"ADAM17 Protein" 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 disintegrin and metalloproteinase domain-containing protein that cleaves the membrane-bound precursor of TUMOR NECROSIS FACTOR-ALPHA to its mature form. It cleaves several other CELL SURFACE PROTEINS, including INTERLEUKIN-1 RECEPTOR TYPE II; TRANSFORMING GROWTH FACTOR ALPHA; L-SELECTIN; MUCIN-1; and AMYLOID BETA-PROTEIN PRECURSOR. It can also function as an activator of the Notch signaling pathway by mediating the cleavage of NOTCH RECEPTORS.
| Descriptor ID |
D000072198
|
| MeSH Number(s) |
D08.811.277.656.675.374.102.375 D09.400.430.500.375 D12.776.395.033.375
|
| Concept/Terms |
ADAM17 Protein- ADAM17 Protein
- TACE (Enzyme)
- TNF-alpha Converting Enzyme
- TNF alpha Converting Enzyme
- Tumor Necrosis Factor Alpha Convertase
- ADAM-17
- Tumor Necrosis Factor-alpha Converting Enzyme
- Tumor Necrosis Factor alpha Converting Enzyme
- TNF-alpha Convertase
- Convertase, TNF-alpha
- TNF alpha Convertase
- CD156b Antigen
- Antigen, CD156b
- ADAM-17 Protein
- ADAM 17 Protein
- Disintegrin and Metalloproteinase Domain-Containing Protein 17
- Disintegrin and Metalloproteinase Domain Containing Protein 17
- TACA (Enzyme)
- Tumor Necrosis Factor-alpha Convertase
|
Below are MeSH descriptors whose meaning is more general than "ADAM17 Protein".
Below are MeSH descriptors whose meaning is more specific than "ADAM17 Protein".
This graph shows the total number of publications written about "ADAM17 Protein" by people in this website by year, and whether "ADAM17 Protein" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2011 | 0 | 1 | 1 |
| 2012 | 0 | 1 | 1 |
| 2013 | 0 | 1 | 1 |
| 2014 | 0 | 2 | 2 |
| 2020 | 1 | 1 | 2 |
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click here.
Below are the most recent publications written about "ADAM17 Protein" by people in Profiles.
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Schreiber B, Patel A, Verma A. Shedding Light on COVID-19: ADAM17 the Missing Link? Am J Ther. 2020 Aug 03; 28(3):e358-e360.
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Han MS, White A, Perry RJ, Camporez JP, Hidalgo J, Shulman GI, Davis RJ. Regulation of adipose tissue inflammation by interleukin 6. Proc Natl Acad Sci U S A. 2020 02 11; 117(6):2751-2760.
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Araya HF, Sepulveda H, Lizama CO, Vega OA, Jerez S, Brice?o PF, Thaler R, Riester SM, Antonelli M, Salazar-Onfray F, Rodr?guez JP, Moreno RD, Montecino M, Charbonneau M, Dubois CM, Stein GS, van Wijnen AJ, Galindo MA. Expression of the ectodomain-releasing protease ADAM17 is directly regulated by the osteosarcoma and bone-related transcription factor RUNX2. J Cell Biochem. 2018 11; 119(10):8204-8219.
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Langjahr P, D?az-Jim?nez D, De la Fuente M, Rubio E, Golenbock D, Bronfman FC, Quera R, Gonz?lez MJ, Hermoso MA. Metalloproteinase-dependent TLR2 ectodomain shedding is involved in soluble toll-like receptor 2 (sTLR2) production. PLoS One. 2014; 9(12):e104624.
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Navasa N, Mart?n I, Iglesias-Pedraz JM, Beraza N, Atondo E, Izadi H, Ayaz F, Fern?ndez-?lvarez S, Hatle K, Som A, Dienz O, Osborne BA, Mart?nez-Chantar ML, Rinc?n M, Anguita J. Regulation of oxidative stress by methylation-controlled J protein controls macrophage responses to inflammatory insults. J Infect Dis. 2015 Jan 01; 211(1):135-45.
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Tsubota Y, Frey JM, Tai PW, Welikson RE, Raines EW. Monocyte ADAM17 promotes diapedesis during transendothelial migration: identification of steps and substrates targeted by metalloproteinases. J Immunol. 2013 Apr 15; 190(8):4236-44.
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Richmond JM, Duffy ER, Lee J, Kaboli K, Kim YS, Remick DG, Kornfeld H, Cruikshank WW. Mannose-capped Lipoarabinomannan from Mycobacterium tuberculosis induces soluble tumor necrosis factor receptor production through tumor necrosis factor alpha-converting enzyme activation. Infect Immun. 2012 Nov; 80(11):3858-68.
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Oguma T, Asano K, Tomomatsu K, Kodama M, Fukunaga K, Shiomi T, Ohmori N, Ueda S, Takihara T, Shiraishi Y, Sayama K, Kagawa S, Natori Y, Lilly CM, Satoh K, Makimura K, Ishizaka A. Induction of mucin and MUC5AC expression by the protease activity of Aspergillus fumigatus in airway epithelial cells. J Immunol. 2011 Jul 15; 187(2):999-1005.