Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Medicine & Life Sciences

• HSP90 Heat-Shock Proteins 100%
• Molecular Chaperones 93%
• Protein Kinases 69%
• Cell Cycle 59%
• Technology 49%
• Biosensing Techniques 30%
• Proteins 18%
• Nanostructures 14%
• Vitamins 12%
• Nucleic Acids 12%
• Quality Control 12%
• Carbohydrates 11%
• Fatty Acids 10%
• Signal Transduction 9%
• Adenosine Triphosphate 9%
• Neoplasms 8%
• Costs and Cost Analysis 7%
• Enzymes 6%
• Growth 6%
• Therapeutics 2%

Engineering & Materials Science

• Proteins 69%
• Hot Temperature 36%
• Cell Cycle Proteins 35%
• Biosensors 18%
• Complex networks 15%
• Labels 12%
• Vitamins 11%
• Signal transduction 11%
• Nucleic acids 11%
• Biomolecules 10%
• Carbohydrates 10%
• Adenosinetriphosphate 9%
• Nanostructured materials 9%
• Fatty acids 9%
• Enzymes 8%
• Cells 7%
• Quality control 7%
• Costs 2%
• Experiments 2%

Chemistry

• Field Effect 74%
• Heat 55%
• Protein 31%
• Signal Transduction 6%
• Vitamin 6%
• Quality Control 5%
• Biocompatible Material 5%
• Nucleic Acid 5%
• Carbohydrate 5%
• Fatty Acid 5%
• Block Like Crystal 4%
• Nanomaterial 3%
• Surface 2%