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- Currently displaying 1841 - 1860 of 2456 publications
Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties.
Biochimica et biophysica acta
(2005)
1764
452
(doi: 10.1016/j.bbapap.2005.10.021)
Rationalising Lysozyme Amyloidosis: Insights from the Structure and Solution Dynamics of T70N Lysozyme
Journal of Molecular Biology
(2005)
352
823
(doi: 10.1016/j.jmb.2005.07.040)
Transition state contact orders correlate with protein folding rates.
J Mol Biol
(2005)
352
495
(doi: 10.1016/j.jmb.2005.06.081)
Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.
Biophysical journal
(2005)
89
4201
(doi: 10.1529/biophysj.105.068726)
Effective interactions between chaotropic agents and proteins
Proteins: Structure, Function, and Bioinformatics
(2005)
61
492
(doi: 10.1002/prot.20626)
Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR.
ChemBioChem
(2005)
6
1619
(doi: 10.1002/cbic.200500196)
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates.
Journal of Molecular Biology
(2005)
351
910
(doi: 10.1016/j.jmb.2005.06.043)
Form of growing strings - art. no. 098103
Physical Review Letters
(2005)
95
098103
Determination of the folding transition states of barnase by using Phi(I)-value-restrained simulations validated by double mutant Phi(IJ)-values
Proc Natl Acad Sci U S A
(2005)
102
12389
(doi: 10.1073/pnas.0408226102)
Oxidative refolding of amyloidogenic variants of human lysozyme
J Mol Biol
(2005)
351
662
(doi: 10.1016/j.jmb.2005.06.035)
A toy model for predicting the rate of amyloid formation from unfolded protein.
Journal of Molecular Biology
(2005)
351
195
(doi: 10.1016/j.jmb.2005.05.013)
Interpreting Dynamically-Averaged Scalar Couplings in Proteins
Journal of biomolecular NMR
(2005)
32
273
(doi: 10.1007/s10858-005-8873-0)
Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation.
Structure
(2005)
13
1143
(doi: 10.1016/j.str.2005.04.022)
Rational design of aggregation-resistant bioactive peptides: Reengineering human calcitonin
Proceedings of the National Academy of Sciences of the United States of America
(2005)
102
10105
(doi: 10.1073/pnas.05012151102)
Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
Journal of molecular biology
(2005)
350
379
(doi: 10.1016/j.jmb.2005.04.016)
Protein misfolding and human disease: what we have learned from 50 years of protein science
FEBS JOURNAL
(2005)
272
1
Frontiers in computational biophysics: A symposium in honor of Martin Karplus
Structure
(2005)
13
949
(doi: 10.1016/j.str.2005.06.003)
Self-assembly of a globular protein into native-like and enzymatically active aggregates that subsequently reorganize to form amyloid structures
FEBS JOURNAL
(2005)
272
493
Fibril formation and aggregation of a model protein can proceed from different structural conformations of the partially unfolded state
FEBS JOURNAL
(2005)
272
366
