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Molecular and Cellular Biology, ISSN 0270-7306, 11/2005, Volume 25, Issue 22, pp. 10005 - 10016
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2018, Volume 115, Issue 50, pp. E11661 - E11670
Long noncoding RNAs (lncRNAs) function through a diverse array of mechanisms that are not presently fully understood. Here, we sought to find lncRNAs... 
C-Myc | Senescence | Proliferation | OVAAL | P27 | APOPTOSIS | proliferation | c-Myc | ORGAN SIZE CONTROL | MULTIDISCIPLINARY SCIENCES | CANCER | senescence | p27 | LONG NONCODING RNA | EMERGING ROLE | PATHWAY | RESISTANCE | MELANOMA-CELLS | RAF-1 ACTIVATION | Colorectal Neoplasms - genetics | Humans | Cell Survival - genetics | Apoptosis - genetics | RNA, Messenger - metabolism | MAP Kinase Signaling System | Cyclin-Dependent Kinase Inhibitor p27 - metabolism | Heterografts | Melanoma - genetics | Protein Stability | Cell Survival - physiology | Colorectal Neoplasms - metabolism | Protein-Serine-Threonine Kinases - metabolism | Melanoma - metabolism | Cellular Senescence - genetics | Cell Proliferation - genetics | Proto-Oncogene Proteins c-raf - genetics | RNA, Messenger - genetics | Cell Proliferation - physiology | Protein-Serine-Threonine Kinases - genetics | Cellular Senescence - physiology | RNA, Long Noncoding - genetics | Melanoma - pathology | TNF-Related Apoptosis-Inducing Ligand - metabolism | Proto-Oncogene Proteins c-myc - metabolism | Proto-Oncogene Proteins c-raf - metabolism | Animals | Mice, Nude | Cell Line, Tumor | Mice | Proto-Oncogene Proteins c-myc - genetics | Apoptosis - physiology | Colorectal Neoplasms - pathology | RNA, Long Noncoding - metabolism | TNF-Related Apoptosis-Inducing Ligand - genetics | Cyclin-Dependent Kinase Inhibitor p27 - genetics | RNA sequencing | Physiological aspects | Phosphotransferases | Methods | Cell proliferation | Adenocarcinoma | Transcription | Xenotransplantation | c-Myc protein | Raf protein | Feedback loops | Myc protein | Kinases | Positive feedback | Ovarian cancer | Proteins | Cell growth | Xenografts | Polypyrimidine tract-binding protein | Cell survival | Threonine | Melanoma | Extracellular signal-regulated kinase | MAP kinase | Gene expression | Survival | Mcl-1 protein | Signaling | Depletion | Cellular biology | Protein kinase | Tumor necrosis factor | TRAIL protein | Control theory | Cancer | Tumors | Apoptosis | Biological Sciences | PNAS Plus
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2013, Volume 8, Issue 5, p. e64783
Polypyrimidine tract-binding (PTB) proteins are RNA-binding proteins that generally contain four RNA recognition motifs (RRMs). In potato, six cDNAs encoding... 
PEPTIDE MOTIF | POTATO | RAVER1 | MULTIDISCIPLINARY SCIENCES | HOT-SPOTS | ARABIDOPSIS | HOMOLOGS | RNA RECOGNITION MOTIFS | DOMAINS | PTB | RNA-Binding Proteins - genetics | Molecular Sequence Data | Peptide Library | Antigens, Neoplasm - chemistry | Polypyrimidine Tract-Binding Protein - chemistry | Nerve Tissue Proteins - chemistry | Antigens, Neoplasm - metabolism | Solanum tuberosum - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Solanum tuberosum - genetics | Amino Acid Sequence | Antigens, Neoplasm - genetics | RNA-Binding Proteins - chemistry | Polypyrimidine Tract-Binding Protein - metabolism | Nerve Tissue Proteins - genetics | Amino Acid Motifs | Protein Interaction Mapping | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Sequence Alignment | Carrier Proteins - metabolism | Cell Surface Display Techniques | Protein Binding | Mutation | RNA-Binding Proteins - metabolism | Polypyrimidine Tract-Binding Protein - genetics | Physiological aspects | RNA | Binding proteins | Glycine | Protein binding | Yeast | Nova protein | Potatoes | Peptides | Phages | Cloning | Plant biology | Proline | Homology | Biochemistry | Biophysics | Metabolism | Ribonucleic acid--RNA | Peptide mapping | Proteins | Phage display | RNA-binding protein | Conserved sequence | Molecular biology | Localization | Bioinformatics | Binding sites | Ribonucleic acid
Journal Article
Cell, ISSN 0092-8674, 08/2016, Volume 166, Issue 5, pp. 1147 - 1162.e15
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2018, Volume 115, Issue 52, pp. E12218 - E12227
The influenza virulence factor NS1 protein interacts with the cellular NS1-BP protein to promote splicing and nuclear export of the viral M mRNAs. The viral M1... 
MRNA export | Splicing | Influenza virus | NS1 protein | Kelch | KELCH FAMILY | mRNA export | MATRIX | METASTASIS | MULTIDISCIPLINARY SCIENCES | INFLUENZA | POLYMERASE | IDENTIFICATION | ULTRACENTRIFUGATION | INTEGRATION | PATHWAY | influenza virus | splicing | ASSOCIATION | Influenza A virus - chemistry | Transcription Factors - chemistry | Humans | Influenza A virus - genetics | Crystallography, X-Ray | RNA, Messenger - metabolism | RNA Splicing | Cell Nucleus - metabolism | Protein Domains | Influenza, Human - virology | Active Transport, Cell Nucleus | Nuclear Proteins - genetics | Dimerization | Influenza, Human - metabolism | RNA, Messenger - genetics | Heterogeneous-Nuclear Ribonucleoproteins - metabolism | Viral Nonstructural Proteins - genetics | Nuclear Proteins - metabolism | Polypyrimidine Tract-Binding Protein - metabolism | Transcription Factors - genetics | Nuclear Proteins - chemistry | Heterogeneous-Nuclear Ribonucleoproteins - genetics | Transcription Factors - metabolism | Influenza A virus - metabolism | Cell Nucleus - genetics | Influenza, Human - genetics | Protein Binding | Viral Nonstructural Proteins - metabolism | Polypyrimidine Tract-Binding Protein - genetics | Microbiological research | Messenger RNA | Genetic aspects | Research | Host-virus relationships | Gene expression | Binding proteins | RNA splicing | Alternative splicing | Trafficking | Virulence | Metastasis | Immunity | Metastases | Proteins | Ion channels | Matrix protein | Crystal structure | RNA-protein interactions | Nuclear transport | Exports | Domains | Polymerase | Influenza | Proteomics | Dimers | Mutation | Splicing factors | Budding | Viral infections | Structure-function relationships | Biological Sciences | PNAS Plus
Journal Article
The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3202 - 3217
RNA–protein interactions play a pivotal role in the function of picornavirus internal ribosome entry site (IRES) elements. Here we analysed the impact of Ras... 
FMDV | G3BP1–RNA interaction | translation control | RNA structure | IRES elements | INITIATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDORIBONUCLEASE G3BP | CAP-INDEPENDENT TRANSLATION | RNA-BINDING PROTEIN | VIRUS-RNA | ELEMENTS | REPLICATION | RIBOSOME-ENTRY SITE | MESSENGER-RNA | G3BP1-RNA interaction | STRESS GRANULE FORMATION | Foot-and-Mouth Disease Virus - metabolism | Protein Biosynthesis | Humans | Ribosomes - metabolism | Internal Ribosome Entry Sites | Poly-ADP-Ribose Binding Proteins | RNA Helicases | RNA, Viral - genetics | Cloning, Molecular | Escherichia coli - metabolism | HEK293 Cells | Carrier Proteins - chemistry | RNA, Viral - metabolism | Nucleic Acid Conformation | RNA Recognition Motif Proteins | Binding Sites | Foot-and-Mouth Disease Virus - chemistry | Eukaryotic Initiation Factors - chemistry | Eukaryotic Initiation Factors - genetics | Eukaryotic Initiation Factors - metabolism | Recombinant Proteins - metabolism | Foot-and-Mouth Disease Virus - genetics | Gene Expression | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Sequence Homology, Nucleic Acid | Carrier Proteins - genetics | DNA Helicases | Sequence Alignment | Carrier Proteins - metabolism | RNA, Viral - chemistry | Ribosomes - genetics | Escherichia coli - genetics | SELEX Aptamer Technique | Protein Binding | Kinetics | Genetic translation | Protein binding | Translation | Internal ribosome entry site | Complex formation | RNA-protein interactions | Foot & mouth disease | Translation initiation | Fragments | Viruses | Ribonucleic acid--RNA | Gene sequencing | Impact analysis | Fragmentation | Electrophoretic mobility | Foot-and-mouth disease | Protein interaction | Guanosinetriphosphatase | Polypyrimidine tract-binding protein
Journal Article
PLoS ONE, ISSN 1932-6203, 08/2016, Volume 11, Issue 8, p. e0158708
Journal Article