Albright, Brandon S; Kosinski, Athena; Szczepaniak, Renata et al. (2015) The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection. J Virol 89:443-53
|
Smith, Samantha; Weller, Sandra K (2015) HSV-I and the cellular DNA damage response. Future Virol 10:383-397
|
Grady, Lorry M; Bai, Ping; Weller, Sandra K (2014) HSV-1 protein expression using recombinant baculoviruses. Methods Mol Biol 1144:293-304
|
Szczepaniak, Renata; Nellissery, Jacob; Jadwin, Joshua A et al. (2011) Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons. J Virol 85:8625-34
|
Albright, Brandon S; Nellissery, Jacob; Szczepaniak, Renata et al. (2011) Disulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation. J Virol 85:8616-24
|
Weller, Sandra K (2010) Herpes simplex virus reorganizes the cellular DNA repair and protein quality control machinery. PLoS Pathog 6:e1001105
|
Bastian, Thomas W; Livingston, Christine M; Weller, Sandra K et al. (2010) Herpes simplex virus type 1 immediate-early protein ICP22 is required for VICE domain formation during productive viral infection. J Virol 84:2384-94
|
Livingston, Christine M; Ifrim, Marius F; Cowan, Ann E et al. (2009) Virus-Induced Chaperone-Enriched (VICE) domains function as nuclear protein quality control centers during HSV-1 infection. PLoS Pathog 5:e1000619
|
Livingston, Christine M; DeLuca, Neal A; Wilkinson, Dianna E et al. (2008) Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation. J Virol 82:6324-36
|
Saffran, Holly A; Pare, Justin M; Corcoran, Jennifer A et al. (2007) Herpes simplex virus eliminates host mitochondrial DNA. EMBO Rep 8:188-93
|
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