The helicase-primase inhibitor BAY 57-1293 reduces the Alzheimer's disease-related molecules induced by herpes simplex virus type 1

Antiviral Research

Volumn 99, Issue 3, 2013, Pages 401-404

  Wozniak, M A ^a   Frost, A L ^a   Itzhaki, R F ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Amyloid; Abnormally phosphorylated tau; Alzheimer's disease; Helicase primase inhibitor; Herpes simplex virus type 1

Indexed keywords

ACICLOVIR; AMYLOID BETA PROTEIN; ANTIVIRUS AGENT; BAY 57 1293; NOOTROPIC AGENT; NUCLEOTIDYLTRANSFERASE INHIBITOR; PROTEIN SYNTHESIS INHIBITOR; TAU PROTEIN; UNCLASSIFIED DRUG; VIRUS DNA; BAY 57-1293; DNA HELICASE; DNA PRIMASE; ENZYME INHIBITOR; HELICASE PRIMASE, HUMAN HERPESVIRUS 1; HELICASE-PRIMASE, HUMAN HERPESVIRUS 1; PYRIDINE DERIVATIVE; THIAZOLE DERIVATIVE; VIRUS PROTEIN; APOLIPOPROTEIN E; BAY 571293; FAMCICLOVIR; PENCICLOVIR; VALACICLOVIR;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; CELL SIZE; COLONY FORMING UNIT; CONCENTRATION RESPONSE; CONTROLLED STUDY; DNA REPLICATION; DRUG EFFECT; DRUG EFFICACY; DRUG MECHANISM; HERPES SIMPLEX VIRUS 1; NONHUMAN; PRIORITY JOURNAL; PROTEIN SYNTHESIS INHIBITION; VERO CELL; VIRUS INHIBITION; VIRUS REPLICATION; Β-AMYLOID; ABNORMALLY PHOSPHORYLATED TAU; DOWN REGULATION; DRUG ANTAGONISM; ENZYMOLOGY; GENETICS; HELICASE-PRIMASE INHIBITOR; HERPES SIMPLEX; HUMAN; METABOLISM; VIROLOGY; ANTAGONISTS AND INHIBITORS; DRUG EFFECTS; ANIMAL EXPERIMENT; ANTIVIRAL ACTIVITY; ENZYME INHIBITION; GENE EXPRESSION; HERPES SIMPLEX VIRUS 1 INFECTION; HUMAN CELL; IMMUNOCYTOCHEMISTRY; MOLECULE; MOUSE; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; VIRUS LOAD; VIRUS STRAIN;

Β-AMYLOID; ABNORMALLY PHOSPHORYLATED TAU; ALZHEIMER'S DISEASE; HELICASE-PRIMASE INHIBITOR; HERPES SIMPLEX VIRUS TYPE 1;

ACYCLOVIR; ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANTIVIRAL AGENTS; DNA HELICASES; DNA PRIMASE; DOWN-REGULATION; ENZYME INHIBITORS; HERPES SIMPLEX; HERPESVIRUS 1, HUMAN; HUMANS; PYRIDINES; TAU PROTEINS; THIAZOLES; VIRAL PROTEINS; VIRUS REPLICATION;

EID: 84884538144     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2013.07.003     Document Type: Article

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