Influenza B virus neuraminidase can synthesize its own inhibitor
about
Molecular insight into substrate recognition by human cytosolic sialidase NEU2Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusionAnalysis of inhibitor binding in influenza virus neuraminidaseThe Structure of Clostridium perfringens NanI Sialidase and Its Catalytic IntermediatesGlycal Formation in Crystals of Uridine Phosphorylase ,The Aspergillus fumigatus Sialidase Is a 3-Deoxy-D-glycero-D-galacto-2-nonulosonic Acid Hydrolase (KDNase): STRUCTURAL AND MECHANISTIC INSIGHTSStructural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesisInfluenza neuraminidase operates via a nucleophilic mechanism and can be targeted by covalent inhibitorsInfluenza Neuraminidase Inhibitors: Synthetic Approaches, Derivatives and Biological ActivityNovel alpha- and beta-amino acid inhibitors of influenza virus neuraminidaseGallus gallus NEU3 sialidase as model to study protein evolution mechanism based on rapid evolving loops.Recent advances in neuraminidase inhibitor development as anti-influenza drugs.Combining crystallographic information and an aspherical-atom data bank in the evaluation of the electrostatic interaction energy in an enzyme-substrate complex: influenza neuraminidase inhibitionStructural basis of sialidase in complex with geranylated flavonoids as potent natural inhibitors.Influenza neuraminidase.Catalytic and framework mutations in the neuraminidase active site of influenza viruses that are resistant to 4-guanidino-Neu5Ac2en.Sequence and structure alignment of Paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin.Detecting the native ligand orientation by interfacial rigidity: SiteInterlock.Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase.Influenza neuraminidase: a druggable target for natural products.Enzymatically inactive trans-sialidase from Trypanosoma cruzi binds sialyl and beta-galactopyranosyl residues in a sequential ordered mechanism.Trans-sialidase-like sequences from Trypanosoma congolense conserve most of the critical active site residues found in other trans-sialidases.A 3D-RISM/RISM study of the oseltamivir binding efficiency with the wild-type and resistance-associated mutant forms of the viral influenza B neuraminidase.The NEU1-selective sialidase inhibitor, C9-butyl-amide-DANA, blocks sialidase activity and NEU1-mediated bioactivities in human lung in vitro and murine lung in vivo.Evidence of ternary complex formation in Trypanosoma cruzi trans-sialidase catalysisExpression, mutagenesis and kinetic analysis of recombinant K1E endosialidase to define the site of proteolytic processing and requirements for catalysis.Computational 3-D modeling and site-directed mutation of an antibody that binds Neu2en5Ac, a transition state analogue of a sialic acid.Sialic acid recognition by Vibrio cholerae neuraminidase.Biotin-, fluorescein- and 'clickable' conjugates of phospha-oseltamivir as probes for the influenza virus which utilize selective binding to the neuraminidase.Molecular modeling of sialyloligosaccharide fragments into the active site of influenza virus N9 neuraminidase.Conformational analysis and design of cross-strand disulfides in antiparallel β-sheets.Two Nucleophilic Mutants of the Micromonospora viridifaciens Sialidase Operate with Retention of Configuration by Two Different Mechanisms
P2860
Q24301390-FBE2AFF6-E26E-40FF-8C1B-88500E2DD1A5Q24600140-77BF2547-A85E-43AB-929D-828FDAA8ABC8Q27630835-BDCD6122-B769-4E18-91DF-C75DD9AF92FCQ27649703-B854CC9B-96B7-400B-9681-341DEAE3AC18Q27660422-D1185338-A003-4C69-A5CF-96C2EAC80132Q27666631-94DF87B3-0C0B-4E3F-BF05-AF3F8BB30A7DQ27678320-47CDBEBE-87B6-4FFE-81C1-2E5501CC6E63Q27684045-193F61E8-814B-493E-88D6-4D54F92354CEQ28079041-E44360DB-07AC-444A-AC93-40BC191127C2Q28345965-D9D87655-A079-4E33-948C-DBA7CD0BA44AQ30406306-A3C1DA20-88EA-4A3F-9AB2-AD6298EDEB50Q30419301-0EEBD8FE-9EB9-48D2-BCC6-4C435367B856Q33434347-BBE1F126-66DF-4BF7-A2CF-13512C565B5AQ33582480-1F4BC201-AA4F-4C70-A424-14F32FDF3B7BQ35791130-403E2ECE-53CF-4576-83FA-88052ED5E372Q35882160-8916CACF-5EAA-491D-A5E0-2C79656E0F12Q35890376-51AD7413-0FD4-4546-930D-20C00DCBEFE8Q36152480-D929D576-C53B-454D-9F83-B9D3B7EAB437Q36617502-5C824F07-A62E-4B73-8BFA-39423D07B189Q37949284-51AEA260-C3EB-46F9-A8FB-3C4EB6CAEA54Q38347663-83FCE103-2944-403A-8018-F9A50AF565EFQ38350428-0ACD09AE-C373-4618-8453-5FC78806128DQ39722037-388A8139-8A5A-4A78-818E-9B35D459A9EBQ39735549-5532CA4F-B0C3-4752-9B9F-35CE686BDD4FQ41848404-ADDEB9B1-1E5F-4069-BBC2-A0E6C630F3F4Q41892061-4A1D0154-D0F7-4088-B1D5-609C2F5F7E93Q43825546-E3972928-0C6C-4761-A327-AEAC8F7E12AEQ44958654-4E56F097-B85E-42FB-A9C6-F3DB66956D30Q45365310-973A434A-AE71-414C-9D87-170C18570405Q45735574-46A3580B-E960-4E2B-9C0C-18B888C48CFAQ46526656-073DFC45-58D3-4835-91CF-5784C0BFBDD9Q58003612-8F65B38A-DA04-488F-908A-32C79A375C0D
P2860
Influenza B virus neuraminidase can synthesize its own inhibitor
description
1993 nî lūn-bûn
@nan
1993 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Influenza B virus neuraminidase can synthesize its own inhibitor
@ast
Influenza B virus neuraminidase can synthesize its own inhibitor
@en
Influenza B virus neuraminidase can synthesize its own inhibitor
@nl
type
label
Influenza B virus neuraminidase can synthesize its own inhibitor
@ast
Influenza B virus neuraminidase can synthesize its own inhibitor
@en
Influenza B virus neuraminidase can synthesize its own inhibitor
@nl
prefLabel
Influenza B virus neuraminidase can synthesize its own inhibitor
@ast
Influenza B virus neuraminidase can synthesize its own inhibitor
@en
Influenza B virus neuraminidase can synthesize its own inhibitor
@nl
P2093
P1433
P1476
Influenza B virus neuraminidase can synthesize its own inhibitor
@en
P2093
R W Ruigrok
W P Burmeister
P356
10.1016/0969-2126(93)90005-2
P577
1993-09-15T00:00:00Z