Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity
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Herpes simplex virus glycoprotein B associates with target membranes via its fusion loopsStructure of a trimeric variant of the Epstein-Barr virus glycoprotein BStructural and Mechanistic Insights into the Tropism of Epstein-Barr VirusStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeThe postfusion structure of baculovirus gp64 supports a unified view of viral fusion machinesStructure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.Extensive Mutagenesis of the HSV-1 gB Ectodomain Reveals Remarkable Stability of Its Postfusion FormFusion of Enveloped Viruses in Endosomes.Assembly and architecture of the EBV B cell entry triggering complexCharacteristics of Epstein-Barr virus envelope protein gp42.Herpes virus fusion and entry: a story with many characters.Modulation of Epstein-Barr virus glycoprotein B (gB) fusion activity by the gB cytoplasmic tail domainMapping regions of Epstein-Barr virus (EBV) glycoprotein B (gB) important for fusion function with gH/gL.Class III viral membrane fusion proteins.Structural characteristics and antiviral activity of multiple peptides derived from MDV glycoproteins B and HEpstein-barr virus vaccines.Neuropilin 1 is an entry factor that promotes EBV infection of nasopharyngeal epithelial cellsFusing structure and function: a structural view of the herpesvirus entry machinery.A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization.Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins.HCMV gB shares structural and functional properties with gB proteins from other herpesviruses.Conservation of the glycoprotein B homologs of the Kaposi׳s sarcoma-associated herpesvirus (KSHV/HHV8) and old world primate rhadinoviruses of chimpanzees and macaquesAnalysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesisCleavage and secretion of Epstein-Barr virus glycoprotein 42 promote membrane fusion with B lymphocytes.Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.Epstein-Barr virus infection mechanismsEBV glycoproteins: where are we now?Structure-based functional analyses of domains II and III of pseudorabies virus glycoprotein H.Pathogenesis of Gastric Cancer: Genetics and Molecular Classification.The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination.Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus.Residues within the C-terminal arm of the herpes simplex virus 1 glycoprotein B ectodomain contribute to its refolding during the fusion step of virus entry.Mutagenesis of varicella-zoster virus glycoprotein B: putative fusion loop residues are essential for viral replication, and the furin cleavage motif contributes to pathogenesis in skin tissue in vivo.Human herpesvirus 8 glycoprotein B binds the entry receptor DC-SIGN.Structure-function dissection of the Pseudorabies virus glycoprotein B fusion loops.Molecular architecture of the bipartite fusion loops of vesicular stomatitis virus glycoprotein G, a class III viral fusion protein.Human MHC-II with Shared Epitope Motifs Are Optimal Epstein-Barr Virus Glycoprotein 42 Ligands-Relation to Rheumatoid Arthritis.
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P2860
Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Hydrophobic residues that form ...... e critical for fusion activity
@ast
Hydrophobic residues that form ...... e critical for fusion activity
@en
type
label
Hydrophobic residues that form ...... e critical for fusion activity
@ast
Hydrophobic residues that form ...... e critical for fusion activity
@en
prefLabel
Hydrophobic residues that form ...... e critical for fusion activity
@ast
Hydrophobic residues that form ...... e critical for fusion activity
@en
P2093
P2860
P921
P356
P1433
P1476
Hydrophobic residues that form ...... e critical for fusion activity
@en
P2093
Marija Backovic
Richard Longnecker
Theodore S Jardetzky
P2860
P304
P356
10.1128/JVI.00758-07
P407
P577
2007-06-06T00:00:00Z