Page last updated: 2024-08-26

n-tert-butylhydroxylamine and Disease Models, Animal

n-tert-butylhydroxylamine has been researched along with Disease Models, Animal in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's3 (100.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bagh, MB; Chandra, G; Moralle, M; Mukherjee, AB; Peng, S; Saha, A; Sarkar, C; Zhang, Z1
Chandra, G; Liu, A; Mukherjee, AB; Peng, S; Sarkar, C; Zhang, Z1
Bagh, MB; Chandra, G; Liu, A; Mukherjee, AB; Pattabiraman, N; Peng, S; Singh, SP; Zhang, Z1

Other Studies

3 other study(ies) available for n-tert-butylhydroxylamine and Disease Models, Animal

ArticleYear
Cln1 gene disruption in mice reveals a common pathogenic link between two of the most lethal childhood neurodegenerative lysosomal storage disorders.
    Human molecular genetics, 2015, Oct-01, Volume: 24, Issue:19

    Topics: Animals; Brain; Cathepsin D; Child; Disease Models, Animal; Gene Expression Regulation; Humans; Hydroxylamines; Lysosomes; Mice; Mutation; Neuronal Ceroid-Lipofuscinoses; Thiolester Hydrolases

2015
Neuroprotection and lifespan extension in Ppt1(-/-) mice by NtBuHA: therapeutic implications for INCL.
    Nature neuroscience, 2013, Volume: 16, Issue:11

    Topics: Animals; Apoptosis; Carbon Isotopes; Cells, Cultured; Cerebral Cortex; Disease Models, Animal; Dose-Response Relationship, Drug; Gene Expression Regulation; Hydroxylamines; Longevity; Mice; Mice, Inbred C57BL; Mice, Knockout; Neuronal Ceroid-Lipofuscinoses; Neurons; Neuroprotective Agents; Palmitoyl Coenzyme A; Thiolester Hydrolases; Time Factors

2013
Misrouting of v-ATPase subunit V0a1 dysregulates lysosomal acidification in a neurodegenerative lysosomal storage disease model.
    Nature communications, 2017, 03-07, Volume: 8

    Topics: Adaptor Protein Complex 2; Animals; Disease Models, Animal; Drug Evaluation, Preclinical; Endosomes; HEK293 Cells; Humans; Hydroxylamines; Lipoylation; Lysosomal Storage Diseases; Lysosomes; Mice; Random Allocation; Thiolester Hydrolases; Vacuolar Proton-Translocating ATPases

2017