نتایج جستجو برای: neuraminidase enzyme

تعداد نتایج: 246210  

Journal: :The Journal of biological chemistry 1983
A Varki S Diaz

The naturally occurring sialic acids can have different types of N- and O-substitutions, resulting in more than 20 known isomers and compounds. Most methods for the detailed study of these various sialic acids require that the molecules be first released from their alpha-glycosidic linkage. When mild acid hydrolysis is used for this purpose, significant destruction of O-substituent groups occur...

2017
Hasan F Kahya Peter W Andrew Hasan Yesilkaya

Pneumococcal neuraminidase is a key enzyme for sequential deglycosylation of host glycans, and plays an important role in host survival, colonization, and pathogenesis of infections caused by Streptococcus pneumoniae. One of the factors that can affect the activity of neuraminidase is the amount and position of acetylation present in its substrate sialic acid. We hypothesised that pneumococcal ...

Journal: :Antimicrobial agents and chemotherapy 2006
Arnold S Monto Jennifer L McKimm-Breschkin Catherine Macken Alan W Hampson Alan Hay Alexander Klimov Masato Tashiro Robert G Webster Michelle Aymard Frederick G Hayden Maria Zambon

Emergence of influenza viruses with reduced susceptibility to neuraminidase inhibitors (NAIs) develops at a low level following drug treatment, and person-to-person transmission of resistant virus has not been recognized to date. The Neuraminidase Inhibitor Susceptibility Network (NISN) was established to follow susceptibility of isolates and occurrence of NAI resistance at a population level i...

A. Merat, J. Zamani M. H. Roozitalab R. Arabsolghar

Background: Sialic acid is a component of serum that is elevated in diseases such as diabetes and certain malignancies.  The normal range of SSA concentration and serum neuraminidase activity in different populations are varied, probably due to racial differences. Objective: The purpose of the present study was to obtain the average SSA concentration and serum neuraminidase activity, in an Iran...

Journal: :Current Biology 1999
John McCauley

How does Relenza work? It blocks the action of the enzyme neuraminidase (also called sialidase) on the surface of types A and B influenza viruses, preventing them from spreading to other cells. Influenza viruses bind to sialic acids on the surface of host cells through the viral haemagglutinin glycoprotein. The haemagglutinin causes the virus envelope to fuse with the membrane of the endosome, ...

Journal: :The Journal of Experimental Medicine 1992
S Schenkman L Pontes de Carvalho V Nussenzweig

Trans-sialidase and neuraminidase activities have been detected on the surface membrane of trypomastigotes of Trypanosoma cruzi, and both have been implicated in the parasite's invasion of host cells. We show here that these enzymes are structurally related. They are recognized by two independently derived monoclonal antibodies, are anchored to the membrane by glycosylphosphatidylinositol, copu...

Journal: :Science 2013
Jin-Hyo Kim Ricardo Resende Tom Wennekes Hong-Ming Chen Nicole Bance Sabrina Buchini Andrew G Watts Pat Pilling Victor A Streltsov Martin Petric Richard Liggins Susan Barrett Jennifer L McKimm-Breschkin Masahiro Niikura Stephen G Withers

Influenza antiviral agents play important roles in modulating disease severity and in controlling pandemics while vaccines are prepared, but the development of resistance to agents like the commonly used neuraminidase inhibitor oseltamivir may limit their future utility. We report here on a new class of specific, mechanism-based anti-influenza drugs that function through the formation of a stab...

Journal: :Bioorganic & medicinal chemistry 2012
Hirokazu Kai Hiroshi Hinou Shin-Ichiro Nishimura

A selective and potent inhibitor of neuraminidases, a hydrolase that is responsible for processing sialylated glycoconjugates, is a promising drug candidate for various infective diseases. The current study demonstrates that the use of an aglycone-focused library of 2-difluoromethylphenyl α-sialosides is an effective technique to find potent and selective mechanism-based labeling reagents for n...

Journal: :Applied microbiology 1973
P Palese D Bucher E D Kilbourne

A rapid and precise assay for neuraminidase using 2-(3'-methoxyphenyl)-N-acetyl-alpha-neuraminic acid (MPN) is described. It is proposed that this substrate be used for the standardization of activity of neuraminidases from viral, bacterial, and mammalian sources. MPN is also used as a chromogenic substrate to localize influenza and parainfluenza virus foci in tissue culture. This technique per...

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