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The Journal of biological chemistry, ISSN 1083-351X, 07/2016, Volume 291, Issue 29, pp. 14973 - 14985
Journal Article
Biochemistry (Easton), ISSN 0006-2960, 08/2017, Volume 56, Issue 30, pp. 3972 - 3982
Proteins typically interact with multiple binding partners, and often different parts of their surfaces are employed to establish these protein... 
Research Support, Non-U.S. Gov't | Biochemistry | Journal Article | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Exoribonucleases - genetics | Phosphorylation | Transcription Factors - chemistry | Humans | Exoribonucleases - chemistry | Crystallography, X-Ray | Peptide Library | Recombinant Fusion Proteins - metabolism | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Gene Deletion | Biomarkers, Tumor - metabolism | Conserved Sequence | Nuclear Magnetic Resonance, Biomolecular | Protein Interaction Domains and Motifs | Binding Sites | Peptide Fragments - genetics | 14-3-3 Proteins - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Peptide Fragments - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Transcription Factors - genetics | Protein Interaction Mapping | 14-3-3 Proteins - metabolism | Transcription Factors - metabolism | Peptide Fragments - chemistry | 14-3-3 Proteins - chemistry | Ligands | Protein Conformation | Biomarkers, Tumor - genetics | Protein Processing, Post-Translational | Kinetics | Biomarkers, Tumor - chemistry | Exoribonucleases - metabolism | Protein Isoforms - genetics | X-ray crystallography | Usage | Ligand binding (Biochemistry) | Analysis | Research | Nuclear magnetic resonance | Protein-protein interactions | Index Medicus
Journal Article
Chembiochem : a European journal of chemical biology, ISSN 1439-4227, 02/2017, Volume 18, Issue 3, pp. 331 - 335
Journal Article
Nature chemistry, ISSN 1755-4349, 02/2013, Volume 5, Issue 3, pp. 234 - 239
Journal Article
PloS one, ISSN 1932-6203, 06/2017, Volume 12, Issue 6, pp. e0178933 - 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 | Index Medicus
Journal Article
Journal Article
Structure (London), 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... 
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 | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | 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