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- Currently displaying 1741 - 1760 of 2393 publications
A PDZ domain recapitulates a unifying mechanism for protein folding
Proceedings of the National Academy of Sciences
(2007)
104
128
(doi: 10.1073/pnas.0602770104)
“Human Lysozyme” in Part B, Protein misfolding, aggregation and conformational diseases
(2007)
285
“Diseases of Protein Misfolding” in Genes and common diseases
(2007)
113
Analysis of structural order in amyloid fibrils
Nanotechnology
(2006)
18
044031
The determination of the structure of proteins in solution: lysozyme.
Ann N Y Acad Sci
(2006)
222
163
BPPred: A Web-based computational tool for predicting biophysical parameters of proteins
Protein science : a publication of the Protein Society
(2006)
16
125
(doi: 10.1110/ps.062383807)
Geometry, energetics, and dynamics of hydrogen bonds in proteins: structural information derived from NMR scalar couplings.
Journal of the American Chemical Society
(2006)
128
15127
(doi: 10.1021/ja0614722)
The application of high resolution nuclear magnetic resonance to biological systems
Methods of Biochemical Analysis
(2006)
25
1
(doi: 10.1002/9780470110454.ch1)
Characterization of the nanoscale properties of individual amyloid fibrils
Proceedings of the National Academy of Sciences USA
(2006)
103
15806
(doi: 10.1073/pnas.0604035103)
Recombinant amyloidogenic domain of ApoA-I:: Analysis of its fibrillogenic potential
Biochem Biophys Res Commun
(2006)
351
223
(doi: 10.1016/j.bbrc.2006.10.026)
Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes.
Biochemistry
(2006)
45
12806
(doi: 10.1021/bi0610653)
Dynamic Visions of Enzymatic Reactions
Science (New York, N.Y.)
(2006)
313
1586
(doi: 10.1126/science.1132851)
X-ray scattering study of the effect of hydration on the cross-beta structure of amyloid fibrils.
J Am Chem Soc
(2006)
128
11738
(doi: 10.1021/ja063751v)
Identification of the Core Structure of Lysozyme Amyloid Fibrils by Proteolysis
Journal of Molecular Biology
(2006)
361
551
(doi: 10.1016/j.imb.2006.06.055)
Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms
J Neurosci
(2006)
26
8160
Characterization of the residual structure in the unfolded state of the Delta 131 Delta fragment of staphylococcal nuclease
Proteins
(2006)
65
145
(doi: 10.1002/prot.21077)
Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions.
Chem Soc Rev
(2006)
35
908
(doi: 10.1039/b517761h)
Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants
Accounts of Chemical Research
(2006)
39
603
(doi: 10.1021/ar050070g)
