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  1. Neuraminidase inhibitor. Neuraminidase inhibitors (NAIs) are a class of drugs which block the neuraminidase enzyme. They are a commonly used antiviral drug type against influenza. Viral neuraminidases are essential for influenza reproduction, facilitating viral budding from the host cell.

  2. Discovery and development of neuraminidase inhibitors. Neuraminidase inhibitors inhibit enzymatic activity of the enzyme neuraminidase (sialidase). These type of inhibitors have been introduced as anti-influenza drugs as they prevent the virus from exiting infected cells and thus stop further spreading of the virus.

  3. An analog of its neuraminic acid substrate, used as an inhibitor drug, is the small white and red molecule in the center. N-Acetylneuraminic acid. Exo-α-sialidase (EC 3.2.1.18, sialidase, neuraminidase; systematic name acetylneuraminyl hydrolase) is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids:

  4. Neuraminidase inhibitors are stockpiled and recommended by public health agencies for treating and preventing seasonal and pandemic influenza. They are used clinically worldwide. An official website of the United States government

  5. Neuraminidase inhibitors are antiviral medications used for the treatment and prophylaxis of influenza A and influenza B, which are known to cause the flu. Neuraminidase inhibitors work by blocking an enzyme called neuraminidase produced by the influenza virus. The function of neuraminidase is to help new viruses to get released from infected ...

  6. At present, two inhibitors of sialidase (also known as neuraminidase), a viral enzyme that has a key role in the life cycle of influenza viruses, would be the mainstay of pharmacological...

  7. Feb 16, 2022 · Inhibitors, Monomers, Peptides and proteins. Abstract. This Perspective describes the classification, structures, substrates, mechanisms of action, and implications of human neuraminidases (hNEUs) in various pathologies. Some inhibitors have been developed for each isoform, leading to more precise interactions with hNEUs.

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