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Accounts of Chemical Research, ISSN 0001-4842, 09/2006, Volume 39, Issue 9, pp. 671 - 679
With some exceptions, amyloids appear to be accidental aggregated structures whose formation was not selected for in molecular evolution. Despite this, amyloid... 
MUTAGENESIS | FRAGMENTS | MECHANISM | POLYGLUTAMINE AGGREGATION NUCLEATION | ELONGATION | DISEASE | ENERGETICS | BETA-PROTEIN | CHEMISTRY, MULTIDISCIPLINARY | Thermodynamics | Amyloid - chemistry | Kinetics | Glycoproteins | Research | Structure | Properties | Protein folding
Journal Article
1970, Emily Chamberlain Cook contest, Volume 1969-1970, [3] leaves.
Book
2006, Methods in enzymology, ISBN 9780121828189, Volume 413., xxxvi, 375
The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a... 
Amyloid | Prions | Amyloid beta-protein | Amyloid beta-Peptides
Book
2006, Methods in enzymology, ISBN 0121828174, Volume 412., xl, 403
The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a... 
Amyloid | Prions | Amyloid beta-protein | Amyloid beta-Peptides
Book
Current Opinion in Structural Biology, ISSN 0959-440X, 02/2007, Volume 17, Issue 1, pp. 48 - 57
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 08/2010, Volume 401, Issue 3, pp. 503 - 517
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 04/2014, Volume 289, Issue 15, pp. 10254 - 10260
Journal Article
Neuron, ISSN 0896-6273, 12/2009, Volume 64, Issue 6, pp. 828 - 840
The N-terminal 17 amino acids of huntingtin (NT17) can be phosphorylated on serines 13 and 16; however, the significance of these modifications in Huntington's... 
humdisease | molneuro | NEURONAL INTRANUCLEAR INCLUSIONS | NUCLEAR | PHOSPHORYLATION | EXPANSION | NEURODEGENERATION | TOXICITY | PATHOLOGY | TRANSGENIC MOUSE MODEL | NEUROSCIENCES | AGGREGATION | TRINUCLEOTIDE REPEAT | Molecular Weight | Humans | Nerve Degeneration - physiopathology | Nerve Degeneration - genetics | Alanine - chemistry | Amino Acid Sequence - genetics | Nerve Degeneration - metabolism | Aspartic Acid - genetics | Nerve Tissue Proteins - chemistry | Alanine - genetics | Amyloid - metabolism | Nuclear Proteins - genetics | Huntington Disease - physiopathology | Disease Models, Animal | Amyloid - genetics | Genetic Predisposition to Disease - genetics | Gene Expression Regulation - genetics | Serine - genetics | Alanine - metabolism | Mice, Transgenic | Protein Structure, Tertiary - genetics | Mutation - genetics | Nuclear Proteins - chemistry | Serine - chemistry | Huntington Disease - metabolism | Nerve Tissue Proteins - genetics | Serine - metabolism | Huntingtin Protein | Phenotype | Animals | Huntington Disease - genetics | Trinucleotide Repeat Expansion - genetics | Amino Acid Substitution - genetics | Aspartic Acid - metabolism | Mice | Aspartic Acid - chemistry | Proteins | Medical colleges | Alanine | Nervous system diseases | Neurosciences | Huntington's chorea | Neurons | Physiological aspects | Aspartate | Huntingtons disease | Phosphorylation | Neurodegeneration | Pathogenesis | Neuropathology | Rodents | Mutation
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 04/2009, Volume 16, Issue 4, pp. 380 - 389
Journal Article