [articolo]
Foa-Tomasi L.; Avitabile E.; Ke L.; Campadelli-Fiume G., Polyvalent and monoclonal antibodies identify major immunogenic proteins specific for human herpesvirus 7-infected cells and have weak cross-reactivity with human herpesvirus 6, «JOURNAL OF GENERAL VIROLOGY», 1994, 75, pp. 2719 - 2727 [articolo]
Avitabile E.; Ward P.L.; Di Lazzaro C.; Torrisi M.R.; Roizman B.; Campadelli- Fiume G., The herpes simplex virus U(L)20 protein compensates for the differential disruption of exocytosis of virions and viral membrane glycoproteins associated with fragmentation of the Golgi apparatus, «JOURNAL OF VIROLOGY», 1994, 68, pp. 7397 - 7405 [articolo]
Foa-Tomasi L.; Avitabile E.; Boscaro A.; Brandimarti R.; Gualandri R.; Manservigi R.; Dall'olioj F.; Serafini-Cessij F.; Campadelli Fiume G., Herpes simplex virus (HSV) glycoprotein h is partially processed in a cell line that expresses the glycoprotein and fully processed in cells infected with deletion or is mutants in the known hsv glycoproteins, «VIROLOGY», 1991, 180, pp. 474 - 482 [articolo]
Campadelli-Fiume G.; Stirpe D.; Boscaro A.; Avitabile E.; Foa-Tomasi L.; Barker D.; Roizman B., Glycoprotein C-dependent attachment of herpes simplex virus to susceptible cells leading to productive infection, «VIROLOGY», 1990, 178, pp. 213 - 222 [articolo]
