Skip to main content

Structure and Functions of Influenza Virus Neuraminidase

Buy Article:

$63.00 plus tax (Refund Policy)

Abstract:

Influenza is a disease that deeply affects millions of people every year. There has not been any drug effective against all strains. Neuraminidase (NA) is the major surface glycoprotein of the influenza virus, which possesses critical enzymatic activity and has been considered as a suitable target for designing agents against influenza viruses. Here we review the structure and functions of this enzyme and touch upon the structureactivity relationship (SAR) of existing influenza neuraminidase inhibitors (NAIs).





Keywords: Functions; Influenza virus; Neuraminidase; Neuraminidase inhibitors; Structure; Structure-activity relationship

Document Type: Research Article

DOI: https://doi.org/10.2174/092986707779313444

Affiliations: Department of Medicinal Chemistry, School of Pharmaceutical Sciences, ShanDong University, 44,West Culture Road, 250012, Ji'nan, ShanDong, P.R.China.

Publication date: 2007-01-01

More about this publication?
  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.
  • Access Key
  • Free ContentFree content
  • Partial Free ContentPartial Free content
  • New ContentNew content
  • Open Access ContentOpen access content
  • Partial Open Access ContentPartial Open access content
  • Subscribed ContentSubscribed content
  • Partial Subscribed ContentPartial Subscribed content
  • Free Trial ContentFree trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more