3.4.24.81: ADAM10 endopeptidase
This is an abbreviated version!
For detailed information about ADAM10 endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.81
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3.4.24.81
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alzheimer
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adam17
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amyloid
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ectodomain
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sheddase
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alpha-secretase
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endothelial
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metalloproteases
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neuroprotective
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plaque
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amyloidogenic
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non-amyloidogenic
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tnf
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sh-sy5y
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synaptic
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secretase
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membrane-anchored
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tetraspanins
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gamma-secretase
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n-cadherin
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presenilins
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notch1
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intramembrane
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abeta
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cxcl16
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prpc
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prion
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amyloid-beta
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prodomains
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psen1
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beta-secretase
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sappalpha
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hb-egf
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beta-site
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trans-signaling
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amphiregulin
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fractalkine
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meprin
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disintegrin-like
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adam17-mediated
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app-cleaving
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betacellulin
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nicastrin
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timp-3
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molecular biology
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anti-amyloidogenic
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medicine
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srage
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notch-dependent
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ad-like
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juxtamembrane
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bace-1
- 3.4.24.81
- alzheimer
- adam17
-
amyloid
- ectodomain
- sheddase
- alpha-secretase
- endothelial
- metalloproteases
-
neuroprotective
- plaque
-
amyloidogenic
-
non-amyloidogenic
- tnf
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sh-sy5y
- synaptic
-
secretase
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membrane-anchored
- tetraspanins
- gamma-secretase
- n-cadherin
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presenilins
- notch1
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intramembrane
- abeta
- cxcl16
- prpc
- prion
- amyloid-beta
- prodomains
- psen1
- beta-secretase
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sappalpha
- hb-egf
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beta-site
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trans-signaling
- amphiregulin
- fractalkine
- meprin
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disintegrin-like
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adam17-mediated
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app-cleaving
- betacellulin
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nicastrin
- timp-3
- molecular biology
-
anti-amyloidogenic
- medicine
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srage
-
notch-dependent
-
ad-like
-
juxtamembrane
- bace-1
Reaction
endopeptidase of broad specificity =
Synonyms
a disintegrin and metalloprotease 10, a disintegrin and metalloproteinase 10, a disintegrin and metalloproteinase-10, a-disintegrin-and-metalloprotease 10, AD10, ADAM 10, ADAM-10, ADAM10, CD156c, CD23 metalloprotease, HsT18717, kuz, kuzbanian, Kuzbanian protein, MADM, mammalian disintegrin-metalloprotease, metalloproteinase 10, metalloproteinase ADAM10, metalloproteinase Kuzbanian, metalloproteinase MADM, metalloproteinase-disintegrin, myelin-associated disintegrin metalloproteinase, notch proteinase, transmembrane metzinkin-protease of the a disintegrin and metalloproteinase family-10
ECTree
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medicine
molecular biology
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cleavage by ADAM10 of beta-amyloid precursor protein could abolish production of longer peptides and slow down or arrest Alzheimer disease
medicine
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ADAM10 participates in the response to infection by Staphylococcus aureus
medicine
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cleavage by metalloproteinase ADAM10 of PrP cellular protein is constitutive and could inhibit the maintenance of the toxic core of the protein PrP scrapie in spongiform encephalopathies
medicine
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reduction of ADAM10 in Alzheimer disease could allow beta-secretase cleavage of amyloid precursor protein
medicine
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pharmacotherapeutic target for the treatment of cerebral amyloidosis in Alzheimer disease
medicine
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Kuzbanian is required for pericardial cell and lymph gland development
medicine
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ADAM 10, 12 and 17 show different expression pattern in basal cell carcinomas histologic subtypes, indicating their different role in the basal cell carcinoma pathogenesis. Overexpression of ADAM 10, 12 and 17 immunoreactivity in deep invasion area of BCC indicates that these three proteases may play an important role in the locally invasive and highly destructive growth behavior of basal cell carcinomas
medicine
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since C4.4A is likely involved in tumor invasion, these results indicate that the cleavage of C4.4A by ADAM10 and ADAM17 contributes to tumor progression
medicine
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ADAM10 plays a critical role in Alzheimers disease. Tetraspanin12 serves as a robust partner for ADAM10 and promotes ADAM10 maturation, thereby facilitating ADAM10-dependent proteolysis of amyloid precursor protein. This mode of regulating amyloid precursor protein cleavage is of relevance to Alzheimers disease therapy. Promotion of TSPAN12-ADAM10-dependent functions should be therapeutically beneficial in Alzheimers disease, whereas inhibition of TSPAN12-ADAM functions may be beneficial in cancer
medicine
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upregulation of ADAM10 is a therapeutic target in Alzheimers disease
medicine
Staphylococcus aureus alpha-hemolysin, a pore-forming cytotoxin, is required for full virulence in a murine sepsis model. The alpha-hemolysin binding to its receptor A-disintegrin and metalloprotease ADAM10 upregulates the receptors metalloprotease activity on endothelial cells, causing vascular endothelial-cadherin cleavage and concomitant loss of endothelial barrier function
medicine
patients with nasopharyngeal carcinoma with high expression of the enzyme have shorter overall survival rates
medicine
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Kuzbanian is required for pericardial cell and lymph gland development
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ADAM10 is regulator of vascular permeability and possesses a function VE-cadherin-dependent endothelial cell functions and leukocyte transendothelial migration
molecular biology
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Kuzbanian, the ADAM10 orthologue in Drosophila melanogaster plays an important role in axon guidance by building a complex with ephrinA2, which is cleaved off from the membrane in a moment of EphA3 receptor binding
molecular biology
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tetraspanins regulate the activity of ADAM10 toward several substrates. It is illustrated how membrane compartmentalization by tetraspanins can control the function of cell surface proteins such as ectoproteases
molecular biology
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there is only a moderate alteration of gene expression in ADAM10 overexpressing mice. Genes coding for pro-inflammatory or pro-apoptotic proteins are not overrepresented among differentially regulated genes. Even a decrease of inflammation markers is observed. This further supports the strategy to treat alzheimers disease by increasing the beta-secretase activity