“Heparin-binding EGF-like growth factor gene is induced in the mouse uterus temporally by the blastocyst solely at the site of its apposition: a possible ligand for interaction with blastocyst EGF-receptor in implantation”. Development120 (5): 1071–83. (May 1994). doi:10.1242/dev.120.5.1071. PMID8026321.
“Roles of charged amino acid residues in the cytoplasmic domain of proHB-EGF”. Biochem. Biophys. Res. Commun.320 (2): 376–82. (July 2004). doi:10.1016/j.bbrc.2004.05.176. PMID15219838.
“BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparin-binding EGF-like growth factor: a unique role for proHB-EGF in cell survival regulation”. J. Biol. Chem.276 (32): 30127–32. (August 2001). doi:10.1074/jbc.M010237200. PMID11340068.
“Nardilysin, a basic residues specific metallopeptidase that mediates cell migration and proliferation”. Protein Pept. Lett.11 (5): 501–8. (October 2004). doi:10.2174/0929866043406508. PMID15544571.
“Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy”. Cancer Sci.97 (5): 341–7. (May 2006). doi:10.1111/j.1349-7006.2006.00188.x. PMID16630129.
“Proliferative effects of heparin-binding epidermal growth factor-like growth factor on pterygium epithelial cells and fibroblasts”. Invest. Ophthalmol. Vis. Sci.45 (1): 110–3. (January 2004). doi:10.1167/iovs.03-0046. PMID14691161.
Miyazono K (January 2012). “Ectodomain shedding of HB-EGF: a potential target for cancer therapy”. J. Biochem.151 (1): 1–3. doi:10.1093/jb/mvr120. PMID21976708.
“ErbB and HB-EGF signaling in heart development and function”. Cell Struct. Funct.31 (1): 1–14. (2006). doi:10.1247/csf.31.1. PMID16508205.
“Heparin-binding EGF-like growth factor modulation by antiprogestin and CG in the baboon (Papio anubis)”. J. Clin. Endocrinol. Metab.86 (9): 4520–8. (September 2001). doi:10.1210/jcem.86.9.7835. PMID11549702.
“Heparin-binding EGF-like growth factor gene is induced in the mouse uterus temporally by the blastocyst solely at the site of its apposition: a possible ligand for interaction with blastocyst EGF-receptor in implantation”. Development120 (5): 1071–83. (May 1994). doi:10.1242/dev.120.5.1071. PMID8026321.
“Roles of charged amino acid residues in the cytoplasmic domain of proHB-EGF”. Biochem. Biophys. Res. Commun.320 (2): 376–82. (July 2004). doi:10.1016/j.bbrc.2004.05.176. PMID15219838.
“BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparin-binding EGF-like growth factor: a unique role for proHB-EGF in cell survival regulation”. J. Biol. Chem.276 (32): 30127–32. (August 2001). doi:10.1074/jbc.M010237200. PMID11340068.
“Nardilysin, a basic residues specific metallopeptidase that mediates cell migration and proliferation”. Protein Pept. Lett.11 (5): 501–8. (October 2004). doi:10.2174/0929866043406508. PMID15544571.
“Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy”. Cancer Sci.97 (5): 341–7. (May 2006). doi:10.1111/j.1349-7006.2006.00188.x. PMID16630129.
“Proliferative effects of heparin-binding epidermal growth factor-like growth factor on pterygium epithelial cells and fibroblasts”. Invest. Ophthalmol. Vis. Sci.45 (1): 110–3. (January 2004). doi:10.1167/iovs.03-0046. PMID14691161.
Miyazono K (January 2012). “Ectodomain shedding of HB-EGF: a potential target for cancer therapy”. J. Biochem.151 (1): 1–3. doi:10.1093/jb/mvr120. PMID21976708.
“ErbB and HB-EGF signaling in heart development and function”. Cell Struct. Funct.31 (1): 1–14. (2006). doi:10.1247/csf.31.1. PMID16508205.
“Heparin-binding EGF-like growth factor modulation by antiprogestin and CG in the baboon (Papio anubis)”. J. Clin. Endocrinol. Metab.86 (9): 4520–8. (September 2001). doi:10.1210/jcem.86.9.7835. PMID11549702.