Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2. - Test2 - elhamkhani - TriplyDB

Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.

Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.

http://www.wikidata.org/entity/Q27670489

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X-ray crystallography over the past decade for novel drug discovery - where are we heading next?Crystal Structure of the Marburg Virus GP2 Core Domain in Its Postfusion Conformation Ebolavirus entry requires a compact hydrophobic fist at the tip of the fusion loop.Fusion of Enveloped Viruses in Endosomes.The phosphatidylinositol-3-phosphate 5-kinase inhibitor apilimod blocks filoviral entry and infection Mapping of Ebolavirus Neutralization by Monoclonal Antibodies in the ZMapp Cocktail Using Cryo-Electron Tomography and Studies of Cellular Entry The Roles of Histidines and Charged Residues as Potential Triggers of a Conformational Change in the Fusion Loop of Ebola Virus Glycoprotein.Ebola virus and severe acute respiratory syndrome coronavirus display late cell entry kinetics: evidence that transport to NPC1+ endolysosomes is a rate-defining step Induction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a Trigger Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.A new player in the puzzle of filovirus entry.Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.The three lives of viral fusion peptides Ebola virus entry: a curious and complex series of events.Cell-cell membrane fusion induced by p15 fusion-associated small transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix.Marburg virus glycoprotein GP2: pH-dependent stability of the ectodomain α-helical bundle Filovirus entry into cells - new insights.Ready, set, fuse! The coronavirus spike protein and acquisition of fusion competence Structural and Functional Studies on the Marburg Virus GP2 Fusion Loop Endocytic pathways involved in filovirus entry: advances, implications and future directions.Cell-cell contact promotes Ebola virus GP-mediated infection.Direct Visualization of Ebola Virus Fusion Triggering in the Endocytic Pathway.Two synthetic antibodies that recognize and neutralize distinct proteolytic forms of the ebola virus envelope glycoprotein.Identification of the Fusion Peptide-Containing Region in Betacoronavirus Spike Glycoproteins Role of electrostatic repulsion in controlling pH-dependent conformational changes of viral fusion proteins Membrane association and destabilization by Aggregatibacter actinomycetemcomitans leukotoxin requires changes in secondary structures Conformational properties of peptides corresponding to the ebolavirus GP2 membrane-proximal external region in the presence of micelle-forming surfactants and lipids.Selective inhibition of Ebola entry with selective estrogen receptor modulators by disrupting the endolysosomal calcium.Filovirus entry: a novelty in the viral fusion world.Host cell factors in filovirus entry: novel players, new insights Chasing Ebola through the Endosomal Labyrinth.Ebola virus entry into host cells: identifying therapeutic strategies.Designed protein mimics of the Ebola virus glycoprotein GP2 α-helical bundle: stability and pH effects.Spontaneous Mutation at Amino Acid 544 of the Ebola Virus Glycoprotein Potentiates Virus Entry and Selection in Tissue Culture.A Polymorphism within the Internal Fusion Loop of the Ebola Virus Glycoprotein Modulates Host Cell Entry.Toremifene interacts with and destabilizes the Ebola virus glycoprotein Membrane insertion of fusion peptides from Ebola and Marburg viruses studied by replica-exchange molecular dynamics simulations.Host Factors Involved in Ebola Virus Replication.Functional mutations in spike glycoprotein of Zaire ebolavirus associated with an increase in infection efficiency.Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity.

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Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.

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2011年の論文

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P2860

Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1

Ebola haemorrhagic fever

The central proline of an internal viral fusion peptide serves two important roles

Viral membrane fusion

Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme

Ebolavirus glycoprotein structure and mechanism of entry

Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution

Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin

Structure of the dengue virus envelope protein after membrane fusion

Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts

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