Viral Fusion Peptides: A Tool Set to Disrupt and Connect Biological Membranes
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[1] L. Tamm,et al. pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers. , 2000, Journal of molecular biology.
[2] L. Tamm,et al. A host-guest system to study structure-function relationships of membrane fusion peptides. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[3] R. T. Armstrong,et al. The Transmembrane Domain of Influenza Hemagglutinin Exhibits a Stringent Length Requirement to Support the Hemifusion to Fusion Transition , 2000, The Journal of cell biology.
[4] S. Lindquist,et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. , 2000, Science.
[5] S. Peisajovich,et al. The polar region consecutive to the HIV fusion peptide participates in membrane fusion. , 2000, Biochemistry.
[6] S. Tatulian,et al. Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin. , 2000, Biochemistry.
[7] D. Steinhauer,et al. Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: probing the role of hydrophobic residue size in the central region of the fusion peptide. , 1999, Biochemistry.
[8] R. Doms,et al. Effect of nonpolar substitutions of the conserved Phe11 in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes. , 1999, Biochemistry.
[9] J. Skehel,et al. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[10] F S Cohen,et al. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype. , 1999, Molecular biology of the cell.
[11] S. White,et al. Membrane protein folding and stability: physical principles. , 1999, Annual review of biophysics and biomolecular structure.
[12] R. Epand. Lipid polymorphism and protein-lipid interactions. , 1998, Biochimica et biophysica acta.
[13] L. Tamm,et al. pH‐Induced conformational changes of membrane‐bound influenza hemagglutinin and its effect on target lipid bilayers , 1998, Protein science : a publication of the Protein Society.
[14] R. Epand,et al. Modulation of lipid polymorphism by the feline leukemia virus fusion peptide: implications for the fusion mechanism. , 1998, Biochemistry.
[15] R. Epand,et al. The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: implications for membrane fusion mechanisms. , 1997, Biophysical journal.
[16] S. Tatulian,et al. Infrared spectroscopy of proteins and peptides in lipid bilayers , 1997, Quarterly Reviews of Biophysics.
[17] F. Goñi,et al. Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: dose and sequence effects. , 1997, Biophysical journal.
[18] L. Tamm,et al. Structural studies on membrane‐embedded influenza hemagglutinin and its fragments , 1997, Protein science : a publication of the Protein Society.
[19] R. Epand,et al. Structural study of the relationship between the rate of membrane fusion and the ability of the fusion peptide of influenza virus to perturb bilayers. , 1997, Biochemistry.
[20] Y. Shai,et al. Fusion Peptides Derived from the HIV Type 1 Glycoprotein 41 Associate within Phospholipid Membranes and Inhibit Cell-Cell Fusion , 1997, The Journal of Biological Chemistry.
[21] Y. Shin,et al. The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR. , 1997, Journal of molecular biology.
[22] S. Durell,et al. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events , 1996, The Journal of cell biology.
[23] Thompson Te,et al. Design of membrane-inserting peptides: spectroscopic characterization with and without lipid bilayers. , 1996 .
[24] T. Vorherr,et al. H+-induced Membrane Insertion of Influenza Virus Hemagglutinin Involves the HA2 Amino-terminal Fusion Peptide but Not the Coiled Coil Region* , 1996, The Journal of Biological Chemistry.
[25] C. Gray,et al. Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers. , 1996, Biophysical journal.
[26] S. Pelletier,et al. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers , 1996, The Journal of cell biology.
[27] J. Ruysschaert,et al. Structural study of the interaction between the SIV fusion peptide and model membranes. , 1996, Biochemistry.
[28] J. Ruysschaert,et al. Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer , 1996, Journal of virology.
[29] J. Ruysschaert,et al. Structure and Topology of the Influenza Virus Fusion Peptide in Lipid Bilayers (*) , 1995, The Journal of Biological Chemistry.
[30] S. Tatulian,et al. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. , 1995, The EMBO journal.
[31] F. Goñi,et al. Liposome destabilization induced by the HIV‐1 fusion peptide Effect of a single amino acid substitution , 1995, FEBS letters.
[32] J. Skehel,et al. Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. , 1995, The EMBO journal.
[33] J. Ruysschaert,et al. Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion. , 1994, Biochemical and biophysical research communications.
[34] J. Seelig,et al. Binding of apolipoprotein A-I model peptides to lipid bilayers. Measurement of binding isotherms and peptide-lipid headgroup interactions. , 1994, The Journal of biological chemistry.
[35] J. Skehel,et al. Structure of influenza haemagglutinin at the pH of membrane fusion , 1994, Nature.
[36] R. Epand,et al. Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers. , 1994, Biochemical and biophysical research communications.
[37] C. Deber,et al. Erratum: A measure of helical propensity for amino acids in membrane environments , 1994, Nature Structural Biology.
[38] D. Siegel,et al. Energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms. , 1993, Biophysical journal.
[39] S. Takahashi,et al. Orientation of fusion-active synthetic peptides in phospholipid bilayers: determination by Fourier transform infrared spectroscopy. , 1993, Biochemistry.
[40] P. S. Kim,et al. A spring-loaded mechanism for the conformational change of influenza hemagglutinin , 1993, Cell.
[41] R. Brasseur,et al. Orientation and structure of the NH2-terminal HIV-1 gp41 peptide in fused and aggregated liposomes. , 1993, Biochimica et biophysica acta.
[42] V A Parsegian,et al. Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces. , 1992, Biophysical journal.
[43] T. McIntosh,et al. Modulation of poly(ethylene glycol)-induced fusion by membrane hydration: importance of interbilayer separation. , 1992, Biochemistry.
[44] R. Brasseur,et al. Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins. , 1990, Biochimica et biophysica acta.
[45] W. DeGrado,et al. Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41. , 1990, Biochemistry.
[46] S. Takahashi. Conformation of membrane fusion-active 20-residue peptides with or without lipid bilayers. Implication of alpha-helix formation for membrane fusion. , 1990, Biochemistry.
[47] J. Israelachvili,et al. Molecular mechanisms and forces involved in the adhesion and fusion of amphiphilic bilayers. , 1989, Science.
[48] S. Gruner. Stability of lyotropic phases with curved interfaces , 1989 .
[49] S. Hui,et al. Effects of lipid packing on polymorphic phase behavior and membrane properties. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[50] I. Wilson,et al. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin , 1987, The Journal of cell biology.
[51] S. Gruner. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[52] L. J. Lis,et al. Interactions between neutral phospholipid bilayer membranes. , 1982, Biophysical journal.
[53] I. Wilson,et al. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. , 1982, Proceedings of the National Academy of Sciences of the United States of America.
[54] I. Wilson,et al. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution , 1981, Nature.
[55] P. Y. Chou,et al. Empirical predictions of protein conformation. , 1978, Annual review of biochemistry.