Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core - Wikidata - awgldk - TriplyDB

Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

http://www.wikidata.org/entity/Q34348035

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Structural Basis of Rotavirus Strain Preference toward N-Acetyl- or N-Glycolylneuraminic Acid-Containing Receptors Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen Glycosphingolipid-Protein Interaction in Signal Transduction Glycan Specificity of P[19] Rotavirus and Comparison with Those of Related P Genotypes Monkey rotavirus binding to alpha2beta1 integrin requires the alpha2 I domain and is facilitated by the homologous beta1 subunit Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8.Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry Binding to decay-accelerating factor is not required for infection of human leukocyte cell lines by enterovirus 70.Crystallization and preliminary X-ray diffraction analysis of the carbohydrate-recognizing domain (VP8*) of bovine rotavirus strain NCDV Structural insights into the coupling of virion assembly and rotavirus replication.Diversity in Rotavirus-Host Glycan Interactions: A "Sweet" Spectrum.Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens.The Polyomaviridae: Contributions of virus structure to our understanding of virus receptors and infectious entry.Using viral vectors as gene transfer tools (Cell Biology and Toxicology Special Issue: ETCS-UK 1 day meeting on genetic manipulation of cells).Relative roles of GM1 ganglioside, N-acylneuraminic acids, and α2β1 integrin in mediating rotavirus infection.Glycosphingolipids as receptors for non-enveloped viruses.Bitter-sweet symphony: glycan-lectin interactions in virus biology.Carbohydrate recognition by rotaviruses.STD NMR spectroscopy and molecular modeling investigation of the binding of N-acetylneuraminic acid derivatives to rhesus rotavirus VP8* core.Single-particle detection of transcription following rotavirus entry.Characterization of neuraminidase-resistant mutants derived from rotavirus porcine strain OSU.Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites.Molecular dynamics of sialic acid analogues complex with cholera toxin and DFT optimization of ethylene glycol-mediated zinc nanocluster conjugation.Molecular modeling of methyl-α-Neu5Ac analogues docked against cholera toxin--a molecular dynamics study.Revisiting the role of histo-blood group antigens in rotavirus host-cell invasion.Recognition of the GM3 ganglioside glycan by Rhesus rotavirus particles.Sialic acid recognition by Vibrio cholerae neuraminidase.Structural basis of glycan specificity of P[19] VP8*: Implications for rotavirus zoonosis and evolution.

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

http://www.wikidata.org/entity/Q34348035

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2002 nî lūn-bûn

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2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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type

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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JVI.76.20.10512-10517.2002

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Journal of Virology

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Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core

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Gerhard Wagner

http://www.w3.org/2001/XMLSchema#string

James C Paulson

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Ola Blixt

http://www.w3.org/2001/XMLSchema#string

Philip R Dormitzer

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Stephen C Harrison

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Zhen-Yu J Sun

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P2860

A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence

Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies

The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site.

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

The VP8 fragment of VP4 is the rhesus rotavirus hemagglutinin.

Structure and function of a ganglioside receptor for porcine rotavirus

Differential 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* core

Initial interaction of rotavirus strains with N-acetylneuraminic (sialic) acid residues on the cell surface correlates with VP4 genotype, not species of origin.

A structural difference between the cell surfaces of humans and the great apes.

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10512-10517

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scholarly article

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10.1128/JVI.76.20.10512-10517.2002

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76

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2002-10-01T00:00:00Z

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12239329

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136543

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