Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Zsuzsanna Sasvari"'
Publikováno v:
PLoS Pathogens, Vol 14, Iss 5, p e1007028 (2018)
Positive-strand RNA viruses assemble numerous membrane-bound viral replicase complexes within large replication compartments to support their replication in infected cells. Yet the detailed mechanism of how given subcellular compartments are subverte
Externí odkaz:
https://doaj.org/article/dfd4196b2a0f49a8bc966384ec2a74a8
Autor:
Miaoying Tian, Zsuzsanna Sasvari, Paulina Alatriste Gonzalez, Giulia Friso, Elden Rowland, Xiao-Min Liu, Klaas J. van Wijk, Peter D. Nagy, Daniel F. Klessig
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 28, Iss 4, Pp 379-386 (2015)
Although the plant hormone salicylic acid (SA) plays a central role in signaling resistance to viral infection, the underlying mechanisms are only partially understood. Identification and characterization of SA’s direct targets have been shown to b
Externí odkaz:
https://doaj.org/article/a9fcb59f2fa04d159b791a081f6f2c87
Autor:
Muhammad Shah Nawaz-ul-Rehman, K Reddisiva Prasanth, Kai Xu, Zsuzsanna Sasvari, Nikolay Kovalev, Isabel Fernández de Castro Martín, Daniel Barajas, Cristina Risco, Peter D Nagy
Publikováno v:
PLoS Pathogens, Vol 12, Iss 2, p e1005440 (2016)
RNA viruses exploit host cells by co-opting host factors and lipids and escaping host antiviral responses. Previous genome-wide screens with Tomato bushy stunt virus (TBSV) in the model host yeast have identified 18 cellular genes that are part of th
Externí odkaz:
https://doaj.org/article/83cca94d80094031a410b7a5d28e8155
Autor:
Zsuzsanna Sasvari, Peter D. Nagy
Publikováno v:
Viruses, Vol 2, Iss 11, Pp 2436-2442 (2010)
Positive-stranded RNA (+RNA) viruses exploit host cell machinery by subverting host proteins and membranes and altering cellular pathways during infection. To achieve robust replication, some +RNA viruses, such as poliovirus (PV), build special intra
Externí odkaz:
https://doaj.org/article/bb00f682b967417b91442eef89591a0b
Autor:
Daniel Barajas, Kai Xu, Isabel Fernández de Castro Martín, Zsuzsanna Sasvari, Federica Brandizzi, Cristina Risco, Peter D Nagy
Publikováno v:
PLoS Pathogens, Vol 10, Iss 10, p e1004388 (2014)
Viruses recruit cellular membranes and subvert cellular proteins involved in lipid biosynthesis to build viral replicase complexes and replication organelles. Among the lipids, sterols are important components of membranes, affecting the shape and cu
Externí odkaz:
https://doaj.org/article/a26601ff79ed4100ba2eb901d6c561ec
Publikováno v:
PLoS Pathogens, Vol 7, Iss 12, p e1002438 (2011)
Host factors are recruited into viral replicase complexes to aid replication of plus-strand RNA viruses. In this paper, we show that deletion of eukaryotic translation elongation factor 1Bgamma (eEF1Bγ) reduces Tomato bushy stunt virus (TBSV) replic
Externí odkaz:
https://doaj.org/article/a5c6ce80110546439bd4d9c1ab35e89e
Publikováno v:
PLoS ONE, Vol 4, Iss 10, p e7376 (2009)
BACKGROUND: Small molecule inhibitors of RNA virus replication are potent antiviral drugs and useful to dissect selected steps in the replication process. To identify antiviral compounds against Tomato bushy stunt virus (TBSV), a model positive stran
Externí odkaz:
https://doaj.org/article/8ecfbefeb46a4e49b0ecb944d9367d53
Publikováno v:
J Virol
Positive-strand RNA [(+)RNA] viruses assemble numerous membrane-bound viral replicase complexes (VRCs) with the help of viral replication proteins and co-opted host proteins within large viral replication compartments in the cytosol of infected cells
Publikováno v:
PLoS Pathogens, Vol 14, Iss 5, p e1007028 (2018)
PLoS Pathogens
PLoS Pathogens
Positive-strand RNA viruses assemble numerous membrane-bound viral replicase complexes within large replication compartments to support their replication in infected cells. Yet the detailed mechanism of how given subcellular compartments are subverte
Publikováno v:
Virology. 448:43-54
Replication of tombusviruses and other plus-strand RNA viruses depends on several host factors that are recruited into viral replicase complexes. Previous studies have shown that eukaryotic translation elongation factor 1A (eEF1A) is one of the resid