Pub. Date : 2019 Oct 31
PMID : 31673058
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Since the bioactive form of several cytokines is represented by dimers/oligomers and oligomerization is promoted by binding to heparin or HSPGs, here we evaluated if heparin/HSPGs also promote p17 oligomerization. | Heparin | family with sequence similarity 72 member B | Homo sapiens |
| 2 | Heparin-induced p17 oligomerization is of electrostatic nature, being it prevented by NaCl, by removing negative sulfated groups of heparin and by neutralizing positive lysine residues in the p17 N-terminus. | Heparin | family with sequence similarity 72 member B | Homo sapiens |
| 3 | A new computational protocol has been implemented to study heparin chains up to 24-mer accommodating a p17 dimer. | Heparin | family with sequence similarity 72 member B | Homo sapiens |
| 4 | Molecular dynamics show that, in the presence of heparin, two p17 molecules undergo conformational modifications creating a continuous "electropositive channel" in which heparin sulfated groups interact with p17 basic amino acids, promoting its dimerization. | Heparin | family with sequence similarity 72 member B | Homo sapiens |
| 5 | Molecular dynamics show that, in the presence of heparin, two p17 molecules undergo conformational modifications creating a continuous "electropositive channel" in which heparin sulfated groups interact with p17 basic amino acids, promoting its dimerization. | Heparin | family with sequence similarity 72 member B | Homo sapiens |
| 6 | Molecular dynamics show that, in the presence of heparin, two p17 molecules undergo conformational modifications creating a continuous "electropositive channel" in which heparin sulfated groups interact with p17 basic amino acids, promoting its dimerization. | Heparin | family with sequence similarity 72 member B | Homo sapiens |
| 7 | Molecular dynamics show that, in the presence of heparin, two p17 molecules undergo conformational modifications creating a continuous "electropositive channel" in which heparin sulfated groups interact with p17 basic amino acids, promoting its dimerization. | Heparin | family with sequence similarity 72 member B | Homo sapiens |