Hydrophobie Binding of the Ectodomain of Influenza Hemagglutinin to Membranes Occurs through the “Fusion Peptide”

Hydrophobie Binding of the Ectodomain of Influenza Hemagglutinin to Membranes Occurs through the “Fusion Peptide”

The abbreviations used are: HA, influenza virus hemagglutinin; BHA, BHA1, and BHA2, bromelain-solubilized ectodomain of HA (BHA) and the two subunits derived therefrom; ["sI]TID, 3-(trifluo-r0methyl)-3-(['~~I]iodophenyl)diazirine; [3H]PTPC/11, l-palmitoyl-2-[ll-[4-[3-(trifluoromethyl)diazi...

Deskribapen osoa

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Xehetasun bibliografikoak
Egile Nagusiak:	Cordula Harter, P L James, Thomas Bächi, Giorgio Semenza, Josef Brunner
Formatua:	Artigo
Hizkuntza:	ingelesa
Argitaratua:	1989
Sarrera elektronikoa:	https://doi.org/10.1016/s0021-9258(18)83370-1
Etiketak:	Etiketa erantsi Etiketarik gabe, Izan zaitez lehena erregistro honi etiketa jartzen!

Antzeko izenburuak

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Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively-Correlated with Membrane Fusion
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Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
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The Lipid-anchored Ectodomain of Influenza Virus Hemagglutinin (GPI-HA) Is Capable of Inducing Nonenlarging Fusion Pores
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The Lipid-anchored Ectodomain of Influenza Virus Hemagglutinin (GPI-HA) Is Capable of Inducing Nonenlarging Fusion Pores
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Capturing Spontaneous Membrane Insertion of the Influenza Virus Hemagglutinin Fusion Peptide
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Capturing Spontaneous Membrane Insertion of the Influenza Virus Hemagglutinin Fusion Peptide
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Length Requirements for Membrane Fusion of Influenza Virus Hemagglutinin Peptide Linkers to Transmembrane or Fusion Peptide Domains
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Analysis of Residues Near the Fusion Peptide in the Influenza Hemagglutinin Structure for Roles in Triggering Membrane Fusion
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Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion
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Ectodomain Pulling Combines with Fusion Peptide Inserting to Provide Cooperative Fusion for Influenza Virus and HIV
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Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex
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Structure of influenza hemagglutinin in complex with an inhibitor of membrane fusion
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The Final Conformation of the Complete Ectodomain of the HA2 Subunit of Influenza Hemagglutinin Can by Itself Drive Low pH-dependent Fusion
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Hydrogen-deuterium exchange supports independent membrane-interfacial fusion peptide and transmembrane domains in subunit 2 of influenza virus hemagglutinin protein, a structured and aqueous-protected connection between the fusion peptide and soluble ectodomain, and the importance of membrane apposition by the trimer-of-hairpins structure
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Murine Leukemia Virus R Peptide Inhibits Influenza Virus Hemagglutinin-Induced Membrane Fusion
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Membrane Fusion Mechanisms: The Influenza Hemagglutinin Paradigm and its Implications for Intracellular Fusion
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Mutations in the Ectodomain of Newcastle Disease Virus Fusion Protein Confer a Hemagglutinin-Neuraminidase-Independent Phenotype
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Binding of Hemagglutinin and Influenza Virus to a Peptide-Conjugated Lipid Membrane
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Fusion Peptide from Influenza Hemagglutinin Increases Membrane Surface Order: An Electron-Spin Resonance Study
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Fusion Peptide from Influenza Hemagglutinin Increases Membrane Surface Order: An Electron-Spin Resonance Study
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Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
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2752. Peptide Vaccines Utilizing Conserved Hemagglutinin, Neuraminidase, and Matrix Ectodomain Influenza Epitopes Demonstrate Functional Activity Against Group 1 and 2 Influenza Strains
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