Functional Domains of HSV-1 Glycoproteins Gb and Gc

Holland, Thomas C.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Allergy and Infectious Diseases (NIAID)
• Type: Research Project (R01)
• Project #: 5R01AI022162-11
• Application #: 2061731
• Study Section: Experimental Virology Study Section (EVR)
• Project Start: 1985-04-01
• Project End: 1998-06-30
• Budget Start: 1996-01-01
• Budget End: 1998-06-30
• Support Year: 11
• Fiscal Year: 1996

Institution

• Name: Wayne State University
• Department: Microbiology/Immun/Virology
• Type: Schools of Medicine
• City: Detroit
• State: MI
• Country: United States
• Zip Code: 48202

Publications

Mo, C; Holland, T C (1997) Determination of the transmembrane topology of herpes simplex virus type 1 glycoprotein K. J Biol Chem 272:33305-11

Dolter, K E; Ramaswamy, R; Holland, T C (1994) Syncytial mutations in the herpes simplex virus type 1 gK (UL53) gene occur in two distinct domains. J Virol 68:8277-81

Dolter, K E; King, S R; Holland, T C (1993) Incorporation of CD4 into virions by a recombinant herpes simplex virus. J Virol 67:189-95

Skoff, A M; Holland, T C (1993) The effect of cytoplasmic domain mutations on membrane anchoring and glycoprotein processing of herpes simplex virus type 1 glycoprotein C. Virology 196:804-16

Ramaswamy, R; Holland, T C (1992) In vitro characterization of the HSV-1 UL53 gene product. Virology 186:579-87

Martin, L B; Montgomery, P C; Holland, T C (1992) Soluble glycoprotein D blocks herpes simplex virus type 1 infection of rat eyes. J Virol 66:5183-9