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Folding & design, ISSN 1359-0278, 1996
Journal
Journal
Trends in Biochemical Sciences, ISSN 0968-0004, 02/2015, Volume 40, Issue 2, pp. 117 - 125
The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins. Emerging data explain how... 
protein–protein interactions | protein folding | molecular chaperones | Alzheimer disease | heat shock proteins | intrinsically disordered proteins | HSP72 Heat-Shock Proteins | Molecular Chaperones | HSP90 Heat-Shock Proteins | Humans | Intrinsically Disordered Proteins | Protein Binding | Substrate Specificity | Ligands | Alzheimer Disease | Protein Folding | Protein Interaction Maps | Heat shock proteins | Molecular chaperones | Intrinsically disordered proteins | Protein folding | Protein-protein interactions | X-RAY SOLUTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | STRUCTURAL-ANALYSIS | ESCHERICHIA-COLI HSP90 | POSTTRANSLATIONAL MODIFICATIONS | protein-protein interactions | HEAT-SHOCK-PROTEIN | GLUCOCORTICOID-RECEPTOR | SUBSTRATE-BINDING | N-TERMINAL DOMAIN | MOLECULAR CHAPERONE | Protein Binding - genetics | Molecular Chaperones - metabolism | Molecular Chaperones - genetics | HSP72 Heat-Shock Proteins - metabolism | Molecular Chaperones - chemistry | HSP72 Heat-Shock Proteins - chemistry | Alzheimer Disease - pathology | HSP72 Heat-Shock Proteins - genetics | Protein Interaction Maps - genetics | Intrinsically Disordered Proteins - chemistry | Alzheimer Disease - metabolism | HSP90 Heat-Shock Proteins - chemistry | HSP90 Heat-Shock Proteins - metabolism | HSP90 Heat-Shock Proteins - genetics | Alzheimer Disease - genetics | Intrinsically Disordered Proteins - metabolism | Proteins | Protein binding
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 6714 - 6722
The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a particularly rich set of interactions with disordered and partly ordered... 
ACTIVATION DOMAIN | UNSTRUCTURED PROTEINS | viral oncoprotein | intrinsically disordered protein | coupled folding and binding | intrinsically disordered region | BIOCHEMISTRY & MOLECULAR BIOLOGY | structure-function | STAT transcription factor | C-MYB | transcriptional coactivator | VIRAL-PROTEINS | transcriptional activation | P53 TRANSACTIVATION DOMAIN | COMPLEX-FORMATION | cAMP response element-binding protein (CREB) | hypoxia-inducible factor (HIF) | IDP | STRUCTURAL BASIS | IDR | KIX DOMAIN | TAZ2 DOMAIN | PEPTIDE MOTIFS | protein-protein interaction | Humans | E1A-Associated p300 Protein - genetics | STAT Transcription Factors - metabolism | CREB-Binding Protein - chemistry | NF-kappa B - metabolism | E1A-Associated p300 Protein - metabolism | NF-kappa B - chemistry | Viral Proteins - metabolism | Tumor Suppressor Protein p53 - genetics | CREB-Binding Protein - genetics | CREB-Binding Protein - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - chemistry | Transcription, Genetic | Protein Interaction Domains and Motifs | Protein Structure, Secondary | Hypoxia-Inducible Factor 1, alpha Subunit - genetics | Viral Proteins - chemistry | E1A-Associated p300 Protein - chemistry | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | Viral Proteins - genetics | Intrinsically Disordered Proteins - genetics | Protein Folding | STAT Transcription Factors - genetics | NF-kappa B - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | STAT Transcription Factors - chemistry | Tumor Suppressor Protein p53 - chemistry | Intrinsically Disordered Proteins - metabolism | Minireviews
Journal Article
Developmental Cell, ISSN 1534-5807, 07/2016, Volume 38, Issue 1, pp. 86 - 99
Journal Article
Journal of Molecular Recognition, ISSN 0952-3499, 03/2010, Volume 23, Issue 2, pp. 105 - 116
Recognition requires protein flexibility because it facilitates conformational rearrangements and induced‐fit mechanisms upon target binding. Intrinsic... 
disorder‐to‐order transition | NMR | Sic1 | polyelectrostatic effect | dynamic complex | protein dynamics | disordered complex | conformational disorder | Dynamic complex | Disordered complex | Polyelectrostatic effect | Protein dynamics | Conformational disorder | Disorder-to-order transition | SIDE-CHAIN DYNAMICS | DEUTERIUM SPIN PROBES | BIOCHEMISTRY & MOLECULAR BIOLOGY | disorder-to-order transition | INTRINSICALLY UNSTRUCTURED PROTEINS | UBIQUITIN LIGASES | SUBSTRATE RECOGNITION | BIOPHYSICS | HUB PROTEINS | RECEPTOR ZETA-CHAIN | STRUCTURAL DISORDER | ORDER PARAMETERS | INTERACTION NETWORKS | Adaptor Proteins, Signal Transducing - chemistry | Receptors, Antigen, T-Cell - chemistry | Phosphorylation | Receptors, Antigen, T-Cell - metabolism | F-Box Proteins - metabolism | F-Box Proteins - chemistry | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Cyclin-Dependent Kinase Inhibitor Proteins - metabolism | Ubiquitin-Protein Ligases - chemistry | Protein Folding | Cell Cycle Proteins - chemistry | Thermodynamics | Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Cyclin-Dependent Kinase Inhibitor Proteins - chemistry | Protein Binding | Protein Conformation | Proteins - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Evolution, Molecular | Saccharomyces cerevisiae Proteins - chemistry | Binding | Proteins | Dynamics | Evolutionary | Disorders | Charge | Order disorder | Recognition
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 6689 - 6695
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions... 
signaling | residual structure | electrostatics | coupled folding and binding | BIOCHEMISTRY & MOLECULAR BIOLOGY | protein electrostatics | C-MYB | TRANSITION-STATE | INDUCED FIT | protein-protein interactions | INTRINSICALLY DISORDERED PROTEINS | LINEAGE LEUKEMIA PROTEIN | IDP | MOLECULAR RECOGNITION | KIX DOMAIN | SEQUENCE | protein folding | phi-value | TRANSACTIVATION DOMAIN | kinetics | biophysics | protein dynamic | CONFORMATIONAL SELECTION | Cyclic AMP Response Element-Binding Protein - chemistry | Humans | Myeloid Cell Leukemia Sequence 1 Protein - metabolism | CREB-Binding Protein - chemistry | Proto-Oncogene Proteins - chemistry | CREB-Binding Protein - genetics | CREB-Binding Protein - metabolism | Thermodynamics | Apoptosis Regulatory Proteins - genetics | Myeloid Cell Leukemia Sequence 1 Protein - chemistry | Protein Interaction Domains and Motifs | Proto-Oncogene Proteins - metabolism | Signal Transduction | Apoptosis Regulatory Proteins - chemistry | Proto-Oncogene Proteins - genetics | Static Electricity | Intrinsically Disordered Proteins - genetics | Molecular Dynamics Simulation | Myeloid Cell Leukemia Sequence 1 Protein - genetics | Protein Folding | Apoptosis Regulatory Proteins - metabolism | Cyclic AMP Response Element-Binding Protein - genetics | Intrinsically Disordered Proteins - chemistry | Cyclic AMP Response Element-Binding Protein - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Kinetics | Intrinsically Disordered Proteins - metabolism | Minireviews
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
Journal Article