Joan-Emma Shea
Joan-Emma Shea
確認したメール アドレス: ucsb.edu
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引用先
引用先
Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
SL Bernstein, NF Dupuis, ND Lazo, T Wyttenbach, MM Condron, G Bitan, ...
Nature chemistry 1 (4), 326-331, 2009
8562009
FROM FOLDING THEORIES TO FOLDING PROTEINS: A Review and Assessment of Simulation Studies of Protein Folding and Unfolding
JE Shea, CL Brooks III
Annual review of physical chemistry 52 (1), 499-535, 2001
5742001
Amyloid β-Protein:  Monomer Structure and Early Aggregation States of Aβ42 and Its Pro19 Alloform
SL Bernstein, T Wyttenbach, A Baumketner, JE Shea, G Bitan, DB Teplow, ...
Journal of the American Chemical Society 127 (7), 2075-2084, 2005
3872005
Amyloid β‐protein monomer structure: A computational and experimental study
A Baumketner, SL Bernstein, T Wyttenbach, G Bitan, DB Teplow, ...
Protein Science 15 (3), 420-428, 2006
2762006
Elucidating amyloid β-protein folding and assembly: a multidisciplinary approach
DB Teplow, ND Lazo, G Bitan, S Bernstein, T Wyttenbach, MT Bowers, ...
Accounts of chemical research 39 (9), 635-645, 2006
2512006
Exploring the origins of topological frustration: design of a minimally frustrated model of fragment B of protein A
JE Shea, JN Onuchic, CL Brooks
Proceedings of the National Academy of Sciences 96 (22), 12512-12517, 1999
2401999
Human islet amyloid polypeptide monomers form ordered β-hairpins: a possible direct amyloidogenic precursor
NF Dupuis, C Wu, JE Shea, MT Bowers
Journal of the American Chemical Society 131 (51), 18283-18292, 2009
2062009
The amyloid formation mechanism in human IAPP: dimers have β-strand monomer− monomer interfaces
NF Dupuis, C Wu, JE Shea, MT Bowers
Journal of the American Chemical Society 133 (19), 7240-7243, 2011
2012011
Coarse-grained models for protein aggregation
C Wu, JE Shea
Current opinion in structural biology 21 (2), 209-220, 2011
1882011
Role of water in mediating the assembly of Alzheimer amyloid-β Aβ16− 22 protofilaments
MG Krone, L Hua, P Soto, R Zhou, BJ Berne, JE Shea
Journal of the American Chemical Society 130 (33), 11066-11072, 2008
1872008
Effects of solvent on the structure of the Alzheimer amyloid-β (25–35) peptide
G Wei, JE Shea
Biophysical journal 91 (5), 1638-1647, 2006
1702006
Probing the folding free energy landscape of the src-SH3 protein domain
JE Shea, JN Onuchic, CL Brooks
Proceedings of the National Academy of Sciences 99 (25), 16064-16068, 2002
1672002
Structure of the 21–30 fragment of amyloid β‐protein
A Baumketner, SL Bernstein, T Wyttenbach, ND Lazo, DB Teplow, ...
Protein Science 15 (6), 1239-1247, 2006
1592006
The structure of the Alzheimer amyloid β 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent
A Baumketner, JE Shea
Journal of molecular biology 366 (1), 275-285, 2007
1462007
The binding of thioflavin T and its neutral analog BTA-1 to protofibrils of the Alzheimer’s disease Aβ16–22 peptide probed by molecular dynamics simulations
C Wu, Z Wang, H Lei, Y Duan, MT Bowers, JE Shea
Journal of molecular biology 384 (3), 718-729, 2008
1412008
Computational studies of protein aggregation: methods and applications
A Morriss-Andrews, JE Shea
Annual review of physical chemistry 66, 643-666, 2015
1342015
Regulation and aggregation of intrinsically disordered peptides
ZA Levine, L Larini, NE LaPointe, SC Feinstein, JE Shea
Proceedings of the National Academy of Sciences 112 (9), 2758-2763, 2015
1322015
Binding of Congo red to amyloid protofibrils of the Alzheimer Aβ9–40 peptide probed by molecular dynamics simulations
C Wu, J Scott, JE Shea
Biophysical journal 103 (3), 550-557, 2012
1312012
Effects of confinement in chaperonin assisted protein folding: rate enhancement by decreasing the roughness of the folding energy landscape
A Baumketner, A Jewett, JE Shea
Journal of molecular biology 332 (3), 701-713, 2003
1232003
Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway
AI Jewett, A Baumketner, JE Shea
Proceedings of the National Academy of Sciences 101 (36), 13192-13197, 2004
1212004
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