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- Currently displaying 1661 - 1680 of 2456 publications
Towards quantitative predictions in cell biology using chemical properties of proteins
FEBS JOURNAL
(2009)
276
12
Protein misfolding and disease: from the test tube to the organism
JOURNAL OF NEUROCHEMISTRY
(2009)
110
35
Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins
Proceedings of the National Academy of Sciences of the United States of America
(2009)
106
10159
(doi: 10.1073/pnas.0812414106)
Bridging the gap: From protein misfolding to protein misfolding diseases
FEBS Letters
(2009)
583
2581
Competition between Intramolecular and Intermolecular Interactions in an Amyloid-Forming Protein
Journal of Molecular Biology
(2009)
389
776
(doi: 10.1016/j.jmb.2009.04.042)
Biosensor-based label-free assays of amyloid growth.
FEBS letters
(2009)
583
2587
Probing side-chain dynamics of a ribosome-bound nascent chain using methyl NMR spectroscopy
J Am Chem Soc
(2009)
131
8366
(doi: 10.1021/ja902778n)
Probing Protein Folding on the Ribosome by Solution State NMR Spectroscopy
J BIOMOL STRUCT DYN
(2009)
26
846
Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy.
J Mol Biol
(2009)
390
775
(doi: 10.1016/j.jmb.2009.05.066)
Amyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate
PLoS ONE
(2009)
4
e5562
(doi: 10.1371/journal.pone.0005562)
Position-dependent electrostatic protection against protein aggregation.
ChemBioChem
(2009)
10
1309
(doi: 10.1002/cbic.200900144)
Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.
Proceedings of the National Academy of Sciences of the United States of America
(2009)
106
7828
(doi: 10.1073/pnas.0812227106)
Use of protonless NMR spectroscopy to alleviate the loss of information resulting from exchange-broadening.
Journal of the American Chemical Society
(2009)
131
7222
(doi: 10.1021/ja902307q)
Physical principles of protein behavior in the cell.
J Proteome Res
(2009)
8
2615
(doi: 10.1021/pr900340d)
Folding of small proteins by Monte Carlo simulations with chemical shift restraints without the use of molecular fragment replacement or structural homology.
The journal of physical chemistry. B
(2009)
113
7890
(doi: 10.1021/jp900780b)
Chemical modification of proteins at cysteine: Opportunities in chemistry and biology
Chemistry an Asian Journal
(2009)
4
630
(doi: 10.1002/asia.200800427)
Competition between intramolecular and intermolecular interactions in an amyloid-forming protein.
Journal of Molecular Biology
(2009)
389
776
(doi: 10.1016/j.jmb.2009.04.042)
A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea
Protein Science
(2009)
11
2417
(doi: 10.1110/ps.0217702)
Combined approaches to the synthesis and study of glycoproteins
ACS Chemical Biology
(2009)
4
703
(doi: 10.1021/cb900014n)
“Protein Misfolding Diseases and the Key Role Played by the Interactions of Polypeptides with Water”, in Water and Biomolecules
(2009)