Literature DB >> 3033131

A major phosphoprotein of cells infected with pseudorabies virus is phosphorylated by cellular casein kinase II.

T Jakubowicz, D P Leader.   

Abstract

Endogenous protein phosphorylation was studied in extracts of hamster fibroblasts infected with pseudorabies virus. The major phosphorylation was detected quite late in infection and involved an acidic protein of Mr 62,000. It was catalysed by an enzyme activity with the properties of cellular casein kinase II. Two-dimensional gel analysis was used to demonstrate that this same protein was also phosphorylated in vivo. The phosphoprotein was detected in mature virions and is most likely viral in origin.

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Year:  1987        PMID: 3033131     DOI: 10.1099/0022-1317-68-4-1159

Source DB:  PubMed          Journal:  J Gen Virol        ISSN: 0022-1317            Impact factor:   3.891


  4 in total

1.  Phosphorylation of simian cytomegalovirus assembly protein precursor (pAPNG.5) and proteinase precursor (pAPNG1): multiple attachment sites identified, including two adjacent serines in a casein kinase II consensus sequence.

Authors:  S M Plafker; A S Woods; W Gibson
Journal:  J Virol       Date:  1999-11       Impact factor: 5.103

2.  Identification of new protein kinase-related genes in three herpesviruses, herpes simplex virus, varicella-zoster virus, and Epstein-Barr virus.

Authors:  R F Smith; T F Smith
Journal:  J Virol       Date:  1989-01       Impact factor: 5.103

3.  Phosphorylation of varicella-zoster virus glycoprotein gpI by mammalian casein kinase II and casein kinase I.

Authors:  C Grose; W Jackson; J A Traugh
Journal:  J Virol       Date:  1989-09       Impact factor: 5.103

4.  Proteomic characterization of pseudorabies virus extracellular virions.

Authors:  T Kramer; T M Greco; L W Enquist; I M Cristea
Journal:  J Virol       Date:  2011-04-27       Impact factor: 5.103

  4 in total

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