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- Currently displaying 1661 - 1680 of 2403 publications
Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance
Protein Science
(2008)
5
2583
(doi: 10.1002/pro.5560051221)
Protein engineering as a strategy to avoid formation of amyloid fibrils.
Protein science : a publication of the Protein Society
(2008)
9
1700
(doi: 10.1110/ps.9.9.1700)
Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation
Protein Sci
(2008)
10
879
(doi: 10.1110/ps.42401)
The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments.
Protein Science
(2008)
5
693
(doi: 10.1002/pro.5560050414)
Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB
Protein science : a publication of the Protein Society
(2008)
8
1350
(doi: 10.1110/ps.8.6.1350)
A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding.
Protein Science
(2008)
10
1216
(doi: 10.1110/ps.52801)
Selective association of protein molecules followed by mass spectrometry
Protein Science
(2008)
8
1368
(doi: 10.1110/ps.8.6.1368)
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
Protein science : a publication of the Protein Society
(2008)
6
1316
(doi: 10.1002/pro.5560060620)
Analysis of the interactions between streptokinase domains and human plasminogen.
Protein Science
(2008)
7
2190
(doi: 10.1002/pro.5560071017)
Competition between Folding, Native-State Dimerisation and Amyloid Aggregation in β-Lactoglobulin
Journal of molecular biology
(2008)
386
878
(doi: 10.1016/j.jmb.2008.12.038)
1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states.
Biomolecular NMR assignments
(2008)
3
29
(doi: 10.1007/s12104-008-9134-4)
Self-templated nucleation in peptide and protein aggregation
Physical Review Letters
(2008)
101
258101
Amyloid formation by globular proteins under native conditions
Nature Chemical Biology
(2008)
5
15
(doi: 10.1038/nchembio.131)
alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species.
Journal of Biological Chemistry
(2008)
284
4246
(doi: 10.1074/jbc.m807242200)
Determination of Protein Structures in the Solid State from NMR Chemical Shifts
Structure (London, England : 1993)
(2008)
16
1764
(doi: 10.1016/j.str.2008.10.016)
Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins
Proceedings of the National Academy of Sciences
(2008)
105
19241
(doi: 10.1073/pnas.0804774105)
Stochastic reconstruction of protein structures from effective connectivity profiles.
PMC Biophys
(2008)
1
5
(doi: 10.1186/1757-5036-1-5)
1H, 15N and 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli.
Biomol NMR Assign
(2008)
3
17
(doi: 10.1007/s12104-008-9130-8)
A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates
PLOS Computational Biology
(2008)
4
e1000222
(doi: 10.1371/journal.pcbi.1000222)
Structure determination of protein-protein complexes using NMR chemical shifts: case of an endonuclease colicin-immunity protein complex.
J Am Chem Soc
(2008)
130
15990
(doi: 10.1021/ja805258z)
