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PLoS ONE, ISSN 1932-6203, 2010, Volume 5, Issue 11, p. e15394
Autophagy is a highly orchestrated intracellular bulk degradation process that is activated by various environmental stresses. The serine/threonine kinase... 
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 | Yeast | Homology | Kinases | Inactivation | Proteins | Cell growth | Cell cycle | Binding | Biodegradation | Deactivation | Threonine | Pharmacology | Metabolism | Mammals | Environmental stress | Medicine | TSC2 protein | 14-3-3 protein | Insects | Environmental degradation | Protein-serine/threonine kinase | Regulation | Phagocytosis | Cancer | Apoptosis
Journal Article
Biochemical Journal, ISSN 0264-6021, 04/2010, Volume 427, Issue 1, pp. 69 - 78
More than 200 phosphorylated 14-3-3-binding sites in the literature were analysed to define 14-3-3 specificities, identify relevant protein kinases, and give... 
Evolution | 14-3-3 protein | Disrupted-in-schizophrenia 1 (DISC1) | calmodulin-dependent protein kinase | AGC protein kinase | NEURONAL MIGRATION | SIGNALING PATHWAYS | MEMBRANE H+-ATPASE | REGULATING 14-3-3 BINDING | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | EUKARYOTIC PROTEIN-KINASES | evolution | NUCLEAR-LOCALIZATION | EXOENZYME-S | STRUCTURAL BASIS | Ca2+/calmodulin-dependent protein kinase | disrupted-in-schizophrenia 1 (DISC1) | ENDOPLASMIC-RETICULUM | Protein Kinases - metabolism | Phosphorylation | Immunoprecipitation | Humans | RNA, Messenger - genetics | Cells, Cultured | Computational Biology | Kidney - cytology | RNA, Messenger - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | 14-3-3 Proteins - metabolism | Nerve Tissue Proteins - metabolism | Kidney - metabolism | Carrier Proteins - metabolism | Protein Binding | Binding Sites | Dimerization | Calcium-Calmodulin-Dependent Protein Kinases - metabolism | 14-3-3 Proteins - genetics | Bcl-2-associated death promoter | AANAT, serotonin acetyltransferase | FOXO, Forkhead box O | KLC, kinesin light chain | CDK5, cyclin-dependent kinase 5 | HEK, human embryonic kidney | MARK, microtubule affinity-regulating kinase | AMPK, AMP-activated protein kinase | EST, expressed sequence tag | PKB, protein kinase B | RSK, ribosomal S6 kinase | CaMK, Ca2 | GLUT4, glucose transporter 4 | protein kinase G | GST, glutathione transferase | HDAC, histone deacetylase | HAP1A, Huntingtin-associated protein 1A | DIG, digoxigenin | PKC, protein kinase C | BAD, Bcl-XL | PP2A, protein phosphatase 2A | DSTT, Division of Signal Transduction Therapy | HA, haemagglutinin | AGC, protein kinase A | Ca2 | PI4K, phosphoinositide 4-kinase | DISC1, disrupted-in-schizophrenia 1 | protein kinase C family kinase | YAP1, yes-associated protein 1
Journal Article
Nature Chemistry, ISSN 1755-4330, 03/2013, Volume 5, Issue 3, pp. 234 - 239
Journal Article
The Plant Cell, ISSN 1040-4651, 5/2007, Volume 19, Issue 5, pp. 1617 - 1634
Regulation of the trans-plasma membrane pH gradient is an important part of plant responses to several hormonal and environmental cues, including auxin, blue... 
Proteins | 14-3-3 proteins | Yeasts | Phosphorylation | Plant roots | Cell membranes | Plants | Seedlings | Plant cells | CELLS | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BLUE-LIGHT | PLANT SCIENCES | CELL BIOLOGY | ION FLUXES | PLANT SALT TOLERANCE | C-TERMINAL REGION | CALCIUM | STRESS SIGNAL-TRANSDUCTION | BINDING-SITE | REGULATORY DOMAIN | Protons | Gene Expression Regulation, Enzymologic - drug effects | Arabidopsis - enzymology | Adaptation, Physiological - drug effects | Molecular Sequence Data | DNA, Bacterial | Plant Roots - drug effects | Arabidopsis Proteins - metabolism | Saccharomyces cerevisiae - metabolism | RNA Interference | Protein Binding - drug effects | Ethyl Methanesulfonate | Proton-Translocating ATPases - antagonists & inhibitors | Cell Membrane - drug effects | Protein-Serine-Threonine Kinases - metabolism | Membrane Potentials - drug effects | Amino Acid Sequence | Arabidopsis Proteins - genetics | Arabidopsis - drug effects | Plant Roots - metabolism | Arabidopsis - cytology | Protein-Serine-Threonine Kinases - genetics | Down-Regulation - drug effects | Mutation - genetics | Phosphoserine - metabolism | Proton-Translocating ATPases - chemistry | 14-3-3 Proteins - metabolism | Arabidopsis - genetics | Cell Membrane - enzymology | Gene Expression Regulation, Plant - drug effects | Arabidopsis Proteins - chemistry | Calcium Signaling - drug effects | Alleles | Plant Growth Regulators - pharmacology | Arabidopsis Proteins - antagonists & inhibitors | Hydrogen-Ion Concentration
Journal Article
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 | small angle X-ray scattering
Journal Article
The FEBS Journal, ISSN 1742-464X, 05/2017, Volume 284, Issue 9, pp. 1279 - 1295
The ubiquitous eukaryotic 14‐3‐3 proteins coordinate multiple cellular processes due to their well‐known regulatory function, which is based on specific... 
hydrophobicity | signal transduction | dimer interface | aggregation | oligomeric structure | neurodegenerative disorders | chaperones | phosphorylation | 14‐3‐3 proteins | dimer–monomer equilibrium | 14-3-3 proteins | TAU-PROTEIN | FUNCTIONAL INTERACTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ISOFORM-SPECIFIC MANNER | SUBCELLULAR-LOCALIZATION | ALPHA-CRYSTALLIN | RAT-LIVER CYTOSOL | PRECURSOR PROTEINS | dimer-monomer equilibrium | MOLECULAR CHAPERONE | C-TERMINAL EXTENSION | MITOCHONDRIAL IMPORT | Phosphorylation | Molecular Chaperones - metabolism | Humans | Protein Multimerization | Protein Refolding | Models, Molecular | Molecular Chaperones - chemistry | Amino Acid Motifs | 14-3-3 Proteins - metabolism | Animals | Hydrophobic and Hydrophilic Interactions | 14-3-3 Proteins - chemistry | Protein Conformation | Protein Interaction Domains and Motifs | Protein Processing, Post-Translational | Binding Sites | Dimerization | Molecular Chaperones - agonists | Heat shock proteins | Control systems | Nervous system diseases | Prions | Huntingtin | Aggresomes | Neurodegenerative diseases | Hydrophobicity | Chaperones | Small heat shock proteins | Synuclein | Proteins | 14-3-3 protein | Eukaryotes | Molecular modelling | Tau protein | Protein folding | Quality control | Proteasomes | Molecular biology | Prion protein
Journal Article