The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
about
Inflammatory and oxidative stress in rotavirus infectionpH-Induced Conformational Change of the Rotavirus VP4 Spike: Implications for Cell Entry and Antibody NeutralizationCharacterization of viroplasm formation during the early stages of rotavirus infectionBiochemical characterization of rotavirus receptors in MA104 cellsDifferential infection of polarized epithelial cell lines by sialic acid-dependent and sialic acid-independent rotavirus strains.Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* coreVLA-2 (alpha2beta1) integrin promotes rotavirus entry into cells but is not necessary for rotavirus attachment.Initial interaction of rotavirus strains with N-acetylneuraminic (sialic) acid residues on the cell surface correlates with VP4 genotype, not species of origin.Heat shock cognate protein 70 is involved in rotavirus cell entry.Interaction of rotaviruses with Hsc70 during cell entry is mediated by VP5Identification of Equine Lactadherin-derived Peptides That Inhibit Rotavirus Infection via Integrin Receptor CompetitionIntegrin alpha(v)beta(3) mediates rotavirus cell entry.Rotavirus VP8*: phylogeny, host range, and interaction with histo-blood group antigensModeling of the rotavirus group C capsid predicts a surface topology distinct from other rotavirus speciesThe spike protein VP4 defines the endocytic pathway used by rotavirus to enter MA104 cells.VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site.STD NMR spectroscopy and molecular modeling investigation of the binding of N-acetylneuraminic acid derivatives to rhesus rotavirus VP8* core.Design and Construction of Chimeric VP8-S2 Antigen for Bovine Rotavirus and Bovine Coronavirus.Solar and temperature treatments affect the ability of human rotavirus wa to bind to host cells and synthesize viral RNAThe peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity.Fine mapping of sequential neutralization epitopes on the subunit protein VP8 of human rotavirus.Rotavirus virus-like particles (RV-VLPs) vaccines: An update.Histo-blood group antigen-binding specificities of human rotaviruses are associated with gastroenteritis but not with in vitro infection
P2860
Q26749801-4FD4E26A-31AF-4541-BB07-A66873C86288Q27469845-C70D18FF-6ED5-4EBF-9DE6-DF4A55C8961CQ33757919-F7A0F70A-DB4D-42FC-8C6A-4C437D36DF6EQ33811226-927D4BAC-DF53-4C95-A356-0131F9EBD786Q33850214-5F9BC5B6-BC62-4A5F-84AE-057656A25BA6Q33852569-3AD7AE07-9CF3-4FBF-A28C-ACDF8E1B3C62Q34329341-52CD368F-D852-474F-91D7-7121D167C1E2Q34335469-92E6CFDD-FD18-420A-9F1F-D8FA634E8E70Q34335581-90FBA2D0-0D14-4460-8430-83F37A0C3B10Q35149035-DACE0DD0-A798-4472-B3FC-F5EB5B2D7A81Q35583219-11E0ACEB-8B9A-4D96-8E72-58F9E02CEEC7Q35852198-45AEF9B3-D60B-4DA2-8DF8-D6BECAD23443Q36246385-A88C0841-9CE9-4213-B489-02D7F2C15431Q36373266-68DC7377-316D-490B-90AC-AF9F2947C7D4Q36559900-488C88EE-EDA8-4199-8759-27B817355ADAQ37567855-229F9C8B-63DA-403F-A172-2101FE5CD966Q38309625-F7DBCD14-E46C-4165-A813-5AF2BA4BA42AQ38874728-B84B9FC2-C740-4738-9D1C-776C8D558387Q38888775-27467394-D104-49AF-BD6E-580C08757978Q40304966-7D19BB65-1304-486C-98AB-11A8B5CE30C2Q42157032-F6D70556-D9C4-4938-85BF-D3D9E8B093A8Q45326050-7E1D848D-710F-478D-94ED-ADB68B3AC8DCQ58699643-91222E23-3ED3-476F-B44A-1B4614E4E6D8
P2860
The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
@ast
The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
@en
type
label
The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
@ast
The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
@en
prefLabel
The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
@ast
The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
@en
P2093
P2860
P1433
P1476
The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.
@en
P2093
P2860
P304
P356
10.1128/JVI.74.2.593-599.2000
P577
2000-01-01T00:00:00Z