Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition

Medicine & Life Sciences

• human EBP protein 100%
• emopamil 85%
• Carrier Proteins 37%
• Cholesterol 32%
• Isomerases 25%
• 3-beta-(2-(diethylamino)ethoxy)androst-5-en-17-one 15%
• Chondrodysplasia Punctata 14%
• Hydroxysteroids 13%
• Anticholesteremic Agents 13%
• Sterols 10%
• Oligodendroglia 9%
• Protein Biosynthesis 9%
• Tamoxifen 9%
• Amines 9%
• Mutagenesis 8%
• Autophagy 8%
• Endoplasmic Reticulum 8%
• Drug Resistance 8%
• Membrane Proteins 7%
• Pharmaceutical Preparations 7%
• Binding Sites 6%
• Ligands 6%
• Pharmacology 5%
• Breast Neoplasms 5%
• Membranes 5%
• Mutation 4%

Physics & Astronomy

• biosynthesis 67%
• cholesterol 56%
• proteins 35%
• drugs 16%
• mutagenesis 8%
• membranes 8%
• endoplasmic reticulum 7%
• amines 6%
• mutations 6%
• inhibitors 6%
• isomerization 6%
• breast 5%
• helices 5%
• ligands 5%
• cancer 5%
• crystal structure 4%
• cavities 3%
• causes 3%

Chemical Compounds

• Sterol 48%
• Cholesterol 39%
• Biosynthesis 37%
• Protein 18%
• Tamoxifen 8%
• Binding Agent 5%
• Mutation 5%
• Isomerization 4%
• Error 4%
• Binding Site 4%
• Amine 4%
• Drug 3%
• Crystal Structure 3%
• Ligand 2%