Pub. Date : 2016 Apr
PMID : 26896299
15 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
2 | We determined the first structure of PTN and analyzed its interactions with CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
3 | Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
4 | Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
5 | Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
6 | Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
7 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
8 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
9 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
10 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
11 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
12 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
13 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
14 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |
15 | NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. | Chondroitin Sulfates | pleiotrophin | Homo sapiens |