The concentration of Ca2+ that solubilizes outer capsid proteins from rotavirus particles is dependent on the strain
about
Expression of nonstructural rotavirus protein NSP4 mimics Ca2+ homeostasis changes induced by rotavirus infection in cultured cells.Adenovirus protein VI mediates membrane disruption following capsid disassembly.Requirement for vacuolar H+ -ATPase activity and Ca2+ gradient during entry of rotavirus into MA104 cellsIonic strength- and temperature-induced K(Ca) shifts in the uncoating reaction of rotavirus strains RF and SA11: correlation with membrane permeabilization.Assembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins.Cross-linking of rotavirus outer capsid protein VP7 by antibodies or disulfides inhibits viral entryInfluence of Epicuticular Physicochemical Properties on Porcine Rotavirus Adsorption to 24 Leafy Green Vegetables and Tomatoes.Poliovirus protein 2BC increases cytosolic free calcium concentrations.Rotaviruses induce an early membrane permeabilization of MA104 cells and do not require a low intracellular Ca2+ concentration to initiate their replication cycle.Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles.Rotaviruses reach late endosomes and require the cation-dependent mannose-6-phosphate receptor and the activity of cathepsin proteases to enter the cell.The molecular chaperone calnexin interacts with the NSP4 enterotoxin of rotavirus in vivo and in vitro.Rotavirus capsid protein VP5* permeabilizes membranes.Characterization of a membrane calcium pathway induced by rotavirus infection in cultured cells.Selective membrane permeabilization by the rotavirus VP5* protein is abrogated by mutations in an internal hydrophobic domain.Antibodies to rotavirus outer capsid glycoprotein VP7 neutralize infectivity by inhibiting virion decapsidation.Identification of rotavirus VP6 residues located at the interface with VP2 that are essential for capsid assembly and transcriptase activity.Geometric mismatches within the concentric layers of rotavirus particles: a potential regulatory switch of viral particle transcription activity.Two proline residues are essential in the calcium-binding activity of rotavirus VP7 outer capsid protein.Discrete domains within the rotavirus VP5* direct peripheral membrane association and membrane permeability.
P2860
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P2860
The concentration of Ca2+ that solubilizes outer capsid proteins from rotavirus particles is dependent on the strain
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
The concentration of Ca2+ that ...... les is dependent on the strain
@ast
The concentration of Ca2+ that ...... les is dependent on the strain
@en
type
label
The concentration of Ca2+ that ...... les is dependent on the strain
@ast
The concentration of Ca2+ that ...... les is dependent on the strain
@en
prefLabel
The concentration of Ca2+ that ...... les is dependent on the strain
@ast
The concentration of Ca2+ that ...... les is dependent on the strain
@en
P2093
P2860
P1433
P1476
The concentration of Ca2+ that ...... les is dependent on the strain
@en
P2093
Charpilienne A
Liprandi F
Michelangeli F
P2860
P304
P407
P577
1996-08-01T00:00:00Z