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1. Full Text Alba-domain proteins of trypanosoma brucei are cytoplasmic RNA-Binding proteins that interact with the translation machinery
by Mani, Jan and Güttinger, Andreas and Schimanski, Bernd and Heller, Manfred and Acosta-Serrano, Alvaro and Pescher, Pascale and Späth, Gerald and Roditi, Isabel
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 7, p. e22463
Trypanosoma brucei and related pathogens transcribe most genes as polycistronic arrays that are subsequently processed into monocistronic mRNAs. Expression is... 
METHIONYL-TRANSFER-RNA | MESSENGER-RNA | SURFACE PROTEIN | BLOOD-STREAM FORMS | MULTIDISCIPLINARY SCIENCES | 3 UNTRANSLATED REGION | RIBONUCLEASE-P | GENE-EXPRESSION | INSECT FORMS | ARCHAEBACTERIUM SULFOLOBUS-ACIDOCALDARIUS | PROCYCLIN EXPRESSION SITE | RNA-Binding Proteins - genetics | Protein Biosynthesis | Immunoprecipitation | Membrane Glycoproteins - metabolism | Trypanosoma brucei brucei - metabolism | RNA, Messenger - genetics | RNA-Binding Proteins - chemistry | Cytoplasm - metabolism | Phylogeny | Protozoan Proteins - genetics | RNA, Messenger - metabolism | Membrane Glycoproteins - genetics | Protein Transport | Multiprotein Complexes - metabolism | Chromatography, Affinity | Protozoan Proteins - metabolism | Cytoplasmic Granules - metabolism | Protein Binding | Protozoan Proteins - chemistry | RNA-Binding Proteins - metabolism | Regulatory Sequences, Ribonucleic Acid - genetics | Glycerin | Messenger RNA | Genes | Glycerol | Binding proteins | Genetic translation | Cells | Protein binding | Post-transcription | Poly(A) | Yeast | Sucrose | Transcription | Midgut | Protein purification | Biological evolution | Material requirements planning | Ribosomal protein P0 | Biology | Regulatory sequences | Mammalian cells | Proteins | Plasticity (functional) | Ribonuclease P | Ribonuclease MRP | DNA-binding protein | User interface | Cell cycle | Cap-binding protein | Phylogenetics | Polyribosomes | Myelin P0 protein | Sugars | Deoxyribonucleic acid--DNA | Parasitology | Starvation | Translation | Nucleotide sequence | RNA-mediated interference | mRNA turnover | Archaea | Heat shock proteins | Gene expression | Ribonucleic acid--RNA | RNA-binding protein | Acids | Insects | 3' Untranslated regions | Phenols | Column chromatography | Life Sciences | Microbiology and Parasitology | RNA | Deoxyribonucleic acid | Ribonucleic acid | DNA
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2. Full Text Comprehensive analysis of diverse ribonucleoprotein complexes
by Rout, Michael P and Oeffinger, Marlene and Rogers, Richard and Aitchison, John D and Wei, Karen E and Chait, Brian T and DeGrasse, Jeffrey A
Nature Methods, ISSN 1548-7091, 11/2007, Volume 4, Issue 11, pp. 951 - 956
The study of the dynamic interactome of cellular ribonucleoprotein (RNP) particles has been hampered by severe methodological limitations. In particular, the... 
YEAST | TRANSCRIPTS | TRANSPORT | MEX67P | NUCLEAR-PORE COMPLEX | BIOCHEMICAL RESEARCH METHODS | MESSENGER-RNA EXPORT | BINDING PROTEIN | RIBOSOMAL-RNA | IDENTIFICATION | SACCHAROMYCES-CEREVISIAE | Ribosomal Proteins - analysis | RNA, Fungal - analysis | RNA-Binding Proteins - genetics | Nuclear Proteins - analysis | Oligonucleotide Array Sequence Analysis | Saccharomyces cerevisiae - genetics | RNA, Messenger - analysis | DNA-Binding Proteins - analysis | Green Fluorescent Proteins - genetics | Ribonucleoproteins - analysis | Porins | Saccharomyces cerevisiae - metabolism | Immunosorbent Techniques | Mass Spectrometry | Ribonucleoproteins - genetics | Nuclear Proteins - genetics | RNA-Binding Proteins - analysis | Staphylococcal Protein A - genetics | Green Fluorescent Proteins - analysis | Ribosomal Proteins - genetics | Electrophoresis, Polyacrylamide Gel | Staphylococcal Protein A - analysis | Saccharomyces cerevisiae Proteins - genetics | DNA-Binding Proteins - genetics | Nucleocytoplasmic Transport Proteins - genetics | Nucleocytoplasmic Transport Proteins - analysis | RNA, Ribosomal - analysis | RNA Cap-Binding Proteins | Saccharomyces cerevisiae Proteins - analysis | RNA | Ribonucleoproteins | Research | Proteins | Cellular biology | Ribonucleic acid--RNA | Research methodology | Ribonucleic acid
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3. Full Text Subunit architecture of multimeric complexes isolated directly from cells
by Robinson, Carol V and Hernández, Helena and Séraphin, Bertrand and Dziembowski, Andrzej and Taverner, Thomas
EMBO reports, ISSN 1469-221X, 06/2006, Volume 7, Issue 6, pp. 605 - 610
Recent developments in purification strategies, together with mass spectrometry (MS)‐based proteomics, have identified numerous in vivo protein complexes and... 
tandem affinity purification | mass spectrometry | cap‐binding complex | scavenger decapping complex | exosome | Exosome | Mass spectrometry | Cap-binding complex | Scavenger decapping complex | Tandem affinity purification | cap-binding complex | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | MESSENGER-RNA DEGRADATION | YEAST | RING | PURIFICATION | FRAMEWORK | PROTEIN-PROTEIN INTERACTIONS | LINK | Fungal Proteins - chemistry | Saccharomyces cerevisiae - genetics | Protein Subunits - analysis | Proteome - chemistry | Protein Subunits - metabolism | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Protein Subunits - isolation & purification | Gene Deletion | Mass Spectrometry | Protein Structure, Quaternary | Isotope Labeling | Genes, Fungal | Saccharomyces cerevisiae Proteins - isolation & purification | Proteomics - methods | Fungal Proteins - isolation & purification | Dimerization | Saccharomyces cerevisiae - chemistry | Protein Interaction Mapping | Saccharomyces cerevisiae - cytology | Fungal Proteins - analysis | Multiprotein Complexes - chemistry | Chromatography, Affinity | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Subunits - chemistry | Proteome - metabolism | Exoribonucleases - metabolism | Fungal Proteins - metabolism | Multiprotein Complexes - isolation & purification | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Molecular biology | Spectrum analysis | Research methodology | Cells | Proteomics | Protein Subunits | Exoribonucleases | Multiprotein Complexes | Biochemistry, Molecular Biology | Proteome | Fungal Proteins | Life Sciences | Saccharomyces cerevisiae Proteins | Biomolecules | Saccharomyces cerevisiae | Scientific Report
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4. Full Text Site-specific binding of a PPR protein defines and stabilizes 5′ and 3′ mRNA termini in chloroplasts
by Prikryl, Jana and Barkan, Alice and Bayraktar, Omer Ali and Pfalz, Jeannette
The EMBO Journal, ISSN 0261-4189, 07/2009, Volume 28, Issue 14, pp. 2042 - 2052
Chloroplast mRNA populations are characterized by overlapping transcripts derived by processing from polycistronic precursors. The mechanisms and functional... 
RNA stability | pentatricopeptide repeat | plastid | RNA‐binding protein | mitochondria | Mitochondria | RNA-binding protein | Pentatricopeptide repeat | Plastid | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | RIBOSOMAL-RNA | TRANSLATION | CELL BIOLOGY | MAIZE CHLOROPLASTS | CHLAMYDOMONAS-REINHARDTII | IN-VIVO | GENE-EXPRESSION | PENTATRICOPEPTIDE REPEAT PROTEIN | ARABIDOPSIS | NUCLEUS-ENCODED FACTOR | RNA Cap-Binding Proteins - metabolism | Zea mays - genetics | RNA Processing, Post-Transcriptional | RNA, Messenger - genetics | Gene Expression Regulation, Plant | Molecular Sequence Data | Plant Proteins - metabolism | Zea mays - metabolism | RNA Stability | RNA, Messenger - metabolism | Chloroplasts - genetics | Chloroplasts - metabolism | Plant biology | Plant mitochondria | RNA-protein interactions | Cellular biology | Chloroplasts | Molecular biology
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5. Full Text Scaffold function of long non-coding RNA HOTAIR in protein ubiquitination
by Yoon, Je-Hyun and Abdelmohsen, Kotb and Kim, Jiyoung and Yang, Xiaoling and Martindale, Jennifer L and Tominaga-Yamanaka, Kumiko and White, Elizabeth J and Orjalo, Arturo V and Rinn, John L and Kreft, Stefan G and Wilson, Gerald M and Gorospe, Myriam
Nature Communications, ISSN 2041-1723, 12/2013, Volume 4, Issue 1, pp. 2939 - 2939
Although mammalian long non-coding (lnc) RNAs are best known for modulating transcription, their post-transcriptional influence on mRNA splicing, stability and... 
INTERACTION NETWORK | HUR | DECAY | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | DIFFERENTIATION | BINDING PROTEIN | IDENTIFICATION | EXPRESSION | ATAXIN-1 | REPLICATIVE SENESCENCE | Cellular Senescence - genetics | RNA-Binding Proteins - genetics | Argonaute Proteins - metabolism | Ataxin-1 | Humans | ELAV Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | RNA Stability | Nerve Tissue Proteins - metabolism | Proteins - genetics | RNA Cap-Binding Proteins - metabolism | Ataxins | Ubiquitination | Proteins - metabolism | HeLa Cells | Ubiquitin-Protein Ligases - genetics | RNA, Long Noncoding - metabolism | RNA-Binding Proteins - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism
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6. Full Text Biophysical Studies of eIF4E Cap-binding Protein: Recognition of mRNA 5′ Cap Structure and Synthetic Fragments of eIF4G and 4E-BP1 Proteins
by Niedzwiecka, Anna and Marcotrigiano, Joseph and Stepinski, Janusz and Jankowska-Anyszka, Marzena and Wyslouch-Cieszynska, Aleksandra and Dadlez, Michal and Gingras, Anne-Claude and Mak, Pawel and Darzynkiewicz, Edward and Sonenberg, Nahum and Burley, Stephen K and Stolarski, Ryszard
Journal of Molecular Biology, ISSN 0022-2836, 2002, Volume 319, Issue 3, pp. 615 - 635
mRNA 5-cap recognition by the eukaryotic translation initiation factor eIF4E has been exhaustively characterized with the aid of a novel fluorometric,... 
translation | structure–activity relationship | eIF4E | mRNA 5′ cap | fluorescence | Fluorescence | Translation | Structure-activity relationship | FACTOR EIF-4E | mRNA 5 ' cap | THERMODYNAMIC ORIGINS | OSMOTIC-STRESS | MESSENGER-RNA CAP | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | INITIATION-FACTOR 4E | (S/T)P SITES | DEPENDENT TRANSLATION INITIATION | 5'-CAP ANALOGS | RETICULOCYTE LYSATE | structure-activity relationship | Phosphorylation | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | Phosphoproteins - metabolism | RNA Caps - metabolism | Eukaryotic Initiation Factor-4E | Phosphoproteins - chemistry | Peptide Initiation Factors - chemistry | Thermodynamics | Osmolar Concentration | RNA Caps - chemistry | Carrier Proteins - chemistry | RNA Cap Analogs - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Peptide Fragments - metabolism | RNA-Binding Proteins - chemistry | Electrolytes - metabolism | Models, Molecular | Static Electricity | Peptide Fragments - chemical synthesis | Peptide Initiation Factors - metabolism | Peptide Fragments - chemistry | Phosphates - metabolism | Animals | Carrier Proteins - metabolism | Eukaryotic Initiation Factor-4G | Hydrogen Bonding | RNA Cap Analogs - chemistry | Protein Binding | Mice | RNA Cap-Binding Proteins | Methylation | RNA-Binding Proteins - metabolism
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7. Full Text A homolog of splicing factor SF1 is essential for development and is involved in the alternative splicing of pre‐mRNA in Arabidopsis thaliana
by Jang, Yun Hee and Park, Hyo‐Young and Lee, Keh Chien and Thu, May Phyo and Kim, Soon‐Kap and Suh, Mi Chung and Kang, Hunseung and Kim, Jeong‐Kook
The Plant Journal, ISSN 0960-7412, 05/2014, Volume 78, Issue 4, pp. 591 - 603
Summary During initial spliceosome assembly, SF1 binds to intron branch points and interacts with U2 snRNP auxiliary factor 65 (U2AF65). Here, we present... 
development | alternative splicing | abnormal abscisic acid | SF1 | Arabidopsis thaliana Heynh | COMPLEX | PLANT DEVELOPMENT | SACCHAROMYCES-CEREVISIAE | PLANT SCIENCES | YEAST | ACID SIGNAL-TRANSDUCTION | CAP-BINDING PROTEIN | SR45 PROTEIN | IN-VIVO | PROTEIN-PROTEIN INTERACTIONS | SCHIZOSACCHAROMYCES-POMBE | RNA-Binding Proteins - genetics | Alternative Splicing | Oligonucleotide Array Sequence Analysis | Arabidopsis - growth & development | Transcriptome | Green Fluorescent Proteins - genetics | Promoter Regions, Genetic - genetics | Heat Shock Transcription Factors | Arabidopsis Proteins - metabolism | DNA-Binding Proteins - metabolism | Heat-Shock Proteins - genetics | Splicing Factor U2AF | Seeds - growth & development | Gene Expression Regulation, Developmental | Germination - genetics | Plants, Genetically Modified | Gene Expression Regulation, Plant | RNA Precursors - metabolism | Ribonucleoproteins - genetics | Plant Proteins - metabolism | Nuclear Proteins - genetics | Genes, Essential - genetics | Germination - drug effects | Green Fluorescent Proteins - metabolism | Arabidopsis Proteins - genetics | Seeds - drug effects | Seeds - genetics | Heat-Shock Proteins - metabolism | RNA Splicing Factors | Nuclear Proteins - metabolism | RNA Precursors - genetics | Ribonucleoproteins - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Reverse Transcriptase Polymerase Chain Reaction | Arabidopsis - metabolism | Arabidopsis - genetics | Transcription Factors - metabolism | Abscisic Acid - pharmacology | Microscopy, Confocal | Plant Proteins - genetics | DNA, Bacterial - genetics | Protein Binding | Mutation | Plant Growth Regulators - pharmacology | RNA-Binding Proteins - metabolism | Proteins | Arabidopsis thaliana | DNA microarrays | Messenger RNA | Gene mutations | Analysis | Abscisic acid | Heat shock proteins | Plant biology | Genes
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8. Full Text Architecture of the Nuclease Module of the Yeast Ccr4-Not Complex: the Not1-Caf1-Ccr4 Interaction
by Basquin, Claire and Basquin, Jérôme and Roudko, Vladimir V and Rode, Michaela and Séraphin, Bertrand and Conti, Elena
Molecular Cell, ISSN 1097-2765, 10/2012, Volume 48, Issue 2, pp. 207 - 218
Shortening eukaryotic poly(A) tails represses mRNA translation and induces mRNA turnover. The major cytoplasmic deadenylase, the Ccr4-Not complex, is a... 
MESSENGER-RNA DEADENYLATION | CAF1 PROTEINS | TURNOVER | DECAY | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENE-EXPRESSION | POLY(A)-BINDING PROTEIN | SACCHAROMYCES-CEREVISIAE | SUBUNIT | CELL BIOLOGY | Protein Structure, Tertiary | Transcription Factors - chemistry | Ribonucleases - chemistry | RNA, Messenger - genetics | Cell Cycle Proteins - metabolism | Crystallography, X-Ray | Multiprotein Complexes - genetics | Nuclear Proteins - metabolism | Eukaryotic Initiation Factor-4G - metabolism | RNA, Messenger - metabolism | Ribonucleases - metabolism | Saccharomyces cerevisiae - chemistry | Cell Cycle Proteins - chemistry | RNA Cap-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Transcription Factors - metabolism | Multiprotein Complexes - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | RNA, Messenger - chemistry | Binding Sites | Saccharomyces cerevisiae Proteins - chemistry | Nucleases | Messenger RNA | Ribonuclease | DNA binding proteins | Genetic translation | Protein binding | NOT protein | Translation | scaffolds | Not1 protein | mRNA turnover | Polyadenylation | Evolution | Nuclease | Initiation factor eIF-4G | Life Sciences | Cellular Biology
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9. Full Text Interaction Profiling Identifies the Human Nuclear Exosome Targeting Complex
by Lubas, Michal and Christensen, Marianne S and Kristiansen, Maiken S and Domanski, Michal and Falkenby, Lasse G and Lykke-Andersen, Søren and Andersen, Jens S and Dziembowski, Andrzej and Jensen, Torben Heick
Molecular Cell, ISSN 1097-2765, 2011, Volume 43, Issue 4, pp. 624 - 637
The RNA exosome is a conserved degradation machinery, which obtains full activity only when associated with cofactors. The most prominent activator of the... 
TRANSCRIPTS | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | SURVEILLANCE | POLYADENYLATION | DEGRADATION | REQUIRES | MESSENGER-RNA DECAY | CAP-BINDING COMPLEX | RIBOSOMAL-RNA | ARS2 | CELL BIOLOGY | RNA Helicases - metabolism | Nuclear Proteins - analysis | Humans | RNA Helicases - analysis | Ribonucleases - metabolism | RNA Helicases - physiology | Cell Nucleolus - metabolism | Exoribonucleases - analysis | Carrier Proteins - analysis | RNA-Binding Proteins - analysis | Carrier Proteins - physiology | Exoribonucleases - physiology | Chromosomal Proteins, Non-Histone - metabolism | RNA-Binding Proteins - physiology | DNA-Directed DNA Polymerase - analysis | Nuclear Proteins - metabolism | Transcription Factors - metabolism | Carrier Proteins - metabolism | Models, Biological | Chromosomal Proteins, Non-Histone - analysis | Cell Nucleolus - enzymology | Nuclear Proteins - physiology | Transcription Factors - analysis | DNA-Directed DNA Polymerase - metabolism | Exosome Multienzyme Ribonuclease Complex | Exoribonucleases - metabolism | RNA-Binding Proteins - metabolism | Zinc compounds | Universities and colleges | RNA | Analysis | Protein binding
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10. Full Text BH3-only protein Bmf mediates apoptosis upon inhibition of CAP-dependent protein synthesis
by Grespi, F and Soratroi, C and Krumschnabel, G and Sohm, B and Ploner, C and Geley, S and Hengst, L and Häcker, G and Villunger, A
Cell Death and Differentiation, ISSN 1350-9047, 11/2010, Volume 17, Issue 11, pp. 1672 - 1683
Tight transcriptional regulation, alternative splicing and/or post-translational modifications of BH3-only proteins fine-tune their proapoptotic function. In... 
BH3-only proteins | Bmf | Apoptosis | Bcl-2 family | HOMEOSTASIS | INITIATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIM | apoptosis | DEFICIENT MICE | TRANSLATION | CELL BIOLOGY | LYMPHOCYTIC-LEUKEMIA CELLS | RIBOSOME ENTRY SITES | BCL-2 PROTEINS | PUMA | EXPRESSION | Protein Biosynthesis | Alternative Splicing | TOR Serine-Threonine Kinases - metabolism | Humans | Eukaryotic Initiation Factor-4E - metabolism | Apoptosis - genetics | RNA, Messenger - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Protein Isoforms - metabolism | Bcl-2-Like Protein 11 | Base Sequence | bcl-Associated Death Protein - metabolism | Transcription, Genetic | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | Proto-Oncogene Proteins - metabolism | Cell Line | Membrane Proteins - genetics | RNA, Messenger - genetics | Genes, bcl-2 | Apoptosis Regulatory Proteins - metabolism | Mitochondrial Membranes - metabolism | RNA Cap-Binding Proteins - metabolism | RNA Cap-Binding Proteins - genetics | Animals | Adaptor Proteins, Signal Transducing - genetics | Mice | Protein Processing, Post-Translational | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics
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