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Computational investigation in inhibitory effects of amantadine on classical swine fever virus p7 ion channel activity. [PDF]
Sci RepChen X, Wang X.
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Too many cooks in the kitchen: HPV driven carcinogenesis - The result of collaboration or competition? [PDF]
Tumour Virus ResKathleen W.
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Targeting the US21 viroporin of human cytomegalovirus by calcium channel blockers as a new antiviral strategy. [PDF]
Curr Res Microb SciSibille G +9 more
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Minimal Genome, Maximal Effect: How Polyomavirus Genomes Are Capable of Complex Pathogenesis. [PDF]
VirusesLano M, Milavetz B.
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FEBS Letters, 2003 Viroporins are a group of proteins that participate in several viral functions, including the promotion of release of viral particles from cells. These proteins also affect cellular functions, including the cell vesicle system, glycoprotein trafficking ...
Maria Eugenia Gonzalez, Luis Carrasco
exaly +6 more sources
The minimalist architectures of viroporins and their therapeutic implications
Biochimica Et Biophysica Acta - Biomembranes, 2014 Many viral genomes encode small, integral membrane proteins that form homo-oligomeric channels in membrane, and they transport protons, cations, and other molecules across the membrane barrier to aid various steps of viral entry and maturation.
Bo Ouyang, James J Chou
exaly +4 more sources
Targeting the Channel Activity of Viroporins
Advances in Protein Chemistry and Structural Biology, 2016 Since the discovery that certain small viral membrane proteins, collectively termed as viroporins, can permeabilize host cellular membranes and also behave as ion channels, attempts have been made to link this feature to specific biological roles. In parallel, most viroporins identified so far are virulence factors, and interest has focused toward the ...
Janet To, Wahyu Surya, Jaume Torres
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Viroporins from RNA viruses induce caspase-dependent apoptosis
Cellular Microbiology, 2008 The virus‐encoded viroporins are known to modify membrane permeability and play an essential role in virus budding. Here, a comparative analysis of the membrane permeabilization capacity of a number of viroporins was performed in baby hamster kidney ...
Alfredo Castello, Luis Carrasco
exaly +2 more sources
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Functional and Structural Characterization of 2B Viroporin Membranolytic Domains
Biochemistry, 2008Nonstructural 2B viroporin is an intracellularly produced pore-forming protein required for effective enteroviral and rhinoviral replication. The sequence of 2B displays two putative interconnected transmembrane domains, which are predicted to insert into the negatively charged membranes of target organelles forming an integral hairpin.
Silvia, Sánchez-Martínez +5 more
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