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Molecular Cell, ISSN 1097-2765, 10/2015, Volume 60, Issue 2, pp. 220 - 230
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
Cell, ISSN 0092-8674, 04/2016, Volume 165, Issue 3, pp. 643 - 655
Oncogenic activation of genes via point mutations occurs in 20%–30% of human cancers. The development of effective RAS inhibitors has been challenging,... 
rigosertib | RAS-binding domain | PI3K | MAPK | RAS | RAF | POINT MUTATIONS | BLADDER-CARCINOMA ONCOGENE | MUTANT | SELECTIVE INHIBITOR | ACTIVATION | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | KINASE | BINDING | TRANSFORMING PROPERTIES | CELL BIOLOGY | Glycine - analogs & derivatives | Phosphorylation | Humans | Molecular Sequence Data | ras Proteins - metabolism | Crystallography, X-Ray | Proto-Oncogene Proteins - chemistry | Sulfones - pharmacology | MAP Kinase Signaling System | Cell Cycle Proteins - chemistry | Pancreatic Neoplasms - drug therapy | Glycine - chemistry | Sulfones - chemistry | Nuclear Magnetic Resonance, Biomolecular | Dimerization | Glycine - administration & dosage | Protein-Serine-Threonine Kinases - metabolism | Proto-Oncogene Proteins B-raf - metabolism | Proto-Oncogene Proteins B-raf - chemistry | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | Models, Molecular | Sequence Alignment | Animals | Glycine - pharmacology | Signal Transduction - drug effects | Mice, Nude | Mice | Protein-Serine-Threonine Kinases - chemistry | Cell Transformation, Neoplastic - drug effects | RNA-Binding Proteins - metabolism | Sulfones - administration & dosage | Proteins | Medical colleges | Gene mutations | Protein binding | Jewish schools | Phosphotransferases
Journal Article
eLife, ISSN 2050-084X, 08/2014, Volume 3, Issue 2014, pp. 1 - 17
The Cdc45/Mcm2-7/GINS ( CMG) helicase separates DNA strands during replication in eukaryotes. How the CMG is assembled and engages DNA substrates remains... 
replication fork | DNA replication | helicase | motor proteins | AAA+ ATPase | Mcm2-7 | MCM2-7 HELICASE | HEXAMERIC HELICASE | MINICHROMOSOME MAINTENANCE PROTEIN | ARCHAEAL MCM | BUDDING YEAST | STRUCTURAL BASIS | BIOLOGY | REPLICATIVE HELICASE | ELECTRON-MICROSCOPY | 26S PROTEASOME | CRYO-EM STRUCTURE | Minichromosome Maintenance Proteins - metabolism | Protein Multimerization | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Minichromosome Maintenance Proteins - chemistry | Protein Subunits - metabolism | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Repressor Proteins - metabolism | Protein Structure, Tertiary | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | DNA, Single-Stranded - metabolism | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | RNA Splicing Factors | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA Replication | DNA - metabolism | Drosophila Proteins - chemistry | Microscopy, Electron | DNA-Binding Proteins - chemistry | Adenosine Triphosphate - analogs & derivatives | DNA, Single-Stranded - chemistry | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | RNA-Binding Proteins - metabolism | Medical research | Single-stranded DNA | Hexamers | Electron microscopy | DNA biosynthesis | DNA helicase | Handedness | Microscopy | Insects | Cdc45 protein | Cell cycle | Polarity | Dimerization | Deoxyribonucleic acid--DNA | Adenosine triphosphatase
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
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 | 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) | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES | second messenger
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 12764 - 12771
Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular systems coordinating the uptake and distribution of metal cofactors.... 
metalloprotein | HUMAN BOLA2 | HEME-BIOSYNTHESIS | DEOXYHYPUSINE HYDROXYLASE | BolA2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | glutaredoxin | SACCHAROMYCES-CEREVISIAE | iron metabolism | molecular chaperone | PHP4 FUNCTION | FERRITIN DEGRADATION | poly C-binding protein | IN-VIVO | GENE-EXPRESSION | iron | iron-sulfur protein | SULFUR CLUSTER | MONOTHIOL GLUTAREDOXIN | Molecular Chaperones - metabolism | Humans | Protein Multimerization | Iron-Sulfur Proteins - chemistry | Molecular Chaperones - chemistry | Nuclear Receptor Coactivators - chemistry | Autophagy | Apoferritins - metabolism | Ferritins - metabolism | Cation Transport Proteins - metabolism | Apoenzymes - metabolism | Carrier Proteins - chemistry | Dimerization | Nuclear Receptor Coactivators - metabolism | Erythroid Precursor Cells - cytology | RNA-Binding Proteins - chemistry | Heterogeneous-Nuclear Ribonucleoproteins - metabolism | Models, Molecular | Apoferritins - chemistry | Iron - metabolism | Protein Transport | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Models, Biological | Heterogeneous-Nuclear Ribonucleoproteins - chemistry | Apoenzymes - chemistry | Erythroid Precursor Cells - metabolism | Cytosol - metabolism | Iron-Sulfur Proteins - metabolism | Proteins - chemistry | Cation Transport Proteins - chemistry | Ferritins - chemistry | RNA-Binding Proteins - metabolism | iron–sulfur protein | Minireviews
Journal Article