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- Currently displaying 1721 - 1740 of 2336 publications
Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties.
Biochim Biophys 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
Biophys J
(2005)
89
4201
(doi: 10.1529/biophysj.105.068726)
Effective interactions between chaotropic agents and proteins.
Proteins
(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 : a European journal of chemical biology
(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)
Determination of the folding transition states of barnase by using ΦI-value-restrained simulations validated by double mutant ΦIJ-values
Proceedings of the National Academy of Sciences
(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 (London, England : 1993)
(2005)
13
1143
(doi: 10.1016/j.str.2005.04.022)
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)
Rational design of aggregation-resistant bioactive peptides: Reengineering human calcitonin
Proceedings of the National Academy of Sciences
(2005)
102
10105
(doi: 10.1073/pnas.05012151102)
Protein misfolding and human disease: what we have learned from 50 years of protein science
FEBS JOURNAL
(2005)
272
1
Fibril formation and aggregation of a model protein can proceed from different structural conformations of the partially unfolded state
FEBS JOURNAL
(2005)
272
366
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
Frontiers in computational biophysics: A symposium in honor of Martin Karplus
Structure
(2005)
13
949
(doi: 10.1016/j.str.2005.06.003)