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Lancet Neurology, The, ISSN 1474-4422, 2014, Volume 13, Issue 2, pp. 150 - 158
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2010, Volume 107, Issue 5, pp. 2295 - 2300
Journal Article
Journal Article
Antioxidants & Redox Signaling, ISSN 1523-0864, 09/2017, Volume 27, Issue 9, pp. 567 - 582
Journal Article
Ricerca e Pratica, ISSN 1120-379X, 2000, Volume 16, Issue 4, pp. 144 - 152
Journal Article
Journal of Alzheimer's Disease, ISSN 1387-2877, 03/2018, Volume 62, Issue 3, pp. 1247 - 1259
Translational neuroscience integrates the knowledge derived by basic neuroscience with the development of new diagnostic and therapeutic tools that may be... 
Translation | Neurosciences | Disease | Neurodegenerative diseases | Disorders | Nervous system | Drug development | Neurological diseases | Biological effects | Molecular modelling | Diagnostic software | Biomarkers | Bioindicators | Diagnostic systems | Alzheimer's disease
Journal Article
International Journal of Molecular Sciences, ISSN 1422-0067, 09/2019, Volume 20, Issue 18, p. 4641
The pathological aggregation of amyloidogenic proteins is a hallmark of many neurological diseases, including Alzheimer’s disease and prion diseases. We have... 
amyloid-beta protein | Alzheimer’s disease | doxycycline | molecular dynamics | iododoxorubicin | curcumin
Journal Article
Journal Article
Science, ISSN 0036-8075, 3/2009, Volume 323, Issue 5920, pp. 1473 - 1477
Journal Article
1974, Monographs of the Mario Negri institute for pharmacological research, Milan, 226
Book
Chemistry – A European Journal, ISSN 0947-6539, 10/2014, Volume 20, Issue 42, pp. 13793 - 13800
By combining NMR spectroscopy, transmission electron microscopy, and circular dichroism we have identified the structural determinants involved in the... 
structure–activity relationship | molecular recognition | circular dichroism | NMR spectroscopy | amyloid peptides | Molecular recognition | Amyloid peptides | Structure-activity relationship | Circular dichroism | structure-activity relationship | Ataxin-3 | Humans | Neurodegenerative Diseases - prevention & control | Molecular Sequence Data | Biological Products - pharmacology | Nerve Tissue Proteins - chemistry | Protein Aggregation, Pathological - prevention & control | Amyloid beta-Peptides - metabolism | Nuclear Magnetic Resonance, Biomolecular | Flavonoids - pharmacology | Catechin - pharmacology | Repressor Proteins - metabolism | Amino Acid Sequence | Prions - metabolism | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Neurodegenerative Diseases - metabolism | Prions - chemistry | Nuclear Proteins - chemistry | Nerve Tissue Proteins - metabolism | Biological Products - chemistry | Peptide Fragments - chemistry | Amyloid beta-Peptides - chemistry | Flavonoids - chemistry | Catechin - chemistry | Protein Aggregation, Pathological - metabolism | Tea - chemistry | Amyloidogenesis | Neurodegenerative diseases | Proteins | Neurological diseases | Oligomers | Magnetic resonance spectroscopy | Tea | Catechins | Transmission electron microscopy | Ataxin | Dichroism | Amyloid | Green tea
Journal Article