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

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

10.1371/journal.pone.0055184

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Bibliographic Details
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
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Institution:	National University of Singapore

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Summary:	10.1371/journal.pone.0055184