Tyrosine sulfation of the amino terminus of PSGL-1 is critical for enterovirus 71 infection.
about
Cellular receptors for human enterovirus species aStructure of human enterovirus 71 in complex with a capsid-binding inhibitorComplement factor H, vitronectin, and opticin are tyrosine-sulfated proteins of the retinal pigment epitheliumThe Suramin Derivative NF449 Interacts with the 5-fold Vertex of the Enterovirus A71 Capsid to Prevent Virus Attachment to PSGL-1 and Heparan SulfateCell surface vimentin is an attachment receptor for enterovirus 71.Enterovirus 71 binding to PSGL-1 on leukocytes: VP1-145 acts as a molecular switch to control receptor interactionP-selectin glycoprotein ligand regulates the interaction of multiple myeloma cells with the bone marrow microenvironmentMolecular determinants of enterovirus 71 viral entry: cleft around GLN-172 on VP1 protein interacts with variable region on scavenge receptor B 2.Caveolar endocytosis is required for human PSGL-1-mediated enterovirus 71 infectionSuramin interacts with the positively charged region surrounding the 5-fold axis of the EV-A71 capsid and inhibits multiple enterovirus A.The molecule of DC-SIGN captures enterovirus 71 and confers dendritic cell-mediated viral trans-infection.Cell and tissue tropism of enterovirus 71 and other enteroviruses infectionsThe virology and developments toward control of human enterovirus 71.Emerging sulfated flavonoids and other polyphenols as drugs: nature as an inspiration.Update of enterovirus 71 infection: epidemiology, pathogenesis and vaccine.Tyrosine sulfation as a protein post-translational modification.Role of tyrosine-sulfated proteins in retinal structure and functionAntibodies to P-selectin glycoprotein ligand-1 block dendritic cell-mediated enterovirus 71 transmission and prevent virus-induced cells death.Functional comparison of SCARB2 and PSGL1 as receptors for enterovirus 71.Receptors for enterovirus 71.Post-translational Modifications of Natural Antimicrobial Peptides and Strategies for Peptide Engineering.Pneumococcal immune evasion: ZmpC inhibits neutrophil influx.Immunopathogenesis and Virus-Host Interactions of Enterovirus 71 in Patients with Hand, Foot and Mouth Disease.Immune Evasion of Enteroviruses Under Innate Immune MonitoringPreparation of Tyrosylprotein Sulfotransferases for In Vitro One-Pot Enzymatic Synthesis of Sulfated Proteins/PeptidesDimerization and ligand binding in tyrosylprotein sulfotransferase-2 are influenced by molecular motionsConformational flexibility influences structure–function relationships in tyrosyl protein sulfotransferase-2
P2860
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P2860
Tyrosine sulfation of the amino terminus of PSGL-1 is critical for enterovirus 71 infection.
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Tyrosine sulfation of the amin ...... for enterovirus 71 infection.
@ast
Tyrosine sulfation of the amin ...... for enterovirus 71 infection.
@en
type
label
Tyrosine sulfation of the amin ...... for enterovirus 71 infection.
@ast
Tyrosine sulfation of the amin ...... for enterovirus 71 infection.
@en
prefLabel
Tyrosine sulfation of the amin ...... for enterovirus 71 infection.
@ast
Tyrosine sulfation of the amin ...... for enterovirus 71 infection.
@en
P2093
P2860
P1433
P1476
Tyrosine sulfation of the amin ...... for enterovirus 71 infection.
@en
P2093
Hiroyuki Shimizu
Takaji Wakita
Yorihiro Nishimura
P2860
P304
P356
10.1371/JOURNAL.PPAT.1001174
P577
2010-11-04T00:00:00Z