castanospermine has been researched along with deoxyglucose in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (25.00) | 18.7374 |
1990's | 1 (25.00) | 18.2507 |
2000's | 2 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Ishii, S; Volpe, JJ | 1 |
Connolly, JA; Simard, G | 1 |
Gibson, JM; Marshman, E; Siddals, KW; Westwood, M | 1 |
Bass, J; Ramos, RR; Swanson, AJ | 1 |
4 other study(ies) available for castanospermine and deoxyglucose
Article | Year |
---|---|
N-linked glycoprotein synthesis and transport during G1 are necessary for astrocytic proliferation.
Topics: Alkaloids; Animals; Animals, Newborn; Astrocytes; beta-Glucosidase; Cell Division; Cells, Cultured; Deoxyglucose; DNA; Endoplasmic Reticulum; Fluorescent Antibody Technique; Glycoproteins; Indolizines; Lectins; Lipid Metabolism; Mannose; Monensin; Nerve Tissue Proteins; Neuroglia; Oligosaccharides; Rats | 1990 |
Membrane glycoproteins are involved in the differentiation of the BC3H1 muscle cell line.
Topics: 1-Deoxynojirimycin; Acetylglucosamine; Alkaloids; Animals; Cell Differentiation; Cell Line; Creatine Kinase; Deoxy Sugars; Deoxyglucose; Enzyme Induction; Glucosamine; Glycoproteins; Indolizines; Leupeptins; Membrane Glycoproteins; Membrane Proteins; Mice; Muscles; Oligosaccharides; Swainsonine; Tunicamycin | 1987 |
Abrogation of insulin-like growth factor-I (IGF-I) and insulin action by mevalonic acid depletion: synergy between protein prenylation and receptor glycosylation pathways.
Topics: 3T3-L1 Cells; Animals; Apoptosis; Biotinylation; Blotting, Western; Cell Differentiation; Cell Division; Cell Membrane; Deoxyglucose; Dose-Response Relationship, Drug; Glucose; Glycosylation; Hydroxymethylglutaryl-CoA Reductase Inhibitors; Indolizines; Insulin; Insulin-Like Growth Factor I; Mevalonic Acid; Mice; Precipitin Tests; Protein Prenylation; Pyridines; ras Proteins; Receptor, Insulin; Signal Transduction; Thymidine; Tunicamycin | 2004 |
Calreticulin and Hsp90 stabilize the human insulin receptor and promote its mobility in the endoplasmic reticulum.
Topics: Antigens, CD; Antimetabolites; Calreticulin; Cell Line; Deoxyglucose; Endoplasmic Reticulum; Enzyme Inhibitors; Green Fluorescent Proteins; HSP90 Heat-Shock Proteins; Humans; Indolizines; Insulin Resistance; Molecular Chaperones; Mutation, Missense; Proteasome Endopeptidase Complex; Protein Folding; Protein Structure, Tertiary; Receptor, Insulin; Recombinant Fusion Proteins; Time Factors | 2007 |