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Literature summary for 5.3.4.1 extracted from

  • Manickam, N.; Sun, X.; Li, M.; Gazitt, Y.; Essex, D.W.
    Protein disulphide isomerase in platelet function (2008), Br. J. Haematol., 140, 223-229.
    View publication on PubMed

Application

Application Comment Organism
medicine protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin. Anti-PDI antibodies inhibit signalling-independent activation of the thiol-containing fibrinogen receptor alphaIIbbeta3 by Mn2+ Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
blood platelet the thiol-containing form of PDI increases in the platelet surface with platelet activition Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin Homo sapiens ?
-
?