Mutagenic analysis of herpes simplex virus type 1 glycoprotein L reveals the importance of an arginine-rich region for function

Virology

Volumn 374, Issue 1, 2008, Pages 23-32

  Klyachkin, Yuri M ^a   Geraghty, Robert J ^a  

^a UNIVERSITY OF KENTUCKY   (United States)

Author keywords

Arginine; Cysteine; Fusion; gH; gL; Glycoprotein; Herpes simplex virus; Virus entry

Indexed keywords

ALANINE; ARGININE; CYSTEINE; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; VIRUS GLYCOPROTEIN L;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL FUSION; CONTROLLED STUDY; HERPES SIMPLEX VIRUS 1; MEMBRANE FUSION; MUTAGENESIS; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN TRANSPORT; VIRUS ENTRY;

AMINO ACID SUBSTITUTION; DNA, VIRAL; HERPESVIRUS 1, HUMAN; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; VIRAL ENVELOPE PROTEINS; VIRUS INTERNALIZATION;

HUMAN HERPESVIRUS 1; SIMPLEXVIRUS;

EID: 41649121281     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2007.11.014     Document Type: Article

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