Uncoupled binding and folding of immune signaling-related intrinsically disordered proteins

This publication has 86 references indexed in Scilit:

• Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
  Biomolecular NMR Assignments, 2011
• Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition
  Biochemical and Biophysical Research Communications, 2009
• Limitations of Induced Folding in Molecular Recognition by Intrinsically Disordered Proteins
  Chemphyschem, 2009
• The Intrinsically Disordered Cytoplasmic Domain of the T Cell Receptor ζ Chain Binds to the Nef Protein of Simian Immunodeficiency Virus without a Disorder-to-Order Transition
  Biochemistry, 2008
• Regulation of T Cell Receptor Activation by Dynamic Membrane Binding of the CD3ɛ Cytoplasmic Tyrosine-Based Motif
  Cell, 2008
• Intrinsically Disordered Human C/EBP Homologous Protein Regulates Biological Activity of Colon Cancer Cells during Calcium Stress
  Journal of Molecular Biology, 2008
• Characterization of the Neuron-Specific L1-CAM Cytoplasmic Tail: Naturally Disordered in Solution It Exercises Different Binding Modes for Different Adaptor Proteins
  Biochemistry, 2008
• Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form
  Biochimie, 2007
• Lipid-Binding Activity of Intrinsically Unstructured Cytoplasmic Domains of Multichain Immune Recognition Receptor Signaling Subunits
  Biochemistry, 2006
• Assessing protein disorder and induced folding
  Proteins: Structure, Function, and Bioinformatics, 2005