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Relevant bibliographies by topics / N1 neuraminidase

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Academic literature on the topic 'N1 neuraminidase'

Author: Grafiati

Published: 5 June 2025

Last updated: 2 August 2025

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Journal articles on the topic "N1 neuraminidase"

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Thai, Quynh Mai, Trung Hai Nguyen, Huong Thi Thu Phung, et al. "MedChemExpress compounds prevent neuraminidase N1 via physics- and knowledge-based methods." RSC Advances 14, no. 27 (2024): 18950–56. http://dx.doi.org/10.1039/d4ra02661f.

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Hurt, Aeron C., Ian G. Barr, Christopher J. Durrant, Robert P. Shaw, Helen M. Sjogren, and Alan W. Hampson. "Surveillance for neuraminidase inhibitor resistance in human influenza viruses from Australia." Communicable Diseases Intelligence 27 (December 31, 2003): 542–47. https://doi.org/10.33321/cdi.2003.27.91.

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Two hundred and forty-five human influenza A and B viruses isolated in Australia between 1996 and 2003 were tested for their sensitivity to the NA inhibitor drugs, zanamivir and oseltamivir using a fluorescence-based neuraminidase inhibition assay. Based on mean IC50 values, influenza A viruses (with neuraminidase subtypes N1 and N2) were more sensitive to both the NA inhibitors than were influenza B strains. Influenza A viruses with a N1 subtype and influenza B strains both demonstrated a greater sensitivity to zanamivir than to oseltamivir carboxylate, whereas influenza A strains with a N2 s

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Kati, Warren M., Debra Montgomery, Robert Carrick, et al. "In Vitro Characterization of A-315675, a Highly Potent Inhibitor of A and B Strain Influenza Virus Neuraminidases and Influenza Virus Replication." Antimicrobial Agents and Chemotherapy 46, no. 4 (2002): 1014–21. http://dx.doi.org/10.1128/aac.46.4.1014-1021.2002.

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ABSTRACT A-315675 is a novel, pyrrolidine-based compound that was evaluated in this study for its ability to inhibit A and B strain influenza virus neuraminidases in enzyme assays and influenza virus replication in cell culture. A-315675 effectively inhibited influenza A N1, N2, and N9 and B strain neuraminidases with inhibitor constant (Ki ) values between 0.024 and 0.31 nM. These values were comparable to or lower than the Ki values measured for oseltamivir carboxylate (GS4071), zanamivir, and BCX-1812, except for the N1 enzymes that were found to be the most sensitive to BCX-1812. The time-

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Desheva, Yulia, Nadezhda Petkova, Igor Losev, et al. "Establishment of a Pseudovirus Platform for Neuraminidase Inhibiting Antibody Analysis." International Journal of Molecular Sciences 24, no. 3 (2023): 2376. http://dx.doi.org/10.3390/ijms24032376.

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Neuraminidase (NA)-based immunity to influenza can be useful for protecting against novel antigenic variants. To develop safe and effective tools to assess NA-based immunity, we generated a baculovirus-based pseudotyped virus, N1-Bac, that expresses the full-length NA of the influenza A/California/07/2009 (H1N1)pdm09 strain. We evaluated the level of NA-inhibiting (NI) antibodies in the paired blood sera of influenza patients by means of an enzyme-linked lectin assay (ELLA) using the influenza virus or N1-Bac. Additionally, we evaluated the level of NA antibodies by means of the enzyme-linked

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Charlotte, D'Souza, Kanyalkar Meena, Srivastava Sudha, and Govil G. "Design of novel, potent neuraminidase inhibitor for H5N1 avian influenza using molecular docking, multinuclear NMR and DSC methods." Journal of Indian Chemical Society Vol. 87, Jan 2010 (2010): 97–104. https://doi.org/10.5281/zenodo.5775498.

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Prin K. M. Kundnani College of Pharmacy, Cuffe Parade, Mumbai-400 005, India "National Facility for High Field NMR, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai-400 005, India <em>E-mail :</em> sudha@tifr.res.in <em>Manuscript received 13 October 2009, accepted 15 October 2009</em> To probe more effective inhibitors for neuraminidase subtype N1, four potential inhibitor were synthetically designed by substitution at the C5 position of oseltamivir to provide additional interaction with the 150-eavlty, a well know a active site in the neuraminidase subtype N1. Molec

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Hartawan, Risza, Karl Robinson, Timothy Mahony, and Joanne Meers. "Characterisation of the H5 and N1 genes of an Indonesian highly pathogenic Avian Influenza virus isolate by sequencing of multiple clone approach." Jurnal Ilmu Ternak dan Veteriner 15, no. 3 (2012): 240–51. https://doi.org/10.14334/jitv.v15i3.663.

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Hemagglutinin and neuraminidase are the main antigenic determinants of highly pathogenic avian influenza (HPAI) virus. The features of these surface glycoproteins have been intensively studied at the molecular level. The objective of this research was to characterise the genes encoding these glycoproteins by sequencing of multiple clones. The H5 and N1 genes of isolate A/duck/Tangerang/Bbalitvet-ACIAR-TE11/2007 were each amplified in one or two fragments using reverse transcriptase-PCR (RT-PCR), and subsequently cloned into pGEM-T Easy TA cloning system. The sequencing result demonstrated high

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Hartawan, Risza, K. Robinson, T. Mahony, and J. Meer. "In vitro expression of native H5 and N1 genes of avian influenza virus by using Green Fluorescent Protein as reporter." Jurnal Ilmu Ternak dan Veteriner 16, no. 3 (2012): 234–42. https://doi.org/10.14334/jitv.v16i3.618.

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The hemagglutinin and neuraminidase are important immunogen of avian influenza virus that are suitable for recombinant experimentation. However, both genes have been experienced rapid mutation resulting in diverse variety of genotypes. Hence, gene expression in recombinant systems will be difficult to predict. The objective of the study was to examine expression level of H5 and N1 genes from a field isolate by cloning the genes into expression vector pEGFP-C1. Two clones respresenting fulllength of H5 and N1 gene in plasmid pEGFP-C1 were transfected into chicken embryo fibroblasts (CEF), rabbi

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Abed, Yacine, Mariana Baz, and Guy Boivin. "Impact of Neuraminidase Mutations Conferring Influenza Resistance to Neuraminidase Inhibitors in the N1 and N2 Genetic Backgrounds." Antiviral Therapy 11, no. 8 (2006): 971–76. http://dx.doi.org/10.1177/135965350601100804.

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Subtype-specific neuraminidase (NA) mutations conferring resistance to NA inhibitors (NAIs) have been reported during in vitro passages and in clinic. In this study, we evaluated the impact of various NA mutations (E119A/G/V, H274Y, R292K and N294S) on the susceptibility profiles to different NAIs (oseltamivir, zanamivir and peramivir) using recombinant NA proteins of influenza A/WSN/33 (H1N1) and A/Sydney/5/97-like (H3N2) viruses. In the N1 subtype, the E119V mutation conferred cross-resistance to oseltamivir, zanamivir and peramivir [1,727–2,144 and 5,050-fold increase in IC50 values compare

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Xu, Xiaojin, Xueyong Zhu, Raymond A. Dwek, James Stevens, and Ian A. Wilson. "Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase." Journal of Virology 82, no. 21 (2008): 10493–501. http://dx.doi.org/10.1128/jvi.00959-08.

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ABSTRACT Influenza virus neuraminidase (NA) plays a crucial role in facilitating the spread of newly synthesized virus in the host and is an important target for controlling disease progression. The NA crystal structure from the 1918 “Spanish flu” (A/Brevig Mission/1/18 H1N1) and that of its complex with zanamivir (Relenza) at 1.65-Å and 1.45-Å resolutions, respectively, corroborated the successful expression of correctly folded NA tetramers in a baculovirus expression system. An additional cavity adjacent to the substrate-binding site is observed in N1, compared to N2 and N9 NAs, including

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Hooper, Kathryn A., James E. Crowe, and Jesse D. Bloom. "Influenza Viruses with Receptor-Binding N1 Neuraminidases Occur Sporadically in Several Lineages and Show No Attenuation in Cell Culture or Mice." Journal of Virology 89, no. 7 (2015): 3737–45. http://dx.doi.org/10.1128/jvi.00012-15.

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ABSTRACTIn nearly all characterized influenza viruses, hemagglutinin (HA) is the receptor-binding protein while neuraminidase (NA) is a receptor-cleaving protein that aids in viral release. However, in recent years, several groups have described point mutations that confer receptor-binding activity on NA, albeit in laboratory rather than natural settings. One of these mutations, D151G, appears to arise in the NA of recent human H3N2 viruses upon passage in tissue culture. We inadvertently isolated the second of these mutations, G147R, in the NA of the lab-adapted A/WSN/33 (H1N1) strain while w

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Dissertations / Theses on the topic "N1 neuraminidase"

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Deckers, Daniela [Verfasser]. "Aviäre Influenzavirus (AIV) Markervakzinen auf Basis des Newcastle Disease Virus (NDV) als Vektor : Herstellung, Charakterisierung und Prüfung einer AIV-9-Hämagglutinin (HA)-exprimierenden NDV-Rekombinante gegen niedrigpathogenes AIV, sowie Prüfung H5 bzw. N1 Neuraminidase-exprimierender NDV-Rekombinanten gegen hochpathogenes AIV / Daniela Deckers." Berlin : Freie Universität Berlin, 2010. http://d-nb.info/1025087968/34.

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Wu, I.-Ching, and 吳依青. "In silico Investigation of Drug-Target Interactions for N1 Neuraminidase." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/63244554536870783405.

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碩士<br>國立陽明大學<br>生物醫學資訊研究所<br>96<br>H5N1 avian influenza have caused a severe and overwhelming epidemic among birds and humans. To develop new drugs against the pathogen, an easily-mutated virus, much more efforts have been putting on fully understanding the viral entry and leave the cell, especially on neuraminidases and hemagglutinins. Here we used molecular dynamics simulations to test different ligands, including sialic acid, Peramivir, Oseltamivir and Zanamivir binding to N1 neuraminidases and to compare Oseltamivir binding to wild type and mutant N1 neuraminidases. Binding energy and bind

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Books on the topic "N1 neuraminidase"

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Alexander, D. J., N. Phin, and M. Zuckerman. Influenza. Edited by I. H. Brown. Oxford University Press, 2011. http://dx.doi.org/10.1093/med/9780198570028.003.0037.

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Influenza is a highly infectious, acute illness which has affected humans and animals since ancient times. Influenza viruses form the Orthomyxoviridae family and are grouped into types A, B, and C on the basis of the antigenic nature of the internal nucleocapsid or the matrix protein. Infl uenza A viruses infect a large variety of animal species, including humans, pigs, horses, sea mammals, and birds, occasionally producing devastating pandemics in humans, such as in 1918 when it has been estimated that between 50–100 million deaths occurred worldwide.There are two important viral surface glyc

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Conference papers on the topic "N1 neuraminidase"

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CHENG, YUHUI, MICHAEL J. HOLST, and J. A. MCCAMMON. "FINITE ELEMENT ANALYSIS OF DRUG ELECTROSTATIC DIFFUSION: INHIBITION RATE STUDIES IN N1 NEURAMINIDASE." In Proceedings of the Pacific Symposium. WORLD SCIENTIFIC, 2008. http://dx.doi.org/10.1142/9789812836939_0027.

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