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Journal Article
Molecular Cell, ISSN 1097-2765, 10/2015, Volume 60, Issue 2, pp. 208 - 219
Eukaryotic cells possess numerous dynamic membrane-less organelles, RNP granules, enriched in RNA and RNA-binding proteins containing disordered regions. We... 
TRANSITION | EUKARYOTIC STRESS GRANULES | CELL-FREE FORMATION | PRION-LIKE DOMAINS | NUCLEOLI | BEHAVIOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | REGIONS | BODIES | P GRANULES | AGGREGATION | CELL BIOLOGY | Organelles - chemistry | Fluorescence Recovery After Photobleaching | Humans | Polyethylene Glycols - chemistry | Amyloid - chemistry | Cytoplasmic Granules - chemistry | Molecular Mimicry | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Solutions | Cytoplasmic Granules - metabolism | Escherichia coli - metabolism | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Protein Aggregation, Pathological - genetics | RNA - metabolism | Sodium Chloride - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amyloid - genetics | Gene Expression | Recombinant Proteins - chemistry | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Recombinant Proteins - genetics | RNA - chemistry | Intrinsically Disordered Proteins - genetics | Heterogeneous Nuclear Ribonucleoprotein A1 | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | Organelles - metabolism | Protein Aggregation, Pathological - metabolism | Intrinsically Disordered Proteins - metabolism | Fluorescence | Marine biology | Chemical properties | RNA | Binding proteins | Protein binding | Yuan (China) | Index Medicus
Journal Article
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
Cell, ISSN 0092-8674, 03/2017, Volume 168, Issue 6, pp. 1028 - 1040.e19
In eukaryotic cells, diverse stresses trigger coalescence of RNA-binding proteins into stress granules. In vitro, stress-granule-associated proteins can demix... 
membraneless organelle | RNA-binding protein | poly(A)-binding protein | intrinsically disordered protein | quinary structure | stress granules | heat shock | low-complexity region | energy depletion | pH | HEAT-STRESS | MESSENGER-RNAS | TEMPERATURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE | LIQUID DROPLETS | DISORDERED PROTEINS | TRANSITIONS | SACCHAROMYCES-CEREVISIAE | GRANULES | BINDING | CELL BIOLOGY | Amino Acid Sequence | Saccharomyces cerevisiae - physiology | Poly(A)-Binding Proteins - genetics | Proline - metabolism | Stress, Physiological | Hot Temperature | Saccharomyces cerevisiae Proteins - genetics | Cytoplasmic Granules - chemistry | Proline - analysis | Ribonucleases - metabolism | Saccharomyces cerevisiae - cytology | Sequence Alignment | Mutagenesis | Poly(A)-Binding Proteins - chemistry | Intrinsically Disordered Proteins - chemistry | Poly(A)-Binding Proteins - metabolism | Cytoplasmic Granules - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Domains | Saccharomyces cerevisiae - growth & development | Hydrogen-Ion Concentration | Intrinsically Disordered Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | RNA | Physiological aspects | Stress (Physiology) | Sensors | Molecular biology | Binding proteins | Protein binding | Stress (Psychology) | Index Medicus | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES | second messenger
Journal Article
Journal Article
Developmental Cell, ISSN 1534-5807, 07/2016, Volume 38, Issue 1, pp. 86 - 99
Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of... 
YEAST | KINASE COMPLEX | EARLY STEPS | MACHINERY | RECRUITS ATG9 | HORMA DOMAIN | MECHANISMS | DEVELOPMENTAL BIOLOGY | MICROSCOPY | SACCHAROMYCES-CEREVISIAE | ASSOCIATION | CELL BIOLOGY | Adaptor Proteins, Signal Transducing - chemistry | Protein Kinases - metabolism | Phosphorylation | Protein Kinases - genetics | Saccharomyces cerevisiae - genetics | Phagosomes - physiology | Protein Kinases - chemistry | Multiprotein Complexes - genetics | Autophagy | Autophagy-Related Proteins - chemistry | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Membrane Proteins - metabolism | Autophagy-Related Proteins - genetics | Amino Acid Sequence | Membrane Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Intrinsically Disordered Proteins - genetics | Sequence Homology, Amino Acid | Multiprotein Complexes - chemistry | Membrane Proteins - chemistry | Intrinsically Disordered Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Adaptor Proteins, Signal Transducing - metabolism | Autophagy-Related Proteins - metabolism | Saccharomyces cerevisiae - growth & development | Intrinsically Disordered Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 03/2017, Volume 65, Issue 6, pp. 1044 - 1055.e5
Liquid-liquid phase separation (LLPS) of RNA-binding proteins plays an important role in the formation of multiple membrane-less organelles involved in RNA... 
LLPS | hnRNP | intrinsically disordered protein | FUS | protein aggregation | low complexity domain | prion-like domain | phase transition | amyotrophic lateral sclerosis | frontotemporal lobar degeneration | RNA-BINDING PROTEINS | NEURODEGENERATIVE DISEASE | IN-VITRO | PRION-LIKE DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALS | LIQUID DROPLETS | C-TERMINAL DOMAIN | HEXANUCLEOTIDE REPEAT | GGGGCC REPEAT | NUCLEOCYTOPLASMIC TRANSPORT | CELL BIOLOGY | Phosphorylation | Humans | Poly-ADP-Ribose Binding Proteins | RNA Helicases | Transfection | Time Factors | Cytoplasmic Granules - metabolism | Eukaryotic Initiation Factor-2 - metabolism | Protein Domains | C9orf72 Protein | Dipeptides - metabolism | Lipid Droplets - metabolism | RNA Recognition Motif Proteins | RNA - metabolism | Cytoplasmic Granules - pathology | Amyotrophic Lateral Sclerosis - genetics | Dipeptides - chemistry | Arginine - chemistry | Carrier Proteins - genetics | Amyotrophic Lateral Sclerosis - pathology | DNA Helicases | Carrier Proteins - metabolism | Proteins - metabolism | Intrinsically Disordered Proteins - chemistry | Eukaryotic Initiation Factor-2 - genetics | Amyotrophic Lateral Sclerosis - metabolism | HeLa Cells | Proteins - chemistry | Arginine - metabolism | Intrinsically Disordered Proteins - metabolism | Physiological aspects | Amino acids | Neurosciences | RNA | Binding proteins | Protein binding | Arginine | Glutamine | Index Medicus
Journal Article
Journal Article