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Literature summary for 3.4.24.81 extracted from

  • Rapti, M.; Atkinson, S.J.; Lee, M.H.; Trim, A.; Moss, M.; Murphy, G.
    The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition (2008), Biochem. J., 411, 433-439.
    View publication on PubMed
Search for more literature for 3.4.24.81

Protein Variants

Protein Variants Comment Organism
additional information using siRNA to knockdown ADAM10 in highly invasive glioblastoma cell line U251 it is shown that CD44 shedding is compromised in a dose-dependent manner Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
TIMP-1 tissue inhibitors of metalloproteinase 1, it is shown that the N-terminal domain of TIMP-1 is not sufficient for inhibition of ADAM10, 37% of ADAM10-mediated CD44 shedding is observed Homo sapiens
TIMP-3 tissue inhibitors of metalloproteinase 3, it is shown that the N-terminal domain of TIMP-3 is not sufficient for inhibition of ADAM10, 72% of ADAM10-mediated CD44 shedding is observed Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens TIMP1 and TIMP-3 (tissue inhibitors of metalloproteinase) interact and inhibit ADAM10 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information TIMP1 and TIMP-3 (tissue inhibitors of metalloproteinase) interact and inhibit ADAM10 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
ADAM10
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 Homo sapiens