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Biorxiv : the Preprint Server for Biology|December 15, 2021
Critical Negatively Charged Residues Are Important for the Activity of SARS-CoV-1 and SARS-CoV-2 Fusion PeptidesAlex L Lai, Jack H FreedThe Journal of Biological Chemistry|June 15, 2007
Locking the kink in the influenza hemagglutinin fusion domain structureAlex L Lai, Lukas K TammJournal of Molecular Biology|March 21, 2021
SARS-CoV-2 Fusion Peptide has a Greater Membrane Perturbating Effect than SARS-CoV with Highly Specific Dependence on Ca<sup>2</sup>Alex L Lai, Jack H FreedBiophysical Journal|January 14, 2014
HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashionAlex L Lai, Jack H FreedThe Journal of Biological Chemistry|September 10, 2010
Shallow boomerang-shaped influenza hemagglutinin G13A mutant structure promotes leaky membrane fusionAlex L Lai, Lukas K TammBiophysical Journal|December 20, 2021
Negatively charged residues in the membrane ordering activity of SARS-CoV-1 and -2 fusion peptidesAlex L Lai, Jack H FreedBiophysical Journal|December 20, 2015
The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane StructureAlex L Lai, Jack H FreedBiochimica Et Biophysica Acta|October 30, 2007
Combined NMR and EPR spectroscopy to determine structures of viral fusion domains in membranesLukas K Tamm, Alex L Lai, Yinling LiBiopolymers|December 20, 2002
Structure and function of membrane fusion peptidesLukas K Tamm, Xing Han, Yinling Li, et al.The Journal of Biological Chemistry|January 13, 2006
Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activityAlex L Lai, Heather Park, Judith M White, et al.Pageof 3