Caspase 9
"Caspase 9" 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 CASPASE RECRUITMENT DOMAIN in its pro-domain region. Caspase 9 is activated during cell stress by mitochondria-derived proapoptotic factors and by CARD SIGNALING ADAPTOR PROTEINS such as APOPTOTIC PROTEASE-ACTIVATING FACTOR 1. It activates APOPTOSIS by cleaving and activating EFFECTOR CASPASES.
Descriptor ID |
D053453
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MeSH Number(s) |
D08.811.277.656.262.500.126.550.900 D08.811.277.656.300.200.126.550.900 D12.644.360.024.131.155 D12.644.360.075.358.155 D12.644.360.075.405.550.900 D12.776.157.057.006.155 D12.776.476.024.139.155 D12.776.476.075.358.155 D12.776.476.075.405.550.900
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Concept/Terms |
Caspase 9- Caspase 9
- ICE-Like Apoptotic Protease 6
- ICE Like Apoptotic Protease 6
- Apoptotic Protease Activating Factor 3
- ICE-LAP6 Protein
- ICE LAP6 Protein
- Caspase-9
Procaspase-9- Procaspase-9
- Procaspase 9
- Pro-Caspase-9
- Pro Caspase 9
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Below are MeSH descriptors whose meaning is more general than "Caspase 9".
Below are MeSH descriptors whose meaning is more specific than "Caspase 9".
This graph shows the total number of publications written about "Caspase 9" by people in this website by year, and whether "Caspase 9" 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 |
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2000 | 0 | 1 | 1 | 2001 | 0 | 2 | 2 | 2002 | 0 | 1 | 1 | 2003 | 0 | 3 | 3 | 2004 | 0 | 2 | 2 | 2005 | 0 | 4 | 4 | 2006 | 0 | 3 | 3 | 2007 | 2 | 1 | 3 | 2008 | 0 | 2 | 2 | 2009 | 0 | 2 | 2 | 2010 | 0 | 3 | 3 | 2011 | 0 | 1 | 1 | 2012 | 0 | 1 | 1 | 2013 | 0 | 3 | 3 | 2015 | 0 | 1 | 1 | 2018 | 0 | 1 | 1 | 2020 | 0 | 1 | 1 | 2023 | 0 | 1 | 1 |
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Below are the most recent publications written about "Caspase 9" by people in Profiles.
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Muro I, Qualman AC, Kovacs EJ, Idrovo JP. Burn-Induced Apoptosis in the Livers of Aged Mice Is Associated With Caspase Cleavage of Bcl-xL. J Surg Res. 2023 10; 290:147-155.
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Zhang X, Xu Q, Zi Z, Liu Z, Wan C, Crisman L, Shen J, Liu X. Programmable Extracellular Vesicles for Macromolecule Delivery and Genome Modifications. Dev Cell. 2020 12 21; 55(6):784-801.e9.
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Mukherjee AK, Saviola AJ, Mackessy SP. Cellular mechanism of resistance of human colorectal adenocarcinoma cells against apoptosis-induction by Russell's Viper venom l-amino acid oxidase (Rusvinoxidase). Biochimie. 2018 Jul; 150:8-15.
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Milanovic D, Pesic V, Loncarevic-Vasiljkovic N, Pavkovic Z, Popic J, Kanazir S, Jevtovic-Todorovic V, Ruzdijic S. The Fas Ligand/Fas Death Receptor Pathways Contribute to Propofol-Induced Apoptosis and Neuroinflammation in the Brain of Neonatal Rats. Neurotox Res. 2016 10; 30(3):434-52.
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Caprariello AV, Batt CE, Zippe I, Romito-DiGiacomo RR, Karl M, Miller RH. Apoptosis of Oligodendrocytes during Early Development Delays Myelination and Impairs Subsequent Responses to Demyelination. J Neurosci. 2015 Oct 14; 35(41):14031-41.
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Kumar S, Tomar MS, Acharya A. Activation of p53-dependent/-independent pathways of apoptotic cell death by chelerythrine in a murine T cell lymphoma. Leuk Lymphoma. 2015 Jun; 56(6):1846-55.
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White MJ, McArthur K, Metcalf D, Lane RM, Cambier JC, Herold MJ, van Delft MF, Bedoui S, Lessene G, Ritchie ME, Huang DC, Kile BT. Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production. Cell. 2014 Dec 18; 159(7):1549-62.
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Clarke P, Leser JS, Quick ED, Dionne KR, Beckham JD, Tyler KL. Death receptor-mediated apoptotic signaling is activated in the brain following infection with West Nile virus in the absence of a peripheral immune response. J Virol. 2014 Jan; 88(2):1080-9.
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Mishra A, Rao S, Mittal A, Jayaram B. Capturing native/native like structures with a physico-chemical metric (pcSM) in protein folding. Biochim Biophys Acta. 2013 Aug; 1834(8):1520-31.
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Nahomi RB, Wang B, Raghavan CT, Voss O, Doseff AI, Santhoshkumar P, Nagaraj RH. Chaperone peptides of a-crystallin inhibit epithelial cell apoptosis, protein insolubilization, and opacification in experimental cataracts. J Biol Chem. 2013 May 03; 288(18):13022-35.
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