Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc, Science, vol.251, issue.4998, pp.1211-1217, 1991. ,
DOI : 10.1126/science.2006410
Max and C-Myc Max DNA-Binding Activities in Cell-Extracts, Oncogene, vol.7, pp.1783-1792, 1992. ,
An Overview of MYC and Its Interactome, Csh. Perspect. Med, vol.4, pp.1-24, 2014. ,
The NMR Solution Structure of a Mutant of the Max b/HLH/LZ Free of DNA: Insights into the Specific and Reversible DNA Binding Mechanism of Dimeric Transcription Factors, Journal of Molecular Biology, vol.342, issue.3, pp.813-832, 2004. ,
DOI : 10.1016/j.jmb.2004.07.058
The crystal structure of an intact human Max???DNA complex: new insights into mechanisms of transcriptional control, Structure, vol.5, issue.4, pp.509-520, 1997. ,
DOI : 10.1016/S0969-2126(97)00207-4
Structure, function, and dynamics of the dimerization and DNA-binding domain of oncogenic transcription factor v-Myc11Edited by P. E. Wright, Journal of Molecular Biology, vol.307, issue.5, pp.1395-1410, 2001. ,
DOI : 10.1006/jmbi.2001.4537
Compensatory Adaptations of Structural Dynamics in an Intrinsically Disordered Protein Complex, Angewandte Chemie International Edition, vol.135, issue.15, pp.3840-3843, 2014. ,
DOI : 10.1021/ja4047872
Intrinsically disordered proteins: regulation and disease, Current Opinion in Structural Biology, vol.21, issue.3, pp.432-440, 2011. ,
DOI : 10.1016/j.sbi.2011.03.011
Improved 3D triple resonance experiments, HNN and HN(C)N, for H-N and N-15 sequential correlations in (C-13, N-15) labeled proteins: Application to unfolded proteins, Journal of Biomolecular NMR, vol.20, issue.2, pp.135-147, 2001. ,
DOI : 10.1023/A:1011239023422
Probing Invisible, Low-Populated States of Protein Molecules by Relaxation Dispersion NMR Spectroscopy: An Application to Protein Folding, Accounts of Chemical Research, vol.41, issue.3, pp.442-451, 2008. ,
DOI : 10.1021/ar700189y
A general two-site solution for the chemical exchange produced dependence of T2 upon the carr-Purcell pulse separation, Journal of Magnetic Resonance (1969), vol.6, issue.1, pp.89-105, 1972. ,
DOI : 10.1016/0022-2364(72)90090-X
Nuclear Magnetic Resonance Study of the Protolysis of Trimethylammonium Ion in Aqueous Solution???Order of the Reaction with Respect to Solvent, The Journal of Chemical Physics, vol.82, issue.2, pp.366-370, 1963. ,
DOI : 10.1021/ja00883a011
Theory, Practice, and Applications of Paramagnetic Relaxation Enhancement for the Characterization of Transient Low-Population States of Biological Macromolecules and Their Complexes, Chemical Reviews, vol.109, issue.9, pp.4108-4139, 2009. ,
DOI : 10.1021/cr900033p
The DOSY Toolbox: A new tool for processing PFG NMR diffusion data, Journal of Magnetic Resonance, vol.200, issue.2 ,
DOI : 10.1016/j.jmr.2009.07.022
Effective rotational correlation times of proteins from NMR relaxation interference, Cooperative Unfolding of Compact Conformations of the Intrinsically Disordered Protein Osteopontin, pp.72-76, 2006. ,
DOI : 10.1016/j.jmr.2005.08.014
The Metastasis-Associated Extracellular Matrix Protein Osteopontin Forms Transient Structure in Ligand Interaction Sites, Biochemistry, vol.50, pp.6113-6124, 2011. ,
Protonation-dependent conformational variability of intrinsically disordered proteins, Protein Science, vol.37, issue.Suppl 1, pp.1196-1205, 2013. ,
DOI : 10.1002/(SICI)1521-3773(19981102)37:20<2833::AID-ANIE2833>3.0.CO;2-7
Singlemolecule spectroscopy of the temperature-induced collapse of unfolded proteins, Proc. Nat ,
Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy, Proc. Nat ,
Polymer Physics, 2003. ,
Distribution of Pico-and Nanosecond Motions in Disordered Proteins from Nuclear Spin Relaxation, Biophys. J. 2015, vol.109, pp.988-999 ,
URL : https://hal.archives-ouvertes.fr/hal-01191810
Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry NMR probing and visualization of correlated structural fluctuations in intrinsically disordered proteins, J, Am. Chem. Soc, vol.135, issue.19, pp.18665-18672, 2013. ,
The Meandering of Disordered Proteins in Conformational Space, Structure, vol.18, issue.4, pp.416-419, 2010. ,
DOI : 10.1016/j.str.2010.03.003
Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation, The Journal of Physical Chemistry Letters, vol.7, issue.13, pp.7-2483 ,
DOI : 10.1021/acs.jpclett.6b00885
URL : https://hal.archives-ouvertes.fr/hal-01396234
(PAF) Is an Intrinsically Disordered Protein with Nonrandom Structural Preferences at Sites of Interaction with Other Proteins, Biophys. J, vol.106, pp.15-865, 2014. ,
URL : https://hal.archives-ouvertes.fr/hal-00967481
Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease, Biochemistry, vol.28, issue.23, pp.8972-8979, 1989. ,
DOI : 10.1021/bi00449a003
Heteropolymer Collapse Theory for Protein Folding in the Pressure-Temperature Plane, Biophysical Journal, vol.91, issue.7, pp.2427-2435, 2006. ,
DOI : 10.1529/biophysj.106.081802