sorbitol has been researched along with leupeptins in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Alarcon-Vargas, D; Deb, S; Fuchs, SY; Ronai, Z | 1 |
| Ardley, HC; Markham, AF; Robinson, PA; Rose, SA; Scott, GB; Tan, NG | 1 |
| Cai, LF; Erdjument-Bromage, H; Kaufman, AJ; Pandolfi, PP; Scaglioni, PP; Singh, B; Tempst, P; Teruya-Feldstein, J; Yung, TM | 1 |
3 other study(ies) available for sorbitol and leupeptins
| Article | Year |
|---|---|
p73 transcriptional activity increases upon cooperation between its spliced forms.
Topics: Animals; Anisomycin; Cell Line; Dactinomycin; DNA-Binding Proteins; Fibroblasts; Gene Expression Regulation; Genes, p53; Genes, Reporter; Genes, Synthetic; Genes, Tumor Suppressor; Humans; Hypertonic Solutions; Leupeptins; Mice; Nuclear Proteins; Nucleic Acid Synthesis Inhibitors; Promoter Regions, Genetic; Protein Isoforms; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-mdm2; Recombinant Fusion Proteins; RNA Splicing; Sorbitol; Transcriptional Activation; Tumor Protein p73; Tumor Suppressor Protein p53; Tumor Suppressor Proteins | 2000 |
Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin.
Topics: Animals; Carrier Proteins; Chlorocebus aethiops; Cloning, Molecular; COS Cells; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; Humans; Hydrogen Peroxide; Inclusion Bodies; Leupeptins; Lewy Body Disease; Microscopy, Confocal; Multienzyme Complexes; Neurons; Osmotic Pressure; Oxidative Stress; Parkinson Disease; Proteasome Endopeptidase Complex; Sorbitol; Tubulin; Tumor Cells, Cultured; Tunicamycin; Ubiquitin; Ubiquitin-Protein Ligases; Vimentin | 2003 |
A CK2-dependent mechanism for degradation of the PML tumor suppressor.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Apoptosis; Carcinoma, Non-Small-Cell Lung; Casein Kinase II; Cell Line; Cell Line, Transformed; Cell Line, Tumor; Enzyme Activation; Enzyme Inhibitors; Genes, Tumor Suppressor; Green Fluorescent Proteins; Hemagglutinins; Humans; Leupeptins; Lung Neoplasms; Mice; Mice, Transgenic; Molecular Sequence Data; Neoplasm Proteins; NIH 3T3 Cells; Nuclear Proteins; p38 Mitogen-Activated Protein Kinases; Phosphorylation; Promyelocytic Leukemia Protein; Proteasome Endopeptidase Complex; Protein Structure, Tertiary; Protein Subunits; RNA, Small Interfering; Sequence Deletion; Serine; Sorbitol; Transcription Factors; Transcriptional Activation; Triazoles; Tumor Suppressor Proteins; Ubiquitin | 2006 |