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Education:
Dr. Shea received her B.Sc. in Chemistry from McGill University, Quebec in 1992 and her Ph.D. in physical chemistry from MIT in 1997. She pursued her postdoctoral studies at the Scripps Research Institute. After a year as an assistant professor of chemistry at the University of Chicago, Dr. Shea joined the faculty at UCSB in 2001.
Research:
Research Group Website: http://www.chem.ucsb.edu/~sheagroup/
Current Research
Research in the Shea group focuses on developing and applying the techniques of statistical and computational physics to the study of biological problems. Current work involves the investigation of cellular processes such as in-vivo protein folding and protein aggregation.
Please go to the Shea Group website for more information about the Shea group.
Publications:
Selected Research Publications
X. Wang, C. Wu, A. Vu, J.-E. Shea, F. W. Dahlquist, Computational and experimental analyses reveal the essential roles of inter-domain linkers in the biological function of chemotaxis histidine kinase CheA, J. Am. Chem. Soc. 2012 134:16107-16110.
W. W. Grabow, Z. Zhang. Z. N. Swank, J.-E. Shea, L. Jaeger, The right angle (RA) motif: A prevalent ribosomal RNA structural pattern found in group I introns, J. Mol. Biol. 2012 424:54-67.
A. Morris-Andrews, G. Bellesia, J.-E. Shea, ?-Sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation, J. Chem. Phys. 2012 137:145104.
C. Wu, J. Scott, J.-E. Shea, Binding of Congo red to amyloid protofibrils of the Alzheimer A?9-40 peptide probed by molecular dynamics simulations, Biophys. J. 2012 103:550-557.
L. Larini, J.-E. Shea, Role of ?-hairpin formation in aggregation: The self-assembly of the amyloid-?(25-35) peptide, Biophys. J. 2012 103:576-586.
L. Larini, J.-E. Shea, Coarse-grained modeling of simple molecules at different resolutions in the absence of good sampling., J. Phys. Chem. B 2012 116:8337-8349.
A. Morris-Andrews, J.-E. Shea, Kinetic pathways to peptide aggregation on surfaces: The effects of ?-sheet propensity and surface attraction, J. Chem. Phys. 2012 136:065103.
A. Morris-Andrews, G. Bellesia, J.-E. Shea, Effects of surfaces on peptide aggregate morphology., J. Chem. Phys. 2011 135:085102.
N. F. Dupuis, C. Wu,J.-E. Shea, M. T. Bowers, The Amyloid Formation Mechanism in Human IAPP: Dimers Have ?-Strand Monomer-Monomer Interfaces, J. Am. Chem. Soc. 2011 133:7240-7243.
G. Bellesia, A. I. Jewett, J.-E. Shea, Relative stability of de novo four-helix bundle proteins: Insights from coarse grained molecular simulations, Prot. Sci. 2011 20:818-826.
C. Wu, J.-E. Shea, Coarse-grained models for protein aggregation, Curr. Opin. Struct. Biol. 2011 21:209-220.
P. Jiang, W. Li, J.-E. Shea, Resveratrol inhibits the formation of multiple-layered ?-sheet oligomers of the human islet amyloid polypeptide segment 22-27, Biophys. J. 2011 100:1550-1558.
C. Wu, M. T. Bowers, J-E. Shea, On the Origin of the Stronger Binding of PIB over Thioflavin T to Protofibrils of the Alzheimer Amyloid-? Peptide: A Molecular Dynamics Study., Biophys. J. 2011 100:1316-1324.
Z. Zhuang, A. I. Jewett, S. Kuttimalai, G. Bellesia , S. Gnanakaran, J.-E. Shea, Assisted peptide folding by surface pattern recognition, Biophys. J. 2011 100:1306-1315.
Z. Zhuang, A. I. Jewett, S. Kuttimalai, G. Bellesia , S. Gnanakaran, _J.-E. Shea_, Assisted peptide folding by surface pattern recognition., /Biophys. J./, 100 *2011* 1306-1315.
C. Wu, M. T. Bowers, _J.-E. Shea_, On the origin of the stronger binding of PIB over thioflavin T to protofibrils of the Alzheimer amyloid-? peptide: A molecular dynamics study., /Biophys. J./, 100 *2011* 1316-1324.
P. Jiang, W. Li, _J.-E. Shea_, Resveratrol inhibits the formation of multiple-layered ?-sheet oligomers of the human islet amyloid polypeptide segment 22-27, /Biophys. J./, 100 *2011* 1550-1558.
C. Wu, _J.-E. Shea_, Coarse-grained models for protein aggregation., /Curr. Opin. Struct. Biol./, 21 *2011* 209-220.
G. Bellesia, A. I. Jewett, _J.-E. Shea_, Relative stability of de novo four-helix bundle proteins: Insights from coarse grained molecular simulations., /Prot. Sci./, 20 *2011* 818-826.
N. F. Dupuis, C. Wu, _J.-E. Shea_, M. T. Bowers, The Amyloid Formation Mechanism in Human IAPP: Dimers Have ?-Strand Monomer-Monomer Interfaces., /J. Am. Chem. Soc./, 133 *2011* 7240-7243.
A. Morris-Andrews, G. Bellesia, _J.-E. Shea_, Effects of surfaces on peptide aggregate morphology., /J. Chem. Phys./, 135 *2011* 085102.
A. Morris-Andrews, _J.-E. Shea_, Kinetic pathways to peptide aggregation on surfaces: The effects of ?-sheet propensity and surface attraction., /J. Chem. Phys./, 136 *2012* 065103.
L. Larini, _J.-E. Shea_, Coarse-grained modeling of simple molecules at different resolutions in the absence of good sampling., /J. Phys. Chem. B/, 116 *2012* 8337-8349.
L. Larini, _J.-E. Shea_, Role of ?-hairpin formation in aggregation: The self-assembly of the amyloid-?(25-35) peptide., /Biophys. J./, 103 *2012* 576-586.
C. Wu, J. Scott, _J.-E. Shea_, Binding of Congo red to amyloid protofibrils of the Alzheimer A?9-40 peptide probed by molecular dynamics simulations., /Biophys. J./, 103 *2012* 550-557.
A. Morris-Andrews, G. Bellesia, _J.-E. Shea_, ?-Sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation., /J. Chem. Phys./, 137 *2012* 145104.
W. W. Grabow, Z. Zhang. Z. N. Swank, _J.-E. Shea_, L. Jaeger, The right angle (RA) motif: A prevalent ribosomal RNA structural pattern found in group I introns., /J. Mol. Biol./ 424 *2012* 54-67.
X. Wang, C. Wu, A. Vu, _J.-E. Shea_, F. W. Dahlquist, Computational and experimental analyses reveal the essential roles of inter-domain linkers in the biological function of chemotaxis histidine kinase CheA., /J. Am. Chem. Soc./, 134 *2012* 16107-16110.
Molecular structures of quiescently-grown and brain-derived polymorphic fibrils of the Alzheimer amyloid A?9-40 peptide: A comparison to agitated fibrils. Wu, C.; Bowers, M. T.; Shea, J.-E. PLoS Comput. Biol. 2010, 6, e1000693
Sequence periodicity and secondary structure propensity in model proteins. Bellesia, G.; Jewett, A. I.; Shea, J.-E. Protein Sci. 2010, 19, 141-154.
Human islet amyloid polypeptide monomers form ordered ?-hairpins: A possible direct amyloidogenic precursor. Dupuis, N. F.; Wu, C.; Shea, J.-E.; Bowers, M. T. J. Am. Chem. Soc., 2009, 131, 18283-18292.
Reconciling theories of chaperonin accelerated folding with experimental evidence. Jewett, A. I.; Shea, J.-E. Cell. Mol. Life Sci. 2009, 67, 255?276.
Diversity of kinetic pathways in amyloid fibril formation. Bellesia, G.; Shea, J.-E. J. Chem. Phys. 2009, 131, 111102.
Reconciling theories of chaperonin accelerated folding with experimental evidence. Jewett, A. I.; Shea, J.-E. Cell. Mol. Life Sci. 2009, in press.
What determines the structure and stability of KFFE monomers, dimers, and protofibrils? Bellesia, G.; Shea, J.-E. Biophys. J. 2009, 96, 875-886.
The binding of thioflavin T and its neutral analog BTA-1 to protofibrils of the Alzheimer's disease AB16-22 peptide probed by molecular dynamics simulations. Wu, C.; Wang, Z. X.; Lei, H. X.; Duan, Y.; Bowers, M. T.; Shea, J.-E. J. Mol. Biol. 2008, 384, 718-729.
Effects of familial Alzheimer's disease mutations on the folding nucleation of the amyloid b-protein. Krone, M. G.; Baumketner, A.; Bernstein, S. L.; Wyttenbach, T.; Lazo, N. D.; Teplow, D. B.; Bowers, M. T.; Shea, J.-E. J. Mol. Biol. 2008, 381, 221-228.
Andrij Baumketner, Summer L. Bernstein, Thomas Wyttenbach, Gal Bitan, David B. Teplow, Michael T. Bowers, and Joan-Emma Shea, Structure of the 21-30 fragment of amyloid-beta protein, Prot. Sci., 2006, 15: 1239-1247.