"Caspase 8" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A long pro-domain caspase that contains a death effector domain in its pro-domain region. Caspase 8 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS.
| Descriptor ID |
D053181
|
| MeSH Number(s) |
D08.811.277.656.262.500.126.550.800 D08.811.277.656.300.200.126.550.800 D12.644.360.024.285.037 D12.644.360.075.405.550.800 D12.644.360.075.421.037 D12.776.157.057.018.037 D12.776.476.024.320.025 D12.776.476.075.405.550.800 D12.776.476.075.421.037
|
| Concept/Terms |
Caspase 8- Caspase 8
- FLICE Protein
- Mch5 Protease
- Caspase-8
- CAP4 Protease
- MACH Protein
Procaspase-8- Procaspase-8
- Procaspase 8
- Pro-Caspase-8
- Pro Caspase 8
|
Below are MeSH descriptors whose meaning is more general than "Caspase 8".
Below are MeSH descriptors whose meaning is more specific than "Caspase 8".
This graph shows the total number of publications written about "Caspase 8" by people in this website by year, and whether "Caspase 8" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1999 | 0 | 1 | 1 |
| 2000 | 0 | 1 | 1 |
| 2001 | 0 | 2 | 2 |
| 2002 | 0 | 1 | 1 |
| 2003 | 0 | 1 | 1 |
| 2004 | 0 | 2 | 2 |
| 2005 | 0 | 1 | 1 |
| 2007 | 0 | 3 | 3 |
| 2008 | 0 | 4 | 4 |
| 2009 | 0 | 2 | 2 |
| 2010 | 0 | 3 | 3 |
| 2011 | 0 | 2 | 2 |
| 2013 | 0 | 2 | 2 |
| 2014 | 0 | 2 | 2 |
| 2016 | 0 | 1 | 1 |
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Below are the most recent publications written about "Caspase 8" by people in Profiles.
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Anti-tumor activities of luteolin and silibinin in glioblastoma cells: overexpression of miR-7-1-3p augmented luteolin and silibinin to inhibit autophagy and induce apoptosis in glioblastoma in vivo. Apoptosis. 2016 Mar; 21(3):312-28.
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JNK1/2 regulate Bid by direct phosphorylation at Thr59 in response to ALDH1L1. Cell Death Dis. 2014 Jul 31; 5:e1358.
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Receptor-interacting protein kinases modulate noise-induced sensory hair cell death. Cell Death Dis. 2014 May 29; 5:e1262.
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N-Myc knockdown and apigenin treatment controlled growth of malignant neuroblastoma cells having N-Myc amplification. Gene. 2013 Oct 15; 529(1):27-36.
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Integrative genomic characterization of oral squamous cell carcinoma identifies frequent somatic drivers. Cancer Discov. 2013 Jul; 3(7):770-81.
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Spectral imaging-based methods for quantifying autophagy and apoptosis. Cancer Biol Ther. 2011 Aug 15; 12(4):349-56.
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Valproic acid induced differentiation and potentiated efficacy of taxol and nanotaxol for controlling growth of human glioblastoma LN18 and T98G cells. Neurochem Res. 2011 Dec; 36(12):2292-305.
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Genistein induces receptor and mitochondrial pathways and increases apoptosis during BCL-2 knockdown in human malignant neuroblastoma SK-N-DZ cells. J Neurosci Res. 2010 Mar; 88(4):877-86.
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The inhibition of apoptosis by melatonin in VSC4.1 motoneurons exposed to oxidative stress, glutamate excitotoxicity, or TNF-alpha toxicity involves membrane melatonin receptors. J Pineal Res. 2010 Mar; 48(2):157-69.
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Flavonoids activated caspases for apoptosis in human glioblastoma T98G and U87MG cells but not in human normal astrocytes. Cancer. 2010 Jan 01; 116(1):164-76.