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Viroporins: structure and biological functions [PDF]
Nature Reviews Microbiology, 2012 Viroporins are small, hydrophobic proteins that are encoded by a wide range of clinically relevant animal viruses. When these proteins oligomerize in host cell membranes, they form hydrophilic pores that disrupt a number of physiological properties of the cell. Viroporins are crucial for viral pathogenicity owing to their involvement in several diverse
Vanesa Madan, Luis Carrasco
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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 and membrane permeability.
Maria Eugenia Gonzalez, Luis Carrasco
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Pathophysiological Consequences of Calcium-Conducting Viroporins [PDF]
Annual Review of Virology, 2015 Eukaryotic cells have evolved a myriad of ion channels, transporters, and pumps to maintain and regulate transmembrane ion gradients. As intracellular parasites, viruses also have evolved ion channel proteins, called viroporins, which disrupt normal ionic homeostasis to promote viral replication and pathogenesis.
Joseph M Hyser, Mary K Estes
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Viroporins: structure, function and potential as antiviral targets [PDF]
Journal of General Virology, 2015 The channel-forming activity of a family of small, hydrophobic integral membrane proteins termed 'viroporins' is essential to the life cycles of an increasingly diverse range of RNA and DNA viruses, generating significant interest in targeting these proteins for antiviral development.
Stephen D Griffin
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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. These viral proteins, collectively named viroporins, are crucial for viral pathogenicity.
Bo OuYang, James J Chou
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[The antiviral targeting potential of viroporins].
Ugeskrift for laeger, 2022Viroporins are ion channels found in many viruses, where they contribute to virus life cycle and thereby pathogenesis. Viroporin targeting is a known, yet largely unexplored, therapeutic strategy so far only used in Influenza A with the drugs amantadine and rimantadine.
John D, Sund +9 more
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Lipid composition modulates interactions of p7 viroporin during membrane insertion
Journal of Structural Biology, 2023Viral proteins interact with lipid membranes during various stages in the viral life cycle to propagate infection. p7 is an ion channel forming protein of Hepatitis C virus (HCV) that participates in viral assembly. Studies show that it has close ties to lipid metabolism in the cell and anionic phosphatidylserine (PS) lipids are suggested to be key for
Oluwatoyin Campbell +1 more
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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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Oligomeric states of an Influenza-encoded PB1-F2 viroporin
2023ABSTRACTInfluenza Viruses have always been a major health concern due to their highly contagious nature. The PB1-F2 viroporin encoded by the influenza A virus is known to be a pro-apoptotic protein involved in cell death induction of the host immune cells.
Sehrish Jamal +2 more
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