Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P25774 and P28325 Pubmed SVM Score :0.0
By comparison with corresponding results for wild type cystatins C and D , it was concluded ( 1 ) that both the N terminal and framework part of the molecules significantly contribute to the observed differences in inhibitory activities of cystatins C and D and ( 2 ) that the N terminal segment of cystatin C increases the inhibitory activity of cystatin D against cathepsin S and cathepsin L but results in decreased activity against cathepsin H . ^^^
Interacting proteins: P25774 and P28325 Pubmed SVM Score :0.0
Compared with its homologues , cystatin D presents an unusual inhibition profile with a preferential inhibition cathepsin S > cathepsin H > cathepsin L and no inhibition of cathepsin B or pig legumain . ^^^
Interacting proteins: P25774 and P28325 Pubmed SVM Score :0.0
The inhibitory properties displayed by cystatin D suggest that it has a function in saliva as inhibitor of either endogenous or exogenous enzymes with cathepsin S or H like properties . . ^^^
Interacting proteins: P28325 and P25774 Pubmed SVM Score :0.0
The inhibitory properties displayed by cystatin D suggest that it has a function in saliva as inhibitor of either endogenous or exogenous enzymes with cathepsin S or H like properties . . ^^^
Interacting proteins: P28325 and P25774 Pubmed SVM Score :0.0
By comparison with corresponding results for wild type cystatins C and D , it was concluded ( 1 ) that both the N terminal and framework part of the molecules significantly contribute to the observed differences in inhibitory activities of cystatins C and D and ( 2 ) that the N terminal segment of cystatin C increases the inhibitory activity of cystatin D against cathepsin S and cathepsin L but results in decreased activity against cathepsin H . ^^^
Interacting proteins: P28325 and P25774 Pubmed SVM Score :0.0
Compared with its homologues , cystatin D presents an unusual inhibition profile with a preferential inhibition cathepsin S > cathepsin H > cathepsin L and no inhibition of cathepsin B or pig legumain . ^^^