N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle

Keyphrases

• Heat Shock Protein 90 (Hsp90) 100%
• ATPase Cycle 100%
• Catalytic Efficiency 100%
• Terminal Residue 100%
• N-terminal Domain 62%
• In Vitro Study 12%
• Amino Acids 12%
• Dimerization 12%
• Intermolecular Interactions 12%
• Signal Transduction 12%
• Viral Replication 12%
• Deletion Variant 12%
• Deletion mutant 12%
• Transactivation 12%
• Conformational Change 12%
• Molecular Chaperone 12%
• Nucleotide Binding 12%
• Cellular Processes 12%
• ATP Synthase 12%
• ATP Hydrolysis 12%
• ATP Binding 12%
• N-terminal Modification 12%
• Hydrolysis Reaction 12%
• Turnover Rate 12%

Biochemistry, Genetics and Molecular Biology

• N-Terminus 100%
• Hsp90 100%
• Catalytic Efficiency 100%
• ATPase 100%
• Enzymatic Hydrolysis 50%
• Adenosine Triphosphate 50%
• Wild Type 25%
• In Vitro Study 12%
• Amino Acids 12%
• Signal Transduction 12%
• Conformational Change 12%
• Dimerization 12%
• Transactivation 12%
• C-Terminus 12%
• Deletion Mutant 12%
• Virus Replication 12%

Immunology and Microbiology

• Amino Terminal Sequence 100%
• Catalytic Efficiency 100%
• Hydrolysis 42%
• Wild Type 28%
• Viral Replication 14%
• Intermolecular Interaction 14%
• Conformational Transition 14%
• Carboxy Terminal Sequence 14%
• Deletion Mutant 14%
• Dimerization 14%
• Signal Transduction 14%
• Transactivation 14%