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- Currently displaying 1881 - 1900 of 2520 publications
Recombinant amyloidogenic domain of ApoA-I: Analysis of its fibrillogenic potential
Biochemical and Biophysical Research Communications
(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)
CARB 97-One-pot direct protein glycosylation
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2006)
232
X-ray Scattering Study of the Effect of Hydration on the Cross-β 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.
J Mol Biol
(2006)
361
551
(doi: 10.1016/j.imb.2006.06.055)
Prefibrillar amyloid aggregates could be generic toxins in higher organisms
The Journal of Neuroscience
(2006)
26
8160
Characterization of the residual structure in the unfolded state of the Δ131Δ 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.
Chemical Society reviews
(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)
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.
Physical review letters
(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
Annual review of biochemistry
(2006)
75
333
The Direct Formation of Glycosyl Thiols from Reducing Sugars Allows One‐Pot Protein Glycoconjugation
Angewandte Chemie (International ed. in English)
(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 Histochem
(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
Journal of molecular biology
(2006)
360
497
(doi: 10.1016/j.jmb.2006.05.007)
