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- Currently displaying 1821 - 1840 of 2486 publications
The Distribution of Residues in a Polypeptide Sequence Is a Determinant of Aggregation Optimized by Evolution
Biophysical Journal
(2007)
93
4382
(doi: 10.1529/biophysj.107.111336)
COMP 492-Caught in atomistic detailed action: Modeling of protein-G monomers forming oligomers
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2007)
234
Magnetic-phase transitions of ising surfaces with modified surface-bulk coupling: A Monte Carlo study
Europhysics Letters (EPL)
(2007)
20
547
(doi: 10.1209/0295-5075/20/6/013)
Molecular dynamics simulations from putative transition states of α‐spectrin SH3 domain
Proteins Structure Function and Bioinformatics
(2007)
69
536
(doi: 10.1002/prot.21491)
Mechanism of Hsp70's inhibition of alpha synuclein fibrillation
FEBS JOURNAL
(2007)
274
262
Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alpha A-, alpha beta- and R120G alpha B-Crystallins
J Mol Biol
(2007)
372
470
(doi: 10.1016/j.jmb.2007.06.060)
Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass
Proc Natl Acad Sci U S A
(2007)
104
10016
(doi: 10.1073/pnas.0610659104)
Protein structure determination from NMR chemical shifts.
Proceedings of the National Academy of Sciences
(2007)
104
9615
(doi: 10.1073/pnas.0610313104)
Life on the edge: a link between gene expression levels and aggregation rates of human proteins.
Trends Biochem Sci
(2007)
32
204
(doi: 10.1016/j.tibs.2007.03.005)
The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
The FASEB Journal
(2007)
21
2312
(doi: 10.1096/fj.06-7986com)
The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.
Journal of Molecular Biology
(2007)
369
157
(doi: 10.1016/j.jmb.2007.02.095)
Prediction of Local Structural Stabilities of Proteins from Their Amino Acid Sequences
Structure
(2007)
15
139
(doi: 10.1016/j.str.2006.12.007)
Determination of conformationally heterogeneous states of proteins.
Curr Opin Struct Biol
(2007)
17
15
(doi: 10.1016/j.sbi.2007.01.002)
The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins
Journal of biomolecular NMR
(2007)
37
117
(doi: 10.1007/s10858-006-9117-7)
A PDZ domain recapitulates a unifying mechanism for protein folding
Proceedings of the National Academy of Sciences
(2007)
104
128
(doi: 10.1073/pnas.0602770104)
“Diseases of Protein Misfolding” in Genes and common diseases
(2007)
113
