The charged linker region is an important regulator of Hsp90 function

Keyphrases

• Heat Shock Protein 90 (Hsp90) 100%
• Charged Linker 100%
• Linker Region 100%
• Linker 33%
• ATP Synthase 33%
• Middle Domain 33%
• Large Set 16%
• Temperature Sensitivity 16%
• Partial Reconstruction 16%
• Mild Temperature 16%
• Deletion Variant 16%
• Conformational Flexibility 16%
• N-terminal Domain 16%
• Molecular Chaperone 16%
• Co-chaperone 16%
• ATP-dependent 16%
• Client Proteins 16%
• Aha1 16%
• ATP-binding Domain 16%
• Hsp90 Family 16%
• Higher Eukaryotes 16%
• Linker Sequence 16%
• Eukaryotic Organisms 16%
• Artificial Sequences 16%
• Highly Charged 16%
• SBA-1 16%
• Lethal Phenotype 16%
• Core Architectures 16%
• Dimerization Domain 16%

Immunology and Microbiology

• Amino Terminal Sequence 100%
• Eukaryote 50%
• Maturation 50%
• Carboxy Terminal Sequence 50%
• Dimerization 50%
• Temperature Sensitivity 50%
• Chaperone Protein 50%
• In Vitro 50%

Biochemistry, Genetics and Molecular Biology

• Hsp90 100%
• N-Terminus 28%
• Adenosine Triphosphate 28%
• ATPase 28%
• Reconstruction 14%
• Dimerization 14%
• Binding Domain 14%
• Co-Chaperone 14%
• Chaperone Protein 14%
• Eukaryote 14%
• C-Terminus 14%
• Maturation 14%
• Temperature Sensitivity 14%