Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
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Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
Interestingly , CTSD is transported by IGF2R from the trans Golgi network to the lysosome . . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
The initial steps of proteolytic processing of newly synthesized cathepsin D were investigated in prelysosomal membranes , which were defined by their contents of 300 kDa mannose 6 phosphate receptor ( MPR 300 ) . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
Newly synthesized CI MPR and cathepsin D were shown to traverse through an early endocytic compartment , and functional rab 7 was crucial for delivery to later compartments . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
Immunogold labeling showed that the vesicles with desmosomal plaques were not enriched in MPR ( cation independent mannose 6 phosphate receptor ) , cathepsin D or the lysosome associated membrane protein lamp 1 . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
Rab 7 containing vesicles were enriched in the cation independent mannose 6 phosphate receptor and especially in the precursor forms of cathepsin D . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
Overexpression of the N terminal fragment of Doc 2 containing the tctex 1 interacting domain induces changes in the intracellular localization of cation independent mannose 6 phosphate receptor and its ligand , cathepsin D , which are transported from trans Golgi network to late endosomes . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
This was associated with impaired incorporation of the cation independent mannose 6 phosphate receptor into clathrin coated vesicles at the TGN , partial redistribution of the receptor to endosomes , and missorting of cathepsin D . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
Cathepsin D and B levels were higher in PS FAD neocortex than in SAD and , unlike neurons in SAD , expressed higher levels of the cation independent mannose 6 phosphate receptor . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
Interestingly , and consistent with a localization to endosomes , knock down of RME 8 also leads to alterations in the trafficking of the cation independent mannose 6 phosphate receptor and improper sorting of the lysosomal hydrolase cathepsin D . ^^^
Interacting proteins: P11717 and P07339 Pubmed SVM Score :0.0
Here we show that the cation independent M6PR does not become enriched in the endocytic pathway en route to the lysosome , but if a pulse of M6PR or an M6PR ligand , cathepsin D , is followed , a significant fraction of these proteins are routed from the trans Golgi to MVBs . ^^^