Log in

Relevant bibliographies by topics / N1 neuraminidase / Journal articles

To see the other types of publications on this topic, follow the link: N1 neuraminidase.

Journal articles on the topic 'N1 neuraminidase'

Author: Grafiati

Published: 5 June 2025

Last updated: 2 August 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'N1 neuraminidase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

Abstract:

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-

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

5

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

10

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

11

Nagashima, Kaito, Nada Abbadi, Ved Vyas, Abigail Roegner, Ted M. Ross, and Jarrod J. Mousa. "Adjuvant-Mediated Differences in Antibody Responses to Computationally Optimized Hemagglutinin and Neuraminidase Vaccines." Viruses 15, no. 2 (2023): 347. http://dx.doi.org/10.3390/v15020347.

Full text

Abstract:

Computationally optimized broadly reactive antigens (COBRAs) are a next-generation universal influenza vaccine candidate. However, how these COBRAs induce antibody responses when combined with different adjuvants has not previously been well-characterized. Therefore, we performed in vivo studies with an HA-based H1 COBRA, Y2, and an NA-based N1 COBRA, N1-I, to assess this effect for the H1N1 subtype. We tested the adjuvants AddaVax, AddaS03, CpG, and Alhydrogel. AddaS03 performed the best, eliciting high IgG titers and hemagglutination inhibition (HAI) activity for Y2 immunizations. Interestin

APA, Harvard, Vancouver, ISO, and other styles

12

da Silva, Diogo V., Johan Nordholm, Dan Dou, Hao Wang, Jeremy S. Rossman, and Robert Daniels. "The Influenza Virus Neuraminidase Protein Transmembrane and Head Domains Have Coevolved." Journal of Virology 89, no. 2 (2014): 1094–104. http://dx.doi.org/10.1128/jvi.02005-14.

Full text

Abstract:

ABSTRACTTransmembrane domains (TMDs) from single-spanning membrane proteins are commonly viewed as membrane anchors for functional domains. Influenza virus neuraminidase (NA) exemplifies this concept, as it retains enzymatic function upon proteolytic release from the membrane. However, the subtype 1 NA TMDs have become increasingly more polar in human strains since 1918, which suggests that selection pressure exists on this domain. Here, we investigated the N1 TMD-head domain relationship by exchanging a prototypical “old” TMD (1933) with a “recent” (2009), more polar TMD and an engineered hyd

APA, Harvard, Vancouver, ISO, and other styles

13

Skarlupka, Amanda L., Xiaojian Zhang, Uriel Blas-Machado, Spencer F. Sumner, and Ted M. Ross. "Multi-Influenza HA Subtype Protection of Ferrets Vaccinated with an N1 COBRA-Based Neuraminidase." Viruses 15, no. 1 (2023): 184. http://dx.doi.org/10.3390/v15010184.

Full text

Abstract:

The influenza neuraminidase (NA) is a promising target for next-generation vaccines. Protection induced by vaccination with the computationally optimized broadly reactive NA antigen (N1-I COBRA NA) was characterized in both influenza serologically naive and pre-immune ferret models following H1N1 (A/California/07/2009, CA/09) or H5N1 (A/Vietnam/1203/2004, Viet/04) influenza challenges. The N1-I COBRA NA vaccine elicited antibodies with neutralizing ELLA activity against both seasonal and pandemic H1N1 influenza, as well as the H5N1 influenza virus. In both models, N1-I COBRA NA-vaccinated ferr

APA, Harvard, Vancouver, ISO, and other styles

14

Kongkamnerd, Jarinrat, Adelaide Milani, Giovanni Cattoli, et al. "A screening assay for neuraminidase inhibitors using neuraminidases N1 and N3 from a baculovirus expression system." Journal of Enzyme Inhibition and Medicinal Chemistry 27, no. 1 (2011): 5–11. http://dx.doi.org/10.3109/14756366.2011.568415.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Bi, Yuhai, Haixia Xiao, Quanjiao Chen, et al. "Changes in the Length of the Neuraminidase Stalk Region Impact H7N9 Virulence in Mice." Journal of Virology 90, no. 4 (2015): 2142–49. http://dx.doi.org/10.1128/jvi.02553-15.

Full text

Abstract:

The neuraminidase stalk of the newly emerged H7N9 influenza virus possesses a 5-amino-acid deletion. This study focuses on characterizing the biological functions of H7N9 with varied neuraminidase stalk lengths. Results indicate that the 5-amino-acid deletion had no impact on virus infectivity or replicationin vitroorin vivocompared to that of a virus with a full-length stalk, but enhanced virulence in mice was observed for H7N9 encoding a 19- to 20-amino-acid deletion, suggesting that N9 stalk length impacts virulence in mammals, as N1 stalk length does.

APA, Harvard, Vancouver, ISO, and other styles

16

Shoji, Yoko, Jessica A. Chichester, Gene A. Palmer, et al. "An influenza N1 neuraminidase-specific monoclonal antibody with broad neuraminidase inhibition activity against H5N1 HPAI viruses." Human Vaccines 7, sup1 (2011): 199–204. http://dx.doi.org/10.4161/hv.7.0.14595.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Wan, Hongquan, Ishrat Sultana, Laura K. Couzens, Samuel Mindaye, and Maryna C. Eichelberger. "Assessment of influenza A neuraminidase (subtype N1) potency by ELISA." Journal of Virological Methods 244 (June 2017): 23–28. http://dx.doi.org/10.1016/j.jviromet.2017.02.015.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Williamson, R., S. Inglis, and J. McCauley. "Deletions in the stalk of the avian influenza N1 neuraminidase." Virus Research 3 (September 1985): 11. http://dx.doi.org/10.1016/0168-1702(85)90274-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Odhar, Hasanain Abdulhameed, Azher Abdulmutaleb Ibrahim, and Ahmed Fadhil Hashim. "Computational Screening of Traditional Chinese Medicine (TCM) Library to Identify Potential Inhibitors of H5N1 Avian Influenza Neuraminidase: A Molecular Docking and Dynamics Simulation Study." Biomedical and Pharmacology Journal 18, no. 2 (2025): 1611–21. https://doi.org/10.13005/bpj/3196.

Full text

Abstract:

The influenza virus is a highly mutagenic pathogen that can drive a pandemic threat. This pandemic threat is currently very probable due to the recent outbreak of avian influenza H5N1 among cattle herds in United States. It is possible that this pathogenic strain can undergo evolution to easily infect other mammals including human beings. Therefore, it is of interest to identify novel antiviral molecules that can fight both the circulating or novel strains of influenza. In this in-silico study, a library of Traditional Chinese Medicine (TCM) was screened against neuraminidase enzyme for H5N1 i

APA, Harvard, Vancouver, ISO, and other styles

20

Majid, Nadzreeq Nor, Abdul Rahman Omar, and Abdul Razak Mariatulqabtiah. "Negligible effect of chicken cytokine IL-12 integration into recombinant fowlpox viruses expressing avian influenza virus neuraminidase N1 on host cellular immune responses." Journal of General Virology 101, no. 7 (2020): 772–77. http://dx.doi.org/10.1099/jgv.0.001428.

Full text

Abstract:

In comparison to the extensive characterization of haemagglutinin antibodies of avian influenza virus (AIV), the role of neuraminidase (NA) as an immunogen is less well understood. This study describes the construction and cellular responses of recombinant fowlpox viruses (rFWPV) strain FP9, co-expressing NA N1 gene of AIV A/Chicken/Malaysia/5858/2004, and chicken IL-12 gene. Our data shows that the N1 and IL-12 proteins were successfully expressed from the recombinants with 48 kD and 70 kD molecular weights, respectively. Upon inoculation into specific-pathogen-free (SPF) chickens at 105 p.f.

APA, Harvard, Vancouver, ISO, and other styles

21

Abed, Yacine, Benjamin Nehmé, Mariana Baz, and Guy Boivin. "Activity of the neuraminidase inhibitor A-315675 against oseltamivir-resistant influenza neuraminidases of N1 and N2 subtypes." Antiviral Research 77, no. 2 (2008): 163–66. http://dx.doi.org/10.1016/j.antiviral.2007.08.008.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Kim, Ki-Hye, Young-Tae Lee, Soojin Park, et al. "Neuraminidase expressed on virus-like particles is superior to inactivated split virus vaccine in conferring cross protection via humoral and cellular immunity." Journal of Immunology 202, no. 1_Supplement (2019): 139.18. http://dx.doi.org/10.4049/jimmunol.202.supp.139.18.

Full text

Abstract:

Abstract Neuraminidase (NA) is the second major surface antigen on influenza virus but often ignored as a vaccine component. In this study, we developed N1 virus-like particles (N1 VLP) containing NA derived from 2009 pandemic H1N1 influenza virus (2009H1N1), and compared with inactivated split virus vaccine in the immune mechanisms of cross protection. Intramuscular immunization of mice with N1 VLP induced IgG antibody responses to 2009H1N1 virus and NA inhibition activity. Mice immunized with N1 VLP induced superior cross protection against lethal infection compared to a current vaccine plat

APA, Harvard, Vancouver, ISO, and other styles

23

HO, H., A. HURT, J. MOSSE, and I. BARR. "Neuraminidase inhibitor drug susceptibility differs between influenza N1 and N2 neuraminidase following mutagenesis of two conserved residues." Antiviral Research 76, no. 3 (2007): 263–66. http://dx.doi.org/10.1016/j.antiviral.2007.08.002.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Choi, JooYoung, Sharon J. H. Martin, Ralph A. Tripp, S. Mark Tompkins, and Richard A. Dluhy. "Detection of neuraminidase stalk motifs associated with enhanced N1 subtype influenza A virulence via Raman spectroscopy." Analyst 140, no. 22 (2015): 7748–60. http://dx.doi.org/10.1039/c5an00977d.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Sung, Jeffrey C., Adam W. Van Wynsberghe, Rommie E. Amaro, Wilfred W. Li, and J. Andrew McCammon. "Role of Secondary Sialic Acid Binding Sites in Influenza N1 Neuraminidase." Journal of the American Chemical Society 132, no. 9 (2010): 2883–85. http://dx.doi.org/10.1021/ja9073672.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Sriwilaijaroen, Nongluk, Sadagopan Magesh, Akihiro Imamura, et al. "A Novel Potent and Highly Specific Inhibitor against Influenza Viral N1–N9 Neuraminidases: Insight into Neuraminidase–Inhibitor Interactions." Journal of Medicinal Chemistry 59, no. 10 (2016): 4563–77. http://dx.doi.org/10.1021/acs.jmedchem.5b01863.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Strohmeier, Shirin, Juan Manuel Carreño, Ruhi Nichalle Brito, and Florian Krammer. "Introduction of Cysteines in the Stalk Domain of Recombinant Influenza Virus N1 Neuraminidase Enhances Protein Stability and Immunogenicity in Mice." Vaccines 9, no. 4 (2021): 404. http://dx.doi.org/10.3390/vaccines9040404.

Full text

Abstract:

Influenza virus surface glycoproteins represent the main targets of the immune system during infection and vaccination. Current influenza virus vaccines rely mostly on the hemagglutinin, requiring a close match between the vaccine and circulating strains. Recently, the neuraminidase (NA) has become an attractive target; however low immunogenicity and stability in vaccine preparations remain an obstacles. Here, we took advantage of the hypervariable stalk domain of the NA to introduce cysteines at different positions and to produce more stable multimeric forms of the protein. We generated 11 N1

APA, Harvard, Vancouver, ISO, and other styles

28

Lobova, T. G., D. M. Danilenko, N. I. Konovalova, et al. "The Flu Epidemic in Russia in the 2013 - 2014 Season: Etiology, Antigenic Properties of Hemagglutinin and Neuraminidase Activity." Epidemiology and Vaccine Prevention 14, no. 2 (2015): 30–38. http://dx.doi.org/10.31631/2073-3046-2015-14-2-30-38.

Full text

Abstract:

The present study describes etiological structure of population of influenza viruses that circulated in Russian Federation in epidemic season 2013 - 2014. It was shown that from 495 isolates influenza A(H1N1)pdm09 viruses comprise 46.3%, influenza A(H3N2) - 44.2% and influenza B - 9.5% with domination of Yamagata lineage. Comparative study of antigenic properties of major influenza surface protein hemagglutinin was conducted based on the results of HI test and three-dimensional antigenic cartography. The correspondence between WHO recommended strains for vaccine composition 2013 - 2014 and Rus

APA, Harvard, Vancouver, ISO, and other styles

29

Kang, Hae-Ji, Ki-Back Chu, Keon-Woong Yoon, et al. "Multiple Neuraminidase Containing Influenza Virus-like Particle Vaccines Protect Mice from Avian and Human Influenza Virus Infection." Viruses 14, no. 2 (2022): 429. http://dx.doi.org/10.3390/v14020429.

Full text

Abstract:

Avian influenza virus remains a threat for humans, and vaccines preventing both avian and human influenza virus infections are needed. Since virus-like particles (VLPs) expressing single neuraminidase (NA) subtype elicited limited heterosubtypic protection, VLPs expressing multiple NA subtypes would enhance the extent of heterosubtypic immunity. Here, we generated avian influenza VLP vaccines displaying H5 hemagglutinin (HA) antigen with or without avian NA subtypes (N1, N6, N8) in different combinations. BALB/c mice were intramuscularly immunized with the VLPs to evaluate the resulting homolo

APA, Harvard, Vancouver, ISO, and other styles

30

Nelson, Martha I., Susan E. Detmer, David E. Wentworth, et al. "Genomic reassortment of influenza A virus in North American swine, 1998–2011." Journal of General Virology 93, no. 12 (2012): 2584–89. http://dx.doi.org/10.1099/vir.0.045930-0.

Full text

Abstract:

Revealing the frequency and determinants of reassortment among RNA genome segments is fundamental to understanding basic aspects of the biology and evolution of the influenza virus. To estimate the extent of genomic reassortment in influenza viruses circulating in North American swine, we performed a phylogenetic analysis of 139 whole-genome viral sequences sampled during 1998–2011 and representing seven antigenically distinct viral lineages. The highest amounts of reassortment were detected between the H3 and the internal gene segments (PB2, PB1, PA, NP, M and NS), while the lowest reassortme

APA, Harvard, Vancouver, ISO, and other styles

31

Hausmann, J., E. Kretzschmar, W. Garten, and H. D. Klenk. "N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity." Journal of General Virology 76, no. 7 (1995): 1719–28. http://dx.doi.org/10.1099/0022-1317-76-7-1719.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Wu, Ying, Christopher J. Vavricka, Yan Wu, et al. "Atypical group 1 neuraminidase pH1N1-N1 bound to a group 1 inhibitor." Protein & Cell 6, no. 10 (2015): 771–73. http://dx.doi.org/10.1007/s13238-015-0197-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Lawrenz, Morgan, Jeff Wereszczynski, Rommie Amaro, Ross Walker, Adrian Roitberg, and J. Andrew McCammon. "Impact of calcium on N1 influenza neuraminidase dynamics and binding free energy." Proteins: Structure, Function, and Bioinformatics 78, no. 11 (2010): 2523–32. http://dx.doi.org/10.1002/prot.22761.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Pozza, M., A. B. Simonetti, P. A. Esteves, F. A. M. Rijsewijk, and P. M. Roehe. "Detecção do vírus da cinomose canina por RT-PCR utilizando-se oligonucleotídeos para os genes da fosfoproteína, hemaglutinina e neuraminidase." Arquivo Brasileiro de Medicina Veterinária e Zootecnia 59, no. 5 (2007): 1154–62. http://dx.doi.org/10.1590/s0102-09352007000500010.

Full text

Abstract:

Empregou-se a técnica de reação em cadeia pela polimerase precedida de transcrição reversa para detecção do vírus da cinomose canina (CC). Para a padronização da técnica foram selecionados quatro pares de oligonucleotídeos (P1, P2, N1, H1), baseados em seqüências dos genes da fosfoproteína, neuraminidase e hemaglutinina, sendo utilizadas três cepas vacinais de vírus da CC como controles positivos. Foram analisadas três amostras isoladas de cães com cinomose e quatro amostras provenientes de cães com suspeita clínica de cinomose. Não houve amplificação nas amostras com suspeita clínica da doenç

APA, Harvard, Vancouver, ISO, and other styles

35

Stoner, Terri D., Scott Krauss, Rebecca M. DuBois, et al. "Antiviral Susceptibility of Avian and Swine Influenza Virus of the N1 Neuraminidase Subtype." Journal of Virology 84, no. 19 (2010): 9800–9809. http://dx.doi.org/10.1128/jvi.00296-10.

Full text

Abstract:

ABSTRACT Influenza viruses of the N1 neuraminidase (NA) subtype affecting both animals and humans caused the 2009 pandemic. Anti-influenza virus NA inhibitors are crucial early in a pandemic, when specific influenza vaccines are unavailable. Thus, it is urgent to confirm the antiviral susceptibility of the avian viruses, a potential source of a pandemic virus. We evaluated the NA inhibitor susceptibilities of viruses of the N1 subtype isolated from wild waterbirds, swine, and humans. Most avian viruses were highly or moderately susceptible to oseltamivir (50% inhibitory concentration [IC50], &

APA, Harvard, Vancouver, ISO, and other styles

36

Shikov, A. N., E. I. Sergeeva, O. K. Demina, et al. "Development of DNA-Biochip for Identification of Influenza A Virus Subtypes." Problems of Particularly Dangerous Infections, no. 2(112) (April 20, 2012): 89–93. http://dx.doi.org/10.21055/0370-1069-2012-2(112)-89-93.

Full text

Abstract:

Developed was the DNA-biochip to identify subtypes of influenza A virus, pathogenic for humans. Microchip was capable of detecting H1, H3, H5-subtypes of hemagglutinin (including H1-subtype of pandemic A/H1N1(2009) influenza virus ) and neuraminidase subtypes N1,N2 of influenza virus. This microchip was successfully tested on the strains of A/H5N1 highly pathogenic avian influenza virus, A/H1N1(2009) pandemic influenza virus, A/H1N1 and A/H3N2 seasonal influenza viruses.

APA, Harvard, Vancouver, ISO, and other styles

37

Smet, Anouk, Joao Paulo Portela Catani, Tine Ysenbaert, et al. "Antibodies directed towards neuraminidase restrict influenza virus replication in primary human bronchial epithelial cells." PLOS ONE 17, no. 1 (2022): e0262873. http://dx.doi.org/10.1371/journal.pone.0262873.

Full text

Abstract:

Influenza neuraminidase (NA) is implicated in various aspects of the virus replication cycle and therefore is an attractive target for vaccination and antiviral strategies. Here we investigated the potential for NA-specific antibodies to interfere with A(H1N1)pdm09 replication in primary human airway epithelial (HAE) cells. Mouse polyclonal anti-NA sera and a monoclonal antibody could block initial viral entry into HAE cells as well as egress from the cell surface. NA-specific polyclonal serum also reduced virus replication across multiple rounds of infection. Restriction of virus entry correl

APA, Harvard, Vancouver, ISO, and other styles

38

Sharp, G. B., Y. Kawaoka, S. M. Wright, B. Turner, V. Hinshaw, and R. G. Webster. "Wild ducks are the reservoir for only a limited number of influenza A subtypes." Epidemiology and Infection 110, no. 1 (1993): 161–76. http://dx.doi.org/10.1017/s0950268800050780.

Full text

Abstract:

SUMMARYAnalysis of cloacal samples collected from 12321 wild ducks in Alberta, Canada, from 1976 to 1990 showed influenza A infections to be seasonal, with prevalences increasing as the population became increasingly more dense. Viruses with 3 haemagglutinin (H3, H4, and H6) and 3 neuraminidase subtypes (N2, N6, and N8) were found consistently to infect both adult and juvenile ducks each year, indicating that wild ducks may be a reservoir for these viruses. In contrast, viruses with 7 haemagglutinin (H2, H5, H7, H8, H9, H11, and H12) and 3 neuraminidase subtypes (N1, N3, and N4) were not found

APA, Harvard, Vancouver, ISO, and other styles

39

Changsom, Don, Hatairat Lerdsamran, Witthawat Wiriyarat, et al. "Influenza Neuraminidase Subtype N1: Immunobiological Properties and Functional Assays for Specific Antibody Response." PLOS ONE 11, no. 4 (2016): e0153183. http://dx.doi.org/10.1371/journal.pone.0153183.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Barr, I. G., M. McCaig, C. Durrant, and R. Shaw. "The rapid identification of human influenza neuraminidase N1 and N2 subtypes by ELISA." Vaccine 24, no. 44-46 (2006): 6675–78. http://dx.doi.org/10.1016/j.vaccine.2006.05.047.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Basler, Christopher F., Adolfo García-Sastre, and Peter Palese. "Mutation of Neuraminidase Cysteine Residues Yields Temperature-Sensitive Influenza Viruses." Journal of Virology 73, no. 10 (1999): 8095–103. http://dx.doi.org/10.1128/jvi.73.10.8095-8103.1999.

Full text

Abstract:

ABSTRACT The influenza virus neuraminidase (NA) is a tetrameric, virus surface glycoprotein possessing receptor-destroying activity. This enzyme facilitates viral release and is a target of anti-influenza virus drugs. The NA structure has been extensively studied, and the locations of disulfide bonds within the NA monomers have been identified. Because mutation of cysteine residues in other systems has resulted in temperature-sensitive (ts) proteins, we asked whether mutation of cysteine residues in the influenza virus NA would yield ts mutants. The ability to rationally design tight and stabl

APA, Harvard, Vancouver, ISO, and other styles

42

Juan, S. Gómez-Jeria, R. Crisóstomo-Cáceres Sebastián, and Robles-Navarro Andrés. "On the compatibility between formal QSAR results and docking results: the relationship between electronic structure and H5N1 (A/goose/Guangdong/SH7/2013) neuraminidase inhibition by some Tamiflu derivatives as an example." Chemistry Research Journal 6, no. 3 (2021): 46–59. https://doi.org/10.5281/zenodo.11654344.

Full text

Abstract:

<strong>Abstract </strong>A study of the relationships between electronic structure and the inhibition of theN1 neuraminidase of a H5N1 strain was carried out with the Density Functional Theory at the B3lYP/6-31G(d,p) level. A statistically significant equation was obtained allowing us to suggest some of the molecule-site interactions. Also some chemical modifications to the molecules to obtain more active compounds are suggested. The most important result of the QSAR study indicates the possible existence of a C-H ... X hydrogen bond involving a specific carbon atom. As we expect that both, Q

APA, Harvard, Vancouver, ISO, and other styles

43

Chen, Nan, Renxi Wang, Wanlu Zhu, et al. "Development and characterization of an antibody that recognizes influenza virus N1 neuraminidases." PLOS ONE 19, no. 5 (2024): e0302865. http://dx.doi.org/10.1371/journal.pone.0302865.

Full text

Abstract:

Influenza A viruses (IAVs) continue to pose a huge threat to public health, and their prevention and treatment remain major international issues. Neuraminidase (NA) is the second most abundant surface glycoprotein on influenza viruses, and antibodies to NA have been shown to be effective against influenza infection. In this study, we generated a monoclonal antibody (mAb), named FNA1, directed toward N1 NAs. FNA1 reacted with H1N1 and H5N1 NA, but failed to react with the NA proteins of H3N2 and H7N9. In vitro, FNA1 displayed potent antiviral activity that mediated both NA inhibition (NI) and b

APA, Harvard, Vancouver, ISO, and other styles

44

Udommaneethanakit, Thanyarat, Thanyada Rungrotmongkol, Vladimir Frecer, Pierfausto Seneci, Stanislav Miertus, and Urban Bren. "Drugs Against Avian Influenza A Virus: Design of Novel Sulfonate Inhibitors of Neuraminidase N1." Current Pharmaceutical Design 20, no. 21 (2014): 3478–87. http://dx.doi.org/10.2174/13816128113199990629.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Hooper, Kathryn A., and Jesse D. Bloom. "A Mutant Influenza Virus That Uses an N1 Neuraminidase as the Receptor-Binding Protein." Journal of Virology 87, no. 23 (2013): 12531–40. http://dx.doi.org/10.1128/jvi.01889-13.

Full text

Abstract:

In the vast majority of influenza A viruses characterized to date, hemagglutinin (HA) is the receptor-binding and fusion protein, whereas neuraminidase (NA) is a receptor-cleaving protein that facilitates viral release but is expendable for entry. However, the NAs of some recent human H3N2 isolates have acquired receptor-binding activity via the mutation D151G, although these isolates also appear to retain the ability to bind receptors via HA. We report here the laboratory generation of a mutation (G147R) that enables an N1 NA to completely co-opt the receptor-binding function normally perform

APA, Harvard, Vancouver, ISO, and other styles

46

Prachanronarong, Kristina L., Ayşegül Özen, Kelly M. Thayer, et al. "Molecular Basis for Differential Patterns of Drug Resistance in Influenza N1 and N2 Neuraminidase." Journal of Chemical Theory and Computation 12, no. 12 (2016): 6098–108. http://dx.doi.org/10.1021/acs.jctc.6b00703.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Li, Qing, Jianxun Qi, Wei Zhang, et al. "The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site." Nature Structural & Molecular Biology 17, no. 10 (2010): 1266–68. http://dx.doi.org/10.1038/nsmb.1909.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Baek, Yun Hee, Min-Suk Song, Eun-Young Lee, et al. "Profiling and Characterization of Influenza Virus N1 Strains Potentially Resistant to Multiple Neuraminidase Inhibitors." Journal of Virology 89, no. 1 (2014): 287–99. http://dx.doi.org/10.1128/jvi.02485-14.

Full text

Abstract:

ABSTRACTNeuraminidase inhibitors (NAIs) have been widely used to control influenza virus infection, but their increased use could promote the global emergence of resistant variants. Although various mutations associated with NAI resistance have been identified, the amino acid substitutions that confer multidrug resistance with undiminished viral fitness remain poorly understood. We therefore screened a known mutation(s) that could confer multidrug resistance to the currently approved NAIs oseltamivir, zanamivir, and peramivir by assessing recombinant viruses with mutant NA-encoding genes (cata

APA, Harvard, Vancouver, ISO, and other styles

49

Malaisree, Maturos, Thanyada Rungrotmongkol, Panita Decha, Pathumwadee Intharathep, Ornjira Aruksakunwong, and Supot Hannongbua. "Understanding of known drug-target interactions in the catalytic pocket of neuraminidase subtype N1." Proteins: Structure, Function, and Bioinformatics 71, no. 4 (2008): 1908–18. http://dx.doi.org/10.1002/prot.21897.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Bello, Martiniano. "Impact of tetramerization on the ligand recognition of N1 influenza neuraminidase via MMGBSA approach." Biopolymers 110, no. 5 (2018): e23251. http://dx.doi.org/10.1002/bip.23251.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!