Relevant bibliographies by topics / NS1

Academic literature on the topic 'NS1'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "NS1"

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Kumar, Chaudhary, Lu, Duff, Heffel, McKinney, Bedenice, and Marthaler. "Metagenomic Next-Generation Sequencing Reveal Presence of a Novel Ungulate Bocaparvovirus in Alpacas." Viruses 11, no. 8 (July 31, 2019): 701. http://dx.doi.org/10.3390/v11080701.

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Viruses belonging to the genus Bocaparvovirus (BoV) are a genetically diverse group of DNA viruses known to cause respiratory, enteric, and neurological diseases in animals, including humans. An intestinal sample from an alpaca (Vicugna pacos) herd with reoccurring diarrhea and respiratory disease was submitted for next-generation sequencing, revealing the presence of a BoV strain. The alpaca BoV strain (AlBoV) had a 58.58% whole genome nucleotide percent identity to a camel BoV from Dubai, belonging to a tentative ungulate BoV 8 species (UBoV8). Recombination events were lacking with other UBoV strains. The AlBoV genome was comprised of the NS1, NP1, and VP1 proteins. The NS1 protein had the highest amino acid percent identity range (57.89–67.85%) to the members of UBoV8, which was below the 85% cut-off set by the International Committee on Taxonomy of Viruses. The low NS1 amino acid identity suggests that AlBoV is a tentative new species. The whole genome, NS1, NP1, and VP1 phylogenetic trees illustrated distinct branching of AlBoV, sharing a common ancestor with UBoV8. Walker loop and Phospholipase A2 (PLA2) motifs that are vital for virus infectivity were identified in NS1 and VP1 proteins, respectively. Our study reports a novel BoV strain in an alpaca intestinal sample and highlights the need for additional BoV research.
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Shen, Weiran, Xuefeng Deng, Wei Zou, John F. Engelhardt, Ziying Yan, and Jianming Qiu. "Analysis ofcisandtransRequirements for DNA Replication at the Right-End Hairpin of the Human Bocavirus 1 Genome." Journal of Virology 90, no. 17 (June 22, 2016): 7761–77. http://dx.doi.org/10.1128/jvi.00708-16.

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ABSTRACTParvoviruses are single-stranded DNA viruses that use the palindromic structures at the ends of the viral genome for their replication. The mechanism of parvovirus replication has been studied mostly in the dependoparvovirus adeno-associated virus 2 (AAV2) and the protoparvovirus minute virus of mice (MVM). Here, we used human bocavirus 1 (HBoV1) to understand the replication mechanism of bocaparvovirus. HBoV1 is pathogenic to humans, causing acute respiratory tract infections, especially in young children under 2 years old. By using the duplex replicative form of the HBoV1 genome in human embryonic kidney 293 (HEK293) cells, we identified the HBoV1 minimal replication origin at the right-end hairpin (OriR). Mutagenesis analyses confirmed the putative NS1 binding and nicking sites within the OriR. Of note, unlike the large nonstructural protein (Rep78/68 or NS1) of other parvoviruses, HBoV1 NS1 did not specifically bind OriRin vitro, indicating that other viral and cellular components or the oligomerization of NS1 is required for NS1 binding to the OriR.In vivostudies demonstrated that residues responsible for NS1 binding and nicking are within the origin-binding domain. Further analysis identified that the small nonstructural protein NP1 is required for HBoV1 DNA replication at OriR. NP1 and other viral nonstructural proteins (NS1 to NS4) colocalized within the viral DNA replication centers in both OriR-transfected cells and virus-infected cells, highlighting a direct involvement of NP1 in viral DNA replication at OriR. Overall, our study revealed the characteristics of HBoV1 DNA replication at OriR, suggesting novel characteristics of autonomous parvovirus DNA replication.IMPORTANCEHuman bocavirus 1 (HBoV1) causes acute respiratory tract infections in young children. The duplex HBoV1 genome replicates in HEK293 cells and produces progeny virions that are infectious in well-differentiated airway epithelial cells. A recombinant AAV2 vector pseudotyped with an HBoV1 capsid has been developed to efficiently deliver the cystic fibrosis transmembrane conductance regulator gene to human airway epithelia. Here, we identified bothcis-acting elements andtrans-acting proteins that are required for HBoV1 DNA replication at the right-end hairpin in HEK293 cells. We localized the minimal replication origin, which contains both NS1 nicking and binding sites, to a 46-nucleotide sequence in the right-end hairpin. The identification of these essential elements of HBoV1 DNA replication acting both incisand intranswill provide guidance to develop antiviral strategies targeting viral DNA replication at the right-end hairpin and to design next-generation recombinant HBoV1 vectors, a promising tool for gene therapy of lung diseases.
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Agger, Sean A., Fernando Lopez-Gallego, Thomas R. Hoye, and Claudia Schmidt-Dannert. "Identification of Sesquiterpene Synthases from Nostoc punctiforme PCC 73102 and Nostoc sp. Strain PCC 7120." Journal of Bacteriology 190, no. 18 (July 25, 2008): 6084–96. http://dx.doi.org/10.1128/jb.00759-08.

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ABSTRACT Cyanobacteria are a rich source of natural products and are known to produce terpenoids. These bacteria are the major source of the musty-smelling terpenes geosmin and 2-methylisoborneol, which are found in many natural water supplies; however, no terpene synthases have been characterized from these organisms to date. Here, we describe the characterization of three sesquiterpene synthases identified in Nostoc sp. strain PCC 7120 (terpene synthase NS1) and Nostoc punctiforme PCC 73102 (terpene synthases NP1 and NP2). The second terpene synthase in N. punctiforme (NP2) is homologous to fusion-type sesquiterpene synthases from Streptomyces spp. shown to produce geosmin via an intermediate germacradienol. The enzymes were functionally expressed in Escherichia coli, and their terpene products were structurally identified as germacrene A (from NS1), the eudesmadiene 8a-epi-α-selinene (from NP1), and germacradienol (from NP2). The product of NP1, 8a-epi-α-selinene, so far has been isolated only from termites, in which it functions as a defense compound. Terpene synthases NP1 and NS1 are part of an apparent minicluster that includes a P450 and a putative hybrid two-component protein located downstream of the terpene synthases. Coexpression of P450 genes with their adjacent located terpene synthase genes in E. coli demonstrates that the P450 from Nostoc sp. can be functionally expressed in E. coli when coexpressed with a ferredoxin gene and a ferredoxin reductase gene from Nostoc and that the enzyme oxygenates the NS1 terpene product germacrene A. This represents to the best of our knowledge the first example of functional expression of a cyanobacterial P450 in E. coli.
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Young, L. B., E. Balmori Melian, and A. A. Khromykh. "NS1' Colocalizes with NS1 and Can Substitute for NS1 in West Nile Virus Replication." Journal of Virology 87, no. 16 (June 12, 2013): 9384–90. http://dx.doi.org/10.1128/jvi.01101-13.

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Wolff, Thorsten, Robert E. O’Neill, and Peter Palese. "NS1-Binding Protein (NS1-BP): a Novel Human Protein That Interacts with the Influenza A Virus Nonstructural NS1 Protein Is Relocalized in the Nuclei of Infected Cells." Journal of Virology 72, no. 9 (September 1, 1998): 7170–80. http://dx.doi.org/10.1128/jvi.72.9.7170-7180.1998.

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ABSTRACT We used the yeast interaction trap system to identify a novel human 70-kDa protein, termed NS1-binding protein (NS1-BP), which interacts with the nonstructural NS1 protein of the influenza A virus. The genetic interaction was confirmed by the specific coprecipitation of the NS1 protein from solution by a glutathioneS-transferase–NS1-BP fusion protein and glutathione-Sepharose. NS1-BP contains an N-terminal BTB/POZ domain and five kelch-like tandem repeat elements of ∼50 amino acids. In noninfected cells, affinity-purified antibodies localized NS1-BP in nuclear regions enriched with the spliceosome assembly factor SC35, suggesting an association of NS1-BP with the cellular splicing apparatus. In influenza A virus-infected cells, NS1-BP relocalized throughout the nucleoplasm and appeared distinct from the SC35 domains, which suggests that NS1-BP function may be disturbed or altered. The addition of a truncated NS1-BP mutant protein to a HeLa cell nuclear extract efficiently inhibited pre-mRNA splicing but not spliceosome assembly. This result could be explained by a possible dominant-negative effect of the NS1-BP mutant protein and suggests a role of the wild-type NS1-BP in promoting pre-mRNA splicing. These data suggest that the inhibition of splicing by the NS1 protein may be mediated by binding to NS1-BP.
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Alonso-Caplen, F. V., and R. M. Krug. "Regulation of the extent of splicing of influenza virus NS1 mRNA: role of the rates of splicing and of the nucleocytoplasmic transport of NS1 mRNA." Molecular and Cellular Biology 11, no. 2 (February 1991): 1092–98. http://dx.doi.org/10.1128/mcb.11.2.1092.

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Influenza virus NS1 mRNA is spliced by host nuclear enzymes to form NS2 mRNA, and this splicing is regulated in infected cells such that the steady-state amount of spliced NS2 mRNA is only about 10% of that of unspliced NS1 mRNA. This regulation would be expected to result from a suppression in the rate of splicing coupled with the efficient transport of unspliced NS1 mRNA from the nucleus. To determine whether the rate of splicing of NS1 mRNA was controlled by trans factors in influenza virus-infected cells, the NS1 gene was inserted into an adenovirus vector. The rates of splicing of NS1 mRNA in cells infected with this vector and in influenza virus-infected cells were measured by pulse-labeling with [3H]uridine. The rates of splicing of NS1 mRNA in the two systems were not significantly different, strongly suggesting that the rate of splicing of NS1 mRNA in influenza virus-infected cells is controlled solely by cis-acting sequences in NS1 mRNA itself. In contrast to the rate of splicing, the extent of splicing of NS1 mRNA in the cells infected by the adenovirus recombinant was dramatically increased relative to that occurring in influenza virus-infected cells. This could be attributed largely, if not totally, to a block in the nucleocytoplasmic transport of unspliced NS1 mRNA in the recombinant-infected cells. Most of the unspliced NS1 mRNA was in the nuclear fraction, and no detectable NS1 protein was synthesized. When the 3' splice site of NS1 mRNA was inactivated by mutation, NS1 mRNA was transported and translated, indicating that the transport block occurred because NS1 rRNA was committed to the splicing pathway. This transport block is apparently obviated in influenza virus-infected cells. These experiments demonstrate the important role of the nucleocytoplasmic transport of unspliced NS1 mRNA in regulating the extent of splicing of NS1 mRNA.
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Alonso-Caplen, F. V., and R. M. Krug. "Regulation of the extent of splicing of influenza virus NS1 mRNA: role of the rates of splicing and of the nucleocytoplasmic transport of NS1 mRNA." Molecular and Cellular Biology 11, no. 2 (February 1991): 1092–98. http://dx.doi.org/10.1128/mcb.11.2.1092-1098.1991.

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Influenza virus NS1 mRNA is spliced by host nuclear enzymes to form NS2 mRNA, and this splicing is regulated in infected cells such that the steady-state amount of spliced NS2 mRNA is only about 10% of that of unspliced NS1 mRNA. This regulation would be expected to result from a suppression in the rate of splicing coupled with the efficient transport of unspliced NS1 mRNA from the nucleus. To determine whether the rate of splicing of NS1 mRNA was controlled by trans factors in influenza virus-infected cells, the NS1 gene was inserted into an adenovirus vector. The rates of splicing of NS1 mRNA in cells infected with this vector and in influenza virus-infected cells were measured by pulse-labeling with [3H]uridine. The rates of splicing of NS1 mRNA in the two systems were not significantly different, strongly suggesting that the rate of splicing of NS1 mRNA in influenza virus-infected cells is controlled solely by cis-acting sequences in NS1 mRNA itself. In contrast to the rate of splicing, the extent of splicing of NS1 mRNA in the cells infected by the adenovirus recombinant was dramatically increased relative to that occurring in influenza virus-infected cells. This could be attributed largely, if not totally, to a block in the nucleocytoplasmic transport of unspliced NS1 mRNA in the recombinant-infected cells. Most of the unspliced NS1 mRNA was in the nuclear fraction, and no detectable NS1 protein was synthesized. When the 3' splice site of NS1 mRNA was inactivated by mutation, NS1 mRNA was transported and translated, indicating that the transport block occurred because NS1 rRNA was committed to the splicing pathway. This transport block is apparently obviated in influenza virus-infected cells. These experiments demonstrate the important role of the nucleocytoplasmic transport of unspliced NS1 mRNA in regulating the extent of splicing of NS1 mRNA.
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Kasiyati, Menik, Jusak Nugraha, and Hartono Kahar. "Chymase level in dengue virus infection with or without positive Non-Structural 1(NS1)." Jurnal Teknologi Laboratorium 8, no. 2 (December 30, 2019): 41–46. http://dx.doi.org/10.29238/teknolabjournal.v8i2.167.

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Thrombocytopenia, leukopenia, and monocytosis are laboratory parameters in the diagnosis of dengue virus infection. In addition to monocyte cells, mast cells also play a role in the innate immune response, where degranulation of mast cells will occur, which will secretion the active vaso mediator, Chymase. Chymase has a role in increasing vascular permeability resulting in plasma leakage in patients with dengue virus infection to determine the number of platelets, leukocytes, monocytes and chymase levels in patients with dengue infection in the acute phase. The platelet count mean in NS1 (+) was 132,140 cells / mm3 and the platelet count in the NS1 group was (-) 176,000 cells / mm3. The mean leukocytes NS1 (+) showed results of 4,350 cells / mm3 and NS1 (-) 5,250 cells / mm3. The mean monocyte NS1 (+) monocyte count was 8.26%, and NS1 (-) group was 8.76%. There were no significant differences in platelet counts, leukocytes and monocytes between NS1 (+) and NS1 (-) (P value> 0.05). The mean Chymase NS1 (+) 23.48, NS1 (-) 23.05 ng / mL and the control group 1.47ng / mL.
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Krishna, Venkatramana D., Manjuladevi Rangappa, and Vijaya Satchidanandam. "Virus-Specific Cytolytic Antibodies to Nonstructural Protein 1 of Japanese Encephalitis Virus Effect Reduction of Virus Output from Infected Cells." Journal of Virology 83, no. 10 (March 4, 2009): 4766–77. http://dx.doi.org/10.1128/jvi.01850-08.

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ABSTRACT We demonstrate the presence of nonstructural protein 1 (NS1)-specific antibodies in a significant proportion of convalescent-phase human serum samples obtained from a cohort in an area where Japanese encephalitis virus (JEV) is endemic. Sera containing antibodies to NS1 but not those with antibodies to other JEV proteins, such as envelope, brought about complement-mediated lysis of JEV-infected BHK-21 cells. Target cells infected with a recombinant poxvirus expressing JEV NS1 on the cell surface confirmed the NS1 specificity of cytolytic antibodies. Mouse anti-NS1 cytolytic sera caused a complement-dependent reduction in virus output from infected human cells, demonstrating their important role in viral control. Antibodies elicited by JEV NS1 did not cross lyse West Nile virus- or dengue virus-infected cells despite immunoprecipitating the NS1 proteins of these related flaviviruses. Additionally, JEV NS1 failed to bind complement factor H, in contrast to NS1 of West Nile virus, suggesting that the NS1 proteins of different flaviviruses have distinctly different mechanisms for interacting with the host. Our results also point to an important role for JEV NS1-specific human immune responses in protection against JE and provide a strong case for inclusion of the NS1 protein in next generation of JEV vaccines.
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Kuo, Rei-Lin, Li-Hsin Li, Sue-Jane Lin, Zong-Hua Li, Guang-Wu Chen, Cheng-Kai Chang, Yi-Ren Wang, et al. "Role of N Terminus-Truncated NS1 Proteins of Influenza A Virus in Inhibiting IRF3 Activation." Journal of Virology 90, no. 9 (February 24, 2016): 4696–705. http://dx.doi.org/10.1128/jvi.02843-15.

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ABSTRACTThe NS1 protein encoded by influenza A virus antagonizes the interferon response through various mechanisms, including blocking cellular mRNA maturation by binding the cellular CPSF30 3′ end processing factor and/or suppressing the activation of interferon regulatory factor 3 (IRF3). In the present study, we identified two truncated NS1 proteins that are translated from internal AUGs at positions 235 and 241 of the NS1 open reading frame. We analyzed the cellular localization and function of the N-truncated NS1 proteins encoded by two influenza A virus strains, Udorn/72/H3N2 (Ud) and Puerto Rico/8/34/H1N1 (PR8). The NS1 protein of PR8, but not Ud, inhibits the activation of IRF3, whereas the NS1 protein of Ud, but not PR8, binds CPSF30. The truncated PR8 NS1 proteins are localized in the cytoplasm, whereas the full-length PR8 NS1 protein is localized in the nucleus. The infection of cells with a PR8 virus expressing an NS1 protein containing mutations of the two in-frame AUGs results in both the absence of truncated NS1 proteins and the reduced inhibition of activation of IRF3 and beta interferon (IFN-β) transcription. The expression of the truncated PR8 NS1 protein by itself enhances the inhibition of the activation of IRF3 and IFN-β transcription in Ud virus-infected cells. These results demonstrate that truncated PR8 NS1 proteins contribute to the inhibition of activation of this innate immune response. In contrast, the N-truncated NS1 proteins of the Ud strain, like the full-length NS1 protein, are localized in the nucleus, and mutation of the two in-frame AUGs has no effect on the activation of IRF3 and IFN-β transcription.IMPORTANCEInfluenza A virus causes pandemics and annual epidemics in the human population. The viral NS1 protein plays a critical role in suppressing type I interferon expression. In the present study, we identified two novel truncated NS1 proteins that are translated from the second and third in-frame AUG codons in the NS1 open reading frame. The N-terminally truncated NS1 encoded by the H1N1 PR8 strain of influenza virus that suppresses IRF3 activation is localized primarily in the cytoplasm. We demonstrate that this truncated NS1 protein by itself enhances this suppression, demonstrating that some strains of influenza A virus express truncated forms of the NS1 protein that function in the inhibition of cytoplasmic antiviral events.
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Dissertations / Theses on the topic "NS1"

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Oliveira, Anibal Silva de. "Clonagem e expressão das proteínas recombinantes NS1 e NS3 do vírus da dengue tipo 3." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/60/60135/tde-21062013-141504/.

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A dengue é uma doença infecciosa com grandes taxas de morbimortalidade, causada pelo vírus da dengue (DENV). Segundo a Organização Mundial de Saúde, cerca de 50 a 100 milhões de pessoas são infectadas anualmente em mais de 100 países tropicais e subtropicais de todos os continentes. O espectro clínico da infecção pelo DENV pode incluir formas assintomáticas ou sintomaticas que variam desde uma febre indeterminada e autolimitada, passando pela febre clássica da dengue (FD) até quadros graves denominados febre hemorrágica da dengue/síndrome do choque da dengue (FHD/SCD). Recentemente, ocorreu um dramático aumento do número de casos de FHD/SCD nas Américas, e este aumento coincidiu com a introdução do dengue sorotipo 3, genótipo III. No presente trabalho, objetivou-se a clonagem e a expressão das proteínas NS1 e NS3 do vírus da dengue tipo 3. As proteínas NS1 e NS3 do DENV-3 foram clonadas e expressas com sucesso em sistema procarioto. A amplificação dos genes das proteínas NS1 e NS3 foi realizada por RT-PCR, o qual gerou amplicons de cerca de 1050 e 1850 pb, respectivamente. Em seguida, os genes foram clonados por inserção dos amplicons no vetor plasmidial pCR-XL. Os genes de NS1 e NS3 foram subclonados no vetor de expressão pQE-30 através de sítios de restrição para as enzimas BamHI e HindIII. A expressão proteica foi obtida em sistema procarioto utilizando a cepa BL21(DE3) de E. coli, resultando em proteínas de 45 e 70 kDa as quais foram confirmadas por análises em Western blot utilizando como anticorpo primário fluido ascítico imune de camundongos e soro de pacientes com dengue. Estas proteínas virais podem ser utilizadas para estudos relacionados à patogênese, replicação e mecanismos de escape do sistema imune do DENV, além disso, podem ser potencias antígenos em métodos de diagnóstico.
Dengue is an infectious disease with high morbidity and mortality rates caused by dengue virus (DENV). According to the World Health Organization, about 50 to 100 million people are infected annually in more than 100 tropical and subtropical countries from all continents. The clinical spectrum of DENV infection can includes asymptomatic or symptomatic forms ranging from undetermined and self-limited fever, through dengue fever (DF) to severe disease called dengue hemorrhagic fever/dengue shock syndrome (DHF/DSS). Recently, there has been a dramatic increase in the number of cases of DHF/DSS in the Americas, and this increase coincided with the introduction of dengue virus type 3 (DENV-3), genotype III. The present study aimed to clone and express NS1 and NS3 proteins of DENV-3. The NS1 and NS3 proteins of DENV-3 was successfully cloned and expressed in a prokaryotic system. Amplification of NS1 and NS3 genes was carried out by RT-PCR, which yielded amplicons of approximately 1050 and 1850 bp, respectively. Then, the genes were cloned by inserting the amplicons into the plasmid vector pCR-XL. NS1 and NS3 genes were subcloned into the expression vector pQE-30 through the restriction sites for BamHI and HindIII enzymes. The protein expression was obtained in a prokaryotic system using the strain BL21 (DE3) of E. coli, resulting in 45 and 70 kDa proteins, which were confirmed by Western blot analysis using immune mouse ascitic fluid and serum of patients with dengue as primary antibody. These viral proteins can be used to study the pathogenesis, mechanisms of replication and immune escape of DENV, moreover, can be potential antigens in diagnostic methods.
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Marozin, Sabrina. "Interferon Escape of Respiratory Syncytial Virus: Functional Analysis of Nonstructural Proteins NS1 and NS2." Diss., lmu, 2006. http://nbn-resolving.de/urn:nbn:de:bvb:19-54265.

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Zwart, Lizahn. "Investigating two AHSV non-structural proteins : tubule-forming protein NS1 and novel protein NS4." Diss., University of Pretoria, 2013. http://hdl.handle.net/2263/62198.

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African horse sickness is an equid disease caused by African horse sickness virus (AHSV). AHSV produces seven structural proteins that form the virion and four non-structural proteins with various roles during replication. The first part of this study investigated the intracellular distribution and co-localisations of NS1 with other AHSV proteins to facilitate its eventual functional characterisation. Confocal microscopy revealed that NS1 formed small cytoplasmic foci early after infection that gradually converged into large fluorescent NS1 tubule bundles. Tubule bundles were more organised in AHSV-infected cells than in cells expressing NS1 alone, suggesting that tubule bundle formation requires the presence of other AHSV proteins or regulation of NS1 expression rates. NS1 occasionally co-localised with VP7 crystalline structures, independently of other AHSV proteins. However, when NS1-eGFP, a modified NS1 protein that contains enhanced green fluorescent protein (eGFP) near the C-terminus, was co-expressed with VP7, co-localisation between these proteins occurred in most co-infected cells. It is not clear how the addition of eGFP to NS1 induces this co-localisation and further investigation will be required to determine the function of NS1 during viral replication. The second part of the study focused on characterising the novel non-structural AHSV protein NS4. The NS4 open reading frame (ORF) occurs on segment 9, overlapping the VP6 ORF in a different reading frame. In silico analysis of segment 9 nucleotide and NS4 predicted amino acid sequences revealed a large amount of variation between serotypes, and two main types of NS4 were identified based on these analyses. These proteins differed in length and amino acid sequence and were named NS4-I and NS4-II. Immunoblotting confirmed that AHSV NS4 is translated in AHSV infected insect and mammalian cells, and also in Sf9 insect cells infected with recombinant baculoviruses that overexpress the genome segment 9 proteins, VP6 and NS4. Confocal microscopy showed that NS4 localised to both the cytoplasm and nucleus, but not the nucleolus, in AHSV-infected cells and recombinant baculovirus infected Sf9 cells. Nucleic acid protection assays using bacterially expressed purified NS4 showed that both types of NS4 bind dsDNA, but not dsRNA. This was the first study to focus on AHSV NS4. Future work will focus on determining the role of non-structural proteins in viral pathogenesis, and will involve the use of a reverse genetics system for AHSV.
Dissertation (MSc)--University of Pretoria, 2013.
Genetics
MSc
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Costa, Simone Morais da. "Vacinas de DNA contra o vírus da dengue utilizando como antígenos as proteínas NS1 e NS3." reponame:Repositório Institucional da FIOCRUZ, 2008. https://www.arca.fiocruz.br/handle/icict/12179.

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Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Rio de Janeiro, RJ, Brasil
O vírus da dengue (DENV) consiste de quatro sorotipos antigenicamente relacionados: DENV-1, DENV-2, DENV-3 e DENV-4. Apesar dos diversos esforços para o desenvolvimento de uma vacina contra dengue, ainda não há nenhuma comercialmente disponível. As proteínas não estruturais 1 e 3 (NS1 e NS3) são indicadas como antígenos promissores para o desenvolvimento de uma vacina contra DENV. Segundo alguns estudos, a proteína NS1 é capaz de induzir uma resposta protetora de anticorpos com atividade de fixação do complemento. A proteína NS3, que realiza reações enzimáticas essenciais para a replicação viral, parece ser imunogênica, contendo um predomínio de epítopos para linfócitos T CD4+ e CD8+. No presente trabalho nós avaliamos o potencial de vacinas de DNA baseadas nas proteínas NS1 e NS3 de DENV-2. Foram construídos cinco plasmídeos, pcTPANS3, pcTPANS3H, pcTPANS3P, pcTPANS3N e pcTPANS3C, contendo a seqüência que codifica o peptídeo sinal do ativador de plasminogênio de tecido humano (t-PA) fusionado ao gene NS3 inteiro ou partes destes. Todos estes plasmídeos mediaram a expressão das proteínas recombinantes in vitro em células eucarióticas Camundongos foram inoculados com estes plasmídeos e desafiados com DENV-2 por via intracerebral (i.c.). Nenhuma destas construções induziu níveis satisfatórios de proteção. Além dos plasmídeos com NS3, foram construídas quatro vacinas de DNA baseadas no gene NS1: 1 - pcENS1, que codifica a região C-terminal da proteína E fusionada à NS1, 2 - pcENS1ANC, similar ao pcENS1 com a adição da porção N-terminal da NS2A (ANC), 3 - pcTPANS1, que codifica o peptídeo sinal t-PA fusionado à NS1 e 4 - pcTPANS1ANC, semelhante ao pcTPANS1 com a adição da seqüência ANC. A proteína NS1 recombinante foi detectada nos extratos celulares e sobrenadante das culturas de células BHK transfectadas com pcTPANS1, pcENS1 e pcENS1ANC. Tais resultados indicam que as seqüências sinais t-PA e E direcionaram a NS1 para secreção. A proteína NS1 também foi observada associada à membrana plasmática de células transfectadas com pcENS1ANC, demonstrando a importância da seqüência ANC para o seu ancoramento. Todos os camundongos imunizados com pcTPANS1 ou pcENS1 produziram altos níveis de anticorpos, direcionados principalmente para epítopos conformacionais da NS1, enquanto que somente metade dos animais inoculados com pcENS1ANC apresentaram níveis detectáveis de anticorpos A resposta de anticorpos se mostrou duradoura (até 56 semanas após a primeira dose das vacinas), e os animais apresentaram uma rápida resposta secundária após um reforço de DNA. Camundongos imunizados com os plasmídeos pcTPANS1 e pcENS1 se mostraram protegidos contra desafios com DENV-2 por via i.c., sendo o pcTPANS1 levemente mais protetor. Estes dois plasmídeos ativaram a produção de diferentes subclasses de IgG específicas contra NS1. Não foi observada proteção interespecífica quando camundongos imunizados com pcTPANS1 foram desafiados por via i.c. com DENV-1. Os animais imunizados com o pcTPANS1 foram desafiados com DENV-2 por via intraperitoneal e também se mostraram protegidos. Neste modelo de desafio, foi observada uma diminuição dos efeitos histopatológicos do vírus no fígado dos animais vacinados. Resultados preliminares sugerem à lise de células infectadas com DENV-2, dependente do complemento, na presença dos anticorpos direcionados contra NS1
Dengue virus (DENV) consists of four antigenically related serotypes: DENV-1, DENV-2, DENV-3 and DENV-4. Although considerable research has been conducted towards the development of a DENV vaccine, no vaccine is yet commercially available. The non-structural proteins 1 and 3 (NS1 and NS3) have been identified as promising antigens for the development of vaccines against DENV. According to some reports, NS1 can elicit a protective antibody response with complement-fixing activities. NS3, a protein that carries out enzymatic reactions essential for viral replication, appears to be immunogenic, presenting a preponderance of the CD4+ and CD8+ T cell epitopes. In the present work we investigate the potential of DNA vaccines based on the DENV-2 NS1 and NS3 proteins. We constructed five recombinant plasmids, pcTPANS3, pcTPANS3H, pcTPANS3P, pcTPANS3N and pcTPANS3C, which contain the sequence that codes the signal peptide derived from the human tissue plasminogen activator (t-PA) fused to the full or partial length of the DENV-2 NS3 gene. Results indicated that these plasmids promoted the expression of recombinant proteins in eukaryotic cells. Mice were inoculated with these plasmids and challenged by the intracerebral (i.c.) route with DENV-2. None of these constructs induced acceptable protection. Moreover, we constructed four DNA vaccines based on the DENV-2 NS1 gene: 1 - pcENS1, coding the C-terminal of the E protein fused to NS1, 2 - pcENS1ANC, similar to pcENS1 with the addition of the N-terminal of NS2A (ANC), 3 - pcTPANS1, coding the t-PA signal sequence fused to NS1 and 4 - pcTPANS1ANC, similar to pcTPANS1 with the addition of the ANC sequence. The recombinant NS1 protein was detected in cell extracts and culture supernatants from pcTPANS1-, pcENS1- and pcENS1ANC-transfected BHK cells. Such results indicated that the E and t-PA sequences targeted NS1 to secretion. NS1 was also observed in association with plasma membrane of pcENS1ANC-transfected cells, which demonstrated the importance of the ANC sequence for cell anchoring. High levels of antibodies, mainly recognizing surface-exposed conformational epitopes of NS1, were induced in all mice immunized with pcTPANS1 and pcENS1, while only half of pcENS1ANC-inoculated animals presented detectable antibody levels. Long-term antibody response was observed in pcTPANS1 and pcENS1 immunized animals (56 weeks after the first vaccine inoculation) and there was a rapid secondary response after a DNA booster. Protection was elicited in pcTPANS1- and pcENS1-immunized mice challenged with DENV- 2 by the i.c. route and the pcTPANS1 seemed to generate a slightly higher protection. Moreover, these two plasmids induced different NS1-specific IgG subclasses. No protection was displayed when pcTPANS1-immunized animals were i.c. challenged with DENV-1. Animals inoculated with pcTPANS1 were also protected when they were challenged with DENV-2 by the intraperitoneal route. Liver tissue from vaccinated animals presented a remarkable decrease of hepatic damages in this challenge mouse model. Preliminary results suggested the complement-mediated lyses of DENV-2 infected cells in the presence of the NS1-specific antibody.
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Figueiredo, Alessandra. "Imunossensores potenciométricos para a detecção da proteína NS1 do vírus da dengue." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/76/76132/tde-13082013-164540/.

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A dengue é uma doença negligenciada que carece de métodos diagnósticos rápidos nos primeiros dias de infecção. São quatro sorotipos diferentes, cuja monitoração é essencial para o controle da ocorrência de casos graves como a dengue hemorrágica. É urgente o desenvolvimento e disponibilização de um dispositivo capaz de suprir essa demanda, de modo que propomos a utilização de imunossensores potenciométricos, devido a facilidade de miniaturização e produção dos dispositivos e seu baixo custo, além da possibilidade de detecção direta (sem marcadores) e simplicidade de manuseio. Dispositivos sensores de pH, como o transistor de efeito de campo de porta estendida e separada (SEGFET) e amplificadores de instrumentação (AI) podem ser utilizados como transdutores de sinal para a reação antígeno-anticorpo, a partir da utilização de materiais não nernstianos, como o ouro, como plataforma sensível. A proteína NS1 do vírus da dengue é um excelente marcador da infecção, pois é secretada em altas concentrações pelo vírus no sangue de pessoas infectadas logo nos primeiros dias, de modo que o sistema preza pelo diagnóstico precoce da doença. Sua detecção é realizada através da imobilização de anticorpos anti-proteína NS1 na plataforma sensível, permitindo sua quantificação através da detecção da alteração local de carga. O eletrodo foi caracterizado por diversas técnicas de microscopia, entre elas de varredura, confocal e de força atômica, além da utilização de espectroscopia de impedância eletroquímica, permitindo um amplo conhecimento da superfície da membrana sensível. Os imunossensores desenvolvidos apresentaram alta sensibilidade, com capacidade de detecção da ordem de ng.mL-1. Na região linear da curva analítica, foram obtidos sensibilidade correspondente a (15.7 ± 4.4) .10-4 μA.μg.mL-1 para o SEGFET e (3.2 ± 0.3) mV.μg.mL-1 para o AI, sendo que este último apresenta uma maior estabilidade de sinal e dispensa a utilização de uma fonte variável de tensão, reduzindo o custo no desenvolvimento de um dispositivo diagnóstico comercial. Estes resultados levaram a um pedido de patente e o prosseguimento do projeto através da miniaturização do sistema e detecção em amostras reais.
Dengue is a neglected disease that lacks fast diagnosis methods in the first days of infection. There are four different serotypes, which monitoring is essential to the occurrence control of severe cases as dengue hemorrhagic fever. The development of a device capable of fulfilling this demand is urgent, so we propose the use of potentiometric immunosensors, since its ease of miniaturization, mass production, low cost and the possibility of direct detection (label-free). pH sensor devices, as the separated extended gate field effect transistors (SEGFET) and instrumentation amplifiers (AI) can be applied as transducers to the antibody-antigen reaction by using non-nernstian materials such as gold as sensitive membrane. The non-structural 1 (NS1) protein is an excellent marker of infection, since its secreted in high concentration in the blood of infected people by the dengue virus in the first days, prioritizing early diagnosis. Its detection is made by immobilization of anti-NS1 protein antibodies, allowing its quantification by local charge changes. The electrode was characterized by many microscopy methods, including scanning electron, confocal and atomic force, besides electrochemistry impedance spectroscopy, providing a wide knowledge of the membrane surface. The developed immunosensors showed high sensitivity with detection capacity in the order of ng.mL-1. In the linear range of the analytic curve, were obtained sensitivities of (15.7 ± 4.4) .10-4 μA.μg.mL-1 for the SEGFET and (3.2 ± 0.3) mV.μg.mL-1 for the AI, whereas the latter has high signal stability sparring the use of a variable voltage source, minimizing the costs in the development of a commercial diagnostic device. These results led to a patent and the project continues by working in miniaturizing and real samples detection.
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Wolff, Michael. "Identifizierung und Charakterisierung von Interaktionen der Nichtstrukturproteine NS1 und NS2 des Respiratorischen Synzytialvirus mit Proteinen der Wirtszelle." Diss., lmu, 2004. http://nbn-resolving.de/urn:nbn:de:bvb:19-24259.

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Evans, Johanna. "Characterisation of the NS1 and the NS2 non-structural protein genes of human respiratory syncytial virus (HRSV)." Thesis, University of Warwick, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.283482.

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SHA, Tim Wai. "Functional studies of Influenza A virus NS1 protein." Kyoto University, 2020. http://hdl.handle.net/2433/259078.

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Bossert, Birgit. "Of Mice and Men and Cattle: Functions of the Pneumovirus Nonstructural Proteins NS1 and NS2 in Interferon Escape." Diss., lmu, 2003. http://nbn-resolving.de/urn:nbn:de:bvb:19-7733.

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Smith, Matthew. "Consequences of variation in the influenza virus NS1 protein." Thesis, Imperial College London, 2010. http://hdl.handle.net/10044/1/6969.

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The NS1 protein is a major virulence factor of influenza virus. Although the protein is encoded by all natural influenza viruses, its sequence shows considerable variation suggesting that it interacts intimately with the host. Indeed this multifunctional protein has been described to bind a plethora of cellular factors. The influenza A NS1 protein from A/PR/8/34 was previously shown to enhance translation of a host expressed gene. This is likely a consequence of its ability to counter basally expressed host antiviral strategies that are activated within the cell upon transfection and transient expression of exogenous genes. This work evaluated a panel of NS1 proteins derived from different strains and subtypes of influenza, for their capacity to enhance translation. Although it is possible that all natural NS1 proteins have the capacity for this function, it was found to be often obscured by a dominant inhibitory function that was mapped to the C terminus of the protein. Only NS1 proteins that lack this second function illustrated translational enhancement without prior mutation. Modification of the C terminal domain of NS1 was able to abrogate binding to the CPSF host factor responsible for the maturation of host genes transcribed by polymerase II. This then revealed the potential of most if not all NS1 proteins to act as translational enhancers. A series of NS1 mutants were engineered to test the proposed mechanism of translational enhancement, and this work confirmed that enhancement required NS1 to be present in the cytoplasm of the transfected cell, and retain an intact dsRNA binding site. The intriguing finding that not all natural NS1 proteins bind to the CPSF host factor was investigated to ask whether CPSF interaction sometimes carried a cost to viral fitness. The hypothesis was that some NS1 proteins adopt this global mechanism for the control of interferon to compensate for high levels of PAMP produced by infection more active viral polymerase. The observations deduced from this work lead to the suggestion that NS1 participates in the regulation of interferon at the level of the polymerase complex by modulating the viral polymerase activity, in addition to its previously characterized function to counter the PRR RIG-I, and disruption of CPSF function. Combining the approaches established during this body of work, it was established that the behaviour of the NS1 protein of the newly emerged swine origin H1N1 2009 pandemic virus were unusual. Interestingly this protein was able to strongly enhance translation despite being predominantly localized to the nucleus. Importantly a reverse genetic approach demonstrated that the levels of interferon induced during infection by the pandemic H1N1 strain could be being under represented, and this may explain discrepancies in the literature between different models of pathogenicity of the pandemic virus.
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Books on the topic "NS1"

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Evans, Johanna. Characterisation of the NS1 and the NS2 non-structural protein genes of human respiratory syncytial virus (HRSV). [s.l.]: typescript, 1994.

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Jacobs, Susan Catherine. Characterisation and analysis of the NS1 gene of tick-borne encephalitis virus. Oxford: Oxford Brookes University, 1992.

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Laul, Ulev. Kodumaast: NSV Liidu Ja Eesti NSV Riigihumnist. Tallinn: Eesti Raamat, 1988.

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Flint, Wendy. NSF development framework. Leicester: National Youth Agency, 2003.

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Heinsalu, Ülo. Eesti NSV koopad. Tallinn: "Valgus", 1987.

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Vanatoa, Endel. Eesti NSV, teatmik. Tallinn: "Perioodika", 1985.

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Roser, Wayne. Sentencing law NSW. Edited by Veltro Frank, Favretto John, and Bellanto Anthony. Chatswood, NSW: LexisNexis Butterworths, 2003.

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Vanatoa, Endel. Eesti NSV, teatmik. Tallinn: Perioodika, 1988.

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Amoako, B. O. Enne nso bio. 2nd ed. Accra: Bureau of Ghana Languages, 1994.

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Groeneveld, Gerard. Zo zong de NSB: Liedcultuur van de NSB, 1931-1945. Nijmegen: Uitgeverij Vantilt, 2007.

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Book chapters on the topic "NS1"

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Ayllon, Juan, and Adolfo García-Sastre. "The NS1 Protein: A Multitasking Virulence Factor." In Current Topics in Microbiology and Immunology, 73–107. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/82_2014_400.

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van Staden, V., C. C. Smit, M. A. Stoltz, F. F. Maree, and H. Huismans. "Characterization of two African horse sickness virus nonstructural proteins, NS1 and NS3." In African Horse Sickness, 251–58. Vienna: Springer Vienna, 1998. http://dx.doi.org/10.1007/978-3-7091-6823-3_22.

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Richt, Jüergen A., and Adolfo García-Sastre. "Attenuated Influenza Virus Vaccines with Modified NS1 Proteins." In Current Topics in Microbiology and Immunology, 177–95. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-92165-3_9.

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de Silva, Aravinda M., Félix A. Rey, Paul R. Young, Rolf Hilgenfeld, and Subhash G. Vasudevan. "Viral Entry and NS1 as Potential Antiviral Drug Targets." In Advances in Experimental Medicine and Biology, 107–13. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-8727-1_8.

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Othman, N. H., Khuan Y. Lee, A. R. M. Radzol, W. Mansor, P. S. Wong, and I. Looi. "PCA-KNN for Detection of NS1 from SERS Salivary Spectra." In Intelligent Information and Database Systems, 335–46. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-75420-8_32.

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Kim, Young Chan, Nallely Garcia-Larragoiti, Cesar Lopez-Camacho, Martha Eva Viveros-Sandoval, and Arturo Reyes-Sandoval. "Production and Purification of Zika Virus NS1 Glycoprotein in HEK293 Cells." In Methods in Molecular Biology, 93–102. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0581-3_8.

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Alcon-LePoder, S., P. Sivard, M. T. Drouet, A. Talarmin, C. Rice, and M. Flamand. "Secretion of Flaviviral Non-Structural Protein NS1: from Diagnosis to Pathogenesis." In Novartis Foundation Symposia, 233–50. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470058005.ch17.

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Krug, Robert M., and Adolfo García-Sastre. "The NS1 protein: A master regulator of host and viral functions." In Textbook of Influenza, 114–32. Oxford, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118636817.ch7.

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Nüesch, Jürg P. F., and Jean Rommelaere. "Tumor Suppressing Properties of Rodent Parvovirus NS1 Proteins and Their Derivatives." In Advances in Experimental Medicine and Biology, 99–124. London: Springer London, 2014. http://dx.doi.org/10.1007/978-1-4471-6458-6_5.

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Pica, Natalie, Peter Palese, and John Steel. "Live Attenuated Influenza Virus Vaccines: NS1 Truncation as an Approach to Virus Attenuation." In Replicating Vaccines, 195–221. Basel: Springer Basel, 2010. http://dx.doi.org/10.1007/978-3-0346-0277-8_8.

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Conference papers on the topic "NS1"

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"Technical session NS1: Network security I." In 2008 International Conference on Computer Engineering & Systems. IEEE, 2008. http://dx.doi.org/10.1109/icces.2008.4773004.

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Argondizzo, Ana, Alessandra Abalo, Laís Alves, Henrique Rocha, Liliane Morais, and Sotiris Missailidis. "Expressão e purificação das proteínas NS1 e NS5 do vírus Zika para utilização na seleção de aptâmeros." In VI Seminário Anual Científico e Tecnológico. Instituto de Tecnologia em Imunobiológicos, 2018. http://dx.doi.org/10.35259/isi.sact.2018_26927.

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Morais, L. M., L. N. Alves, A. P. C. Argondizzo, H. F. Rocha, D. Silva, E. C. N. Valdez, A. M. B. Filippis, and S. Missailidis. "DNA aptamer as molecular tool for ZIKV NS1 protein detection." In INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2018 (ICCMSE 2018). Author(s), 2018. http://dx.doi.org/10.1063/1.5079162.

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Othman, N. H., Khuan Y. Lee, A. R. M. Radzol, W. Mansor, and N. N. M. Ramlan. "Linear discriminant analysis for detection of salivary NS1 from SERS spectra." In TENCON 2017 - 2017 IEEE Region 10 Conference. IEEE, 2017. http://dx.doi.org/10.1109/tencon.2017.8228352.

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Othman, N. H., Khuan Y. Lee, A. R. M. Radzol, W. Mansor, and U. R. M. Rashid. "Classification of Salivary Adulterated NS1 SERS Spectra Using PCA-Cosine-KNN." In 2019 4th International Conference on Intelligent Informatics and Biomedical Sciences (ICIIBMS). IEEE, 2019. http://dx.doi.org/10.1109/iciibms46890.2019.8991490.

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Othman, N. H., Khuan Y. Lee, A. R. M. Radzol, W. Mansor, and U. R. M. Rashid. "K-Nearest Neigbour: Detection of NS1 from SERS spectra of adulterated saliva." In TENCON 2016 - 2016 IEEE Region 10 Conference. IEEE, 2016. http://dx.doi.org/10.1109/tencon.2016.7848314.

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Radzol, A. R. M., Khuan Y. Lee, W. Mansor, and N. Ariffin. "Biostatistical analysis of principle component of salivary Raman spectra for NS1 infection." In 2016 IEEE EMBS Conference on Biomedical Engineering and Sciences (IECBES). IEEE, 2016. http://dx.doi.org/10.1109/iecbes.2016.7843406.

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Othman, N. H., Khuan Y. Lee, A. R. M. Radzol, W. Mansor, and U. R. M. Rashid. "Detection of NS1 from SERS spectra using K-NN integrated with PCA." In 2016 IEEE EMBS Conference on Biomedical Engineering and Sciences (IECBES). IEEE, 2016. http://dx.doi.org/10.1109/iecbes.2016.7843421.

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Saifuzzaman, T. A., Khuan Y. Lee, A. R. M. Radzol, P. S. Wong, and I. Looi. "Optimal Scree-CNN for Detecting NS1 Molecular Fingerprint from Salivary SERS Spectra." In 2020 42nd Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC) in conjunction with the 43rd Annual Conference of the Canadian Medical and Biological Engineering Society. IEEE, 2020. http://dx.doi.org/10.1109/embc44109.2020.9176003.

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Radzol, A. R. M., Khuan Y. Lee, and W. Mansor. "Classification of salivary based NS1 from Raman Spectroscopy with support vector machine." In 2014 36th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2014. http://dx.doi.org/10.1109/embc.2014.6943966.

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Reports on the topic "NS1"

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Robertson, Kent, and Melissa Lee. Pilot Study of Gleevec/Imatinib Mesylate (STI-571, NSC 716051) in Neurofibromatosis (NF1) Patients with Plexiform Neurofibromas. Fort Belvoir, VA: Defense Technical Information Center, July 2013. http://dx.doi.org/10.21236/ada591162.

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Agrimson, Erick Paul, Gordon McIntosh, James Flaten, Kaye Smith, Bernhard Beck-Winchatz, Hank D. Voss, Donald Takehara, and Stacy A. Wenzel. NSF IUSE Workshop. Ames (Iowa): Iowa State University. Library. Digital Press, January 2015. http://dx.doi.org/10.31274/ahac.9774.

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Beck, James B. NSO News - February 2014. Office of Scientific and Technical Information (OSTI), March 2014. http://dx.doi.org/10.2172/1122052.

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Beck, James B. NSO News October 2013. Office of Scientific and Technical Information (OSTI), November 2013. http://dx.doi.org/10.2172/1104903.

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Beck, James B. NSO News September 2013. Office of Scientific and Technical Information (OSTI), November 2013. http://dx.doi.org/10.2172/1104904.

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Beck, James B. NSO News January 2014. Office of Scientific and Technical Information (OSTI), February 2014. http://dx.doi.org/10.2172/1119587.

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Sparks, Valerie, Frederick M. Helsel, Daniel A. Lucero, and Darielle Dexheimer. ARM/NSA Monthly Report. Office of Scientific and Technical Information (OSTI), November 2016. http://dx.doi.org/10.2172/1331868.

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Fieber, Lynne A. Electrophysiological Changes in NF1. Fort Belvoir, VA: Defense Technical Information Center, September 2002. http://dx.doi.org/10.21236/ada410453.

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Fieber, Lynne A. Eletrophysiological Changes in NF1. Fort Belvoir, VA: Defense Technical Information Center, September 2003. http://dx.doi.org/10.21236/ada420897.

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Fieber, Lynne A. Electrophysiological Changes in NF1. Fort Belvoir, VA: Defense Technical Information Center, September 2000. http://dx.doi.org/10.21236/ada392199.

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