Cargando…

Effective suppression of Dengue virus using a novel group-I intron that induces apoptotic cell death upon infection through conditional expression of the Bax C-terminal domain

INTRODUCTION: Approximately 100 million confirmed infections and 20,000 deaths are caused by Dengue virus (DENV) outbreaks annually. Global warming and rapid dispersal have resulted in DENV epidemics in formally non-endemic regions. Currently no consistently effective preventive measures for DENV ex...

Descripción completa

Detalles Bibliográficos
Autores principales:	Carter, James R, Keith, James H, Fraser, Tresa S, Dawson, James L, Kucharski, Cheryl A, Horne, Kate M, Higgs, Stephen, Fraser, Malcolm J
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	BioMed Central 2014
Materias:	Research
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4104402/ https://www.ncbi.nlm.nih.gov/pubmed/24927852 http://dx.doi.org/10.1186/1743-422X-11-111

Ejemplares similares

Suppression of the Arboviruses Dengue and Chikungunya Using a Dual-Acting Group-I Intron Coupled with Conditional Expression of the Bax C-Terminal Domain
por: Carter, James R., et al.
Publicado: (2015)

Targeting of highly conserved Dengue virus sequences with anti-Dengue virus trans-splicing group I introns
por: Carter, James R, et al.
Publicado: (2010)

A novel dengue virus detection method that couples DNAzyme and gold nanoparticle approaches
por: Carter, James R, et al.
Publicado: (2013)

Analysis of the piggyBac transposase reveals a functional nuclear targeting signal in the 94 c-terminal residues
por: Keith, James H, et al.
Publicado: (2008)

Effective suppression of Dengue fever virus in mosquito cell cultures using retroviral transduction of hammerhead ribozymes targeting the viral genome
por: Nawtaisong, Pruksa, et al.
Publicado: (2009)

Mutational analysis of highly conserved aspartate residues essential to the catalytic core of the piggyBac transposase
por: Keith, James H, et al.
Publicado: (2008)

Allosteric Sensitization of Pro-Apoptotic BAX
por: Pritz, Jonathan R., et al.
Publicado: (2017)

Bax Exists in a Dynamic Equilibrium between the Cytosol and Mitochondria to Control Apoptotic Priming
por: Schellenberg, Barbara, et al.
Publicado: (2013)

Membrane insertion of the BAX core, but not latch domain, drives apoptotic pore formation
por: Flores-Romero, Hector, et al.
Publicado: (2017)

Bioactive lipids and the control of Bax pro-apoptotic activity
por: Mignard, V, et al.
Publicado: (2014)

Conformational control of Bax localization and apoptotic activity by Pro168
por: Schinzel, Anna, et al.
Publicado: (2004)

BAX pro-apoptotic gene alterations in repeated pregnancy loss
por: Mohammad Seyedhassani, Seyed, et al.
Publicado: (2011)

Conformational changes and protein stability of the pro-apoptotic protein Bax
por: Bleicken, Stephanie, et al.
Publicado: (2009)

BAX and SMAC regulate bistable properties of the apoptotic caspase system
por: McKenna, Stephanie, et al.
Publicado: (2021)

Expression of Apoptotic Markers Bcl-2 and Bax in the Vascular Wall
por: Klimentova, E.A., et al.
Publicado: (2021)

An amphipathic Bax core dimer forms part of the apoptotic pore wall in the mitochondrial␣membrane
por: Lv, Fujiao, et al.
Publicado: (2021)

Radiotherapy-Induced Neurocognitive Impairment Is Driven by Heightened Apoptotic Priming in Early Life and Prevented by Blocking BAX
por: Singh, Rumani, et al.
Publicado: (2023)

The carboxyl-terminal sequence of bim enables bax activation and killing of unprimed cells
por: Chi, Xiaoke, et al.
Publicado: (2020)

Inhibition of apoptotic Bax translocation to the mitochondria is a central function of parkin
por: Charan, R A, et al.
Publicado: (2014)

Pro-apoptotic Bax molecules densely populate the edges of membrane pores
por: Kuwana, Tomomi, et al.
Publicado: (2016)

Conformational Heterogeneity of Bax Helix 9 Dimer for Apoptotic Pore Formation
por: Liao, Chenyi, et al.
Publicado: (2016)

Effect of L-carnitine on the expression of the apoptotic genes Bcl-2 and Bax
por: Vardiyan, Reyhane, et al.
Publicado: (2020)

Mitochondrial Ceramide-Rich Macrodomains Functionalize Bax upon Irradiation
por: Lee, Hyunmi, et al.
Publicado: (2011)

Molecular Changes in Dengue Envelope Protein Domain III upon Interaction with Glycosaminoglycans
por: Hyatt, James G., et al.
Publicado: (2020)

Antagonistic factors control the unproductive splicing of SC35 terminal intron
por: Dreumont, Natacha, et al.
Publicado: (2010)

The apoptotic response in HCT116(BAX-/- )cancer cells becomes rapidly saturated with increasing expression of a GFP-BAX fusion protein
por: Semaan, Sheila J, et al.
Publicado: (2010)

The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
por: Bloch, Noah B., et al.
Publicado: (2021)

Correction: Mitochondrial Ceramide-Rich Macrodomains Functionalize Bax upon Irradiation
por: Lee, Hyunmi, et al.
Publicado: (2015)

The Rubella Virus Capsid Is an Anti-Apoptotic Protein that Attenuates the Pore-Forming Ability of Bax
por: Ilkow, Carolina S., et al.
Publicado: (2011)

NDV-induced apoptosis in absence of Bax; evidence of involvement of apoptotic proteins upstream of mitochondria
por: Molouki, Aidin, et al.
Publicado: (2012)

Apoptotic stress induces Bax-dependent, caspase-independent redistribution of LINC complex nesprins
por: Lindenboim, Liora, et al.
Publicado: (2020)

Chlamydia trachomatis inhibits apoptosis in infected cells by targeting the pro-apoptotic proteins Bax and Bak
por: Waguia Kontchou, Collins, et al.
Publicado: (2022)

Reconstitution of the Anti-Apoptotic Bcl-2 Protein into Lipid Membranes and Biophysical Evidence for Its Detergent-Driven Association with the Pro-Apoptotic Bax Protein
por: Wallgren, Marcus, et al.
Publicado: (2013)

The C-terminal domain (CTD) in linker histones antagonizes anti-apoptotic proteins to modulate apoptotic outcomes at the mitochondrion
por: Garg, M, et al.
Publicado: (2014)

Integrin-Mediated Survival Signals Regulate the Apoptotic Function of Bax through Its Conformation and Subcellular Localization
por: Gilmore, Andrew P., et al.
Publicado: (2000)

Pro-apoptotic Bax is the major and Bak an auxiliary effector in cytokine deprivation-induced mast cell apoptosis
por: Karlberg, M, et al.
Publicado: (2010)

Ablation of the Pro-Apoptotic Protein Bax Protects Mice from Glucocorticoid-Induced Bone Growth Impairment
por: Zaman, Farasat, et al.
Publicado: (2012)

Wip1 suppresses apoptotic cell death through direct dephosphorylation of BAX in response to γ-radiation
por: Song, J-Y, et al.
Publicado: (2013)

The Effect of Cadmium on Apoptotic Genes mRNA Expression of Bax and Bcl-2 in Small Intestine of Rats
por: Seid Alian, Narjes, et al.
Publicado: (2018)

Two roads to death – Bax targets mitochondria by distinct routes before or during apoptotic cell death
por: Dewson, Grant
Publicado: (2015)

Cannot write session to /tmp/vufind_sessions/sess_n3k0shoa9c1rst0k067eli69fi