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Science, ISSN 0036-8075, 7/2009, Volume 325, Issue 5938, pp. 328 - 332
Amyloids are highly organized cross--β-sheet--rich protein or peptide aggregates that are associated with pathological conditions including Alzheimer's disease... 
Aggregation | Secretory vesicles | Neurons | Cell aggregates | Antibodies | Fluorescence | Reports | Amyloids | Hormones | Solar fibrils | Monomers | CELLS | PROTEIN | FIBRILS | GLYCOSAMINOGLYCANS | MOLECULAR-ORGANIZATION | PROLACTIN GRANULES | BIOGENESIS | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | ALPHA-SYNUCLEIN | AMYLOIDOGENESIS | Humans | Secretory Vesicles - metabolism | Neurons - cytology | Pituitary Gland - chemistry | Amyloid - chemistry | Pituitary Gland, Anterior - metabolism | Pituitary Hormones - chemistry | Peptide Hormones - metabolism | Urocortins - metabolism | beta-Endorphin - metabolism | Amyloid - metabolism | Neurons - physiology | Pituitary Hormones - metabolism | Peptide Hormones - chemistry | Adrenocorticotropic Hormone - metabolism | beta-Endorphin - chemistry | Secretory Vesicles - chemistry | Adrenocorticotropic Hormone - chemistry | Cell Survival | Pituitary Gland, Posterior - chemistry | Heparin, Low-Molecular-Weight - chemistry | Rats | Corticotropin-Releasing Hormone - chemistry | Urocortins - chemistry | Corticotropin-Releasing Hormone - metabolism | Animals | Pituitary Gland, Posterior - metabolism | Protein Conformation | Sheep | Mice | Pituitary Gland, Anterior - chemistry | Hydrogen-Ion Concentration | Glycoproteins | Research | Properties | Peptide hormones | Proteins | Pituitary gland | Physiology | Peptides | Cellular biology | Index Medicus | Medical and Health Sciences | MEDICINE | Medicin och hälsovetenskap | MEDICIN
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2008, Volume 380, Issue 2, pp. 425 - 436
Journal Article
Amyloid, ISSN 1350-6129, 10/2016, Volume 23, Issue 4, pp. 209 - 213
The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XVth Symposium of the Society, 3 July-7 July 2016, Uppsala, Sweden,... 
inclusion body | nomenclature | amyloidosis | Amyloid fibril | amyloid protein | MEDICINE, RESEARCH & EXPERIMENTAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSTHYRETIN AMYLOIDOSIS | MEDICINE, GENERAL & INTERNAL | TRANSMISSION | SEMEN | DISEASE | SENILE SYSTEMIC AMYLOIDOSIS | Staining and Labeling - methods | Prealbumin - genetics | Guidelines as Topic | Apolipoprotein C-III - chemistry | Protein Precursors - chemistry | Humans | Apolipoprotein C-III - metabolism | tau Proteins - metabolism | Amyloidosis - diagnosis | Amyloidogenic Proteins - chemistry | Apolipoprotein C-III - genetics | Apolipoprotein C-II - genetics | tau Proteins - chemistry | Sequence Analysis, Protein | tau Proteins - genetics | Amyloidosis - genetics | Amyloidosis - classification | Prealbumin - chemistry | alpha-Synuclein - genetics | Apolipoprotein C-II - chemistry | Amyloidogenic Proteins - genetics | Biomarkers - metabolism | Gene Expression | Protein Precursors - genetics | Amyloidosis - pathology | Terminology as Topic | Protein Precursors - metabolism | alpha-Synuclein - chemistry | Amyloidogenic Proteins - metabolism | Prealbumin - metabolism | Apolipoprotein C-II - metabolism | Birefringence | Congo Red - chemistry | alpha-Synuclein - metabolism | Coloring Agents - chemistry | Index Medicus | Basic Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | Medicinska och farmaceutiska grundvetenskaper | Cell and Molecular Biology | Cell- och molekylärbiologi
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2015, Volume 60, Issue 2, pp. 231 - 241
Phase-separated states of proteins underlie ribonucleoprotein (RNP) granules and nuclear RNA-binding protein assemblies that may nucleate protein inclusions... 
CELL-FREE FORMATION | PROTEIN | PHOSPHORYLATION | PRION-LIKE DOMAINS | PHASE-TRANSITIONS | TDP-43 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | FUS/TLS | ARGININE METHYLATION | ALPHA-SYNUCLEIN | CELL BIOLOGY | RNA-Binding Proteins - genetics | Humans | Molecular Sequence Data | RNA Polymerase II - metabolism | Cytoplasmic Granules - chemistry | Phase Transition | RNA-Binding Protein FUS - chemistry | Molecular Mimicry | Cytoplasmic Granules - metabolism | Escherichia coli - metabolism | Binding Sites | RNA Polymerase II - chemistry | RNA - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Prions - metabolism | Gene Expression | Rheology | RNA-Binding Proteins - chemistry | RNA-Binding Protein FUS - genetics | Recombinant Proteins - chemistry | RNA-Binding Protein FUS - metabolism | Recombinant Proteins - genetics | Prions - chemistry | RNA - chemistry | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | RNA Polymerase II - genetics | RNA-Binding Proteins - metabolism | Intrinsically Disordered Proteins - metabolism | Proteins | Nervous system diseases | Sarcoma | RNA | Physiological aspects | Fluorescence | Nuclear magnetic resonance spectroscopy | Molecular biology | Fluorescence microscopy | Cells | Protein binding | Analysis | Index Medicus
Journal Article
ACS Nano, ISSN 1936-0851, 01/2016, Volume 10, Issue 1, pp. 333 - 341
Journal Article
Nature Chemistry, ISSN 1755-4330, 10/2016, Volume 8, Issue 10, pp. 974 - 982
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Journal Article
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 04/2017, Volume 139, Issue 14, pp. 4971 - 4986
Posttranslational modification of proteins by ubiquitin (Ub), i.e., ubiquitination, mediates a variety of cellular processes, including protein homeostasis,... 
TOTAL CHEMICAL-SYNTHESIS | DEUBIQUITYLATING ENZYMES | PEPTIDE UBIQUITYLATION | SITE-SPECIFIC UBIQUITINATION | RECOMBINANT PROTEINS | POSTTRANSLATIONAL MODIFICATIONS | DIUBIQUITIN PROBES | ALPHA-SYNUCLEIN | NF-KAPPA-B | CHEMISTRY, MULTIDISCIPLINARY | DEUBIQUITINATING ENZYMES | Proteins | Molecular mechanics | Ubiquitin | Chemical properties | Research
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