Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein.
about
Biological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): G is transported in a fusion-inactive state-like conformationProper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane proteinRabies virus glycoprotein as a carrier for anthrax protective antigenMolecular and cellular aspects of rhabdovirus entryDouble-labeled rabies virus: live tracking of enveloped virus transport.Low-affinity nerve-growth factor receptor (P75NTR) can serve as a receptor for rabies virus.Rabies virus-induced membrane fusion.A permanent host shift of rabies virus from Chiroptera to Carnivora associated with recombination.Vesicular stomatitis virus G protein acquires pH-independent fusion activity during transport in a polarized endometrial cell line.Evidence of two Lyssavirus phylogroups with distinct pathogenicity and immunogenicityThe role of the hepatitis C virus glycoproteins in infection.A single amino acid change in rabies virus glycoprotein increases virus spread and enhances virus pathogenicity.Rhabdovirus-based vectors with human immunodeficiency virus type 1 (HIV-1) envelopes display HIV-1-like tropism and target human dendritic cells.Second-generation rabies virus-based vaccine vectors expressing human immunodeficiency virus type 1 gag have greatly reduced pathogenicity but are highly immunogenicSingle domain antibody multimers confer protection against rabies infection.Molecular epidemiology of rabies virus isolates in India.Recombinant rabies virus as potential live-viral vaccines for HIV-1.The dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcriptionReal-time Imaging of Rabies Virus Entry into Living Vero cellsA recombinant rabies virus expressing vesicular stomatitis virus glycoprotein fails to protect against rabies virus infectionIdentification of amino acids controlling the low-pH-induced conformational change of rabies virus glycoprotein.Rabies virus infects mouse and human lymphocytes and induces apoptosis.Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?Rabies virus-induced membrane fusion pathway.Functional human immunodeficiency virus type 1 (HIV-1) Gag-Pol or HIV-1 Gag-Pol and env expressed from a single rhabdovirus-based vaccine vector genome.Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity.Uses of flow cytometry in virologyLow-pH conformational changes of rabies virus glycoprotein and their role in membrane fusionA novel rabies vaccine based on a recombinant parainfluenza virus 5 expressing rabies virus glycoproteinTargeted transduction of CD34+ hematopoietic progenitor cells in nonpurified human mobilized peripheral blood mononuclear cellsCharacterization of a unique variant of bat rabies virus responsible for newly emerging human cases in North AmericaFolding of rabies virus glycoprotein: epitope acquisition and interaction with endoplasmic reticulum chaperonesRabies vaccine development by expression of recombinant viral glycoprotein.Unraveling the role of membrane microdomains during microbial infections.Rabies - epidemiology, pathogenesis, public health concerns and advances in diagnosis and control: a comprehensive review.Chimeric rabies glycoprotein with a transmembrane domain and cytoplasmic tail from Newcastle disease virus fusion protein incorporates into the Newcastle disease virion at reduced levelsHost switching in Lyssavirus history from the Chiroptera to the Carnivora orders.Neuronal cell surface molecules mediate specific binding to rabies virus glycoprotein expressed by a recombinant baculovirus on the surfaces of lepidopteran cellsMutations 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.Vesicular stomatitis virus glycoprotein mutations that affect membrane fusion activity and abolish virus infectivity.
P2860
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P2860
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein.
@en
type
label
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein.
@en
prefLabel
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein.
@en
P2093
P1433
P1476
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein.
@en
P2093
P304
P356
10.1016/0042-6822(91)90539-N
P407
P577
1991-12-01T00:00:00Z