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Nature, ISSN 0028-0836, 02/2017, Volume 542, Issue 7641, pp. 377 - 380
The spliceosome excises introns from pre-mRNAs in two sequential transesterifications-branching and exon ligation(1)-catalysed at a single catalytic metal site... 
2ND STEP | ANGSTROM RESOLUTION | ELECTRON CRYOMICROSCOPY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | FUNCTIONAL INTERACTIONS | CATALYTIC CENTER | CRYO-EM STRUCTURE | SPLICING FACTOR | SITE CHOICE | PRE-MESSENGER-RNA | RNA Helicases - metabolism | Spliceosomes - chemistry | Saccharomyces cerevisiae - genetics | Cell Cycle Proteins - ultrastructure | Ribonucleoprotein, U5 Small Nuclear - metabolism | RNA Splicing Factors - chemistry | Saccharomyces cerevisiae - ultrastructure | Ribonucleoprotein, U4-U6 Small Nuclear - metabolism | Ribonucleoprotein, U4-U6 Small Nuclear - ultrastructure | RNA Helicases - ultrastructure | RNA Splicing Factors - metabolism | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Spliceosomes - metabolism | RNA Splicing | Ribonucleoproteins, Small Nuclear - ultrastructure | RNA, Small Nuclear - genetics | Protein Domains | Ribonucleoprotein, U5 Small Nuclear - ultrastructure | Adenosine Triphosphatases - ultrastructure | DEAD-box RNA Helicases - metabolism | DEAD-box RNA Helicases - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | Biocatalysis | RNA Splice Sites - genetics | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Exons - genetics | Spliceosomes - ultrastructure | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | DNA-Binding Proteins - ultrastructure | RNA-Binding Proteins - ultrastructure | RNA Splicing Factors - ultrastructure | Ribonuclease H - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Adenosine - metabolism | Protein Binding | DEAD-box RNA Helicases - ultrastructure | RNA-Binding Proteins - metabolism | Ribonucleoproteins, Small Nuclear - metabolism | Saccharomyces cerevisiae Proteins - chemistry | RNA sequencing | Methods | Mutation | Catalysis | Ribonucleic acid--RNA | Binding sites | Crystal structure
Journal Article
Science, ISSN 0036-8075, 12/2012, Volume 338, Issue 6114, pp. 1634 - 1637
The influenza viruses cause annual epidemics of respiratory disease and occasional pandemics, which constitute a major public-health issue. The segmented... 
Pandemics | RNA | Particle interactions | Virions | REPORTS | Ribonucleoproteins | Orthomyxoviridae | Viruses | Viral morphology | Atomic structure | Monomers | LOCALIZATION | NUCLEAR | REPLICATION | PARTICLES | RECONSTRUCTION | MULTIDISCIPLINARY SCIENCES | COMPLEXES | POLYMERASE | A VIRUS NUCLEOPROTEIN | OLIGOMERIZATION | Viral Core Proteins - ultrastructure | RNA Replicase - metabolism | Influenza A Virus, H1N1 Subtype - physiology | Virion - chemistry | Viral Proteins - metabolism | Influenza A Virus, H1N1 Subtype - ultrastructure | RNA Replicase - ultrastructure | Cell Nucleus - metabolism | Cell Nucleus - virology | Madin Darby Canine Kidney Cells | Viral Core Proteins - metabolism | Transcription, Genetic | RNA, Viral - metabolism | Ribonucleoproteins - chemistry | Viral Core Proteins - chemistry | Protein Structure, Secondary | Electron Microscope Tomography | Viral Proteins - chemistry | RNA-Binding Proteins - chemistry | Models, Molecular | Ribonucleoproteins - metabolism | Viral Proteins - ultrastructure | Microscopy, Electron | Cryoelectron Microscopy | RNA-Binding Proteins - ultrastructure | Animals | RNA, Viral - chemistry | Image Processing, Computer-Assisted | RNA Replicase - chemistry | Virion - ultrastructure | Protein Conformation | Influenza A Virus, H1N1 Subtype - chemistry | Ribonucleoproteins - ultrastructure | RNA-Binding Proteins - metabolism | Influenza viruses | Properties | RNA-protein interactions | Influenza | Genomics | Virology | Ribonucleic acids | Mortality | Replication | Genomes | Online | Assembly
Journal Article
Science, ISSN 0036-8075, 12/2012, Volume 338, Issue 6114, pp. 1631 - 1634
Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral... 
RNA | Active sites | Nucleoproteins | Virions | REPORTS | Viral genomes | Orthomyxoviridae | Viruses | Viral morphology | Genomes | Electron microscopy | A VIRUS | RIBONUCLEOPROTEIN COMPLEXES | CRYSTAL-STRUCTURE | HUMAN-CELLS | NUCLEOPROTEIN | MULTIDISCIPLINARY SCIENCES | ELECTRON-MICROSCOPY | VIRAL POLYMERASE | GENERATION | BINDING | Viral Core Proteins - ultrastructure | RNA Replicase - metabolism | Influenza A Virus, H1N1 Subtype - physiology | Crystallography, X-Ray | Viral Proteins - metabolism | Influenza A Virus, H1N1 Subtype - ultrastructure | Protein Subunits - metabolism | RNA Replicase - ultrastructure | Viral Core Proteins - metabolism | Ribonucleoproteins - genetics | Transcription, Genetic | RNA, Viral - metabolism | Ribonucleoproteins - chemistry | Nucleic Acid Conformation | Influenza A Virus, H1N1 Subtype - genetics | Genome, Viral | Viral Core Proteins - chemistry | Viral Proteins - chemistry | RNA-Binding Proteins - chemistry | Models, Molecular | Ribonucleoproteins - metabolism | Viral Proteins - ultrastructure | Microscopy, Electron | Cryoelectron Microscopy | RNA-Binding Proteins - ultrastructure | RNA, Viral - chemistry | Image Processing, Computer-Assisted | Virus Replication | RNA Replicase - chemistry | Protein Conformation | Influenza A Virus, H1N1 Subtype - chemistry | Protein Subunits - chemistry | Ribonucleoproteins - ultrastructure | RNA, Viral - ultrastructure | RNA-Binding Proteins - metabolism | Influenza viruses | Properties | Ribonucleoproteins | RNA polymerase | RNA-protein interactions | Influenza | Genomics | Virology | Ribonucleic acids | Microscopy | Mortality | Replication | Online | Assembly
Journal Article
Nature, ISSN 0028-0836, 02/2017, Volume 542, Issue 7641, pp. 318 - 323
Spliceosome rearrangements facilitated by RNA helicase PRP16 before catalytic step two of splicing are poorly understood. Here we report a 3D cryo-electron... 
2ND STEP | I SPLICEOSOME | U4/U6.U5 TRI-SNRNP | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MOLECULAR ARCHITECTURE | CATALYTIC CORE | PRE-MESSENGER-RNA | PRP8 | INSIGHTS | Spliceosomes - chemistry | Humans | Cell Cycle Proteins - ultrastructure | RNA Splicing Factors - chemistry | RNA, Messenger - metabolism | RNA Splicing Factors - metabolism | Cell Cycle Proteins - chemistry | Spliceosomes - metabolism | RNA Splicing | Ribonucleoproteins, Small Nuclear - ultrastructure | Base Sequence | Protein Domains | Ribonucleoproteins, Small Nuclear - chemistry | DEAD-box RNA Helicases - metabolism | DEAD-box RNA Helicases - chemistry | Biocatalysis | Introns - genetics | Movement | RNA, Messenger - genetics | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | Models, Molecular | Exons - genetics | Spliceosomes - ultrastructure | RNA Stability | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | RNA-Binding Proteins - ultrastructure | RNA Splicing Factors - ultrastructure | Ribonuclease H - chemistry | Adenosine - metabolism | Saccharomyces cerevisiae - enzymology | RNA, Messenger - chemistry | DEAD-box RNA Helicases - ultrastructure | RNA-Binding Proteins - metabolism | Ribonucleoproteins, Small Nuclear - metabolism | Ribonuclease H - metabolism | Genetic research | Genetic engineering | Research | Methods | RNA splicing | Proteins | Yeast | Catalysis | Molecular structure | Microscopy | Ribonucleic acid--RNA
Journal Article
Journal Article
The EMBO Journal, ISSN 0261-4189, 04/2018, Volume 37, Issue 7, p. n/a
Final maturation of eukaryotic ribosomes occurs in the cytoplasm and requires the sequential removal of associated assembly factors and processing of the... 
ribosome | pre‐40S ribosome | cryo | ribosome assembly | ribosome biogenesis | cryo-EM | pre-40S ribosome | SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | TRANSLATION INITIATION | MATURATION | CLEAVAGE | CELL BIOLOGY | YEAST | FULGIDUS RIO2 | BIOGENESIS | TRANSFER-RNA | 90S | Ribosomal Proteins - chemistry | Ribosome Subunits, Small, Eukaryotic - chemistry | Saccharomyces cerevisiae - genetics | Protein-Serine-Threonine Kinases - ultrastructure | Nuclear Proteins - ultrastructure | Saccharomyces cerevisiae - ultrastructure | Ribosomal Proteins - ultrastructure | Protein Domains | Saccharomyces cerevisiae Proteins - isolation & purification | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Ribosome Subunits, Small, Eukaryotic - genetics | RNA Folding | Saccharomyces cerevisiae Proteins - ultrastructure | Ribosomal Proteins - genetics | RNA, Ribosomal - chemistry | RNA-Binding Proteins - chemistry | Ribosome Subunits, Small, Eukaryotic - ultrastructure | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | Cryoelectron Microscopy | RNA, Ribosomal - ultrastructure | RNA-Binding Proteins - ultrastructure | Ribosomal Proteins - isolation & purification | Protein Conformation | Molecular Docking Simulation | Cytoplasm | Saccharomyces cerevisiae Proteins - chemistry | Yeast | Maturation | Ribonucleic acids | rRNA | Ribosomes | Docking | rRNA 20S | Electron microscopy | Assembly | Binding sites | cryo‐EM | Structural Biology | RNA Biology | Protein Biosynthesis & Quality Control
Journal Article
Science, ISSN 0036-8075, 12/2009, Volume 326, Issue 5958, pp. 1412 - 1415
Journal Article
Nature Neuroscience, ISSN 1097-6256, 02/2018, Volume 21, Issue 2, pp. 228 - 239
The cytoplasmic mislocalization and aggregation of TAR DNA-binding protein-43 (TDP-43) is a common histopathological hallmark of the amyotrophic lateral... 
A315T MUTATION | REPEAT EXPANSION | MESSENGER-RNA | DROSOPHILA MODEL | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | FRONTOTEMPORAL LOBAR DEGENERATION | EXPRESSION | NEUROSCIENCES | RNA-BINDING PROTEIN | C9orf72 Protein - genetics | Active Transport, Cell Nucleus - physiology | Humans | Nuclear Envelope - ultrastructure | Male | Drosophila Proteins - metabolism | Cerebral Cortex - cytology | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Protein Aggregation, Pathological - pathology | Female | C9orf72 Protein - metabolism | Active Transport, Cell Nucleus - genetics | Neuroblastoma - pathology | Frontotemporal Dementia - pathology | Frontotemporal Dementia - genetics | Animals, Genetically Modified | Amyotrophic Lateral Sclerosis - genetics | Drosophila | Mice, Inbred C57BL | Cells, Cultured | Nuclear Pore - genetics | DNA-Binding Proteins - genetics | Nuclear Pore - metabolism | DNA-Binding Proteins - ultrastructure | Amyotrophic Lateral Sclerosis - pathology | Animals | Larva | Amyotrophic Lateral Sclerosis - metabolism | C9orf72 Protein - ultrastructure | Embryo, Nonmammalian | Mice | Drosophila Proteins - genetics | Nuclear Envelope - pathology | Protein Aggregation, Pathological - metabolism | Fibroblasts | Amyotrophic lateral sclerosis | Research | Protein binding | Brain | Neurons | Cortex | Biotin | Ribonucleic acid--RNA | Pathology | DNA-binding protein | Nucleoporins | RNA transport | Aggregates | Stem cells | Dementia disorders | Mutation | Transport | Protein transport | Frontotemporal dementia | Pluripotency | Deoxyribonucleic acid--DNA
Journal Article
Nature, ISSN 0028-0836, 04/2013, Volume 496, Issue 7444, pp. 187 - 192
Journal Article