ADAM17 Protein

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"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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

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".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Hydrolases [D08.811.277]
Peptide Hydrolases [D08.811.277.656]
Metalloproteases [D08.811.277.656.675]
Metalloendopeptidases [D08.811.277.656.675.374]
ADAM Proteins [D08.811.277.656.675.374.102]
ADAM17 Protein [D08.811.277.656.675.374.102.375]
Carbohydrates [D09]
Glycoconjugates [D09.400]
Glycoproteins [D09.400.430]
ADAM Proteins [D09.400.430.500]
ADAM17 Protein [D09.400.430.500.375]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Glycoproteins [D12.776.395]
ADAM Proteins [D12.776.395.033]
ADAM17 Protein [D12.776.395.033.375]

Below are MeSH descriptors whose meaning is related to "ADAM17 Protein".

Below are MeSH descriptors whose meaning is more specific than "ADAM17 Protein".

publications

Timeline | Most Recent

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.

Bar chart showing 8 publications over 5 distinct years, with a maximum of 3 publications in 2014

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
2011	0	1	1
2012	0	1	1
2013	0	1	1
2014	0	3	3
2020	1	1	2

Below are the most recent publications written about "ADAM17 Protein" by people in Profiles.

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.

View in: PubMed
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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Mitchell MJ, Lin KS, King MR. Fluid shear stress increases neutrophil activation via platelet-activating factor. Biophys J. 2014 May 20; 106(10):2243-53.

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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.

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