Disulfide Bond Formation in the Herpes Simplex Virus 1 UL6 Protein Is Required for Portal Ring Formation and Genome Encapsidation

Disulfide Bond Formation Contributes to Herpes Simplex Virus Capsid Stability and Retention of Pentons

(2011) R. Szczepaniak et al.   JOURNAL OF VIROLOGY

Intracellular Redox Compartments: Mechanisms and Significances

(2010) Thomas Kietzmann   ANTIOXIDANTS & REDOX SIGNALING

Redox compartmentalization and cellular stress

(2010) D. P. Jones et al.   DIABETES OBESITY & METABOLISM

Virus-Induced Chaperone-Enriched (VICE) Domains Function as Nuclear Protein Quality Control Centers during HSV-1 Infection

(2009) Christine M. Livingston et al.   PLoS Pathogens

Redox compartmentalization in eukaryotic cells

(2008) Young-Mi Go et al.   BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

Amino Acids 143 to 150 of the Herpes Simplex Virus Type 1 Scaffold Protein Are Required for the Formation of Portal-Containing Capsids

(2008) J. B. Huffman et al.   JOURNAL OF VIROLOGY