The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1
about
Viral Membrane Channels: Role and Function in the Virus Life CycleRotavirus non-structural proteins: structure and functionA new pentameric structure of rotavirus NSP4 revealed by molecular replacementCaveolin-1 influences human influenza A virus (H1N1) multiplication in cell culture.Drebrin restricts rotavirus entry by inhibiting dynamin-mediated endocytosis.Rotaviruses associate with cellular lipid droplet components to replicate in viroplasms, and compounds disrupting or blocking lipid droplets inhibit viroplasm formation and viral replication.Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxinRotavirus NSP4: Cell type-dependent transport kinetics to the exofacial plasma membrane and release from intact infected cellsEmerging role of lipid droplets in host/pathogen interactions.Allergy as an epithelial barrier disease.Elucidation of the Rotavirus NSP4-Caveolin-1 and -Cholesterol Interactions Using Synthetic Peptides.Full-length, glycosylated NSP4 is localized to plasma membrane caveolae by a novel raft isolation technique.Investigation of Stilbenoids as Potential Therapeutic Agents for Rotavirus Gastroenteritis.A new N-terminal recognition domain in caveolin-1 interacts with sterol carrier protein-2 (SCP-2).Mutational analysis of the rotavirus NSP4 enterotoxic domain that binds to caveolin-1.Chicken Egg Yolk Antibodies (IgY) for Prophylaxis and Treatment of Rotavirus Diarrhea in Human and Animal Neonates: A Concise Review.Rotavirus NSP4 interacts with both the amino- and carboxyl-termini of caveolin-1.Epitope mapping and use of epitope-specific antisera to characterize the VP5* binding site in rotavirus SA11 NSP4.Rotaviruses: Extraction and Isolation of RNA, Reassortant Strains, and NSP4 Protein.Rotavirus nonstructural glycoprotein NSP4 is secreted from the apical surfaces of polarized epithelial cells.Conformational Differences Unfold a Wide Range of Enterotoxigenic Abilities Exhibited by rNSP4 Peptides from Different Rotavirus Strains.Rotavirus NSP486-175 interacts with H9c2(2-1) cells in vitro, elevates intracellular Ca2+ levels and can become cytotoxic: a possible mechanism for extra-intestinal pathogenesis.Generation and Characterization of UL21-Null Herpes Simplex Virus Type 1The Molecular Switch of Telomere Phages: High Binding Specificity of the PY54 Cro Lytic Repressor to a Single Operator Site.Severe diffraction anisotropy, rotational pseudosymmetry and twinning complicate the refinement of a pentameric coiled-coil structure of NSP4 of rotavirusRotavirus toxin NSP4 induces diarrhea by activation of TMEM16A and inhibition of Na+ absorption
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P2860
The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1
description
2006 nî lūn-bûn
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2006 թուականի Մարտին հրատարակուած գիտական յօդուած
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2006 թվականի մարտին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
@zh-hant
2006年論文
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2006年論文
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2006年論文
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2006年论文
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name
The rotavirus enterotoxin NSP4 ...... structural protein caveolin-1
@ast
The rotavirus enterotoxin NSP4 ...... structural protein caveolin-1
@en
type
label
The rotavirus enterotoxin NSP4 ...... structural protein caveolin-1
@ast
The rotavirus enterotoxin NSP4 ...... structural protein caveolin-1
@en
prefLabel
The rotavirus enterotoxin NSP4 ...... structural protein caveolin-1
@ast
The rotavirus enterotoxin NSP4 ...... structural protein caveolin-1
@en
P2093
P2860
P1433
P1476
The rotavirus enterotoxin NSP4 ...... structural protein caveolin-1
@en
P2093
Avery L McIntosh
Deanne M Mitchell
Judith M Ball
Kiran D Mir
Minglong Zhou
Rebecca D Parr
Stephen M Storey
P2860
P304
P356
10.1128/JVI.80.6.2842-2854.2006
P577
2006-03-01T00:00:00Z