Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.98 extracted from

  • Aparicio, E.; Franco, S.; Parera, M.; Andres, C.; Tural, C.; Clotet, B.; Martinez, M.A.
    Complexity and catalytic efficiency of hepatitis C virus (HCV) NS3 and NS4A protease quasispecies influence responsiveness to treatment with pegylated interferon plus ribavirin in HCV/HIV-coinfected patients (2011), J. Virol., 85, 5961-5969.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
caspase recruitment domain adaptor-inducing IFN-beta (Cardif) + H2O Hepacivirus C
-
?
-
?

Organism

Organism UniProt Comment Textmining
Hepacivirus C
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
caspase recruitment domain adaptor-inducing IFN-beta (Cardif) + H2O
-
Hepacivirus C ?
-
?

Synonyms

Synonyms Comment Organism
NS3/4A protease
-
Hepacivirus C

General Information

General Information Comment Organism
physiological function the impact of NS3/4A protease activity and quasispecies complexity on virus clearance after IFN-based therapy is examined in HCV-HIV-1-coinfected patients: NS3/4A protease efficiency in cleaving caspase recruitment domain adaptor-inducing IFN-beta (Cardif) may be associated with the pegIFN-RBV treatment response Hepacivirus C