Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
about
Identification of a broad-spectrum antiviral small molecule against severe acute respiratory syndrome coronavirus and Ebola, Hendra, and Nipah viruses by using a novel high-throughput screening assayModes of paramyxovirus fusion: a Henipavirus perspectiveCell entry of enveloped virusesUnity in diversity: shared mechanism of entry among paramyxovirusesHenipavirus mediated membrane fusion, virus entry and targeted therapeuticsUnexpected similarity between the cytosolic West Nile virus NS3 and the secretory furin-like serine proteinasesStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeReceptor Binding and Low pH Coactivate Oncogenic Retrovirus Envelope-Mediated FusionEbolavirus glycoprotein structure and mechanism of entryFusion of Enveloped Viruses in Endosomes.Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers AssemblyCathepsin L plays an important role in the lysosomal degradation of L-lactate dehydrogenaseInduction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a TriggerHendra virus and Nipah virus animal vaccines.Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein.Hendra and Nipah viruses: different and dangerous.Kinetic characterization and molecular docking of a novel, potent, and selective slow-binding inhibitor of human cathepsin LSimulating henipavirus multicycle replication in a screening assay leads to identification of a promising candidate for therapy.Entry and fusion of emerging paramyxoviruses.A small-molecule oxocarbazate inhibitor of human cathepsin L blocks severe acute respiratory syndrome and ebola pseudotype virus infection into human embryonic kidney 293T cells.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Membrane fusion and cell entry of XMRV are pH-independent and modulated by the envelope glycoprotein's cytoplasmic tailA functional henipavirus envelope glycoprotein pseudotyped lentivirus assay system.Cathepsin B & L are not required for ebola virus replicationInhibition of hendra virus fusion.Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.Inhibitors of SARS-CoV entry--identification using an internally-controlled dual envelope pseudovirion assay.Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein.Hendra and nipah infection: pathology, models and potential therapies.Emerging paramyxoviruses: molecular mechanisms and antiviral strategiesCathepsin W Is Required for Escape of Influenza A Virus from Late Endosomes.Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function.Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recyclingEphrin-B2 and ephrin-B3 as functional henipavirus receptorsCathepsin L Mediates the Degradation of Novel APP C-Terminal Fragments.Multiple Novel Functions of Henipavirus O-glycans: The First O-glycan Functions Identified in the Paramyxovirus FamilyParamyxovirus fusion and entry: multiple paths to a common endA conserved region in the F(2) subunit of paramyxovirus fusion proteins is involved in fusion regulation.
P2860
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P2860
Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
@en
Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
@nl
type
label
Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
@en
Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
@nl
prefLabel
Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
@en
Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
@nl
P2860
P921
P1433
P1476
Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.
@en
P2093
Cara Theresia Pager
Rebecca Ellis Dutch
P2860
P304
12714-12720
P356
10.1128/JVI.79.20.12714-12720.2005
P407
P577
2005-10-01T00:00:00Z