个人简介
Julie Forman-Kay is a Senior Scientist in the Molecular Structure and Function Program at the Research Institute of The Hospital for Sick Children and a Professor in the Biochemistry Department at the University of Toronto. The major focus of her work has been to provide biological insights into how dynamic properties of proteins are related to function and methodological tools to enable better understanding of dynamic and disordered states. Her expertise is in using NMR and other biophysical and computational tools to study dynamic and disordered proteins and their interactions, including characterizing their dynamic complexes that are mediated by multivalent interactions. Approaches for calculating computational representations disordered state ensembles have been developed in her group. A related area of interest is the role of post-translational modification, such as phosphorylation and methylation, in regulating structural and binding properties in disordered states and dynamic complexes.
The Forman-Kay lab works on a number of projects of specific relevance to cancer and neurobiology. Most recently her lab has started to probe the role phase separation of disordered proteins in RNA processing bodies, a key regulatory process for neurological function. Her group also has a strong interest in CFTR, the cystic fibrosis transmembrane conductance regulator, particularly its cytoplasmic domains including the disordered regulatory R region. Her work is highly collaborative and has had significant impact, with widely recognized contributions to the fields of intrinsically disordered proteins, protein interaction domains, and CFTR structure, dynamics and interactions. She is co-chair of the CFTR Structure Consortium of the US Cystic Fibrosis Foundation Therapeutics. She is the recipient of the 2012 CSMB Jeanne Manery Fisher Memorial Lectureship and the 2013 Zellers Senior Scientist Award from Cystic Fibrosis Canada.
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Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity
P.A. Chong, H. Lin, J.L. Wrana and J.D. Forman-Kay
PNAS 107(43):18404-9 (2010)
Ensemble modeling of protein disordered states: experimental restraint contributions and validation
J.A. Marsh and J.D. Forman-Kay
Proteins 80(2):556-572 (2012)
Conformational Changes Relevant to Channel Activity and Folding within the NBD1 of CFTR
R.P. Hudson, P.A. Chong, I. Protassevitch, R. Vernon, H. Bihler, M. Mense, E. Noy, H. Senderowitz, P.J. Thomas, C. Brouillette and J.D. Forman-Kay
Journal of Biological Chemistry 287(34):28480-28494 (2012)
Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis
E.J. Stollar, H. Lin, A.R. Davidson, J.D. Forman-Kay
PLOS ONE, 7(12):e51282 (2012)
Characterization of disordered proteins with ENSEMBLE
M. Krzeminski and J.D. Forman-Kay
Bioinformatics, 29(3):398-399 (2013)
Allosteric Coupling between the Intracellular Coupling Helix 4 and Regulatory Sites of the First Nucleotide-binding Domain of CFTR
J.E. Dawson, P. Farber and J.D. Forman-Kay
PLoS One, 8(9):e74347 (2013)
Regulatory R region of the CFTR chloride channel is a dynamic integrator of phospho-dependent intra- and intermolecular interactions
Z. Bozoky, M. Krzeminski, R. Muhandiram, J. Birtley, A. Al-Zahrani, P.J. Thomas, R.A. Frizzell, R.C. Ford and J.D. Forman-Kay
Proc Natl Acad Sci USA, 110(47):E4427-36 (2013)
Interaction of the eukaryotic initiation factor 4E with 4E-BP2 at a dynamic bipartite interface
S. Lukhele, A. Bah, H. Lin, N. Sonenberg, J.D. Forman-Kay
Structure, 3;21(12):2186-96 (2013)