Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion
about
Biological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): G is transported in a fusion-inactive state-like conformationMolecular and cellular aspects of rhabdovirus entryMembrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.Rabies virus envelope glycoprotein targets lentiviral vectors to the axonal retrograde pathway in motor neurons.Mechanism of membrane fusion induced by vesicular stomatitis virus G protein.Design and generation of recombinant rabies virus vectors.Vesicular stomatitis virus G protein acquires pH-independent fusion activity during transport in a polarized endometrial cell line.Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Solubilization and reconstitution of vesicular stomatitis virus envelope using octylglucoside.Molecular basis of neurovirulence of flury rabies virus vaccine strains: importance of the polymerase and the glycoprotein R333Q mutation.Endocytosis is a critical step in entry of subgroup B avian leukosis viruses.Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEMClass III viral membrane fusion proteins.Newcastle disease virus-vectored rabies vaccine is safe, highly immunogenic, and provides long-lasting protection in dogs and catsTemperature dependence of cell-cell fusion induced by the envelope glycoprotein of human immunodeficiency virus type 1.Identification of amino acids controlling the low-pH-induced conformational change of rabies virus glycoprotein.TNFα Impairs Rhabdoviral Clearance by Inhibiting the Host Autophagic Antiviral Response.Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Rabies virus-induced membrane fusion pathway.Internalization and fusion mechanism of vesicular stomatitis virus and related rhabdoviruses.Conformation- and fusion-defective mutations in the hypothetical phospholipid-binding and fusion peptides of viral hemorrhagic septicemia salmonid rhabdovirus protein GRecent observations on Australian bat lyssavirus tropism and viral entryFolding of rabies virus glycoprotein: epitope acquisition and interaction with endoplasmic reticulum chaperonesCharacterization of pH-sensitive molecular switches that trigger the structural transition of vesicular stomatitis virus glycoprotein from the postfusion state toward the prefusion state.Host cell virus entry mediated by Australian bat lyssavirus G envelope glycoprotein occurs through a clathrin-mediated endocytic pathway that requires actin and Rab5.A recombinant vesicular stomatitis virus bearing a lethal mutation in the glycoprotein gene uncovers a second site suppressor that restores fusion.Mutations conferring resistance to neutralization by a soluble form of the neurotrophin receptor (p75NTR) map outside of the known antigenic sites of the rabies virus glycoprotein.Mokola virus glycoprotein and chimeric proteins can replace rabies virus glycoprotein in the rescue of infectious defective rabies virus particles.Growth of recombinant Drosophila melanogaster Schneider 2 cells producing rabies virus glycoprotein in bioreactor employing serum-free medium.Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein.Evidence that rabies virus forms different kinds of fusion machines with different pH thresholds for fusion.Reversible inhibition of spreading of in vitro infection and imbalance of viral protein accumulation at low pH in viral hemorrhagic septicemia rhabdovirus, a salmonid rhabdovirus.Predicted 3D Model of the Rabies Virus Glycoprotein Trimer.Formulation of a protein-free medium based on IPL-41 for the sustained growth of Drosophila melanogaster S2 cells.Distinct structural rearrangements of the VSV glycoprotein drive membrane fusion.
P2860
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P2860
Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion
description
1993 nî lūn-bûn
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1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
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1993年论文
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name
Low-pH conformational changes ...... their role in membrane fusion
@ast
Low-pH conformational changes ...... their role in membrane fusion
@en
type
label
Low-pH conformational changes ...... their role in membrane fusion
@ast
Low-pH conformational changes ...... their role in membrane fusion
@en
prefLabel
Low-pH conformational changes ...... their role in membrane fusion
@ast
Low-pH conformational changes ...... their role in membrane fusion
@en
P2093
P2860
P1433
P1476
Low-pH conformational changes ...... their role in membrane fusion
@en
P2093
P2860
P304
P407
P577
1993-03-01T00:00:00Z