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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2016, Volume 113, Issue 9, pp. E1152 - E1161
Journal Article
Biochemistry, ISSN 0006-2960, 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 protein... 
COMPLEX | SMALL-MOLECULE STABILIZATION | INHIBITION | MEMBRANE H+-ATPASE | STRUCTURAL BASIS | YAP/TAZ | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIPPO PATHWAY | PROTON PUMP ATPASE | CANCER | FAMILY | 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
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