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- Currently displaying 1761 - 1780 of 2399 publications
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-β structure of amyloid fibrils
Journal of the American Chemical Society
(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
Journal of Neuroscience
(2006)
26
8160
Characterization of the residual structure in the unfolded state of the Delta 131 Delta fragment of staphylococcal nuclease
Proteins Structure Function and Bioinformatics
(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 lyspzyme and its amyloidogenic variants
Accounts of Chemical Research
(2006)
39
603
(doi: 10.1021/ar050070g)
Relation between native ensembles and experimental structures of proteins
Proceedings of the National Academy of Sciences of the United States of America
(2006)
103
10901
(doi: 10.1073/pnas.0511156103)
Functionalised fibrils for bio-nanotechnology
2006 International Conference on Nanoscience and Nanotechnology
(2006)
214
(doi: 10.1109/ICONN.2006.340589)
“The Generic Nature of Protein Folding and Misfolding”, in Protein misfolding, aggregation and conformational diseases
(2006)
21
Spatial persistence of angular correlations in amyloid fibrils
Phys Rev Lett
(2006)
96
238301
Enhanced stability of human prion proteins with two disulfide bridges
Biophys J
(2006)
91
1494
(doi: 10.1529/biophysj.106.081653)
Protein misfolding, functional amyloid, and human disease.
Annu Rev Biochem
(2006)
75
333
The direct formation of glycosyl thiols from reducing sugars allows one-pot protein glycoconjugation
Angew Chem Int Ed Engl
(2006)
45
4007
(doi: 10.1002/anie.200600685)
A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank.
BMC Ecology and Evolution
(2006)
6
43
(doi: 10.1186/1471-2148-6-43)
Apomyoglobin reveals a random-nucleation mechanism in amyloid protofibril formation.
Acta Histochemica
(2006)
108
215
(doi: 10.1016/j.acthis.2006.03.012)
The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner
J Mol Biol
(2006)
360
497
(doi: 10.1016/j.jmb.2006.05.007)
Folding and Fibril Formation of the Cell Cycle Protein Cks1*
J Biol Chem
(2006)
281
18816
(doi: 10.1074/jbc.m603628200)
Expanding to fill the gap: A possible role for inert biopolymers in regulating the extent of the ‘macromolecular crowding’ effect
FEBS Letters
(2006)
580
2584
