NMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin

• Main Authors: Chua G.-L., Patra A.T., Tan S.-M., Bhattacharjya S.
• Other Authors: DEAN'S OFFICE (DUKE-NUS MEDICAL SCHOOL)
• Format: Article
• Published: 2019
• Subjects: alpha4 integrin; asparagine; aspartic acid; glutamine; hydrogen; lysine; paxillin; amino acid composition; article; carboxy terminal sequence; chemical bond; cytosol; heteronuclear single quantum coherence; hydrogen bond; molecular docking; nitrogen nuclear magnetic resonance; nuclear magnetic resonance spectroscopy; nucleotide repeat; protein binding; protein conformation; protein interaction; protein structure; proton nuclear magnetic resonance; Amino Acid Sequence; Integrin alpha4; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Paxillin; Peptide Fragments; Protein Binding; Protein Conformation; Protein Folding
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/161345
• Institution: National University of Singapore

10.1371/journal.pone.0055184