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Journal of Molecular Biology, ISSN 0022-2836, 01/2016, Volume 428, Issue 2, pp. 274 - 291
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 01/2016, Volume 428, Issue 2, p. 274
A[beta].sub.43, a product of the proteolysis of the amyloid precursor protein APP, is related to A[beta].sub.42 by an additional Thr residue at the C-terminus.... 
Amino acids | Proteolysis | Alzheimer's disease | Amyloid beta-protein | Hydrogen
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 08/2010, Volume 401, Issue 3, pp. 503 - 517
Journal Article
Biopolymers, ISSN 0006-3525, 03/2014, Volume 102, Issue 2, pp. 206 - 221
Many amyloidogenic peptides are highly hydrophobic, introducing significant challenges to obtaining high quality peptides by chemical synthesis. For example,... 
Journal Article
Methods in Molecular Biology, ISSN 1064-3745, 2018, Volume 1777, pp. 121 - 144
The red shift in the fluorescence excitation spectra of thioflavin dyes upon binding to fibrils has been a boon to the amyloid field, offering simple and... 
Nucleation | Thioflavin T | Centrifugation | Fibrils | Assembly intermediates | Amyloid | Oligomer | Elongation | HPLC | Polymorphic | Protein Aggregates | Data Interpretation, Statistical | Protein Multimerization | Benzothiazoles - chemistry | Amyloid - chemistry | Chromatography, High Pressure Liquid | Protein Aggregation, Pathological
Journal Article
Peptide Science, ISSN 0006-3525, 03/2014, Volume 102, Issue 2, pp. 206 - 221
Journal Article
JOURNAL OF VIROLOGY, ISSN 0022-538X, 08/2019, Volume 93, Issue 16
The host structural maintenance of chromosomes 5/6 complex (Smc5/6) suppresses hepatitis B virus (HBV) transcription. HBV counters this restriction by... 
DISULFIDE BONDS | UBIQUITIN LIGASE | hepatitis B virus | HBX PROTEIN | INTRACELLULAR ZINC | MASS-SPECTROMETRY | DDB1 | VIROLOGY | GENE | Smc5/6 complex | STRUCTURAL BASIS | AMINO-ACIDS | TRANSACTIVATION | EXCHANGE | HBx | Index Medicus
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 08/2010, Volume 401, Issue 3, p. 503
The ability of a single polypeptide sequence to grow into multiple stable amyloid fibrils sets these aggregates apart from most native globular proteins. The... 
Proteins | Zinc compounds | Nervous system diseases | Analysis | Alzheimer's disease
Journal Article
Nature Communications, 08/2016, Volume 7, p. 12419
  Since early oligomeric intermediates in amyloid assembly are often transient and difficult to distinguish, characterize and quantify, the mechanistic basis... 
Journal Article
01/2014, ISBN 9781321615579
The presence in patient's brain tissues of neuritic plaques containing Aβ aggregates is one of the pathological hallmarks of Alzheimer's disease (AD), and Aβ... 
Biochemistry | Biophysics
Dissertation
Journal of molecular biology, 08/2010, Volume 401, Issue 3, p. 503
The ability of a single polypeptide sequence to grow into multiple stable amyloid fibrils sets these aggregates apart from most native globular proteins. The... 
Thermodynamics | Protein Structure, Secondary | Humans | Protein Conformation - drug effects | Amyloid - chemistry | Amyloid beta-Peptides - chemistry | Protein Stability | Zinc - pharmacology | Alzheimer Disease
Journal Article
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