Modulation of human IGF binding protein-3 activity by structural modification
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Cellular internalization of insulin-like growth factor binding protein-3. Distinct endocytic pathways facilitate re-uptake and nuclear localization
2004, Journal of Biological ChemistryCitation Excerpt :Therefore, the predominant destination of the re-uptaken free IGFBP-3 is the nucleus and is dependent on the C-terminal region that binds transferrin. Of note, the residues mutated are also involved in cell surface (15, 16) and importin-β binding (10). IGFBP-3 Binds Transferrin but Not Directly to Transferrin Receptor-1 (TfR1); However, a Ternary Complex May be Formed—We and others (11, 17) have described transferrin as an IGFBP-3 binding partner.
Insulin-like growth factor-binding protein-3 binds fibrinogen and fibrin
1999, Journal of Biological ChemistryInsulin-like growth factor-binding protein (IGFBP)-3 and IGFBP-5 share a common nuclear transport pathway in T47D human breast carcinoma cells
1998, Journal of Biological ChemistryPhosphorylation of insulin-like growth factor binding proteins
1997, Molecular and Cellular EndocrinologyChapter 5 Molecular aspects of insulin-like growth factor binding proteins
1997, Advances in Molecular and Cellular Endocrinology
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