ISBN: 9783639088427 - tia-1 and herpes simplex virus type 1: an interaction: the influence of tia-1 on hsv-1 replication (6 resultados)

Taschenbuch. Condición: Neu. TIA-1 and Herpes Simplex Virus Type 1: An Interaction | The Influence of TIA-1 on HSV-1 Replication | William Stewart | Taschenbuch | 64 S. | Deutsch | 2012 | VDM Verlag Dr. Müller e.K. | EAN 9783639088427 | Verantwortliche Person für die EU: BoD - Books on Demand, In de Tarpen 42, 22848 Norderstedt, info[at]bod[dot]de | Anbieter: preigu.…

Paperback. Condición: Brand New. 156 pages. 8.66x5.90x0.36 inches. In Stock.

Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -During the process of protein translation, phosphorylation of eIF2-alpha prevents its binding to the preinitiation complex and hence the process of translation. The RNA binding protein, TIA-1, then directs these complexes to molecular storage depots known as stress granules. The replication of HSV-1, containing different variants of the ICP34.5 gene and those without the ICP34.5 gene were compared in diploid fibroblasts obtained from normal mice, those lacking TIA-1 and reconstituted with TIA-1. This research showed that HSV-1 replicates better in cells that lack TIA-1. The extent of viral replication was strain dependent. This shows that the cell has a method for preventing viral replication. The functions of TIA-1 include the formation of stress granules in cells which undergo abortive protein translation and cytokine modulation. This study explores the possibility of interaction of the cellular protein, TIA-1 at the viral replication level. The possibility may be that TIA-1 affects, in a strain dependent manner, replication of HSV-1. A potential mechanism for antiviral properties of the cellular protein TIA-1 is be discussed. 64 pp. Deutsch.…

Taschenbuch. Condición: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - During the process of protein translation, phosphorylation of eIF2-alpha prevents its binding to the preinitiation complex and hence the process of translation. The RNA binding protein, TIA-1, then directs these complexes to molecular storage depots known as stress granules. The replication of HSV-1, containing different variants of the ICP34.5 gene and those without the ICP34.5 gene were compared in diploid fibroblasts obtained from normal mice, those lacking TIA-1 and reconstituted with TIA-1. This research showed that HSV-1 replicates better in cells that lack TIA-1. The extent of viral replication was strain dependent. This shows that the cell has a method for preventing viral replication. The functions of TIA-1 include the formation of stress granules in cells which undergo abortive protein translation and cytokine modulation. This study explores the possibility of interaction of the cellular protein, TIA-1 at the viral replication level. The possibility may be that TIA-1 affects, in a strain dependent manner, replication of HSV-1. A potential mechanism for antiviral properties of the cellular protein TIA-1 is be discussed.…

Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. During the process of protein translation, phosphorylation of eIF2-alpha prevents its binding to the preinitiation complex and hence the process of translation. The RNA binding protein, TIA-1, then directs these complexes to molecular storage depots known a. …

Taschenbuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -During the process of protein translation, phosphorylation of eIF2-alpha prevents its binding to the preinitiation complex and hence the process of translation. The RNA binding protein, TIA-1, then directs these complexes to molecular storage depots known as stress granules. The replication of HSV-1, containing different variants of the ICP34.5 gene and those without the ICP34.5 gene were compared in diploid fibroblasts obtained from normal mice, those lacking TIA-1 and reconstituted with TIA-1. This research showed that HSV-1 replicates better in cells that lack TIA-1. The extent of viral replication was strain dependent. This shows that the cell has a method for preventing viral replication. The functions of TIA-1 include the formation of stress granules in cells which undergo abortive protein translation and cytokine modulation. This study explores the possibility of interaction of the cellular protein, TIA-1 at the viral replication level. The possibility may be that TIA-1 affects, in a strain dependent manner, replication of HSV-1. A potential mechanism for antiviral properties of the cellular protein TIA-1 is be discussed.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 64 pp. Deutsch.…