capsaicin and benzyloxycarbonylleucyl-leucyl-leucine aldehyde

capsaicin has been researched along with benzyloxycarbonylleucyl-leucyl-leucine aldehyde 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
Kee, KH; Lee, MJ; Lim, SC; Oh, SH; Suh, CH	1

Other Studies

1 other study(ies) available for capsaicin and benzyloxycarbonylleucyl-leucyl-leucine aldehyde

Article	Year
Capsaicin-induced apoptosis is regulated by endoplasmic reticulum stress- and calpain-mediated mitochondrial cell death pathways. Toxicology, 2009, Oct-29, Volume: 264, Issue:3 Topics: Apoptosis; Apoptosis Inducing Factor; BH3 Interacting Domain Death Agonist Protein; Calcium Signaling; Calpain; Capsaicin; Caspases; Cell Line; Cell Proliferation; Cell Survival; Cysteine Proteinase Inhibitors; Cytochromes c; Dose-Response Relationship, Drug; Endoplasmic Reticulum; Endoplasmic Reticulum Chaperone BiP; Endoribonucleases; Enzyme Activation; Epithelial Cells; Heat-Shock Proteins; Humans; Leupeptins; Membrane Potential, Mitochondrial; Membrane Proteins; Mitochondria; Proteasome Endopeptidase Complex; Protein Serine-Threonine Kinases; Protein Transport; Signal Transduction; Stress, Physiological; Time Factors; Transcription Factor CHOP; Tumor Suppressor Protein p53; Tunicamycin	2009

Article

Year

Capsaicin-induced apoptosis is regulated by endoplasmic reticulum stress- and calpain-mediated mitochondrial cell death pathways.

Toxicology, 2009, Oct-29, Volume: 264, Issue:3

Topics: Apoptosis; Apoptosis Inducing Factor; BH3 Interacting Domain Death Agonist Protein; Calcium Signaling; Calpain; Capsaicin; Caspases; Cell Line; Cell Proliferation; Cell Survival; Cysteine Proteinase Inhibitors; Cytochromes c; Dose-Response Relationship, Drug; Endoplasmic Reticulum; Endoplasmic Reticulum Chaperone BiP; Endoribonucleases; Enzyme Activation; Epithelial Cells; Heat-Shock Proteins; Humans; Leupeptins; Membrane Potential, Mitochondrial; Membrane Proteins; Mitochondria; Proteasome Endopeptidase Complex; Protein Serine-Threonine Kinases; Protein Transport; Signal Transduction; Stress, Physiological; Time Factors; Transcription Factor CHOP; Tumor Suppressor Protein p53; Tunicamycin

2009