Page last updated: 2024-08-21

diazomethane and Alzheimer Disease

diazomethane has been researched along with Alzheimer Disease in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (14.29)18.2507
2000's2 (28.57)29.6817
2010's3 (42.86)24.3611
2020's1 (14.29)2.80

Authors

AuthorsStudies
Chao, H; Ding, W; Kuang, S; Kumar, M; Liang, SH; Mondal, P; Ran, C; Shen, S; Tanzi, RE; Wu, B; Yang, F; Yang, L; Zhang, C; Zhang, J; Zhu, B1
Arai, T; Araya, T; Kanai, M; Kino, R; Sohma, Y1
Bahr, BA; Bowers, MT; Gessel, MM; Viswanathan, K; Wisniewski, ML; Wright, DL; Zheng, X1
Bahr, BA; Butler, D; Wisniewski, ML1
Bahr, BA; Bendiske, J1
Bi, X; Lynch, G; Zhou, J1
Bi, X; Ellman, JA; Haque, TS; Kuntz, ID; Lee, CE; Lin, B; Lynch, G; Skillman, AG; Zhou, J1

Other Studies

7 other study(ies) available for diazomethane and Alzheimer Disease

ArticleYear
A Photolabile Curcumin-Diazirine Analogue Enables Phototherapy with Physically and Molecularly Produced Light for Alzheimer's Disease Treatment.
    Angewandte Chemie (International ed. in English), 2023, 11-06, Volume: 62, Issue:45

    Topics: Alzheimer Disease; Amyloid beta-Peptides; Animals; Curcumin; Diazomethane; Disease Models, Animal; Mice; Mice, Transgenic; Phototherapy

2023
Covalent modifier-type aggregation inhibitor of amyloid-β based on a cyclo-KLVFF motif.
    Bioorganic & medicinal chemistry letters, 2015, Aug-01, Volume: 25, Issue:15

    Topics: Alzheimer Disease; Amyloid beta-Peptides; Animals; Cell Line; Diazomethane; Humans; Peptide Fragments; Peptides, Cyclic; Protein Aggregates; Protein Aggregation, Pathological; Rats

2015
Z-Phe-Ala-diazomethylketone (PADK) disrupts and remodels early oligomer states of the Alzheimer disease Aβ42 protein.
    The Journal of biological chemistry, 2012, Feb-24, Volume: 287, Issue:9

    Topics: Alzheimer Disease; Amyloid beta-Peptides; Amyloidosis; Animals; Diazomethane; Dimerization; Disease Models, Animal; Drug Design; Humans; Mass Spectrometry; Mice; Microscopy, Electron; Peptide Fragments; Protein Folding; Protein Structure, Secondary; Solubility

2012
Positive lysosomal modulation as a unique strategy to treat age-related protein accumulation diseases.
    Rejuvenation research, 2012, Volume: 15, Issue:2

    Topics: Aging; alpha-Synuclein; Alzheimer Disease; Animals; Cathepsins; Dementia; Diazomethane; Humans; Huntingtin Protein; Huntington Disease; Ketones; Lysosomes; Mice; Mice, Transgenic; Nerve Tissue Proteins; Nuclear Proteins; Phagocytosis; Protease Inhibitors; Proteins; rab GTP-Binding Proteins; Synapses; tau Proteins

2012
Lysosomal activation is a compensatory response against protein accumulation and associated synaptopathogenesis--an approach for slowing Alzheimer disease?
    Journal of neuropathology and experimental neurology, 2003, Volume: 62, Issue:5

    Topics: Alzheimer Disease; Amyloid beta-Protein Precursor; Animals; Cathepsins; Chloroquine; Culture Techniques; Cysteine Proteinase Inhibitors; Diazomethane; Disease Models, Animal; Enzyme Activation; Hippocampus; Hydrolases; Lysosomes; Rats; Rats, Sprague-Dawley; Synapses; tau Proteins

2003
Lysosomal protease inhibitors induce meganeurites and tangle-like structures in entorhinohippocampal regions vulnerable to Alzheimer's disease.
    Experimental neurology, 1999, Volume: 158, Issue:2

    Topics: Aged; Alzheimer Disease; Animals; Cathepsin B; Cathepsin L; Cathepsins; Chloroquine; Cysteine Endopeptidases; Diazomethane; Endopeptidases; Entorhinal Cortex; Hippocampus; Humans; Lysosomes; Neurites; Neurofibrillary Tangles; Organ Culture Techniques; Rats; Rats, Sprague-Dawley; Serine Proteinase Inhibitors

1999
Novel cathepsin D inhibitors block the formation of hyperphosphorylated tau fragments in hippocampus.
    Journal of neurochemistry, 2000, Volume: 74, Issue:4

    Topics: Alzheimer Disease; Animals; Cathepsin D; Diazomethane; Dose-Response Relationship, Drug; Enzyme Inhibitors; Excitatory Postsynaptic Potentials; Hippocampus; Lysosomes; Organ Culture Techniques; Peptide Fragments; Phosphoproteins; Phosphorylation; Rats; Rats, Sprague-Dawley; tau Proteins

2000