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Molecular and cellular biology, ISSN 0270-7306, 2008, Volume 28, Issue 7, pp. 2426 - 2436
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
INACTIVATION | APOPTOSIS | PROTEIN | SIGNALING PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | YAP | SIZE-CONTROL | DIFFERENTIATION | DROSOPHILA | TUMOR-SUPPRESSOR PATHWAY | CELL BIOLOGY | 14-3-3 Proteins - physiology | Phosphorylation | Transferases (Other Substituted Phosphate Groups) - genetics | Humans | Receptor Protein-Tyrosine Kinases - physiology | Recombinant Fusion Proteins - physiology | Transferases (Other Substituted Phosphate Groups) - physiology | Mesoderm - cytology | Drosophila Proteins - physiology | Cell Transdifferentiation - physiology | Membrane Proteins - physiology | Cell Division | c-Mer Tyrosine Kinase | Cell Cycle Proteins - genetics | Conserved Sequence | Transcription, Genetic | Epithelial Cells - cytology | Proteins - physiology | Nerve Tissue Proteins - physiology | Transcription Factors - physiology | Membrane Proteins - genetics | Protein-Serine-Threonine Kinases - physiology | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Transcription Factors - genetics | Nerve Tissue Proteins - genetics | Protein Processing, Post-Translational - physiology | Amino Acid Motifs | Proteins - genetics | Receptor Protein-Tyrosine Kinases - genetics | Cell Transformation, Neoplastic | Proto-Oncogene Proteins - physiology | Cell Line, Tumor | Nuclear Proteins - physiology | Drosophila Proteins - genetics | Cell Cycle Proteins - physiology | Cell Movement
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 43, pp. 17368 - 17373
Large tumor suppressor (LATS)1/2 protein kinases transmit Hippo signaling in response to intercellular contacts and serum levels to limit cell growth via the inhibition of Yes-associated protein (YAP... 
Cell growth | Phosphorylation | Starvation | Epithelial cells | Cell lines | Actins | Gene expression regulation | Breast cancer | Cellular immunity | Endothelial cells | Itch | Growth control | YES-ASSOCIATED PROTEIN | MIGRATION | REGULATOR | COMPLEX | DOMAIN | ACTIN | MULTIDISCIPLINARY SCIENCES | growth control | breast cancer | HIPPO PATHWAY REGULATION | FAMILY PROTEINS | Transcription, Genetic - drug effects | Humans | Phosphoproteins - metabolism | Intercellular Signaling Peptides and Proteins - metabolism | MCF-7 Cells | RNA Interference | Tumor Suppressor Proteins - genetics | HEK293 Cells | Membrane Proteins - metabolism | Phosphorylation - drug effects | Culture Media, Serum-Free - pharmacology | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | 14-3-3 Proteins - genetics | Amino Acid Sequence | Cell Line | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Intercellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - genetics | Ubiquitin-Protein Ligases - metabolism | Repressor Proteins - genetics | Serine - genetics | Binding Sites - genetics | Phosphoproteins - genetics | Reverse Transcriptase Polymerase Chain Reaction | Serine - metabolism | Blotting, Western | 14-3-3 Proteins - metabolism | Microscopy, Confocal | Animals | Adaptor Proteins, Signal Transducing - genetics | Cell Line, Tumor | Protein Binding | Cell Proliferation - drug effects | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin-Protein Ligases - genetics | Cell proliferation | Physiological aspects | Genetic transcription | Research | Protein kinases | Biological Sciences
Journal Article
Structure (London), ISSN 0969-2126, 2017, Volume 25, Issue 2, pp. 305 - 316
By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes... 
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 | small angle X-ray scattering
Journal Article
The Journal of cell biology, ISSN 1540-8140, 2015, Volume 210, Issue 3, pp. 435 - 450
The kinase PINK1 and ubiquitin ligase Parkin can regulate the selective elimination of damaged mitochondria through autophagy (mitophagy). Because of the... 
REGULATE AUTOPHAGY | FACTOR EB | PROTEIN-KINASE | MITOCHONDRIAL DEPOLARIZATION | IN-VIVO | AUTOPHAGOSOME FORMATION | ACETYL-COA CARBOXYLASE | CELLULAR CLEARANCE | P70 S6 KINASE | LYSOSOMAL BIOGENESIS | CELL BIOLOGY | Autophagy-Related Proteins | Protein Kinases - genetics | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Vesicular Transport Proteins - metabolism | Homeodomain Proteins - metabolism | Humans | rab GTP-Binding Proteins - genetics | Autophagy - physiology | Mitochondrial Proteins - genetics | Mechanistic Target of Rapamycin Complex 1 | Mitochondrial Degradation - genetics | Multiprotein Complexes - antagonists & inhibitors | TOR Serine-Threonine Kinases - antagonists & inhibitors | Lysosomes - metabolism | RNA Interference | HEK293 Cells | Membrane Proteins - metabolism | Active Transport, Cell Nucleus | Autophagy - genetics | Membrane Proteins - genetics | Phagosomes - metabolism | Ubiquitin-Protein Ligases - metabolism | Mitochondria - metabolism | Gene Knockout Techniques | Mitochondrial Degradation - physiology | 14-3-3 Proteins - metabolism | Autophagy-Related Protein 5 | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - genetics | Cell Line, Tumor | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - metabolism | RNA, Small Interfering | HeLa Cells | Ubiquitin-Protein Ligases - genetics | Microphthalmia-Associated Transcription Factor - genetics | Biosynthesis | Mitochondrial DNA | DNA binding proteins | Analysis
Journal Article
PloS one, ISSN 1932-6203, 2010, Volume 5, Issue 11, p. e15394
... cytoplasmic contents (e.g., proteins, lipids, and organelles) to lysosomes for degradation [1]. There are three major pathways of autophagy in eukaryotic cells, namely... 
COMPLEX | ACTIVATED PROTEIN-KINASE | METABOLISM | PHOSPHORYLATION | MACHINERY | BIOLOGY | INHIBITS CELL-GROWTH | INDUCTION | SACCHAROMYCES-CEREVISIAE | ATG13 | DEGENERATION | AMP-Activated Protein Kinases - metabolism | Phosphorylation | Immunoprecipitation | Humans | Multiprotein Complexes | Immunoblotting | Intracellular Signaling Peptides and Proteins - metabolism | Autophagy | Protein Subunits - metabolism | Autophagy-Related Protein-1 Homolog | Mechanistic Target of Rapamycin Complex 1 | Transfection | RNA Interference | HEK293 Cells | Regulatory-Associated Protein of mTOR | Binding Sites | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | 14-3-3 Proteins - genetics | Protein Subunits - genetics | Cell Line | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Mice, Knockout | 14-3-3 Proteins - metabolism | Proteins - genetics | Animals | Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Cell Line, Tumor | Protein Binding | Mice | TOR Serine-Threonine Kinases | Mutation | Adaptor Proteins, Signal Transducing - metabolism | AMP-Activated Protein Kinases - genetics | Microscopy, Fluorescence | TOR protein | Tuberous Sclerosis Complex 2 | Yeast | Homology | Kinases | Inactivation | Proteins | Cell growth | Cell cycle | Binding | Biodegradation | Deactivation | Threonine | Pharmacology | Metabolism | Mammals | Environmental stress | Medicine | 14-3-3 protein | Insects | Environmental degradation | Protein-serine/threonine kinase | Regulation | Phagocytosis | Cancer | Apoptosis
Journal Article
Cancer Research, ISSN 0008-5472, 03/2011, Volume 71, Issue 6, pp. 2328 - 2338
Pancreatic cancer is an exceptionally aggressive disease in great need of more effective therapeutic options. Epithelial-mesenchymal transition (EMT) plays a... 
INITIATING CELLS | ONCOLOGY | GROWTH | GENES | NOTCH | ACUTE MYELOID-LEUKEMIA | IDENTIFICATION | EXPRESSION | PROGRESSION | CANCER STEM-CELLS | BRAIN-TUMORS | Immunohistochemistry | ras Proteins - genetics | Pancreatic Neoplasms - metabolism | Exoribonucleases | Vimentin - metabolism | Humans | ras Proteins - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Epithelial-Mesenchymal Transition - genetics | Zinc Finger E-box Binding Homeobox 2 | RNA Interference | Biomarkers, Tumor - metabolism | Exonucleases - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Gene Expression | Pancreatic Neoplasms - pathology | Protein-Serine-Threonine Kinases - genetics | Repressor Proteins - genetics | Mice, Transgenic | Pancreatic Neoplasms - genetics | Receptor, Notch1 - metabolism | Transcription Factors - genetics | Reverse Transcriptase Polymerase Chain Reaction | Proto-Oncogene Proteins c-myc - metabolism | Homeodomain Proteins - genetics | 14-3-3 Proteins - metabolism | Animals | Twist-Related Protein 1 - genetics | Cell Line, Tumor | Mice | MicroRNAs - genetics | Proto-Oncogene Proteins c-myc - genetics | Mutation | Receptor, Notch1 - genetics | Zinc Finger E-box-Binding Homeobox 1 | epithelial-mesenchymal transition (EMT) | pancreatic intraepithelial neoplasia (PanIN) | Cancer Stem Cell Marker | miR-144 | 14-3-3 σ | Let-7a | vimentin | miR-200a | DCAMKL-1 | Dclk-1 | Notch-1
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2004, Volume 101, Issue 33, pp. 12288 - 12293
Signaling pathways regulating proliferation, differentiation, and apoptosis are commonly mediated through protein-protein interactions as well as reversible phosphorylation of proteins... 
Proteins | Biological Sciences | Bioluminescence | Phosphorylation | HEK293 cells | Plasmids | Drug interactions | Imaging | Cell lines | Photons | Cells | PATHWAYS | INTERFERON | DOMAIN | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | IN-VIVO | KINASE | DIMERIZATION | TARGETS | CDC25C | CANCER | Protein Kinases - metabolism | Sequence Deletion | Tyrosine 3-Monooxygenase - metabolism | Protein Kinases - genetics | Luciferases - metabolism | Humans | Tacrolimus Binding Proteins - metabolism | Trans-Activators - chemistry | Genetic Complementation Test | Luciferases - genetics | DNA-Binding Proteins - metabolism | Trans-Activators - genetics | Cell Cycle Proteins - genetics | cdc25 Phosphatases - metabolism | Dimerization | Peptide Fragments - genetics | Recombinant Proteins - metabolism | Cell Line | Peptide Fragments - metabolism | Signal Transduction | Cell Cycle Proteins - metabolism | Recombinant Proteins - genetics | cdc25 Phosphatases - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Sirolimus - pharmacology | Tacrolimus Binding Proteins - genetics | Proteins - genetics | Tyrosine 3-Monooxygenase - genetics | Animals | Proteins - metabolism | Protein Binding | STAT1 Transcription Factor | Trans-Activators - metabolism | 14-3-3 Proteins | Mice | TOR Serine-Threonine Kinases | Kinetics | Luciferase | Research
Journal Article
Proteomics (Weinheim), ISSN 1615-9861, 2009, Volume 9, Issue 11, pp. 2967 - 2985
In eukaryotes, 14‐3‐3 dimers regulate hundreds of functionally diverse proteins (clients), typically in phosphorylation... 
14‐3‐3 | Arabidopsis | Interactome | Kinase | Tandem affinity purification | 14-3-3 | PLANT | MEMBRANE H+-ATPASE | PHOSPHOLIPASE-D | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | 14-3-3-PROTEIN GF14-LAMBDA | GLUTAMATE-RECEPTOR | PHOSPHATIDIC-ACID | K+ CHANNEL | EXPRESSION | BINDING | 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 | tandem affinity purification | kinase | proteomics | 18O | iTRAQ | 16O | MudPIT | interactome | phosphorylation
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2016, Volume 291, Issue 29, pp. 14973 - 14985
Cell viability requires adaptation to changing environmental conditions. Ubiquitin-mediated endocytosis plays a crucial role in this process, because it provides a mechanism to remove transport proteins from the membrane... 
COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHEROMONE RESPONSE | TRAFFICKING | PERMEASE | MULTIVESICULAR BODY | CELL-SURFACE | SWITCH | UBIQUITIN-LIGASE | ENDOCYTOSIS | SACCHAROMYCES-CEREVISIAE | Arrestins - chemistry | Saccharomyces cerevisiae - genetics | Arrestins - genetics | Arrestins - metabolism | Recombinant Fusion Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Monosaccharide Transport Proteins - metabolism | Protein-Serine-Threonine Kinases - metabolism | 14-3-3 Proteins - genetics | Monosaccharide Transport Proteins - genetics | Signal Transduction | Membrane Proteins - genetics | Protein-Serine-Threonine Kinases - genetics | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | 14-3-3 Proteins - metabolism | Membrane Proteins - chemistry | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | Recombinant Fusion Proteins - genetics | 14-3-3 Proteins - chemistry | Monosaccharide Transport Proteins - chemistry | Protein-Serine-Threonine Kinases - chemistry | Saccharomyces cerevisiae Proteins - chemistry | 14-3-3 protein | AMP-activated kinase (AMPK) | membrane transport | arrestin | trafficking | yeast | Cell Biology
Journal Article
Molecular cell, ISSN 1097-2765, 2017, Volume 66, Issue 1, pp. 117 - 128.e5
Journal Article
PloS one, ISSN 1932-6203, 2017, Volume 12, Issue 6, p. e0178933
Abundant regulatory 14-3-3 proteins have an extremely wide interactome and coordinate multiple cellular events via interaction with specifically phosphorylated partner proteins... 
Exoribonucleases - genetics | Phosphorylation | Humans | tau Proteins - metabolism | Protein Interaction Maps | Cyclic AMP-Dependent Protein Kinases - genetics | Protein Isoforms - metabolism | tau Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Parkinson Disease - metabolism | Exoribonucleases - analysis | 14-3-3 Proteins - genetics | Cyclic AMP-Dependent Protein Kinases - metabolism | Gene Expression | Biomarkers, Tumor - analysis | Protein Isoforms - analysis | 14-3-3 Proteins - metabolism | Cyclic AMP-Dependent Protein Kinases - analysis | 14-3-3 Proteins - analysis | Escherichia coli - genetics | Alzheimer Disease - metabolism | Biomarkers, Tumor - genetics | tau Proteins - analysis | Exoribonucleases - metabolism | Protein Isoforms - genetics | Research | Protein kinases | Protein-protein interactions | Protein kinase A | Stoichiometry | Residues | Identification methods | Disorders | Displays | Biochemistry | Biology | Kinases | Proteins | Signal transduction | Functional anatomy | E coli | Rodents | Bacteria | Physiology | Binding | Neurodegenerative diseases | Fetuses | Cloning | Diseases | Studies | Neurological diseases | 14-3-3 protein | Tau protein | Protein kinase | Plasmids | Isoforms | Protein expression | Regulation | Alzheimers disease | In vitro methods and tests | Binding sites | Apoptosis
Journal Article