Biomedicine. Avoiding collateral damage in Alzheimer's disease treatment.
Glabe
Charles
C
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA. cglabe@uci.edu
D000544:Alzheimer Disease / Q000188:drug therapy*; D053829:Amyloid Precursor Protein Secretases; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D016282:Aspartic Acid Endopeptidases; D001369:Axons / Q000378:metabolism / Q000502:physiology; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008822:Mice, Transgenic; D009186:Myelin Sheath / Q000502:physiology / Q000648:ultrastructure; D020890:Neuregulin-1 / Q000235:genetics / Q000378:metabolism*; D009474:Neurons / Q000378:metabolism; D011480:Protease Inhibitors / Q000009:adverse effects* / Q000627:therapeutic use; D011487:Protein Conformation; D017510:Protein Folding
D016229:Amyloid beta-Peptides; D020890:Neuregulin-1; D011480:Protease Inhibitors; D053829:Amyloid Precursor Protein Secretases; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C509280:BACE1 protein, human; C509282:Bace1 protein, mouse