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Journal articles on the topic 'NSXA'

Author: Grafiati

Published: 10 January 2023

Last updated: 31 July 2025

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1

Lindenbach, Brett D., Béla M. Prágai, Roland Montserret, et al. "The C Terminus of Hepatitis C Virus NS4A Encodes an Electrostatic Switch That Regulates NS5A Hyperphosphorylation and Viral Replication." Journal of Virology 81, no. 17 (2007): 8905–18. http://dx.doi.org/10.1128/jvi.00937-07.

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ABSTRACT Hepatitis C virus (HCV) nonstructural protein 4A (NS4A) is only 54 amino acids (aa) in length, yet it is a key regulator of the essential serine protease and RNA helicase activities of the NS3-4A complex, as well as a determinant of NS5A phosphorylation. Here we examine the structure and function of the C-terminal acidic region of NS4A through site-directed mutagenesis of a Con1 subgenomic replicon and through biophysical characterization of a synthetic peptide corresponding to this region. Our genetic studies revealed that in 8 of the 15 C-terminal residues of NS4A, individual Ala su

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2

Neddermann, Petra, Angelica Clementi, and Raffaele De Francesco. "Hyperphosphorylation of the Hepatitis C Virus NS5A Protein Requires an Active NS3 Protease, NS4A, NS4B, and NS5A Encoded on the Same Polyprotein." Journal of Virology 73, no. 12 (1999): 9984–91. http://dx.doi.org/10.1128/jvi.73.12.9984-9991.1999.

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ABSTRACT The nonstructural protein NS5A of hepatitis c virus (HCV) has been demonstrated to be a phosphoprotein with an apparent molecular mass of 56 kDa. In the presence of other viral proteins, p56 is converted into a slower-migrating form of NS5A (p58) by additional phosphorylation events. In this report, we show that the presence of NS3, NS4A, and NS4B together with NS5A is necessary and sufficient for the generation of the hyperphosphorylated form of NS5A (p58) and that all proteins must be encoded on the same polyprotein (in cis). Kinetic studies of NS5A synthesis and pulse-chase experim

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Oliver Koch, Jan, and Ralf Bartenschlager. "Modulation of Hepatitis C Virus NS5A Hyperphosphorylation by Nonstructural Proteins NS3, NS4A, and NS4B." Journal of Virology 73, no. 9 (1999): 7138–46. http://dx.doi.org/10.1128/jvi.73.9.7138-7146.1999.

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ABSTRACT NS5A of the hepatitis C virus (HCV) is a highly phosphorylated protein involved in resistance against interferon and required most likely for replication of the viral genome. Phosphorylation of this protein is mediated by a cellular kinase(s) generating multiple proteins with different electrophoretic mobilities. In the case of the genotype 1b isolate HCV-J, in addition to the basal phosphorylated NS5A (designated pp56), a hyperphosphorylated form (pp58) was found on coexpression of NS4A (T. Kaneko, Y. Tanji, S. Satoh, M. Hijikata, S. Asabe, K. Kimura, and K. Shimotohno, Biochem. Biop

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4

De Francesco, Raffaele, Antonello Pessi, and Christian Steinkühler. "The Hepatitis C Virus NS3 Proteinase: Structure and Function of a Zinc-Containing Serine Proteinase." Antiviral Therapy 3, no. 3_suppl (1998): 99–109. http://dx.doi.org/10.1177/135965359800303s01.

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The hepatitis C virus (HCV) NS3 protein contains a serine proteinase domain implicated in the maturation of the viral polyprotein. NS3 forms a stable heterodimer with NS4A, a viral memebrane protein that acts as an activator of the IMS3 proteinase. The three-dimensional structure of the NS3 proteinase complexed with an NS4A-derived peptide has been determined. The NS3 proteinase adopts a chymotrypsin-like fold. A β-strand contributed by NS4A is clamped between two β-strands within the N terminus of NS3. Consistent with the requirement for extraordinarily long peptide substrates (P6-P4’), the s

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5

Bugaru, Mihai, and Ovidiu Vasile. "Dynamic Instability Investigation of the Automotive Driveshaft’s Forced Torsional Vibration Using the Asymptotic Method." Applied Sciences 14, no. 17 (2024): 7681. http://dx.doi.org/10.3390/app14177681.

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This paper aims to investigate using FOAM to analyze the dynamic instability in the APPR for ADFTV based on a dynamic model (DMADFTV). The DMADFTV considers the following aspects: AD kinematic nonuniformity (ADKN), AD geometric nonuniformity (ADGN) of inertial characteristics for the spinning movements (ICSM) of the AD elements (ADE), and the excitations induced by the gearbox–internal combustion engine modulations. The DMADFTV is considered the already-designed dynamic model developed by the first author of the ADFTV in a previous publication. This DMADFTV was used to compute the stationary f

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Bukhtiyarova, Marina, Christopher J. Rizzo, Charles A. Kettner, Bruce D. Korant, Helen T. Scarnati, and Robert W. King. "Inhibition of the Bovine Viral Diarrhoea Virus NS3 Serine Protease by a Boron-Modified Peptidyl Mimetic of its Natural Substrate." Antiviral Chemistry and Chemotherapy 12, no. 6 (2001): 367–73. http://dx.doi.org/10.1177/095632020101200607.

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Bovine viral diarrhoea virus (BVDV) is closely related to hepatitis C virus (HCV), and has been used as a surrogate virus in drug development for HCV infection. Similar to HCV, BVDV-encoded NS3 serine proteinase is responsible for multiple cleavages in the viral polyprotein, generating mature NS4A, NS4B, NS5A and NS5B proteins. NS3-dependent cleavage sites of BVDV contain a strictly conserved leucine at P1, and either serine or alanine at P1′. The full length BVDV NS3/4A serine protease has been cloned and expressed in bacterial cells. The enzyme has been purified from the soluble portion of E

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7

Sudo, Kenji, Kayo Yamaji, Kouich Kawamura, et al. "High-Throughput Screening of Low Molecular Weight NS3-NS4A Protease Inhibitors Using a Fluorescence Resonance Energy Transfer Substrate." Antiviral Chemistry and Chemotherapy 16, no. 6 (2005): 385–92. http://dx.doi.org/10.1177/095632020501600605.

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Hepatitis C virus (HCV) NS3-NS4A protease is an attractive target for anti-HCV agents because of its important role in replication. An optimized fluorescence resonance energy transfer (FRET) substrate for NS3-NS4A protease, based on the sequence of the NS5A-5B cleavage site, was designed and synthesized. High-throughput screening of in-house compound libraries was performed using a FRET substrate FS10 (MOCAc-DKIVPC-SMSYK-Dnp) and MBP-NS3-NS4A fusion protein. Several hit compounds were found, including YZ-9577 (2-oxido-1,2,5-oxadiazole-3,4-diyl) bis (phenylmethanone) with potent inhibitory acti

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8

Butkiewicz, Nancy, Nanhua Yao, Weidong Zhong, et al. "Virus-Specific Cofactor Requirement and Chimeric Hepatitis C Virus/GB Virus B Nonstructural Protein 3." Journal of Virology 74, no. 9 (2000): 4291–301. http://dx.doi.org/10.1128/jvi.74.9.4291-4301.2000.

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ABSTRACT GB virus B (GBV-B) is closely related to hepatitis C virus (HCV) and causes acute hepatitis in tamarins (Saguinus species), making it an attractive surrogate virus for in vivo testing of anti-HCV inhibitors in a small monkey model. It has been reported that the nonstructural protein 3 (NS3) serine protease of GBV-B shares similar substrate specificity with its counterpart in HCV. Authentic proteolytic processing of the HCV polyprotein junctions (NS4A/4B, NS4B/5A, and NS5A/5B) can be accomplished by the GBV-B NS3 protease in an HCV NS4A cofactor-independent fashion. We further characte

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9

Wölk, Benno, Domenico Sansonno, Hans-Georg Kräusslich, et al. "Subcellular Localization, Stability, andtrans-Cleavage Competence of the Hepatitis C Virus NS3-NS4A Complex Expressed in Tetracycline-Regulated Cell Lines." Journal of Virology 74, no. 5 (2000): 2293–304. http://dx.doi.org/10.1128/jvi.74.5.2293-2304.2000.

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ABSTRACT A tetracycline-regulated gene expression system and a panel of novel monoclonal antibodies were used to examine the subcellular localization, stability, and trans-cleavage competence of the hepatitis C virus (HCV) NS3-NS4A complex in inducible cell lines. The NS3 serine protease domain and the full-length NS3 protein expressed in the absence of the NS4A cofactor were diffusely distributed in the cytoplasm and nucleus. Coexpression of NS4A, however, directed NS3 to the endoplasmic reticulum (ER) or an ER-like modified compartment, as demonstrated by colocalization with 3,3′-dihexyloxac

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10

Selimović, Denis, and Mohamed Hassan. "Inhibition of Hepatitis C virus (HCV) Core protein- induced Cell Growth by Non-structural Protein 4A (NS4A) is Mediated by Mitochondrial Dysregulation." Bosnian Journal of Basic Medical Sciences 8, no. 1 (2008): 4–11. http://dx.doi.org/10.17305/bjbms.2008.2988.

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Hepatitis C virus (HCV) is a significant health problem facing the world. More than 170 million people are infected with HCV worldwide. HCV encodes a large polyprotein precursor that is processed into at least 10 distinct products including structural (core, E1 and E2) and non-structural (NS2, NS3, NS4A, NS4B, NS5A and NS5B). Besides its importance in virus replication, NS4A functions as a cofactor for NS3 and contributes to viral pathogenesis by influencing cellular functions. Here, we investigated the effect of NS4A protein on the growth rate induced by core protein in liver cells. Using our

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11

Martin, Morgan M., Stephanie A. Condotta, Jeremy Fenn, Andrea D. Olmstead, and François Jean. "In-cell selectivity profiling of membrane-anchored and replicase-associated hepatitis C virus NS3-4A protease reveals a common, stringent substrate recognition profile." Biological Chemistry 392, no. 10 (2011): 927–35. http://dx.doi.org/10.1515/bc.2011.076.

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AbstractThe need to identify anti-Flaviviridaeagents has resulted in intensive biochemical study of recombinant nonstructural (NS) viral proteases; however, experimentation on viral protease-associated replication complexes in host cells is extremely challenging and therefore limited. It remains to be determined if membrane anchoring and/or association to replicase-membrane complexes of proteases, such as hepatitis C virus (HCV) NS3-4A, plays a regulatory role in the substrate selectivity of the protease. In this study, we examined trans-endoproteolytic cleavage activities of membrane-anchored

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12

Beidas, Meshal, and Wassim Chehadeh. "PCR Array Profiling of Antiviral Genes in Human Embryonic Kidney Cells Expressing Human Coronavirus OC43 Structural and Accessory Proteins." Open Forum Infectious Diseases 4, suppl_1 (2017): S312. http://dx.doi.org/10.1093/ofid/ofx163.728.

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Abstract Background Human coronavirus OC43 (HCoV-OC43) causes common cold, and is associated with severe respiratory symptoms in infants, elderly and immunocompromised patients. HCoV-OC43 is a member of Betacoronavirus genus that includes also the Severe Acute Respiratory Syndrome (SARS) and the Middle East Respiratory Syndrome (MERS) coronaviruses. Both SARS-CoV and MERS-CoV were shown to express proteins with the potential to evade early innate immune responses. However, the ability of HCoV-OC43 to antagonise the intracellular antiviral defences has not yet been investigated. The objective o

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Lee, Jeong Yoon, Thi Thuy Ngan Nguyen та Jinjong Myoung. "Zika Virus-Encoded NS2A and NS4A Strongly Downregulate NF-κB Promoter Activity". Journal of Microbiology and Biotechnology 30, № 11 (2020): 1651–59. http://dx.doi.org/10.4014/jmb.2011.11003.

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14

Nomura-Takigawa, Yuki, Motoko Nagano-Fujii, Lin Deng, et al. "Non-structural protein 4A of Hepatitis C virus accumulates on mitochondria and renders the cells prone to undergoing mitochondria-mediated apoptosis." Journal of General Virology 87, no. 7 (2006): 1935–45. http://dx.doi.org/10.1099/vir.0.81701-0.

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Non-structural protein 4A (NS4A) of Hepatitis C virus (HCV) functions as a cofactor for NS3 by forming a complex with it to augment its enzymic activities. NS4A also forms a complex with other HCV proteins, such as NS4B/NS5A, to facilitate the formation of the viral RNA replication complex on the endoplasmic reticulum (ER) membrane. In addition to its essential role in HCV replication, NS4A is thought to be involved in viral pathogenesis by affecting cellular functions. In this study, it was demonstrated that NS4A was localized not only on the ER, but also on mitochondria when expressed either

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15

Zou, Jing, Xuping Xie, Qing-Yin Wang, et al. "Characterization of Dengue Virus NS4A and NS4B Protein Interaction." Journal of Virology 89, no. 7 (2015): 3455–70. http://dx.doi.org/10.1128/jvi.03453-14.

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ABSTRACTFlavivirus replication is mediated by a membrane-associated replication complex where viral membrane proteins NS2A, NS2B, NS4A, and NS4B serve as the scaffold for the replication complex formation. Here, we used dengue virus serotype 2 (DENV-2) as a model to characterize viral NS4A-NS4B interaction. NS4A interacts with NS4B in virus-infected cells and in cells transiently expressing NS4A and NS4B in the absence of other viral proteins. Recombinant NS4A and NS4B proteins directly bind to each other with an estimatedKd(dissociation constant) of 50 nM. Amino acids 40 to 76 (spanning the f

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Konan, Kouacou V., Thomas H. Giddings, Masanori Ikeda, Kui Li, Stanley M. Lemon, and Karla Kirkegaard. "Nonstructural Protein Precursor NS4A/B from Hepatitis C Virus Alters Function and Ultrastructure of Host Secretory Apparatus." Journal of Virology 77, no. 14 (2003): 7843–55. http://dx.doi.org/10.1128/jvi.77.14.7843-7855.2003.

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ABSTRACT The nonstructural proteins of hepatitis C virus (HCV) have been shown previously to localize to the endoplasmic reticulum (ER) when expressed singly or in the context of other HCV proteins. To determine whether the expression of HCV nonstructural proteins alters ER function, we tested the effect of expression of NS2/3/4A, NS4A, NS4B, NS4A/B, NS4B/5A, NS5A, and NS5B from genotype 1b HCV on anterograde traffic from the ER to the Golgi apparatus. Only the nominal precursor protein NS4A/B affected the rate of ER-to-Golgi traffic, slowing the rate of Golgi-specific modification of the vesi

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17

Klaitong, Paeka, and Duncan R. Smith. "Roles of Non-Structural Protein 4A in Flavivirus Infection." Viruses 13, no. 10 (2021): 2077. http://dx.doi.org/10.3390/v13102077.

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Infections with viruses in the genus Flavivirus are a worldwide public health problem. These enveloped, positive sense single stranded RNA viruses use a small complement of only 10 encoded proteins and the RNA genome itself to remodel host cells to achieve conditions favoring viral replication. A consequence of the limited viral armamentarium is that each protein exerts multiple cellular effects, in addition to any direct role in viral replication. The viruses encode four non-structural (NS) small transmembrane proteins (NS2A, NS2B, NS4A and NS4B) which collectively remain rather poorly charac

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18

Lin, C., J. W. Wu, K. Hsiao, and M. S. Su. "The hepatitis C virus NS4A protein: interactions with the NS4B and NS5A proteins." Journal of virology 71, no. 9 (1997): 6465–71. http://dx.doi.org/10.1128/jvi.71.9.6465-6471.1997.

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Wang, Wenyan, Frederick C. Lahser, MinKyung Yi, et al. "Conserved C-Terminal Threonine of Hepatitis C Virus NS3 Regulates Autoproteolysis and Prevents Product Inhibition." Journal of Virology 78, no. 2 (2004): 700–709. http://dx.doi.org/10.1128/jvi.78.2.700-709.2004.

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ABSTRACT Inspection of over 250 hepatitis C virus (HCV) genome sequences shows that a threonine is strictly conserved at the P1 position in the NS3-NS4A (NS3-4A) autoproteolysis junction, while a cysteine is maintained as the P1 residue in all of the putative trans cleavage sites (NS4A-4B, NS4B-5A, and NS5A-5B). To understand why T631 is conserved at the NS3-4A junction of HCV, a series of in vitro transcription-translation studies were carried out using wild-type and mutant (T631C) NS3-4A constructs bearing native, truncated, and mutant NS4A segments. The autocleavage of the wild-type junctio

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20

Yu, Yufeng, Chengfeng Gao, Chunxia Wen, et al. "Intrinsic features of Zika Virus non-structural proteins NS2A and NS4A in the regulation of viral replication." PLOS Neglected Tropical Diseases 16, no. 5 (2022): e0010366. http://dx.doi.org/10.1371/journal.pntd.0010366.

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Zika virus (ZIKV) is a mosquito-borne flavivirus and can cause neurodevelopmental disorders in fetus. As a neurotropic virus, ZIKV persistently infects neural tissues during pregnancy but the viral pathogenesis remains largely unknown. ZIKV has a positive-sense and single-stranded RNA genome, which encodes 7 non-structural (NS) proteins, participating in viral replication and dysregulation of host immunity. Like those in many other viruses, NS proteins are considered to be products evolutionarily beneficiary to viruses and some are virulence factors. However, we found that some NS proteins enc

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Chang, Yu-Shiu, Ching-Len Liao, Chang-Huei Tsao, et al. "Membrane Permeabilization by Small Hydrophobic Nonstructural Proteins of Japanese Encephalitis Virus." Journal of Virology 73, no. 8 (1999): 6257–64. http://dx.doi.org/10.1128/jvi.73.8.6257-6264.1999.

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ABSTRACT Infection with Japanese encephalitis virus (JEV), a mosquito-borne flavivirus, may cause acute encephalitis in humans and induce severe cytopathic effects in various types of cultured cells. We observed that JEV replication rendered infected baby hamster kidney (BHK-21) cells sensitive to the translational inhibitor hygromycin B or α-sarcine, to which mock-infected cells were insensitive. However, little is known about whether any JEV nonstructural (NS) proteins contribute to virus-induced changes in membrane permeability. Using an inducibleEscherichia coli system, we investigated whi

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Park, Jooyeon, Jinhwa Jang, and Insung Ahn. "Comparison of Genetic Variations in Zika Virus Isolated From Different Geographic Regions." International Journal of Healthcare Information Systems and Informatics 14, no. 3 (2019): 29–39. http://dx.doi.org/10.4018/ijhisi.2019070103.

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The Zika virus (ZIKV) belongs to the genus Flavivirus, together with Dengue virus, yellow fever virus, and West Nile virus. The virus, which was first found in Africa in 1947, has spread across the world owing to a lack of effective drugs or vaccines. The complete genome sequence of ZIKV is now available; it includes three structural and seven non-structure genes arranged in the order of capsid, pre-membrane, envelope, NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5. Two geographically distinct lineages are known, i.e., Asian and African, but ZIKV exhibits differences in clinical progression among r

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Mackenzie, Jason M., Alexander A. Khromykh, Malcolm K. Jones, and Edwin G. Westaway. "Subcellular Localization and Some Biochemical Properties of the Flavivirus Kunjin Nonstructural Proteins NS2A and NS4A." Virology 245, no. 2 (1998): 203–15. http://dx.doi.org/10.1006/viro.1998.9156.

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Grassmann, Claus W., Olaf Isken, Norbert Tautz, and Sven-Erik Behrens. "Genetic Analysis of the Pestivirus Nonstructural Coding Region: Defects in the NS5A Unit Can Be Complemented intrans." Journal of Virology 75, no. 17 (2001): 7791–802. http://dx.doi.org/10.1128/jvi.75.17.7791-7802.2001.

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ABSTRACT The functional analysis of molecular determinants which control the replication of pestiviruses was considerably facilitated by the finding that subgenomic forms of the positive-strand RNA genome of BVDV (bovine viral diarrhea virus) are capable of autonomous replication in transfected host cells. The prototype replicon, BVDV DI9c, consists of the genomic 5′ and 3′ untranslated regions and a truncated open reading frame (ORF) encoding mainly the nonstructural proteins NS3, NS4A, NS4B, NS5A, and NS5B. To gain insight into which of these proteins are essential for viral replication and

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Asabe, S. I., Y. Tanji, S. Satoh, T. Kaneko, K. Kimura, and K. Shimotohno. "The N-terminal region of hepatitis C virus-encoded NS5A is important for NS4A-dependent phosphorylation." Journal of virology 71, no. 1 (1997): 790–96. http://dx.doi.org/10.1128/jvi.71.1.790-796.1997.

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Moriyama, Masaru, Naoya Kato, Motoyuki Otsuka, et al. "Interferon-beta is activated by hepatitis C virus NS5B and inhibited by NS4A, NS4B, and NS5A." Hepatology International 1, no. 2 (2007): 302–10. http://dx.doi.org/10.1007/s12072-007-9003-8.

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Ueno, Takamasa, Satoru Misawa, Yoichi Ohba, et al. "Isolation and Characterization of Monoclonal Antibodies That Inhibit Hepatitis C Virus NS3 Protease." Journal of Virology 74, no. 14 (2000): 6300–6308. http://dx.doi.org/10.1128/jvi.74.14.6300-6308.2000.

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ABSTRACT A series of mouse monoclonal antibodies (MAbs) to the nonstructural protein 3 (NS3) of hepatitis C virus was prepared. One of these MAbs, designated 8D4, was found to inhibit NS3 protease activity. This inhibition was competitive with respect to the substrate peptide (Ki = 39 nM) but was significantly decreased by the addition of the NS4A peptide, a coactivator of the NS3 protease. 8D4 also showed marked inhibition of the NS3-dependentcis processing of the NS3/4A polyprotein but had virtually no effect on the succeeding NS3/4A-dependent transprocessing of the NS5A/5B polyprotein in vi

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Desombere, Isabelle, Hans Van Vlierberghe, Ola Weiland, et al. "Serum levels of anti-NS4a and anti-NS5a predict treatment response of patients with chronic hepatitis C." Journal of Medical Virology 79, no. 6 (2007): 701–13. http://dx.doi.org/10.1002/jmv.20846.

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Wahaab, Abdul, Ke Liu, Muddassar Hameed, et al. "Identification of Cleavage Sites Proteolytically Processed by NS2B-NS3 Protease in Polyprotein of Japanese Encephalitis Virus." Pathogens 10, no. 2 (2021): 102. http://dx.doi.org/10.3390/pathogens10020102.

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Understanding the proteolytic processing of polyprotein mediated by NS2B-NS3 protease contributes to the exploration of the mechanisms underlying infection of Japanese encephalitis virus (JEV), a zoonotic flavivirus. In this study, eukaryotic and prokaryotic cell models were employed to identify the cleavage sites mediated by viral NS2B-NS3 protease in JEV polyprotein. Artificial green fluorescent protein (GFP) substrates that contained the predicted cleavage site sequences of JEV polyprotein were expressed in swine testicle (ST) cells in the presence and absence of JEV infection, or co-expres

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Rawlinson, William. "Pregnancy, the placenta and Zika virus (ZIKV) infection." Microbiology Australia 37, no. 4 (2016): 170. http://dx.doi.org/10.1071/ma16057.

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Zika virus (ZIKV) infections have been recognised in Africa and Asia since 1940. The virus is in the family Flaviviridae and genus Flavivirus, along with Dengue, Japanese encephalitis virus, Tick borne encephalitis, West Nile virus, and Yellow fever virus. These viruses share biological characteristics of an envelope, icosahedral nucleocapsid, and a non-segmented, positive sense, single-strand RNA genome of ~10kb encoding three structural proteins (capsid C pre-membrane/membrane PrM/M, envelope E), and seven non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B and NS5). ZIKV has three kno

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Yi, MinKyung, and Stanley M. Lemon. "Adaptive Mutations Producing Efficient Replication of Genotype 1a Hepatitis C Virus RNA in Normal Huh7 Cells." Journal of Virology 78, no. 15 (2004): 7904–15. http://dx.doi.org/10.1128/jvi.78.15.7904-7915.2004.

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ABSTRACT Despite recent successes in generating subgenomic RNA replicons derived from genotype 1b strains of hepatitis C virus (HCV) that replicate efficiently in cultured cells, it has proven difficult to generate efficiently replicating RNAs from any other genotype of HCV. This includes genotype 1a, even though it is closely related to genotype 1b. We show here that an important restriction to replication of the genotype 1a H77c strain RNA in normal Huh7 cells resides within the amino-terminal 75 residues of the NS3 protease. We identified adaptive mutations located within this NS3 domain an

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Gallinari, Paola, Debra Brennan, Chiara Nardi, et al. "Multiple Enzymatic Activities Associated with Recombinant NS3 Protein of Hepatitis C Virus." Journal of Virology 72, no. 8 (1998): 6758–69. http://dx.doi.org/10.1128/jvi.72.8.6758-6769.1998.

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ABSTRACT The hepatitis C virus (HCV) nonstructural 3 protein (NS3) contains at least two domains associated with multiple enzymatic activities; a serine protease activity resides in the N-terminal one-third of the protein, whereas RNA helicase activity and RNA-stimulated nucleoside triphosphatase activity are associated with the C-terminal portion. To study the possible mutual influence of these enzymatic activities, a full-length NS3 polypeptide of 67 kDa was expressed as a nonfusion protein in Escherichia coli, purified to homogeneity, and shown to retain all three enzymatic activities. The

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Abdullah, Adib Afandi, Yean Kee Lee, Sek Peng Chin, et al. "Discovery of Dengue Virus Inhibitors." Current Medicinal Chemistry 27, no. 30 (2020): 4945–5036. http://dx.doi.org/10.2174/0929867326666181204155336.

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To date, there is still no approved anti-dengue agent to treat dengue infection in the market. Although the only licensed dengue vaccine, Dengvaxia is available, its protective efficacy against serotypes 1 and 2 of dengue virus was reported to be lower than serotypes 3 and 4. Moreover, according to WHO, the risk of being hospitalized and having severe dengue increased in seronegative individuals after they received Dengvaxia vaccination. Nevertheless, various studies had been carried out in search of dengue virus inhibitors. These studies focused on the structural (C, prM, E) and non-structura

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Umareddy, Indira, Alex Chao, Aruna Sampath, Feng Gu, and Subhash G. Vasudevan. "Dengue virus NS4B interacts with NS3 and dissociates it from single-stranded RNA." Journal of General Virology 87, no. 9 (2006): 2605–14. http://dx.doi.org/10.1099/vir.0.81844-0.

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Dengue virus, a member of the family Flaviviridae of positive-strand RNA viruses, has seven non-structural proteins: NS1, NS2A, NS2B, NS3, NS4A, NS4B and NS5. Except for enzymic activities contained within NS3 and NS5, the roles of the other proteins in virus replication and pathogenesis are not well defined. In this study, a physical interaction between NS4B and the helicase domain of NS3 was identified by using a yeast two-hybrid assay. This interaction was further confirmed by biochemical pull-down and immunoprecipitation assays, both with purified proteins and with dengue virus-infected ce

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&NA;. "NSNA." AJN, American Journal of Nursing 88, no. 6 (1988): 892–93. http://dx.doi.org/10.1097/00000446-198806000-00022.

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Rodríguez, Alejandro, Carolina Oliva, and Miguel González. "A comparative QM/MM study of the reaction mechanism of the Hepatitis C virus NS3/NS4A protease with the three main natural substrates NS5A/5B, NS4B/5A and NS4A/4B." Physical Chemistry Chemical Physics 12, no. 28 (2010): 8001. http://dx.doi.org/10.1039/c002116d.

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Sahoo, PK. "Annual NSSA Conference Report-NSSA Spine 2021." Journal of Spinal Surgery 8, no. 4 (2021): 57. http://dx.doi.org/10.4103/joss.joss_16_21.

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Shimizu, Y., K. Yamaji, Y. Masuho, et al. "Identification of the sequence on NS4A required for enhanced cleavage of the NS5A/5B site by hepatitis C virus NS3 protease." Journal of virology 70, no. 1 (1996): 127–32. http://dx.doi.org/10.1128/jvi.70.1.127-132.1996.

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Mamrawk, Chuck. "NSSA update." Neutron News 9, no. 1 (1998): 42. http://dx.doi.org/10.1080/10448639808232014.

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O’Brien, Christopher, and Nicholas Agresti. "NS5A Inhibitors." Current Hepatitis Reports 11, no. 3 (2012): 181–87. http://dx.doi.org/10.1007/s11901-012-0138-2.

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Worsley, Jean. "NSTA recommends." Science and Children 55, no. 6 (2018): 96. http://dx.doi.org/10.1080/00368148.2018.12292164.

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Pfeiffer, Jacqueline. "NSTA Recommends." Science and Children 55, no. 7 (2018): 97–99. http://dx.doi.org/10.1080/00368148.2018.12292189.

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DeVore-Wedding, Bev. "NSTA Recommends." Science and Children 55, no. 5 (2018): 90. http://dx.doi.org/10.1080/00368148.2018.12292144.

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Ruud, Ruth. "NSTA recommends." Science and Children 55, no. 4 (2017): 90. http://dx.doi.org/10.1080/00368148.2017.12292116.

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Pfeiffer, Jacqueline. "NSTA recommends." Science and Children 55, no. 2 (2017): 94–98. http://dx.doi.org/10.1080/00368148.2017.12292071.

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Palmquist, Jane. "From ASTA and NSOA to ASTA with NSOA." American String Teacher 49, no. 2 (1999): 60–69. http://dx.doi.org/10.1177/000313139904900210.

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Lee, Chia Min, Xuping Xie, Jing Zou, et al. "Determinants of Dengue Virus NS4A Protein Oligomerization." Journal of Virology 89, no. 12 (2015): 6171–83. http://dx.doi.org/10.1128/jvi.00546-15.

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ABSTRACTFlavivirus NS4A protein induces host membrane rearrangement and functions as a replication complex component. The molecular details of how flavivirus NS4A exerts these functions remain elusive. Here, we used dengue virus (DENV) as a model to characterize and demonstrate the biological relevance of flavivirus NS4A oligomerization. DENV type 2 (DENV-2) NS4A protein forms oligomers in infected cells or when expressed alone. Deletion mutagenesis mapped amino acids 50 to 76 (spanning the first transmembrane domain [TMD1]) of NS4A as the major determinant for oligomerization, while the N-ter

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Ngueyen, Thi Thuy Ngan, Seong-Jun Kim, Jeong Yoon Lee, and Jinjong Myoung. "Zika Virus Proteins NS2A and NS4A Are Major Antagonists that Reduce IFN-�� Promoter Activity Induced by the MDA5/RIG-I Signaling Pathway." Journal of Microbiology and Biotechnology 29, no. 10 (2019): 1665–74. http://dx.doi.org/10.4014/jmb.1909.09017.

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Awad, Mahmoud, Mohamed Abouhawwash, and H. N. Agiza. "On NSGA-II and NSGA-III in Portfolio Management." Intelligent Automation & Soft Computing 32, no. 3 (2022): 1893–904. http://dx.doi.org/10.32604/iasc.2022.023510.

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Pascut, Devis, Minh Hoang, Nhu N. Q. Nguyen, Muhammad Yogi Pratama, and Claudio Tiribelli. "HCV Proteins Modulate the Host Cell miRNA Expression Contributing to Hepatitis C Pathogenesis and Hepatocellular Carcinoma Development." Cancers 13, no. 10 (2021): 2485. http://dx.doi.org/10.3390/cancers13102485.

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Hepatitis C virus (HCV) genome encodes for one long polyprotein that is processed by cellular and viral proteases to generate 10 polypeptides. The viral structural proteins include the core protein, and the envelope glycoproteins E1 and E2, present at the surface of HCV particles. Non-structural (NS) proteins consist of NS1, NS2, NS3, NS4A, NS4B, NS5a, and NS5b and have a variable function in HCV RNA replication and particle assembly. Recent findings evidenced the capacity of HCV virus to modulate host cell factors to create a favorable environment for replication. Indeed, increasing evidence

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