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Structure, ISSN 0969-2126, 02/2017, Volume 25, Issue 2, pp. 305 - 316
By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6,... 
14-3-3 proteins | smooth muscle relaxation | small heat shock proteins | regulatory complex | crystal structure | protein-protein interaction | phosphopeptides | conformational change | small-angle X-ray scattering | intrinsically disordered regions | PHOSPHORYLATION | MOLECULE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-B-CRYSTALLIN | CELL BIOLOGY | DOMAIN DIMERS | BIOPHYSICS | PURIFICATION | AIRWAY SMOOTH-MUSCLE | BINDING | EXPRESSION | WEB SERVER | HSP20 HSPB6 | Exoribonucleases - genetics | Phosphorylation | Humans | Protein Multimerization | Exoribonucleases - chemistry | Substrate Specificity | Crystallography, X-Ray | HSP20 Heat-Shock Proteins - genetics | Phosphoproteins - metabolism | HSP20 Heat-Shock Proteins - metabolism | Phosphoproteins - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Protein Interaction Domains and Motifs | Binding Sites | HSP20 Heat-Shock Proteins - chemistry | 14-3-3 Proteins - genetics | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Signal Transduction | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Phosphoproteins - genetics | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | 14-3-3 Proteins - metabolism | Protein Conformation, beta-Strand | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | 14-3-3 Proteins - chemistry | Biomarkers, Tumor - genetics | Biomarkers, Tumor - chemistry | Exoribonucleases - metabolism | Intrinsically Disordered Proteins - metabolism | Proteins | Fluorescence spectroscopy | Proteolysis | Analysis | Crystals | Fluorescence | Atoms | Heat shock proteins | Molecular biology | Structure | Protein-protein interactions | Index Medicus | small angle X-ray scattering
Journal Article
Nature, ISSN 0028-0836, 08/2011, Volume 476, Issue 7360, pp. 332 - 335
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2016, Volume 291, Issue 29, pp. 14973 - 14985
Journal Article
Proteomics, ISSN 1615-9853, 06/2009, Volume 9, Issue 11, pp. 2967 - 2985
In eukaryotes, 14-3-3 dimers regulate hundreds of functionally diverse proteins (clients), typically in phosphorylation-dependent interactions. To uncover new... 
14-3-3 | Arabidopsis | Interactome | Kinase | Tandem affinity purification | TRANSCRIPTION FACTORS | PLANT-CELL | MEMBRANE H+-ATPASE | PHOSPHOLIPASE-D | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | 14-3-3-PROTEIN GF14-LAMBDA | SACCHAROMYCES-CEREVISIAE | GLUTAMATE-RECEPTOR | STRESS RESPONSES | PHOSPHATIDIC-ACID | K+ CHANNEL | Consensus Sequence | Electrophoresis, Gel, Two-Dimensional | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Arabidopsis Proteins - metabolism | Tandem Mass Spectrometry | Plant Proteins - chemistry | Plant Proteins - metabolism | Proteomics - methods | Green Fluorescent Proteins - chemistry | 14-3-3 Proteins - genetics | Green Fluorescent Proteins - metabolism | Arabidopsis Proteins - genetics | Arabidopsis - chemistry | Plants, Genetically Modified - genetics | Signal Transduction | Recombinant Fusion Proteins - chemistry | Amino Acid Motifs | Arabidopsis - metabolism | 14-3-3 Proteins - metabolism | Arabidopsis - genetics | Plant Proteins - genetics | Protein Interaction Mapping - methods | Plants, Genetically Modified - metabolism | Arabidopsis Proteins - chemistry | Escherichia coli - genetics | Protein Isoforms | Protein Binding | Recombinant Fusion Proteins - genetics | 14-3-3 Proteins - chemistry | Index Medicus | tandem affinity purification | kinase | proteomics | 18O | iTRAQ | 16O | MudPIT | interactome | phosphorylation
Journal Article
RNA, ISSN 1355-8382, 06/2019, Volume 25, Issue 6, pp. 737 - 746
Human RNA exoribonuclease 2 (Rexo2) is an evolutionarily conserved 3'-to-5' DEDDh-family exonuclease located primarily in mitochondria. Rexo2 degrades small... 
RNA decay | Exonuclease | Protein–RNA interactions | Ribonuclease | Crystal structure | STRANDED-RNA | exonuclease | CRYSTAL-STRUCTURE | DNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | crystal structure | protein-RNA interactions | ribonuclease | OLIGORIBONUCLEASE | FAMILY | Exoribonucleases - genetics | Humans | Protein Multimerization | Exoribonucleases - chemistry | Crystallography, X-Ray | Mitochondrial Proteins - genetics | RNA - genetics | DNA, Single-Stranded - genetics | Oligoribonucleotides - metabolism | Mitochondrial Proteins - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Protein Interaction Domains and Motifs | Oligoribonucleotides - chemistry | Mitochondria - chemistry | Binding Sites | 14-3-3 Proteins - genetics | RNA - metabolism | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | DNA, Single-Stranded - metabolism | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Magnesium - metabolism | Mitochondria - metabolism | Recombinant Proteins - genetics | RNA - chemistry | DNA, Single-Stranded - chemistry | 14-3-3 Proteins - metabolism | Hydrolysis | Magnesium - chemistry | Cations, Divalent | Protein Conformation, beta-Strand | Escherichia coli - genetics | Mitochondrial Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Binding | 14-3-3 Proteins - chemistry | Biomarkers, Tumor - genetics | Biomarkers, Tumor - chemistry | Exoribonucleases - metabolism | Oligoribonucleotides - genetics | Mitochondria | Single-stranded DNA | Oligonucleotides | Nucleotides | Magnesium | Hydrophobicity | Ribonucleic acid--RNA | Deoxyribonucleic acid--DNA | protein–RNA interactions
Journal Article
Genes and Development, ISSN 0890-9369, 11/2007, Volume 21, Issue 21, pp. 2747 - 2761
The Hippo pathway plays a key role in organ size control by regulating cell proliferation and apoptosis in Drosophila. Although recent genetic studies have... 
Contact inhibition | Lats | YAP | NF2 | Hippo | Mst | YES-ASSOCIATED PROTEIN | hippo | PROLIFERATION ARREST | SIZE CONTROL | lats | DEVELOPMENTAL BIOLOGY | mst | CELL BIOLOGY | ORGAN SIZE | SIGNALING PATHWAY | CYCLE EXIT | GENETICS & HEREDITY | IMAGINAL DISC | contact inhibition | BANTAM MICRORNA | TUMOR-SUPPRESSOR PATHWAY | PROMOTES APOPTOSIS | Protein Kinases - metabolism | NIH 3T3 Cells | Phosphorylation | Cell Proliferation | Cell Count | Humans | Drosophila Proteins - metabolism | Trans-Activators - chemistry | Contact Inhibition - genetics | Trans-Activators - physiology | Drosophila Proteins - physiology | Drosophila Proteins - antagonists & inhibitors | Drosophila - genetics | Amino Acid Sequence | Protein-Serine-Threonine Kinases - physiology | Cells, Cultured | Intracellular Signaling Peptides and Proteins | Nuclear Proteins - metabolism | Cell Communication - genetics | Drosophila Proteins - chemistry | Nuclear Proteins - chemistry | Amino Acid Motifs | Protein Transport | 14-3-3 Proteins - metabolism | Animals | Models, Biological | Nuclear Proteins - antagonists & inhibitors | Protein Binding | Signal Transduction - physiology | Trans-Activators - metabolism | Drosophila - growth & development | Mice | Nuclear Proteins - physiology | HeLa Cells | Trans-Activators - antagonists & inhibitors | Cell proliferation | Drosophila | Tumor suppressor genes | Genetic aspects | Research | Genetic transcription | Apoptosis | Index Medicus | Research Paper
Journal Article
The FEBS Journal, ISSN 1742-464X, 02/2018, Volume 285, Issue 3, pp. 467 - 480
The salt‐inducible kinase ( SIK ) family regulates cellular gene expression via the phosphorylation of cAMP‐regulated transcriptional coactivators ( CRTC s)... 
14‐3‐3 protein | protein phosphorylation | catalytic activity | transcriptional regulation | 14-3-3 protein | LOCALIZATION | CREB | STRUCTURAL BASIS | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | LKB1 | Protein Kinases - metabolism | Phosphorylation | Protein Kinases - genetics | Transcription Factors - chemistry | Humans | Protein Kinases - chemistry | Substrate Specificity | Recombinant Fusion Proteins - metabolism | HEK293 Cells | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Conserved Sequence | Protein Interaction Domains and Motifs | Active Transport, Cell Nucleus | Binding Sites | Cyclic AMP - metabolism | Peptide Fragments - genetics | Protein-Serine-Threonine Kinases - metabolism | Cyclic AMP-Dependent Protein Kinases - metabolism | Peptide Fragments - metabolism | Protein-Serine-Threonine Kinases - genetics | Recombinant Fusion Proteins - chemistry | Transcription Factors - genetics | 14-3-3 Proteins - metabolism | Transcription Factors - metabolism | Peptide Fragments - chemistry | Animals | Peptide Fragments - antagonists & inhibitors | Mice | Protein Processing, Post-Translational | Protein-Serine-Threonine Kinases - chemistry | Mutation | Transcription Factors - agonists | Amino Acid Substitution | Proteins | Cyclic adenylic acid | Protein binding | Protein kinase A | Repressing | Salts | Transcription | Cyclic AMP | Substrate inhibition | Catalytic activity | Kinases | Gene expression | Substrates | Signaling | Evolutionary conservation | Salt-inducible kinase | Catalysis | Binding sites | Cytoplasm | Index Medicus
Journal Article
Angewandte Chemie - International Edition, ISSN 0570-0833, 2017, Volume 56, Issue 31, pp. 8998 - 9002
Journal Article
The EMBO Journal, ISSN 0261-4189, 02/2005, Volume 24, Issue 3, pp. 473 - 486
Journal Article