Neuraminidase
From Proteopedia
(Difference between revisions)
| Line 6: | Line 6: | ||
*[[Molecular Playground/Relenza]]<br /> | *[[Molecular Playground/Relenza]]<br /> | ||
*[[Molecular Playground/Tamiflu]]<br /> | *[[Molecular Playground/Tamiflu]]<br /> | ||
| + | *[[Oseltamivir]] (Tamiflu)<br /> | ||
*[[User:Michael Strong/H1N1/NA]] for Influenza virus neuraminidase<br /> | *[[User:Michael Strong/H1N1/NA]] for Influenza virus neuraminidase<br /> | ||
*[[User:Michael Strong/H1N1/NA/MSA]] for multiple sequence alignment.<br /> | *[[User:Michael Strong/H1N1/NA/MSA]] for multiple sequence alignment.<br /> | ||
Revision as of 07:49, 17 February 2016
Neuraminidase (NAN) cleaves the glycosidic bonds of neuraminic acid. The viral NAN is a drug target for prevention of influenza.
See also
- Avian Influenza Neuraminidase, Tamiflu and Relenza
- Molecular Playground/Relenza
- Molecular Playground/Tamiflu
- Oseltamivir (Tamiflu)
- User:Michael Strong/H1N1/NA for Influenza virus neuraminidase
- User:Michael Strong/H1N1/NA/MSA for multiple sequence alignment.
For other inhibitors see
- Neuraminidase Inhibitor Pharmacokinetics
- Carbohydrate binding domain from Streptococcus pneumoniae NanA sialidase complexed with 3'-sialyllactose.
3D structures of Neuraminidase
Updated on 17-February-2016
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Eran Hodis
