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- Currently displaying 1881 - 1900 of 2486 publications
Structure of the regulatory apparatus of a calcium-dependent protein kinase (CDPK): a novel mode of calmodulin-target recognition.
J Mol Biol
(2005)
357
400
(doi: 10.1016/j.jmb.2005.11.093)
The importance of sequence diversity in the aggregation and evolution of proteins
Nature
(2005)
438
878
(doi: 10.1038/nature04195)
Amyloid fibril formation by bovine milk κ-casein and its inhibition by the molecular chaperones αs- and β-casein
Biochemistry
(2005)
44
17027
(doi: 10.1021/bi051352r)
Probing the pressure–temperature stability of amyloid fibrils provides new insights into their molecular properties
Biochimica Et Biophysica Acta Proteins and Proteomics
(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
Journal of Molecular Biology
(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.
J Mol Biol
(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.
J Mol Biol
(2005)
351
195
(doi: 10.1016/j.jmb.2005.05.013)
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)
Interpreting dynamically-averaged scalar couplings in proteins
J Biomol NMR
(2005)
32
273
(doi: 10.1007/s10858-005-8873-0)
Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin.
Proceedings of the National Academy of Sciences
(2005)
102
10105
(doi: 10.1073/pnas.0501215102)
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
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