Literatura científica selecionada sobre o tema "Polymérase de la grippe"
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Artigos de revistas sobre o assunto "Polymérase de la grippe"
Zhang, Kevin, Avika Misra, Patrick J. Kim, Seyed M. Moghadas, Joanne M. Langley e Marek Smieja. "Disparition rapide de la grippe après la mise en œuvre de mesures d'atténuation de la COVID-19 à Hamilton, Ontario". Relevé des maladies transmissibles au Canada 47, n.º 04 (7 de maio de 2021): 221–27. http://dx.doi.org/10.14745/ccdr.v47i04a04f.
Texto completo da fonteCorteggiani, Marie, Lucas Gombert, Callypso Pellegri e Laurent Aussel. "L’ARN polymérase COVID-19". médecine/sciences 37, n.º 3 (março de 2021): 288–92. http://dx.doi.org/10.1051/medsci/2021019.
Texto completo da fonteGautier, A., C. Jestin e M. Jauffret-Roustide. "Grippe saisonnière, grippe aviaire, grippe pandémique : connaissances et attitudes". Médecine et Maladies Infectieuses 38 (junho de 2008): S71—S73. http://dx.doi.org/10.1016/s0399-077x(08)72997-4.
Texto completo da fonteLangelier, Marie-France, Vincent Trinh e Benoit Coulombe. "Gros plan sur l’ARN polymérase II". médecine/sciences 18, n.º 2 (fevereiro de 2002): 210–16. http://dx.doi.org/10.1051/medsci/2002182210.
Texto completo da fonteBouvresse, S., F. Bricaire e P. Bossi. "Grippe". EMC - Traité de médecine AKOS 2, n.º 1 (janeiro de 2007): 1–8. http://dx.doi.org/10.1016/s1634-6939(07)45399-6.
Texto completo da fonteManuguerra, Jean-Claude. "Grippe". EMC - Maladies infectieuses 1, n.º 1 (janeiro de 2004): 1–22. http://dx.doi.org/10.1016/s1166-8598(01)00070-9.
Texto completo da fonteLaunay, O., e B. Lina. "Grippe". Revue des Maladies Respiratoires Actualités 12 (novembro de 2020): A3—A5. http://dx.doi.org/10.1016/j.rmra.2020.08.001.
Texto completo da fonteHoffmann, Jean-Sébastien. "Ciblage de l’ADN-polymérase θ en oncologie". Bulletin du Cancer 108, n.º 3 (março de 2021): 238–41. http://dx.doi.org/10.1016/j.bulcan.2020.10.021.
Texto completo da fonteVassias, I. "Principe de l’amplification en chaîne par polymérase". EMC - Biologie médicale 7, n.º 1 (março de 2012): 1–5. http://dx.doi.org/10.1016/s2211-9698(12)56773-7.
Texto completo da fonteBessis, S., e M. Matt. "La grippe". Médecine et Maladies Infectieuses 49 (2019): S17—S24. http://dx.doi.org/10.1016/s0399-077x(19)30803-0.
Texto completo da fonteTeses / dissertações sobre o assunto "Polymérase de la grippe"
Monod, Alexandre. "Etude structurale et fonctionnelle de l'ARN-polymérase du virus de la grippe". Thesis, Grenoble, 2014. http://www.theses.fr/2014GRENV045/document.
Texto completo da fonteInfluenza A virus is a negative single stranded RNA virus that replicates in the nucleus of infected cells. Its genome contains eight single stranded negative-sense RNA segments (vRNA) covered by the viral nucleoprotein (NP). The highly conserved 3' and 5' ends of the vRNA are bound to the RNA-dependent RNA-polymerase (RdRp) which consists of three subunits, PA, PB1 and PB2. The complex between vRNA, NP and the RdRp forms a particle called ribonucleoprotein (RNP). The RNP acts as an independent molecular machine for transcription and replication in the nucleus. Within the context of the RNP, these two processes are mediated by the RdRp. The influenza A RdRp complex has been remarkably intractable to structural analysis and in the last eight years, crystal structures of independent domains covering roughly half of the heterotrimeric RdRp have been determined. In addition, electron microscopy reconstructions have described the RdRp. Nonetheless, a complete model characterizing the RdRp as a whole is still lacking. To overcome this issue, a new strategy has been developed to obtain the RdRp heterotrimeric complex using the baculovirus infected cells expression system. This method has produced a truncated form of the flu A RdRp which has been studied from a structural and functional point of view. Several three-dimensional reconstructions by electron microscopy have been obtained and a crystal structure at low resolution (7,7 Å) has been solved. Functional studies focused on the activities carried by the truncated RdRp and a particular emphasis was placed on the study of the interactions with RNA. In vitro functional data showed highly metal ion-dependent activities. To know more about the subcellular metal context, metallic ions distribution in influenza A infected cells has been studied by X-ray microscopy giving the opportunity to integrate biochemical and biophysical data in the context of the whole cell
Lukarska, Mariya. "Caractérisation structurale et fonctionnelle de l'intéraction entre la polymérase d'influenza et la machinerie cellulaire de transcription". Thesis, Université Grenoble Alpes (ComUE), 2018. http://www.theses.fr/2018GREAV031.
Texto completo da fonteInfluenza is an infectious disease causing seasonal epidemics and occasional pandemics, which are a significant health burden for the global human population. The causative agent, influenza virus, is a negative-strand segmented RNA virus. Each segment of the viral genome is transcribed and replicated by a virally-encoded RNA-dependent RNA polymerase in the nucleus of the infected cell. In order to produce a functional viral messenger RNA (mRNA) that can be processed by the cellular translation machinery, influenza polymerase employs a mechanism called‘cap-snatching’. The viral polymerase binds to a nascent, capped transcript, produced by the cellular RNA polymerase II, cleaves it shortly after the cap and uses it as a primer for the transcription of its own genomic segments. Viral transcription is therefore functionally dependent on cellular transcription. The studies described in this thesis aimed to investigate the interaction between influenza polymerase and the cellular transcription machinery. The main focus was to characterize structurally and functionally the association of influenza polymerase with the C-terminal domain (CTD) of RNA polymerase II, which serves as a scaffold for coordinating co-transcriptional events during mRNA synthesis and processing. Crystal structures of influenza A and B polymerase bound to phosphorylated peptides mimicking the CTD of RNA polymerase II gave new insight on how the viral polymerase directly recognizes the transcribing cellular polymerase. Moreover, disrupting this interaction was found to be severely detrimental to viral replication, confirming the essentiality of this association. In the second part of this work, an active cap-snatching complex was assembled in vitro and characterized functionally. This comprised a reconstituted RNA polymerase II elongation complex with emerging capped transcript and phosphorylated CTD with bound and transcriptionally active influenza polymerase. Additionally, the interaction of the viral polymerase with two factors involved in the regulation of transcription elongation by RNA polymerase II, DRB sensitivity-inducing factor and Tat stimulatory factor 1, was analyzed biochemically. Overall, the work presented here gives insights into the mechanism of recruitment of the influenza polymerase to the cellular transcription machinery and shows that the association of the viral and cellular polymerase is essential for the viral replication. Targeted disruption of this interaction is therefore a promising avenue for the design of novel anti-influenza drugs
Swale, Christopher. "RNA binding and assembly of human influenza A virus polymerases". Thesis, Université Grenoble Alpes (ComUE), 2015. http://www.theses.fr/2015GREAV053/document.
Texto completo da fonteInfluenza A virus is a negative-strand RNA virus belonging to the Orthomyxoviriadea family whose replication occurs in the nucleus of infected cells. The genome organisation of influenza virus is segmented in eight vRNA segments of negative polarity coding for at least 16 different viral proteins. Each vRNA is bound to multiple copies of nucleoprotein (NP) and to the heterotrimeric RNA-dependent RNA-polymerase complex (PA, PB1 and PB2) through its 5' and 3' extremities. This macromolecular assembly (vRNA/polymerase/NP) forms the ribonucleoprotein (RNP) particle, which acts as a separate genomic entity within the virion. The RNP complex is at the core of viral replication and in the context of RNPs, the polymerase performs both transcription and replication of the vRNA genome. As such, the polymerase constitutes a major antiviral drug target. The research work presented within this thesis focuses on the underlying determinants of the RNA polymerase assembly process and its interaction with its vRNA genome. To fulfill these goals, our lab, in collaboration with other groups, has set up a novel polyprotein expression system to express the polymerase but also to reconstitute polymerase and cellular partner complexes, notably RanBP5, which belongs to the importin-β family
Boulo, Sébastien. "Etudes structurales et fonctionnelles de la nucléoprotéine et de la polymérase du virus de la grippe en association avec leur transporteur nucléaire humain". Phd thesis, Université Claude Bernard - Lyon I, 2008. http://tel.archives-ouvertes.fr/tel-00356602.
Texto completo da fonteBoulo, Sébastien. "Études structurales et fonctionnelles de la nucléoprotéine et de la polymérase du virus de la grippe en association avec leur transporteur nucléaire humain". Lyon 1, 2008. http://tel.archives-ouvertes.fr/docs/00/35/66/02/PDF/These_Sebastien_BOULO.pdf.
Texto completo da fonteThe virus of influenza is a negative-sense RNA virus belonging to the family of Orthomyxoviridae and represents one of the rare RNA viruses to replicate in the nucleus. The ribonucleoprotein particles (RNP) contain the viral RNA, protected by the nucleoproteins (NP) and associated with the RNA viral polymerase (subunits PB1, PB2 and PA). Using biochemical and biophysical tools, we have studied the interaction of the nucleoprotein not only with the viral RNA but also with its human nuclear transporter importin alpha 5. Besides, we have solved the crystallographic structure of a domain of the polymerase (PB2) in complex with importin alpha 5. Our results enable us to better understand the interactions between viral proteins and host proteins and thus, to understand why some amino-acids in the avian influenza virus increase the virulence of the virus in humans
Andrieux, Florian. "Rôle de la protéine PB1 dans la fidélité du complexe polymérase des virus influenza". Thesis, Sorbonne Paris Cité, 2017. http://www.theses.fr/2017USPCC216/document.
Texto completo da fonteInfluenza type A viruses (IAVs) belong to the Orthomyxoviridae family. The genome of these enveloped viruses consists of 8 single-stranded RNA segments of negative polarity. Each segment is encapsidated by oligomers of the nucleoprotein (NP) and associated with the viral polymerase complex, a heterotrimer composed of the PB1, PB2 and PA subunits to form the viral ribonucleoproteins (vRNPs). The PB1 protein is the catalytic subunit of the polymerase complex, harboring the RNA-dependent RNA polymerase activity. The vRNP represents the minimal functional unit for transcription and replication of the viral genome. Given the low fidelity and lack of proofreading activity of their polymerase, IAVs have a high mutation rate leading to the rapid development of viral populations with high genetic diversity, called quasispecies. Recent studies identified mutants with increased replication fidelity, due to single mutations in the PB1 subunit. As described with other RNA viruses, different mutations could have similar effects on the activity of the viral polymerase. To improve the characterization of the PB1 protein, we searched for other positions that may have a role on polymerase fidelity, nucleotide selectivity or complex processivity. For this purpose, random mutagenesis was used to generate libraries of mutated PB1 from influenza A virus subtypes H3N2 and H1N1pdm09, currently circulating in humans. From these libraries, transient reconstitution of functional vRNPs (minigenome) experiments were performed with ribavirin, a mutagenic nucleoside analog, to evaluate the polymerase activity. Upon selection based on the polymerase activity of successively subdivided libraries, PB1 mutations with increased polymerase activity in the presence of ribavirin relative to wild-type were identified in several regions of PB1. These mutations were specifically re-introduced in PB1 by directed mutagenesis. Their impact on polymerase activity was evaluated by minigenome experiments with and without ribavirin. Mutations with confirmed resistance against ribavirin were then introduced in the context of infectious virus by reverse genetics. Most corresponding mutant viruses could be rescued. Their growth characteristics were analysed in MDCK cells and compared to the corresponding wild-type viruses, in the presence or absence of ribavirin. Two mutants carrying two different mutations, located in distinct regions of the PB1 protein, displayed an improved capacity to resist ribavirin relative to the wild-type virus. Viral populations genetic diversity analysis by next-generation sequencing, using Illumina technology, will confirm whether the observed resistance against ribavirin is linked to an increase of the viral polymerase fidelity. This study provides insights into the PB1 domains involved in the activity and potentially the viral replication fidelity of two influenza A virus subtypes
Dias, Alexandre. "Études structurales et fonctionnelles de la sous-unité PA du complexe polymérasique du virus influenza". Grenoble 1, 2009. http://www.theses.fr/2009GRE10292.
Texto completo da fonteThe influenza virus polymerase is a heterotrimeric complex composed of PA, PB1 and PB2 subunits. This complex is dedicated to replication and transcription of the viral genome, inside the nuclear compartment. Despite much research performed on the polymerase, the only structural data available on this complex are reconstructions made by electronic microscopy. Recently, our laboratory has initiated a structural and functional project on this complex, which led to the structure determination of several PB2 domains. My thesis work led to the structure determination of another domain from the PA subunit: the N-terminal domain encompassing the 209 first residues. We have shown that this domain shares structural similarities with type Il restriction enzymes and that it possesses nuclease activity (DNase and RNase). Indeed, this domain belongs to the PD-D/EXK enzyme family. This work, together with structural data collected on PB2, gives a better view of the cap-snatching mechanism, which is specifie of the influenza virus. Eventually, the availability of the structure of the enzymatically active PA-Nter domain should aid the design of a specifie inhibitor of the influenza virus endonuclease
Richard, Marie-Claude. "L'ADN polymérase B d'embryon de blé : une DNA polymérase delta végétale". Bordeaux 2, 1988. http://www.theses.fr/1988BOR22028.
Texto completo da fonteSoerensen, Claudiana. "O Mez da Grippe". reponame:Repositório Institucional da UFPR, 2009. http://hdl.handle.net/1884/19927.
Texto completo da fonteRéminiac, Erwann Le Borgne Marc. "Aviculture et grippe aviaire". [S.l.] : [s.n.], 2008. http://castore.univ-nantes.fr/castore/GetOAIRef?idDoc=41511.
Texto completo da fonteLivros sobre o assunto "Polymérase de la grippe"
Rhume et grippe. Saint-Constant, QC: Broquet, 2007.
Encontre o texto completo da fonte1971-, Dalnoky Cécile, ed. Un cauchemar de grippe. [Paris]: Père Castor Flammarion, 1997.
Encontre o texto completo da fontePrévenir et guérir la grippe. Vergèze: T. Souccar, 2009.
Encontre o texto completo da fonteBiéville, Clémence de. L' amour en grippe: Roman. Paris: Grasset, 1999.
Encontre o texto completo da fonteXavier, Valêncio. O mez da grippe e outros livros. [São Paulo, Brazil]: Companhia das Letras, 1998.
Encontre o texto completo da fonteMuseum, Rose Art, ed. Peter Grippe: The Rose Art Museum, Brandeis University. Waltham, Mass: The Rose Art Museum, Brandeis University, 2006.
Encontre o texto completo da fonteL'anti-grippe aviaire: Se préparer, y faire face. Paris: Médicis, 2005.
Encontre o texto completo da fonteComment survivre à la grippe en 10 leçons. Paris: JC Gawsewitch, 2009.
Encontre o texto completo da fonteWorld Health Organization. Global Influenza Programme. Préparation et action en cas de grippe pandémique. Genève: Organisation mondiale de la santé, 2009.
Encontre o texto completo da fonteSOLBEN, Groupe. Agir face aux crises: Katrina, grippe aviaire, tsunami--. Paris: Plon, 2006.
Encontre o texto completo da fonteCapítulos de livros sobre o assunto "Polymérase de la grippe"
Bréchot, N., C. E. Luyt, J. L. Trouillet, J. Chastre e A. Combes. "Grippe sévère". In Références en réanimation. Collection de la SRLF, 185–201. Paris: Springer Paris, 2013. http://dx.doi.org/10.1007/978-2-8178-0389-0_12.
Texto completo da fonteRenneberg, Reinhard, Viola Berkling e Iris Rapoport. "Fettsenker gegen Grippe". In Alles Bio oder was?, 37–39. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-50278-5_10.
Texto completo da fonteEngst, Ulli. "Historische Pandemien in populären digitalen Spielen. Die Spanische Grippe in Vampyr". In Medical Humanities, 459–68. Bielefeld, Germany: transcript Verlag, 2024. http://dx.doi.org/10.14361/9783839471975-031.
Texto completo da fonteNeumann, G., H. H. Feucht, W. Becker e M. Späth. "Influenza A H1 N1 (Neue Grippe)". In Gynäkologische Infektionen, 135–37. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-05268-2_37.
Texto completo da fonteSchulz, Eva-Cathrin. "Wie verläuft die echte Grippe? Prophylaxe?" In Mikrobiologie für die mündliche Prüfung, 89. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-80349-9_89.
Texto completo da fonteHellwig, Marcus. "Der Unterschied Influenza-Grippe- / COVID-Welle". In Partikelemissionskonzept und probabilistische Betrachtung der Entwicklung von Infektionen in Systemen, 25–28. Wiesbaden: Springer Fachmedien Wiesbaden, 2021. http://dx.doi.org/10.1007/978-3-658-33157-3_5.
Texto completo da fonteRindlisbacher, Stefan. "Rohkost und heiße Bäder gegen die »Spanische Grippe«?" In Wissenskrisen - Krisenwissen, 229–46. Bielefeld, Germany: transcript Verlag, 2023. http://dx.doi.org/10.14361/9783839461600-012.
Texto completo da fontePerbandt, Markus. "Das Grippe‐Virus: Wie ein unsichtbarer Feind sichtbar wird". In Neue und alte Infektionskrankheiten, 161–73. Wiesbaden: Springer Fachmedien Wiesbaden, 2013. http://dx.doi.org/10.1007/978-3-658-04124-3_7.
Texto completo da fonteRaffeiner, Andreas, e Felicita Ratti. "Medizin, Spanische Grippe, Mangelerkrankungen und Verwundete in Salzburg und Umgebung 1918". In Salzburg 1918-1919, 359–70. Wien: Böhlau Verlag, 2018. http://dx.doi.org/10.7767/9783205200765.359.
Texto completo da fonteCzech, Herwig. "Die Spanische Grippe von 1918. Blick auf eine lange vergessene Pandemie". In Corona und die Welt von gestern, 23–46. Wien: Böhlau Verlag, 2021. http://dx.doi.org/10.7767/9783205212607.23.
Texto completo da fonteTrabalhos de conferências sobre o assunto "Polymérase de la grippe"
Horstkötter, N., A. L. Caille-Brillet, L. Seefeld, A. Rose e C. Peter. "Der Grippe zuvorkommen: Impfkommunikation am Beispiel Influenza". In Der Öffentliche Gesundheitsdienst – Rückenwind für Gesundheit! 73. Wissenschaftlicher Kongress | BVÖGD e.V., BZÖG e.V., DGÖG e.V. Georg Thieme Verlag, 2024. http://dx.doi.org/10.1055/s-0044-1781963.
Texto completo da fonteStojanovski, Zoran, Goran Andonovski, Miralem Jukic e Olgica Kuzarevska-Blazevska. "Comparison of efficacy of grippe vaccination and broncho vaxom administration in COPD patients". In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa3670.
Texto completo da fonteRelatórios de organizações sobre o assunto "Polymérase de la grippe"
Prot�ger les employ�s du secteur de la volaille de la grippe aviaire r�sum� des recommendations aux employ�s en Fran�ais. U.S. Department of Health and Human Services, Public Health Service, Centers for Disease Control and Prevention, National Institute for Occupational Safety and Health, fevereiro de 2008. http://dx.doi.org/10.26616/nioshpub2008128fre.
Texto completo da fonte