Relevant bibliographies by topics / Ribosomal entry site and entero viral infection

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  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'Ribosomal entry site and entero viral infection'

Author: Grafiati
Published: 2 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Ribosomal entry site and entero viral infection"

1

Stone, Jeffrey K., Rene Rijnbrand, David A. Stein, et al. "A Morpholino Oligomer Targeting Highly Conserved Internal Ribosome Entry Site Sequence Is Able To Inhibit Multiple Species of Picornavirus." Antimicrobial Agents and Chemotherapy 52, no. 6 (2008): 1970–81. http://dx.doi.org/10.1128/aac.00011-08.

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ABSTRACT Members of the genera Enterovirus and Rhinovirus (family Picornaviridae) cause a wide range of human diseases. An established vaccine is available only for poliovirus, and no effective therapy is available for the treatment of infections caused by any pathogenic picornavirus. Peptide-conjugated phosphorodiamidate morpholino oligomers (PPMO) are single-stranded DNA-like antisense agents that readily enter cells. A panel of PPMO was tested for their antiviral activities against various picornaviruses. PPMO targeting conserved internal ribosome entry site (IRES) sequence were highly acti
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2

Li, Qisheng, Catherine Sodroski, Brianna Lowey, et al. "Hepatitis C virus depends on E-cadherin as an entry factor and regulates its expression in epithelial-to-mesenchymal transition." Proceedings of the National Academy of Sciences 113, no. 27 (2016): 7620–25. http://dx.doi.org/10.1073/pnas.1602701113.

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Hepatitis C virus (HCV) enters the host cell through interactions with a cascade of cellular factors. Although significant progress has been made in understanding HCV entry, the precise mechanisms by which HCV exploits the receptor complex and host machinery to enter the cell remain unclear. This intricate process of viral entry likely depends on additional yet-to-be-defined cellular molecules. Recently, by applying integrative functional genomics approaches, we identified and interrogated distinct sets of host dependencies in the complete HCV life cycle. Viral entry assays using HCV pseudopar
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Muralinath, E., G. Srinivas, D.V. Ramanjaneyulu, et al. "An Important Parameters of Entero Virus Include Etiologhy, Epidemiology, Patho Physiology, Diagnosis, Differential Diagnosis, Treatment, Prognosis and Complications." Journal of Cardiovascular, Cardiopulmonary Rehabilitation Nursing 3, no. 2 (2025): 11–21. https://doi.org/10.5281/zenodo.15532695.

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<em>Enteroviruses are a class of viruses comprising approximately 300 serotypes. These common viruses have a broad range of illnesses, diverse presentations, widespread morbidity, and an economic burden. The pathologic basis of these diseases is explained in this exercise, which also goes over the interprofessional team's involvement in diagnosing and treating patients with enteroviral infections.</em>
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4

Licursi, Maria, Yumiko Komatsu, Theerawat Pongnopparat, and Kensuke Hirasawa. "Promotion of viral internal ribosomal entry site-mediated translation under amino acid starvation." Journal of General Virology 93, no. 5 (2012): 951–62. http://dx.doi.org/10.1099/vir.0.040386-0.

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Cap-dependent and internal ribosomal entry site (IRES)-mediated translation are regulated differently within cells. Viral IRES-mediated translation often remains active when cellular cap-dependent translation is severely impaired under cellular stresses induced by virus infection. To investigate how cellular stresses influence the efficiency of viral IRES-mediated translation, we used a bicistronic luciferase reporter construct harbouring IRES elements from the following viruses: encephalomyocarditis virus (EMCV), foot-and-mouth disease virus (FMDV), hepatitis C virus (HCV) or human rhinovirus
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Tripathi, Sachin Kumar, Ashish Aneja, Teji Borgaonkar, and Saumitra Das. "PSPC1 Binds to HCV IRES and Prevents Ribosomal Protein S5 Binding, Inhibiting Viral RNA Translation." Viruses 16, no. 5 (2024): 738. http://dx.doi.org/10.3390/v16050738.

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Hepatitis C virus (HCV) infects the human liver, and its chronic infection is one of the major causes of Hepatocellular carcinoma. Translation of HCV RNA is mediated by an Internal Ribosome Entry Site (IRES) element located in the 5’UTR of viral RNA. Several RNA Binding proteins of the host interact with the HCV IRES and modulate its function. Here, we demonstrate that PSPC1 (Paraspeckle Component 1), an essential paraspeckle component, upon HCV infection is relocalized and interacts with HCV IRES to prevent viral RNA translation. Competition UV-crosslinking experiments showed that PSPC1 inter
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6

Gallego, J., and G. Varani. "The hepatitis C virus internal ribosome-entry site: a new target for antiviral research." Biochemical Society Transactions 30, no. 2 (2002): 140–45. http://dx.doi.org/10.1042/bst0300140.

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The hepatitis C virus (HCV) is the main causative agent of non-A, non-B hepatitis in humans and a major cause of mortality and morbidity in the world. Currently there is no effective treatment available for the infection caused by this virus, whose replication depends on an unusual translation-initiation mechanism. The viral RNA contains an internal ribosome-entry site (IRES) that is recognized specifically by the small ribosomal subunit and by eukaryotic initiation factor 3, and these interactions allow cap (7-methylguanine nucleotide)-independent initiation of viral protein synthesis. In thi
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7

Chen, L. L., Y. A. Kung, K. F. Weng, J. Y. Lin, J. T. Horng, and S. R. Shih. "Enterovirus 71 Infection Cleaves a Negative Regulator for Viral Internal Ribosomal Entry Site-Driven Translation." Journal of Virology 87, no. 7 (2013): 3828–38. http://dx.doi.org/10.1128/jvi.02278-12.

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8

Svitkin, Yuri V., Barbara Herdy, Mauro Costa-Mattioli, Anne-Claude Gingras, Brian Raught, and Nahum Sonenberg. "Eukaryotic Translation Initiation Factor 4EAvailability Controls the Switch between Cap-Dependent andInternal Ribosomal Entry Site-MediatedTranslation." Molecular and Cellular Biology 25, no. 23 (2005): 10556–65. http://dx.doi.org/10.1128/mcb.25.23.10556-10565.2005.

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ABSTRACT Translation of m7G-capped cellular mRNAs is initiated by recruitment of ribosomes to the 5′ end of mRNAs via eukaryotic translation initiation factor 4F (eIF4F), a heterotrimeric complex comprised of a cap-binding subunit (eIF4E) and an RNA helicase (eIF4A) bridged by a scaffolding molecule (eIF4G). Internal translation initiation bypasses the requirement for the cap and eIF4E and occurs on viral and cellular mRNAs containing internal ribosomal entry sites (IRESs). Here we demonstrate that eIF4E availability plays a critical role in the switch from cap-dependent to IRES-mediated trans
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9

Fernández-Miragall, Olga, and Encarnación Martínez-Salas. "In vivo footprint of a picornavirus internal ribosome entry site reveals differences in accessibility to specific RNA structural elements." Journal of General Virology 88, no. 11 (2007): 3053–62. http://dx.doi.org/10.1099/vir.0.83218-0.

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Internal ribosome entry site (IRES) elements were described in picornaviruses as an essential region of the viral RNA. Understanding of IRES function requires a detailed knowledge of each step involved in the internal initiation process, from RNA folding and IRES–protein interaction to ribosome recruitment. Thus, deciphering IRES accessibility to external agents due to RNA structural features, as well as RNA–protein protection within living cells, is of primary importance. In this study, two chemical reagents, dimethylsulfate (DMS) and aminomethylpsoralen, have been used to footprint the entir
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10

Cheng, Yuan-Lung, Keng-Hsueh Lan, Wei-Ping Lee, et al. "Amiodarone inhibits the entry and assembly steps of hepatitis C virus life cycle." Clinical Science 125, no. 9 (2013): 439–48. http://dx.doi.org/10.1042/cs20120594.

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HCV (hepatitis C virus) infection affects an estimated 180 million people in the world's population. Adverse effects occur frequently with current standard treatment of interferon and ribavirin, while resistance of new direct anti-viral agents, NS3 protease inhibitors, is a major concern because of their single anti-HCV mechanism against the viral factor. New anti-viral agents are needed to resolve the problems. Amiodarone, an anti-arrhythmic drug, has recently been shown to inhibit HCV infection in vitro. The detailed mechanism has yet to be clarified. The aim of the present study was to eluc
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Dissertations / Theses on the topic "Ribosomal entry site and entero viral infection"

1

Chen, Li Lien, and 陳麗蓮. "Enterovirus 71 infection cleaves a negative regulator for viral internal ribosomal entry site-driven translation." Thesis, 2013. http://ndltd.ncl.edu.tw/handle/13880595882051288577.

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博士<br>長庚大學<br>生物醫學研究所<br>101<br>Far upstream element-binding protein 2 (FBP2) is an internal ribosomal entry site (IRES) trans-acting factor (ITAF) that negatively regulates enterovirus 71 (EV71) translation. This study shows that EV71 infection cleaved FBP2. Live EV71 and the EV71 replicon (not UV-inactivated virus particles) induced FBP2 cleavage, suggesting that viral replication results in FBP2 cleavage. The results also showed that virus-induced proteasome, autophagy, and caspase activity co-contribute to EV71-induced FBP2 cleavage. Using FLAG-fused FBP2, we mapped the potential cleavage
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Shwetha, S. "Host-Pathogen Interactions in Hepatitis C Virus Infection : Deciphering the Role of Host Proteins and MicroRNAs." Thesis, 2015. http://etd.iisc.ac.in/handle/2005/3858.

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Host-pathogen interactions in Hepatitis C Virus infection: Deciphering the role of host proteins and microRNAs Hepatitis C virus (HCV) is a positive sense single stranded RNA virus belonging to the Hepacivirus genus of the Flaviviridae family. HCV genome consists of a single open reading frame flanked by highly structured 5‟ and 3‟ untranslated regions (UTRs) at both ends. Unlike cellular mRNAs, HCV RNA translation is independent of the cap structure and is mediated by an internal ribosomal entry site (IRES) present in the 5‟UTR. HCV replication begins with the synthesis of a complementary ne
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3

Shwetha, S. "Host-Pathogen Interactions in Hepatitis C Virus Infection : Deciphering the Role of Host Proteins and MicroRNAs." Thesis, 2015. http://etd.iisc.ernet.in/2005/3858.

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Host-pathogen interactions in Hepatitis C Virus infection: Deciphering the role of host proteins and microRNAs Hepatitis C virus (HCV) is a positive sense single stranded RNA virus belonging to the Hepacivirus genus of the Flaviviridae family. HCV genome consists of a single open reading frame flanked by highly structured 5‟ and 3‟ untranslated regions (UTRs) at both ends. Unlike cellular mRNAs, HCV RNA translation is independent of the cap structure and is mediated by an internal ribosomal entry site (IRES) present in the 5‟UTR. HCV replication begins with the synthesis of a complementary ne
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