Structures of p38α Active Mutants Reveal Conformational Changes in L16 Loop that Induce Autophosphorylation and Activation

Keyphrases

• Conformational Change 100%
• Activation Mechanism 100%
• Autophosphorylation 100%
• Active Site mutant 100%
• Phosphorylation 50%
• Mitogen-activated Protein Kinase 50%
• Alternative Pathway 50%
• P38 Activation 50%
• T Cells 25%
• Inflammatory Diseases 25%
• Mechanistic Insight 25%
• Dimerization 25%
• Normal Function 25%
• Structural Information 25%
• Biochemical Studies 25%
• Kinase Function 25%
• Molecular Switches 25%
• P38 Mitogen-activated Protein Kinase (p38 MAPK) 25%
• Kinase-independent 25%
• Loop Region 25%
• Kinase Activation 25%
• Inflammation-associated Cancer 25%
• High-resolution Crystal Structure 25%
• Signal Process 25%
• Regulatory Characteristics 25%

Biochemistry, Genetics and Molecular Biology

• Conformational Change 100%
• Autophosphorylation 100%
• Mitogen-Activated Protein Kinase Kinase 66%
• T Cell 33%
• Crystal Structure 33%
• Dimerization 33%
• Phosphotransferase 33%
• Kinase 33%
• P38 Mitogen-Activated Protein Kinases 33%

Immunology and Microbiology

• Conformational Transition 100%
• Autophosphorylation 100%
• Mitogen 66%
• T Cell 33%
• Inflammatory Disorder 33%
• Crystal Structure 33%
• Dimerization 33%
• Lip 33%