Miguel De Avila

The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein

K. Bessonov, G. Harauz, Kenrick A. Vassall, 2013, PloS one.

Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5‐kDa myelin basic protein decrease its affinity for the Fyn‐SH3 domain and alter process development and protein localization in oligodendrocytes

P. Paez, G. Harauz, J. Boggs, 2012, Journal of neuroscience research.

Structured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interaction.

G. Harauz, Mumdooh Ahmed, V. Bamm, 2011, Biophysical journal.

Secondary structure and solvent accessibility of a calmodulin-binding C-terminal segment of membrane-associated myelin basic protein.

K. Bessonov, G. Harauz, V. Bamm, 2010, Biochemistry.

The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro

G. Harauz, Kenrick A. Vassall, V. Bamm, 2014, Bioscience reports.

Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles.

K. Bessonov, G. Harauz, Mumdooh Ahmed, 2012, Biochemistry.