EC Number   |
Inhibitors |
Structure  |
|---|
   3.4.21.109 | more |
no inhibition of IGFBP-rP1 processing by leupeptin, pepstatin, and N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-l-3-(2'-naphthyl)alaninyl-l-alanine 2-aminoethyl amide, i.e. TAPI-1; not inhibited by leupeptin, pepstatin and N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-3-(2'-naphthyl)alaninyl-L-alanine 2-aminoethyl amide |
 |
| 3.4.21.109 | more |
wild type eglin c has no effect |
|
| 3.4.21.109 | more |
inhibition of matriptase activation in vitro and in vivo, overview |
|
| 3.4.21.109 | more |
inhibitor design and synthesis, inhibitory potency and structure-activity relationships, overview, matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo |
|
| 3.4.21.109 | more |
autoinhibitory role of the LDLRA modules that may prevent premature activation of matriptase in the absence of appropriate activation stimuli |
|
| 3.4.21.109 | more |
inhibitor synthesis and validation, overview |
|
| 3.4.21.109 | more |
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin |
|
| 3.4.21.109 | more |
the enzyme is competitively inhibited by the anti-MT-SP1 antibody FabE2 |
|
| 3.4.21.109 | more |
design and synthesis of potent, selective inhibitors of matriptase, overview. Design of a class of potent and selective peptidomimetic inhibitors of matriptase based on the P4-P1 (Arg-Gln-Ala-Arg) portion of the activation peptide of matriptase, to which is linked a C-terminal serine trap in the form of a ketobenzothiazole group. The ketobenzothiazole serine trap is selected to form a covalent and reversible bond with the catalytic serine residue of the enzyme. Importance of stereochemistry at the P1 position for inhibitory potency |
|
| 3.4.21.109 | more |
O-(3-carbamimidoylphenyl)-L-serine amides as matriptase inhibitors, overview. Analysis of cytotoxic effects of inhibitors |
|
