sorbitol and guanosine diphosphate

sorbitol has been researched along with guanosine diphosphate in 1 studies

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Browne, GJ; Finn, SG; Proud, CG; Smith, EM; Tee, AR	1

Other Studies

1 other study(ies) available for sorbitol and guanosine diphosphate

Article	Year
The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses. The Journal of biological chemistry, 2005, May-13, Volume: 280, Issue:19 Topics: Adaptor Proteins, Signal Transducing; Adenosine Triphosphate; Amino Acids; AMP-Activated Protein Kinases; Animals; Calcium-Calmodulin-Dependent Protein Kinases; Carrier Proteins; Cell Cycle Proteins; Cell Line; Cells, Cultured; Cycloheximide; Dose-Response Relationship, Drug; Elongation Factor 2 Kinase; Eukaryotic Initiation Factors; Fibroblasts; Gene Expression Regulation; Glucose; Guanine; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Hydrogen Peroxide; Hydrolysis; Immunoblotting; Immunoprecipitation; Mice; Models, Biological; Monomeric GTP-Binding Proteins; Multienzyme Complexes; Mutation; Neuropeptides; Phosphoproteins; Phosphorylation; Protein Kinases; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Protein Synthesis Inhibitors; Ras Homolog Enriched in Brain Protein; Repressor Proteins; Ribosomal Protein S6; Signal Transduction; Sorbitol; Time Factors; TOR Serine-Threonine Kinases; Transgenes; Tuberous Sclerosis Complex 2 Protein; Tumor Suppressor Proteins	2005

Article

Year

The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses.

The Journal of biological chemistry, 2005, May-13, Volume: 280, Issue:19

Topics: Adaptor Proteins, Signal Transducing; Adenosine Triphosphate; Amino Acids; AMP-Activated Protein Kinases; Animals; Calcium-Calmodulin-Dependent Protein Kinases; Carrier Proteins; Cell Cycle Proteins; Cell Line; Cells, Cultured; Cycloheximide; Dose-Response Relationship, Drug; Elongation Factor 2 Kinase; Eukaryotic Initiation Factors; Fibroblasts; Gene Expression Regulation; Glucose; Guanine; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Hydrogen Peroxide; Hydrolysis; Immunoblotting; Immunoprecipitation; Mice; Models, Biological; Monomeric GTP-Binding Proteins; Multienzyme Complexes; Mutation; Neuropeptides; Phosphoproteins; Phosphorylation; Protein Kinases; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Protein Synthesis Inhibitors; Ras Homolog Enriched in Brain Protein; Repressor Proteins; Ribosomal Protein S6; Signal Transduction; Sorbitol; Time Factors; TOR Serine-Threonine Kinases; Transgenes; Tuberous Sclerosis Complex 2 Protein; Tumor Suppressor Proteins

2005