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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
Nature, ISSN 0028-0836, 08/2015, Volume 524, Issue 7564, pp. 186 - 191
Journal Article
Nature, ISSN 0028-0836, 06/2015, Volume 522, Issue 7557, pp. 450 - 454
The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by... 
E3 LIGASE | ANAPHASE-PROMOTING COMPLEX | ACTIVATION | PHOSPHORYLATION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MITOTIC REGULATION | CONJUGATING ENZYME | CHAIN ELONGATION | REVEALS | SUBUNIT | Phosphorylation | Ubiquitin - ultrastructure | Cadherins - metabolism | Humans | Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Ubiquitin - metabolism | Cell Cycle Proteins - ultrastructure | Substrate Specificity | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Structure-Activity Relationship | Anaphase-Promoting Complex-Cyclosome - ultrastructure | Protein Subunits - metabolism | Ubiquitin-Conjugating Enzymes - chemistry | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Cell Cycle Proteins - chemistry | Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Ubiquitination | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Cadherins - chemistry | Cytoskeletal Proteins - metabolism | Lysine - metabolism | Anaphase-Promoting Complex-Cyclosome - chemistry | Cadherins - ultrastructure | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Catalytic Domain | F-Box Proteins - metabolism | Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | F-Box Proteins - chemistry | Cell Cycle Proteins - metabolism | Ubiquitin - chemistry | Models, Molecular | Ubiquitin-Conjugating Enzymes - ultrastructure | Cytoskeletal Proteins - chemistry | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Cryoelectron Microscopy | F-Box Proteins - ultrastructure | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding | Protein Subunits - chemistry | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Anaphase-Promoting Complex-Cyclosome - metabolism | Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Ubiquitin | Physiological aspects | Structure | Ubiquitin-proteasome system | Ligases | Proteins | Peptides | Molecular structure | Cyclin-dependent kinases | Cell division | Kinases | Gene expression
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 2023 - 11
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
Science, ISSN 0036-8075, 01/2017, Volume 355, Issue 6321, pp. 149 - 155
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 06/2011, Volume 18, Issue 6, pp. 715 - 720
No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key... 
EF-TU | CRYSTAL-STRUCTURE | EUKARYOTIC RIBOSOME | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ELECTRON-MICROSCOPY | CRYO-EM | STOP CODON RECOGNITION | RELEASE FACTOR ERF3 | SACCHAROMYCES-CEREVISIAE | CELL BIOLOGY | TERMINATION FACTOR ERF1 | BIOPHYSICS | Endoribonucleases - chemistry | Peptide Elongation Factors - metabolism | Cell Cycle Proteins - ultrastructure | Ribosomes - metabolism | RNA, Messenger - metabolism | Cell Cycle Proteins - chemistry | Saccharomyces cerevisiae - metabolism | HSP70 Heat-Shock Proteins - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Endoribonucleases - ultrastructure | Endoribonucleases - metabolism | GTP-Binding Proteins - chemistry | HSP70 Heat-Shock Proteins - ultrastructure | Cell Cycle Proteins - metabolism | Ribosomes - chemistry | Models, Molecular | GTP-Binding Proteins - ultrastructure | RNA Stability | HSP70 Heat-Shock Proteins - metabolism | Cryoelectron Microscopy | Peptide Elongation Factors - chemistry | Ribosomes - ultrastructure | Peptide Elongation Factors - ultrastructure | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | RNA, Messenger - chemistry | GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Peptides | Cellular biology | Ribonucleic acid--RNA | Molecular biology | Crystal structure
Journal Article
Journal Article