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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 04/2019, Volume 116, Issue 18, pp. 8859 - 8868
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 04/2011, Volume 7, Issue 4, pp. 193 - 194
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 04/2011, Volume 7, Issue 4, pp. 193 - 194
  Detailed biophysical and biochemical studies provide an exquisite example of how conformational flexibility controls the interaction between an intrinsically... 
INHIBITOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | Proteins - metabolism | Protein Conformation | Proteins - analysis | Proteins - chemistry | Binding Sites | Molecular Dynamics Simulation | Protein Folding | Proteins | Biochemistry | Cyclin-dependent kinases | Binding sites | Index Medicus
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 10/2013, Volume 81, Issue 10, pp. 1686 - 1698
Journal Article
Molecular Biology and Evolution, ISSN 0737-4038, 01/2012, Volume 29, Issue 1, p. 443
Journal Article
Nature chemical biology, ISSN 1552-4450, 12/2014, Volume 10, Issue 12, pp. 1000 - 1002
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 10/2013, Volume 81, Issue 10, pp. 1738 - 1747
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2015, Volume 112, Issue 15, pp. 4624 - 4629
The p53 inhibitor MDMX is controlled by multiple stress signaling pathways. Using a proteolytic fragment release (PFR) assay, we detected an intramolecular... 
Acidic domain | Protease | Intramolecular | MDMX | p53 | CELLS | ACTIVATION | MULTIDISCIPLINARY SCIENCES | DNA-DAMAGE | DIMERIZATION | ALPHA | intramolecular | CANCER-THERAPY | protease | DEGRADATION | acidic domain | INHIBITOR | DOMAINS | Proto-Oncogene Proteins c-mdm2 - genetics | Humans | Molecular Sequence Data | Tryptophan - chemistry | Proto-Oncogene Proteins - chemistry | Proto-Oncogene Proteins c-mdm2 - chemistry | Tryptophan - metabolism | Tumor Suppressor Protein p53 - genetics | Molecular Mimicry | Peptides - metabolism | Proteolysis | Nuclear Proteins - genetics | Proto-Oncogene Proteins c-mdm2 - metabolism | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Magnetic Resonance Spectroscopy | Peptides - chemistry | Tryptophan - genetics | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Binding Sites - genetics | Nuclear Proteins - chemistry | Blotting, Western | Sequence Homology, Amino Acid | Cell Line, Tumor | Hydrophobic and Hydrophilic Interactions | Protein Binding | Tumor Suppressor Protein p53 - chemistry | Mutation | Physiological aspects | Tumor suppressor genes | Genetic transcription | Proteins | Peptides | Biological assays | Proteomics | Index Medicus | Biological Sciences
Journal Article
Biochemistry, ISSN 0006-2960, 05/2017, Volume 56, Issue 18, pp. 2379 - 2384
Appropriate integration of cellular signals requires a delicate balance of ligand target binding affinities. Increasing the level of residual structure in... 
UNSTRUCTURED PROTEINS | IMPROVED SENSITIVITY | SPECTROSCOPY | BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | KIX DOMAIN | Myeloid-Lymphoid Leukemia Protein - metabolism | Proline - metabolism | Humans | Myeloid-Lymphoid Leukemia Protein - chemistry | Phosphoproteins - metabolism | Phosphoproteins - chemistry | Tumor Suppressor Protein p53 - genetics | Cloning, Molecular | Escherichia coli - metabolism | Conserved Sequence | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Histone-Lysine N-Methyltransferase - genetics | Membrane Proteins - genetics | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Phosphoproteins - genetics | Intrinsically Disordered Proteins - genetics | Protein Folding | Proline - chemistry | Histone-Lysine N-Methyltransferase - chemistry | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Histone-Lysine N-Methyltransferase - metabolism | Membrane Proteins - chemistry | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Myeloid-Lymphoid Leukemia Protein - genetics | Protein Binding | Mice | Tumor Suppressor Protein p53 - chemistry | Mutation | Intrinsically Disordered Proteins - metabolism | Helix-loop-helix motif | Protein deficiency | Research | Index Medicus
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 08/2018, Volume 430, Issue 16, pp. 2389 - 2402
Journal Article
ISSN 1742-206X, 12/2011, Volume 8, Issue 1, pp. 38 - 319
Developing a comprehensive description of the equilibrium structural ensembles for intrinsically disordered proteins (IDPs) is essential to understanding their... 
Journal Article
Intrinsically Disordered Proteins, ISSN 2169-0693, 01/2015, Volume 3, Issue 1, pp. e984565 - e984565
A short segment of the disordered p53 transactivation domain (p53TAD) forms an amphipathic helix when bound to the E3 ubiquitin ligase, MDM2. In the unbound... 
chemical shift | Intrinsically disordered proteins | ensemble generation | nuclear magnetic resonance | re-weighting | p53 | Ensemble generation | Chemical shift | Re-weighting | Nuclear magnetic resonance | P53
Journal Article
Biophysical Journal, ISSN 0006-3495, 01/2015, Volume 108, Issue 2, pp. 227a - 228a
Journal Article