Littérature scientifique sur le sujet « RNase-L expression »
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Articles de revues sur le sujet "RNase-L expression"
Orlandi, Elisa, Elisa De Tomi, Rachele Campagnari, Francesca Belpinati, Monica Rodolfo, Elisabetta Vergani, Giovanni Malerba, Macarena Gomez-Lira, Marta Menegazzi et Maria Romanelli. « Human Melanoma Cells Differentially Express RNASEL/RNase-L and miR-146a-5p under Sex Hormonal Stimulation ». Current Issues in Molecular Biology 44, no 10 (11 octobre 2022) : 4790–802. http://dx.doi.org/10.3390/cimb44100326.
Texte intégralLi, Xiao-Ling, John A. Blackford et Bret A. Hassel. « RNase L Mediates the Antiviral Effect of Interferon through a Selective Reduction in Viral RNA during Encephalomyocarditis Virus Infection ». Journal of Virology 72, no 4 (1 avril 1998) : 2752–59. http://dx.doi.org/10.1128/jvi.72.4.2752-2759.1998.
Texte intégralBirdwell, L. Dillon, Zachary B. Zalinger, Yize Li, Patrick W. Wright, Ruth Elliott, Kristine M. Rose, Robert H. Silverman et Susan R. Weiss. « Activation of RNase L by Murine Coronavirus in Myeloid Cells Is Dependent on BasalOasGene Expression and Independent of Virus-Induced Interferon ». Journal of Virology 90, no 6 (6 janvier 2016) : 3160–72. http://dx.doi.org/10.1128/jvi.03036-15.
Texte intégralScherbik, Svetlana V., Jayashree M. Paranjape, Bronislava M. Stockman, Robert H. Silverman et Margo A. Brinton. « RNase L Plays a Role in the Antiviral Response to West Nile Virus ». Journal of Virology 80, no 6 (15 mars 2006) : 2987–99. http://dx.doi.org/10.1128/jvi.80.6.2987-2999.2006.
Texte intégralMaitra, Ratan K., et Robert H. Silverman. « Regulation of Human Immunodeficiency Virus Replication by 2′,5′-Oligoadenylate-Dependent RNase L ». Journal of Virology 72, no 2 (1 février 1998) : 1146–52. http://dx.doi.org/10.1128/jvi.72.2.1146-1152.1998.
Texte intégralRath, Sneha, Jesse Donovan, Gena Whitney, Alisha Chitrakar, Wei Wang et Alexei Korennykh. « Human RNase L tunes gene expression by selectively destabilizing the microRNA-regulated transcriptome ». Proceedings of the National Academy of Sciences 112, no 52 (14 décembre 2015) : 15916–21. http://dx.doi.org/10.1073/pnas.1513034112.
Texte intégralWei, Ruhan, Guanmin Chen, Naseh Algehainy, Chun Zeng, Chunfang Liu, Hongli Liu, Wendy Liu, Dennis Stacey et Aimin Zhou. « RNase L Is Involved in Liposaccharide-Induced Lung Inflammation ». Viruses 12, no 1 (7 janvier 2020) : 73. http://dx.doi.org/10.3390/v12010073.
Texte intégralLi, Yize, Shuvojit Banerjee, Yuyan Wang, Stephen A. Goldstein, Beihua Dong, Christina Gaughan, Robert H. Silverman et Susan R. Weiss. « Activation of RNase L is dependent on OAS3 expression during infection with diverse human viruses ». Proceedings of the National Academy of Sciences 113, no 8 (8 février 2016) : 2241–46. http://dx.doi.org/10.1073/pnas.1519657113.
Texte intégralZhang, Ao, Beihua Dong, Aurélien J. Doucet, John B. Moldovan, John V. Moran et Robert H. Silverman. « RNase L restricts the mobility of engineered retrotransposons in cultured human cells ». Nucleic Acids Research 42, no 6 (25 décembre 2013) : 3803–20. http://dx.doi.org/10.1093/nar/gkt1308.
Texte intégralMartinand, Camille, Céline Montavon, Tamim Salehzada, Michelle Silhol, Bernard Lebleu et Catherine Bisbal. « RNase L Inhibitor Is Induced during Human Immunodeficiency Virus Type 1 Infection and Down Regulates the 2-5A/RNase L Pathway in Human T Cells ». Journal of Virology 73, no 1 (1 janvier 1999) : 290–96. http://dx.doi.org/10.1128/jvi.73.1.290-296.1999.
Texte intégralThèses sur le sujet "RNase-L expression"
Souza, Edmárcia Elisa de [UNESP]. « Clonagem, expressão e purificação de domínios da proteína AtRLI2 (RNase L Inhibitor), um supressor endógeno de silenciamento por RNA de Arabidopis thaliana, visando estudos estruturais ». Universidade Estadual Paulista (UNESP), 2010. http://hdl.handle.net/11449/92439.
Texte intégralCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
A RNase L inhibitor (RLI) é uma proteína altamente conservada em Eukatyota e Archaea e foi primeiramente identificada em humanos, onde se mostrou reguladora da via 2'-5' - oligoadenilato sintetase/ribonuclease L (OAS/RNase L), principal via induzida por interferon. Novas funções têm sido descritas para RLI em diferentes organismos, dentre elas o controle do silenciamento por RNA e resistência a vírus. Visando futuros estudos estruturais foi possível subclonar a sequência que codifica para o domínio NBDs (Nucleotide Binding Domain) de AtRLI2 de Arabidopsis thaliana em vetor de expressão pET-28a(+) capaz de expressar a proteína NBDs ligada a um His6 tag. A proteína NBDs foi expressa e purificada por cromatografia de afinidade por níquel em condição nativa utilizando detergente N-lauril-sarcosil, com um rendimento da ordem de 8 mg/L e em condição desnaturante utilizando uréia, com um rendimento da ordem de 10 mg/L. Para renaturação da proteína utilizou-se dATP e cloreto de magnésio com posterior diálise obtendo-se uma diminuição significativa dos corpúsculos de inclusão e o aumento da solubilidade da proteína produzida em condição desnaturante. Para confirmar a presença dos resíduos His6 tag em fusão com a proteína NBDs, testes de Western blot foram realizados utilizando extrato total das células induzi das, a proteína purificada e a proteína originada da diálise. Foi possível concluir que houve o reconhecimento do anticorpo monoclonal anti-HiS6 tag à proteína confirmando o sucesso da obtenção e purificação da proteína fusionada à uma sequência de 6 histidinas. Etapas posteriores de purificação, a partir da proteína NBDs obtida, necessitam ser realizadas a fim de obter a proteína com grau de pureza significativo e em quantidades suficientes para a realização dos ensaios biofisicos e cristalográficos
The RNase L inhibitor (RLI) is a protein highly conserved in Eukaryota and Archaea and it was first identified in humans acting as a regulator of Oligoadenylate SynthetaselRNase L system (OASlRNase L), the main pathway induced by interferon. New functions have been described for RLI in different organisms, among them the control of RNA silencing and virus resistance. In order to further structural studies could subcIoned the coding sequence for the domain NBDs (nucIeotide-binding domain) AtRLI2 of Arabidopsis thaliana in expression vector pET-28a (+) capable of expressing the protein NBDs linked to a His6 tag. NBDs protein was expressed and purified by affinity chromatography on nickel in native condition using detergent Nlaurylsarcosine with a yield of about 8 mgIL and denaturing conditions using urea with a yield of about 10 mgIL. For renaturation of the protein was used dATP and magnesium chloride with subsequent dialysis resulting in a significant reduction in inclusion bodies and increasing the solubility of the protein produced in denaturant condition. To confirm the presence of residues HiS(; tag fusion protein with the NBDs, Western hlot tests were conducted using total extract of induced cells, the purified protein and protein originated from dialysis. It was concIuded that there was recognition of the monocIonal anti-His6 tag protein confirming the success of obtaining and purification of protein fused to a sequence of 6 histidines. Later stages of purification from the protein obtained NBDs are being conducted to obtain the pure protein 10 sufficient quantities for the testing biophysical and crystallographic
Souza, Edmárcia Elisa de. « Clonagem, expressão e purificação de domínios da proteína AtRLI2 (RNase L Inhibitor), um supressor endógeno de silenciamento por RNA de Arabidopis thaliana, visando estudos estruturais / ». Botucatu : [s.n.], 2010. http://hdl.handle.net/11449/92439.
Texte intégralAbstract: The RNase L inhibitor (RLI) is a protein highly conserved in Eukaryota and Archaea and it was first identified in humans acting as a regulator of Oligoadenylate SynthetaselRNase L system (OASlRNase L), the main pathway induced by interferon. New functions have been described for RLI in different organisms, among them the control of RNA silencing and virus resistance. In order to further structural studies could subcIoned the coding sequence for the domain NBDs (nucIeotide-binding domain) AtRLI2 of Arabidopsis thaliana in expression vector pET-28a (+) capable of expressing the protein NBDs linked to a His6 tag. NBDs protein was expressed and purified by affinity chromatography on nickel in native condition using detergent Nlaurylsarcosine with a yield of about 8 mgIL and denaturing conditions using urea with a yield of about 10 mgIL. For renaturation of the protein was used dATP and magnesium chloride with subsequent dialysis resulting in a significant reduction in inclusion bodies and increasing the solubility of the protein produced in denaturant condition. To confirm the presence of residues HiS(; tag fusion protein with the NBDs, Western hlot tests were conducted using total extract of induced cells, the purified protein and protein originated from dialysis. It was concIuded that there was recognition of the monocIonal anti-His6 tag protein confirming the success of obtaining and purification of protein fused to a sequence of 6 histidines. Later stages of purification from the protein obtained NBDs are being conducted to obtain the pure protein 10 sufficient quantities for the testing biophysical and crystallographic
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Castillo-Pérez, Karina. « Étude de l'expression différentielle du génome en relation avec la détermination du sexe chez le palmier dattier (Phoenix dactylifera L.) ». Thesis, Montpellier, 2015. http://www.theses.fr/2015MONTS054.
Texte intégralUnraveling molecular mechanisms involved in sex determination in flowering plants is of outstanding basic and applied interest. Several studies on dioecious species have highlighted the molecular basis of sex determination, such as cell death and ethylene biosynthesis pathway. Sex determination mechanisms in plants are, however, still largely unknown. The date palm, Phoenix dactylifera L, is a dioecious species where sexual dimorphism is observed very early in development of flowers. Differentially expressed genes (DEGs) were identified during the early stages of the male and female flower development. A reference transcriptome including male and female data was constructed to gain insight into this process in the dioecious palm Phoenix dactylifera L. Differentially expressed genes (DEG) were subsequently identified between males and females in the early flower development stages in which the first morphological gender difference occurs in date palms.Gene ontology enrichment analysis of DEG revealed biological processes shared between males and females involved in reproductive development and response to stimulus, indicating that same processes could require different genes during early flower development in date palm. This analysis also suggested that date palm triggers biological processes specifically involved in cellular regulation and gene expression to develop male flowers. Furthermore, two female DEGs related to DNA methylation S-adenosylmethionine synthase and DNA metabolism Flap endonuclease, and one male DEGs, a transposable element were found in non-recombinant date palm regions. This study provided the first insight into biological processes involved in sex determination in date palms and more widely to knowledge of this process in dioecious species