Nonhelical leash and alpha-helical structures determine the potency of a peptide antagonist of human T-cell leukemia virus entry

Keyphrases

• Human T-cell Leukemia Virus Type 1 (HTLV-1) 100%
• Virus Entry 100%
• Leash 100%
• Peptide Antagonist 100%
• α-helical Structure 100%
• Coiled Coil 60%
• Inhibitory Activity 40%
• Trimer 40%
• Membrane Fusion 40%
• Inhibitory Peptide 40%
• α-helical 40%
• Hairpin 40%
• C-helix 40%
• Cell Membrane 20%
• Small Molecule Inhibitors 20%
• Antagonism 20%
• Potent Inhibitor 20%
• Synthetic Peptides 20%
• Fusion Protein 20%
• Viral 20%
• Hydrophobic Pocket 20%
• Conformational Transition 20%
• Single Amino Acid Substitution 20%
• C-terminal Region 20%
• Viral Infection 20%
• Viral Entry 20%
• Clinically Significant 20%
• Peptide-based 20%
• Peptide Inhibitor 20%
• Viral Particles 20%
• Mimetic Peptide 20%
• Proximal End 20%
• Amino Acid Side Chains 20%
• Peptide Interaction 20%
• Lipid Mixing 20%
• Bundle Structure 20%
• Viral Fusion Protein 20%
• Six-helix Bundle 20%
• Deep Pockets 20%
• Entry Inhibitor 20%

Biochemistry, Genetics and Molecular Biology

• Human T-Lymphotropic Virus 1 100%
• Human T Cell Leukemia Virus 100%
• Coiled Coil 100%
• Virus Entry 100%
• C-Terminus 66%
• Membrane Fusion 66%
• Chimeric Protein 66%
• Small Molecule 33%
• Amino Acids 33%
• Cell Membrane 33%
• Lipid 33%
• Target Cell 33%
• Conformational Change 33%
• Amino Acid Substitution 33%
• Peptide Mimetics 33%
• Virus Particle 33%
• Helix Bundle 33%