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The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection.

Albright BS, Kosinski A, Szczepaniak R, Cook EA, Stow ND, Conway JF, Weller SK.

J Virol. 2015 Jan;89(1):443-53. doi: 10.1128/JVI.01913-14. Epub 2014 Oct 15.


Disulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation.

Albright BS, Nellissery J, Szczepaniak R, Weller SK.

J Virol. 2011 Sep;85(17):8616-24. doi: 10.1128/JVI.00123-11. Epub 2011 May 18.

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