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BIOSCIENCE REPORTS, ISSN 0144-8463, 03/2019, Volume 39, Issue 3
A recent study published in Bioscience Reports by Sheng et al. (Bioscience Reports, (2019) 39, pii: BSR20182345] described a small but significant... 
FIBER FORMATION | AMYLOID-BETA | BIOCHEMISTRY & MOLECULAR BIOLOGY | IONS | COPPER | IRON | ALZHEIMERS | ZINC | CELL BIOLOGY | Binding | Amyloidogenesis | Glycosaminoglycans | Accessibility | Self-association | Pathogenesis | Metal concentrations | Agglomeration | Zinc | Cofactors | Golgi apparatus | Proteins | Heparin | Kinetics | Protein interaction | Metal ions
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2018, Volume 13, Issue 10, p. e0206167
Immunoglobulin light chain amyloidosis is the most common form of systemic amyloidosis. However, very little is known about the underlying mechanisms that... 
SELF-ASSOCIATION | CIRCULAR-DICHROISM | PROTEIN | STABILITY | MULTIDISCIPLINARY SCIENCES | SEQUENCE | TRAFFICKING | AMYLOID FIBRIL FORMATION | PEPTIDE | FIBRILLOGENICITY | Cell Line | Protein Structure, Secondary | Myocytes, Cardiac - immunology | Humans | Immunoglobulin Variable Region - chemistry | Immunoglobulin Light-chain Amyloidosis - diagnosis | Immunoglobulin Light Chains - isolation & purification | Rats | Recombinant Proteins - chemistry | Periplasm - immunology | Immunoglobulin Light Chains - chemistry | Immunoglobulin Light Chains - genetics | Recombinant Proteins - isolation & purification | Microscopy, Confocal | Animals | Immunoglobulin Variable Region - isolation & purification | Escherichia coli - genetics | Immunoglobulin Variable Region - genetics | Escherichia coli - growth & development | Immunoglobulin Light-chain Amyloidosis - immunology | Myocytes, Cardiac - ultrastructure | Proteins | Amyloidosis | Analysis | Immunoglobulin G | Escherichia coli | Chromatography | Usage | Fluorescent proteins | Research | Health aspects | Amyloidogenesis | Peptides | Toxicity | Pathogenesis | Multiple myeloma | Fluorescence | Cytotoxicity | Amino acids | Chains | Confocal microscopy | Biochemistry | Biology | E coli | Light | Periplasmic space | Biocompatibility | Localization | Dimerization | Recombinant | Urine | Immunoglobulins | Purification | Computer simulation | Cardiomyocytes | Patients | Domains | Microscopy | Internalization | Dimers | Mutation | Protein interaction
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2018, Volume 114, Issue 3, pp. 172a - 172a
Journal Article
International Journal of Molecular Sciences, ISSN 1661-6596, 05/2018, Volume 19, Issue 5, p. 1357
Journal Article
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 06/2008, Volume 130, Issue 25, pp. 7873 - 7881
Journal Article
Scientific Reports, ISSN 2045-2322, 05/2017, Volume 7, Issue 1, p. 45224
Aortic medial amyloid is the most prevalent amyloid found to date, but remarkably little is known about it. It is characterised by aberrant deposition of a 5.4... 
Amyloidogenesis | Nucleation | Nuclear magnetic resonance--NMR | β-Amyloid | Aorta | Bioinformatics | Arteries
Journal Article
The Journal of thoracic and cardiovascular surgery, ISSN 0022-5223, 09/2019
To explore the micromechanical, biochemical, and microstructural differences between bicuspid aortic valve aneurysm (BAV-A) and tricuspid aortic valve... 
Journal Article
Journal Article
Journal Article
Amyloid, ISSN 1350-6129, 07/2019, Volume 26, Issue 3, pp. 148 - 155
Journal Article