Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P00749 and P98164 Pubmed SVM Score :0.0
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Interacting proteins: P00749 and P98164 Pubmed SVM Score :0.0
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Interacting proteins: P00749 and P98164 Pubmed SVM Score :1.0502929
The activation of pro uPA to the active two chain uPA is accelerated with uPAR bound pro uPA and is achieved by plasmin and proteases of other classes like cathepsins G and L . uPAR bound uPA is susceptible to inhibition by its specific inhibitors ( PAI 1 , PAI 2 , and PN 1 ) . uPA PAI 1 and uPA PN 1 complexes , but not free uPA , are readily internalized and degraded through a mechanism that involves the multiligand receptors alpha 2 macroglobulin receptor / low density lipoprotein receptor associated protein ( alpha 2 MR ) and epithelial glycoprotein 330 ( gp 330 ) . 1.0502929^^^
Interacting proteins: P00749 and P98164 Pubmed SVM Score :0.68929223
Using type 2 pneumocytes , endocytosis of a previously described gp 330 ligand , urokinase ( uPA ) complexed with plasminogen activator inhibitor 1 ( uPA : PAI 1 ) and two new ligands , PAI 1 and pro uPA , was demonstrated . 0.68929223^^^ In addition , gp 330 acts in concert with LRP in type 2 pneumocytes to mediate clearance of a variety of proteins involved in plasminogen activation , including uPA : PAI 1 complexes PAI 1 and pro uPA . ( ABSTRACT TRUNCATED AT 250 WORDS ) . 0.51540886^^^
Interacting proteins: P00749 and P98164 Pubmed SVM Score :1.739154
In the present report , we describe that affinity purified gp 330 from rabbit renal cortex binds plasminogen activator inhibitor type 1 ( PAI 1 ) complexed with urokinase type plasminogen activator ( uPA ) . alpha 2M methylamine , which binds with high affinity to alpha 2MR / LRP , did not bind to gp 330 . 1.739154^^^
Interacting proteins: P00749 and P98164 Pubmed SVM Score :0.0
The alpha 2MR and gp 330 mediated endocytosis of a ligand ( u PA / PAI 1 complex ) initially bound to another receptor ( u PAR ) is a novel kind of interaction between membrane receptors . ^^^