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Nature (London), ISSN 1476-4687, 2013, Volume 505, Issue 7484, pp. 564 - 568
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 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
The EMBO journal, ISSN 1460-2075, 2018, Volume 37, Issue 7, p. n/a
The transition between soluble intrinsically disordered tau protein and aggregated tau in neurofibrillary tangles in Alzheimer's disease is unknown. Here, we... 
tau | aggregation | liquid–liquid phase separation | Alzheimer's disease | phosphorylation | MICROTUBULE-BINDING | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | POSTTRANSLATIONAL MODIFICATIONS | GRANULES | DROPLETS | CELL BIOLOGY | TRANSITION | liquid-liquid phase separation | PAIRED HELICAL FILAMENTS | MUTATIONS | DOMAINS | Phosphorylation | Molecular Weight | Humans | tau Proteins - metabolism | tau Proteins - chemistry | Brain - metabolism | DNA-Binding Proteins - metabolism | Sequence Analysis, Protein | Sf9 Cells | Neurofibrillary Tangles - metabolism | Cloning, Molecular | HEK293 Cells | Aged, 80 and over | Female | Neurons - metabolism | Benzothiazoles - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Biophysical Phenomena | Mice, Transgenic | Recombinant Proteins - genetics | Neurodegenerative Diseases - metabolism | tau Proteins - isolation & purification | Animals | Escherichia coli - genetics | Alzheimer Disease - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Heterogeneous Nuclear Ribonucleoprotein A1 - metabolism | Mice | Neuroblastoma - metabolism | Liquid-Liquid Extraction | Protein Aggregation, Pathological - metabolism | Brain | Seeds | Neurodegenerative diseases | Neurons | Amyotrophic lateral sclerosis | Forming | Agglomeration | Seeding | Molecular weight | Neurological diseases | Proteins | Neurofibrillary tangles | Aggregates | Tau protein | Phase separation | Dementia disorders | Droplets | Mutation | Frontotemporal dementia | Alzheimers disease | Physiology | Protein Biosynthesis & Quality Control
Journal Article
Nature (London), ISSN 1476-4687, 2016, Volume 537, Issue 7619, pp. 197 - 201
Precursor mRNA (pre-mRNA) splicing proceeds by two consecutive transesterification reactions via a lariat-intron intermediate. Here we present the 3.8 angstrom... 
U4/U6.U5 TRI-SNRNP | IN-VITRO | ELECTRON CRYOMICROSCOPY | ACTIVE-SITE | CRYSTAL-STRUCTURE | CONFORMATIONAL REARRANGEMENT | MULTIDISCIPLINARY SCIENCES | SACCHAROMYCES-CEREVISIAE | U6 SNRNA | PRE-MESSENGER-RNA | CATALYTIC ACTIVATION | RNA Precursors - chemistry | RNA Helicases - metabolism | Spliceosomes - chemistry | RNA, Fungal - ultrastructure | Saccharomyces cerevisiae - genetics | Ribonucleoprotein, U5 Small Nuclear - metabolism | Saccharomyces cerevisiae - ultrastructure | Ribonucleoprotein, U4-U6 Small Nuclear - metabolism | RNA Splicing Factors - metabolism | Spliceosomes - metabolism | RNA Splicing | RNA, Small Nuclear - genetics | Base Sequence | RNA Precursors - metabolism | RNA, Fungal - genetics | Ribonucleoprotein, U5 Small Nuclear - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | Introns - genetics | RNA Splice Sites - genetics | RNA, Fungal - chemistry | Adenosine Triphosphatases - metabolism | Models, Molecular | Exons - genetics | Magnesium - metabolism | Nuclear Proteins - metabolism | Spliceosomes - ultrastructure | Esterification | Saccharomyces cerevisiae - chemistry | RNA, Fungal - metabolism | Cryoelectron Microscopy | RNA Precursors - ultrastructure | Base Pairing | Saccharomyces cerevisiae Proteins - metabolism | Adenosine - metabolism | Ribonucleoprotein, U4-U6 Small Nuclear - chemistry | RNA, Small Nuclear - chemistry | RNA, Small Nuclear - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Genetic aspects | Spliceosomes | Structure | Brewer's yeast | Methods | RNA splicing | Proteins | Enzymes | Molecular structure | Microscopy | Catalysis | Ribonucleic acid--RNA | Binding sites
Journal Article
Biochemical journal, ISSN 1470-8728, 2017, Volume 474, Issue 8, pp. 1417 - 1438
Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid... 
EUKARYOTIC STRESS GRANULES | MUTANT FUS PROTEINS | MULTISYSTEM PROTEINOPATHY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHASE-TRANSITION | TARDBP MUTATIONS | HNRNP A1 | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS | NEURODEGENERATIVE DISEASES | Proteostasis Deficiencies - metabolism | RNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - metabolism | Humans | Prion Proteins - metabolism | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | RNA-Binding Protein FUS - chemistry | TDP-43 Proteinopathies - genetics | Protein Domains | TDP-43 Proteinopathies - pathology | Prion Proteins - chemistry | Prion Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Frontotemporal Dementia - pathology | Calmodulin-Binding Proteins - genetics | Frontotemporal Dementia - genetics | Cytoplasmic Granules | Neurodegenerative Diseases - pathology | Amyotrophic Lateral Sclerosis - genetics | RNA-Binding Proteins - chemistry | TDP-43 Proteinopathies - metabolism | Proteostasis Deficiencies - pathology | RNA-Binding Protein FUS - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Neurodegenerative Diseases - genetics | Calmodulin-Binding Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | RNA-Binding Protein FUS - metabolism | Neurodegenerative Diseases - metabolism | TATA-Binding Protein Associated Factors - chemistry | DNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - genetics | DNA-Binding Proteins - chemistry | Heterogeneous Nuclear Ribonucleoprotein A1 | Proteostasis Deficiencies - genetics | Amyotrophic Lateral Sclerosis - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Mutation | RNA-Binding Proteins - metabolism | RNA-Binding Protein EWS
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2014, Volume 289, Issue 9, pp. 6236 - 6247
Journal Article
Nature communications, ISSN 2041-1723, 2018, Volume 9, Issue 1, pp. 1163 - 16
The roles of RNA 5-methylcytosine (RNA: m(5)C) and RNA: m(5)C methyltransferases (RCMTs) in lineage-associated chromatin organization and drug... 
CELLS | MESSENGER-RNA | GENE | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | POLYMERASE-II | BCR/ABL LEUKEMOGENESIS | KINASE INHIBITOR | DNA-BINDING-PROTEINS | SACCHAROMYCES-CEREVISIAE | HNRNP-K | Chromatin - metabolism | RNA, Small Interfering - genetics | Humans | Leukemia, Myeloid, Acute - metabolism | Methyltransferases - metabolism | Methyltransferases - genetics | RNA, Neoplasm - metabolism | DNA (Cytosine-5-)-Methyltransferases - metabolism | Cytosine - metabolism | Bone Marrow - metabolism | Trans-Activators - genetics | Leukemia, Myeloid, Acute - drug therapy | Antineoplastic Agents - pharmacology | Nuclear Proteins - genetics | Chromatin - drug effects | Myelodysplastic Syndromes - drug therapy | Bone Marrow - drug effects | Chromatin - chemistry | Proto-Oncogene Proteins - metabolism | Myelodysplastic Syndromes - metabolism | Signal Transduction | Cyclin-Dependent Kinase 9 - genetics | Leukemia, Myeloid, Acute - pathology | Chromatin Assembly and Disassembly | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Gene Expression Regulation, Leukemic | Transcription Factors - genetics | GATA1 Transcription Factor - metabolism | Heterogeneous-Nuclear Ribonucleoprotein K - genetics | Transcription Factors - metabolism | Azacitidine - pharmacology | DNA (Cytosine-5-)-Methyltransferases - genetics | Drug Resistance, Neoplasm - genetics | Heterogeneous-Nuclear Ribonucleoprotein K - metabolism | Bone Marrow - pathology | GATA1 Transcription Factor - genetics | Cell Line, Tumor | Protein Binding | RNA, Neoplasm - genetics | Trans-Activators - metabolism | Cyclin-Dependent Kinase 9 - metabolism | Myelodysplastic Syndromes - genetics | Methylation | Myelodysplastic Syndromes - pathology | Leukemia, Myeloid, Acute - genetics | RNA, Small Interfering - metabolism | Azacytidine | Chromatin | Transcription factors | Leukemia | Ribonucleic acid--RNA | DNA-directed RNA polymerase | Myelodysplastic syndrome | Polymerase | GATA-1 protein | RNA-binding protein | PU.1 protein | Cell lines | Cytosine
Journal Article
Nature, ISSN 0028-0836, 05/2016, Volume 534, Issue 7605, pp. 133 - 137
Ribosome biogenesis is a highly complex process in eukaryotes, involving temporally and spatially regulated ribosomal protein (r-protein) binding and ribosomal... 
REFINEMENT | COMPLEX | RNA | BIOGENESIS | INITIATION | MULTIDISCIPLINARY SCIENCES | RESOLUTION | MATURATION | IDENTIFICATION | ASSOCIATION | SUBUNIT | RNA, Fungal - ultrastructure | GTP Phosphohydrolases - ultrastructure | Saccharomyces cerevisiae - ultrastructure | DNA, Ribosomal Spacer - metabolism | RNA, Ribosomal - genetics | GTP Phosphohydrolases - chemistry | Saccharomyces cerevisiae - metabolism | Cell Nucleus - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | DNA, Ribosomal Spacer - genetics | Base Sequence | DNA, Ribosomal Spacer - ultrastructure | Ribosome Subunits, Large, Eukaryotic - chemistry | Models, Molecular | Ribonucleoproteins - metabolism | Nuclear Proteins - chemistry | Saccharomyces cerevisiae - chemistry | RNA, Ribosomal - ultrastructure | Saccharomyces cerevisiae - cytology | Ribosomal Proteins - isolation & purification | GTP Phosphohydrolases - metabolism | Saccharomyces cerevisiae Proteins - metabolism | GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Ribosomal Proteins - chemistry | Ribosome Subunits, Large, Eukaryotic - ultrastructure | Nuclear Proteins - ultrastructure | Molecular Sequence Data | Cytoplasm - metabolism | Ribosomal Proteins - metabolism | Ribosomal Proteins - ultrastructure | Saccharomyces cerevisiae Proteins - isolation & purification | RNA, Fungal - genetics | Active Transport, Cell Nucleus | Ribonucleoproteins - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | GTP-Binding Proteins - chemistry | RNA, Ribosomal - metabolism | Nuclear Proteins - metabolism | GTP-Binding Proteins - ultrastructure | DNA, Ribosomal Spacer - chemistry | Cell Nucleus - ultrastructure | Rotation | RNA, Fungal - metabolism | Cryoelectron Microscopy | Protein Binding | Cell Nucleus - chemistry | Ribonucleoproteins - ultrastructure | Nucleolus organizer region | Protein research | Research | Ribosomes | Protein binding | Genetic research | Proteins | G proteins | Ribosomal RNA | Adenosine triphosphatase | Protein biosynthesis | Cell research | Polypeptides | Molecular structure | Ribonucleic acid--RNA
Journal Article