The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein

This publication has 82 references indexed in Scilit:

• Natively unfolded proteins: A point where biology waits for physics
  Protein Science, 2002
• Structure of Recombinant Rabies Virus Nucleoprotein-RNA Complex and Identification of the Phosphoprotein Binding site
  Journal of Virology, 2001
• Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright
  Journal of Molecular Biology, 1998
• Measles Virus Nucleocapsid Protein Binds to FcγRII and Inhibits Human B Cell Antibody Production
  The Journal of Experimental Medicine, 1997
• Protein interaction domains of the measles virus nucleocapsid protein (NP)
  Archiv für die gesamte Virusforschung, 1997
• SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields
  Journal of Structural Biology, 1996
• Protein interactions entered into by the measles virus P, V, and C proteins
  Virus Research, 1995
• Determination of the regularization parameter in indirect-transform methods using perceptual criteria
  Journal of Applied Crystallography, 1992
• High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
  Gene, 1989
• Antigenic analysis of African measles virus field isolates: identification and localisation of one conserved and two variable epitope sites on the NP protein
  Virus Research, 1988