BIOLOGICAL MODEL;
CHEMICAL STRUCTURE;
CHEMISTRY;
DRUG ANTAGONISM;
DRUG DELIVERY SYSTEM;
DRUG EFFECT;
DRUG SCREENING;
GENETICS;
METABOLISM;
NOTE;
ORTHOMYXOVIRUS;
PHYSIOLOGY;
PROTEIN CONFORMATION;
PROTEIN TERTIARY STRUCTURE;
VIRUS REPLICATION;
AMINOBUTYRIC ACIDS;
ANTIVIRAL AGENTS;
DRUG DELIVERY SYSTEMS;
DRUG EVALUATION, PRECLINICAL;
MODELS, BIOLOGICAL;
MODELS, MOLECULAR;
ORTHOMYXOVIRIDAE;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
RNA CAPS;
RNA REPLICASE;
RNA, VIRAL;
VIRAL PROTEINS;
VIRUS REPLICATION;
Crucial role of CA cleavage sites in the cap-snatching mechanism for initiating viral mRNA synthesis
Rao P, Yuan W, Krug RM. Crucial role of CA cleavage sites in the cap-snatching mechanism for initiating viral mRNA synthesis. EMBO J 2003 ; 22 : 1188-1189.
Influenza A virus RNA polymerase subunit PB2 is the endonuclease which cleaves host cell mRNA and functions only as the trimeric enzyme
Shi L, Summers DF, Peng Q, Galarz JM. Influenza A virus RNA polymerase subunit PB2 is the endonuclease which cleaves host cell mRNA and functions only as the trimeric enzyme. Virology 1995 ; 208 : 38-47.
The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits
DOI 10.1093/emboj/20.8.2078
Li ML, Rao P, Krug RM. The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits. EMBO J 2001 ; 20 : 2078-2086. (Pubitemid 32397409)
(2001)EMBO Journal, vol.20, Issue.8, pp. 2078-2086
The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
4 février (online)
Dias A, Bouvier D, Crépin T, et al. The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 2009, 4 février (online).
DNA cleavage by EcoRV endonuclease: Two metal ions in three metal ion binding sites
DOI 10.1021/bi0499056
Horton NC, Perona JJ. DNA cleavage by EcoRV endonuclease: two metal ions in three metal ion binding sites. Biochemistry 2004 ; 43 : 6841-6857. (Pubitemid 38720502)
(2004)Biochemistry, vol.43, Issue.22, pp. 6841-6857
Amino acid residues in the N-terminal region of the PA subunit of influenza a virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding
DOI 10.1128/JVI.00600-06
Hara K, Schmidt FI, Crow M, Brownlee GG. Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding. J Virol 2006 ; 80 : 7789-7798. (Pubitemid 44182280)