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Trends in Neurosciences, ISSN 0166-2236, 10/2019, Volume 42, Issue 10, pp. 693 - 708
Neurons require unique subcellular compartmentalization to function efficiently. Formed from proteins and RNAs through liquid–liquid phase separation,... 
LLPS | neurodegeneration | membraneless organelle | post-translational modification | RNA/RNP granule | RNA-BINDING PROTEINS | CELL-FREE FORMATION | IN-VITRO | LONG-TERM-MEMORY | SOLID-PHASE-TRANSITION | PRION-LIKE DOMAINS | NUCLEAR IMPORT RECEPTOR | AMYOTROPHIC-LATERAL-SCLEROSIS | SEPARATION | NEUROSCIENCES | STRESS GRANULES
Journal Article
Bioconjugate Chemistry, ISSN 1043-1802, 02/2018, Volume 29, Issue 2, pp. 335 - 342
Gene expression is used extensively to describe cellular characteristics and behaviors; however, most methods of assessing gene expression are unsuitable for... 
Journal Article
Methods in Molecular Biology, ISSN 1064-3745, 2018, Volume 1688, pp. 243 - 255
Important biological processes, including enzyme catalysis, signaling, and protein folding, proceed through lowly populated (<5%) states that elude structural... 
Encounter complex | Site-directed spin-labeling | Dark states | Transient interactions | NMR spectroscopy | Lowly populated states | Protein-protein interactions | Models, Molecular | Protein Binding | Protein Conformation | Magnetic Resonance Spectroscopy - methods
Journal Article
Methods in molecular biology (Clifton, N.J.), ISSN 1064-3745, 2018, Volume 1688, pp. 243 - 255
Important biological processes, including enzyme catalysis, signaling and protein folding, proceed through lowly populated (< 5%) states that elude structural... 
site-directed spin-labeling | transient interactions | lowly populated states | dark states | NMR spectroscopy | encounter complex | protein-protein interactions
Journal Article
Biochemistry, ISSN 0006-2960, 05/2014, Volume 53, Issue 19, pp. 3095 - 3105
Recent studies suggest that deposition of amyloid β (Aβ) into oligomeric aggregates and fibrils, hallmarks of Alzheimer’s disease, may be initiated by the... 
Peptide Fragments - chemistry | Peptide Fragments - metabolism | Threonine - chemistry | Protein Structure, Secondary | Humans | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Nuclear Magnetic Resonance, Biomolecular | Amyloid beta-Peptides - chemistry | Threonine - metabolism | Index Medicus
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
Journal Article
Nature Cell Biology, ISSN 1465-7392, 06/2018, Volume 20, Issue 6, pp. 635 - 637
Phase separation can build assemblies and regulate biological function. Two articles link specific forms of protein and RNA degradation to phase separation.... 
Proteins | Nervous system diseases | MicroRNA | Research | Slicing | Ribonucleic acid--RNA | Metals | Phase separation | MiRNA
Journal Article
Journal Article
Trends in Cell Biology, ISSN 0962-8924, 06/2018, Volume 28, Issue 6, pp. 420 - 435
Cellular compartments and organelles organize biological matter. Most well-known organelles are separated by a membrane boundary from their surrounding milieu.... 
RNA-BINDING PROTEINS | INTRINSICALLY DISORDERED PROTEINS | LOW-COMPLEXITY DOMAINS | NUCLEAR-PORE COMPLEX | AMYOTROPHIC-LATERAL-SCLEROSIS | MEMBRANE-LESS ORGANELLES | C-TERMINAL DOMAIN | FRONTOTEMPORAL LOBAR DEGENERATION | STRESS GRANULES | NUCLEOCYTOPLASMIC TRANSPORT | CELL BIOLOGY
Journal Article
Nature, ISSN 0028-0836, 12/2011, Volume 480, Issue 7376, pp. 268 - 272
Journal Article
Bioconjugate Chemistry, ISSN 1043-1802, 02/2018, Volume 29, Issue 2, p. 335
Gene expression is used extensively to describe cellular characteristics and behaviors; however, most methods of assessing gene expression are unsuitable for... 
Nuclear magnetic resonance--NMR | Nucleotide sequence | Fluorine | Fluorescence | Destructive testing | Hybridization | Nucleic acids | Ribonucleic acid--RNA | Gene expression | Nitroxide | Molecules | Historical account | Beacons | Lysis | Magnetism | Resonance | Chemical synthesis | Target detection | Conformation
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 05/2008, Volume 130, Issue 19, pp. 6145 - 6158
We combine molecular dynamics simulations and new high-field NMR experiments to describe the solution structure of the Aβ21–30 peptide fragment that may be... 
Journal Article
The EMBO Journal, ISSN 0261-4189, 10/2017, Volume 36, Issue 20, pp. 2951 - 2967
Neuronal inclusions of aggregated RNA‐binding protein fused in sarcoma (FUS) are hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS's... 
frontotemporal dementia | prion | intrinsically disordered protein | ribonucleoprotein granule | amyotrophic lateral sclerosis | NEURODEGENERATIVE DISEASE | PRION-LIKE DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISORDERED PROTEINS | AMYOTROPHIC-LATERAL-SCLEROSIS | WILD-TYPE FUS | CELL BIOLOGY | RNA-BINDING PROTEINS | CELL-FREE FORMATION | MOTOR-NEURON DEGENERATION | C-TERMINAL DOMAIN | STRESS GRANULES | RNA-Binding Protein FUS - chemistry | Cell Line | Amyotrophic Lateral Sclerosis - pathology | Phosphorylation | Magnetic Resonance Spectroscopy | Humans | Protein Conformation | Protein Processing, Post-Translational | RNA-Binding Protein FUS - metabolism | Protein Aggregation, Pathological | Frontotemporal Dementia - pathology | Cell culture | Salts | Yeast | Nuclear magnetic resonance--NMR | Self-association | Toxicity | DNA damage | Cytotoxicity | Agglomeration | Kinases | Complexity | Magnetic resonance spectroscopy | Proteins | FUS protein | Neurotoxicity | Post-translation | Dementia disorders | Deoxyribonucleic acid--DNA | Spectroscopy | Sarcoma | Therapeutic applications | Amyotrophic lateral sclerosis | Pharmacology | Ribonucleic acid--RNA | RNA-binding protein | DNA-dependent protein kinase | Phase separation | Frontotemporal dementia | Protein interaction | 60 APPLIED LIFE SCIENCES | Neuroscience | Protein Biosynthesis & Quality Control
Journal Article