Ryan Hagglund, Ph.D.
|2003||University of Chicago, Chicago, IL|
Mean distance: 17.48 (cluster 41)
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|Hagglund R, Roizman B. (2004) Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1. Journal of Virology. 78: 2169-78|
|Hagglund R, Roizman B. (2003) Herpes simplex virus 1 mutant in which the ICP0 HUL-1 E3 ubiquitin ligase site is disrupted stabilizes cdc34 but degrades D-type cyclins and exhibits diminished neurotoxicity. Journal of Virology. 77: 13194-202|
|Munger J, Hagglund R, Roizman B. (2003) Infected cell protein No. 22 is subject to proteolytic cleavage by caspases activated by a mutant that induces apoptosis. Virology. 305: 364-70|
|Hagglund R, Roizman B. (2002) Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0. Proceedings of the National Academy of Sciences of the United States of America. 99: 7889-94|
|Hagglund R, Van Sant C, Lopez P, et al. (2002) Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes. Proceedings of the National Academy of Sciences of the United States of America. 99: 631-6|
|Hagglund R, Munger J, Poon AP, et al. (2002) U(S)3 protein kinase of herpes simplex virus 1 blocks caspase 3 activation induced by the products of U(S)1.5 and U(L)13 genes and modulates expression of transduced U(S)1.5 open reading frame in a cell type-specific manner. Journal of Virology. 76: 743-54|
|Advani SJ, Hagglund R, Weichselbaum RR, et al. (2001) Posttranslational processing of infected cell proteins 0 and 4 of herpes simplex virus 1 is sequential and reflects the subcellular compartment in which the proteins localize. Journal of Virology. 75: 7904-12|
|Van Sant C, Hagglund R, Lopez P, et al. (2001) The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity. Proceedings of the National Academy of Sciences of the United States of America. 98: 8815-20|