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催产素酶 (Chinese Wikipedia)

Analysis of information sources in references of the Wikipedia article "催产素酶" in Chinese language version.

refsWebsite
Global rank Chinese rank
7nih.gov
4th place
5th place
6doi.org
2nd place
23rd place
1worldcat.org
5th place
12th place

doi.org

  • Tsujimoto M, Hattori A. The oxytocinase subfamily of M1 aminopeptidases. Biochim. Biophys. Acta. 2005, 1751 (1): 9–18. PMID 16054015. doi:10.1016/j.bbapap.2004.09.011. 
  • Nomura S, Ito T, Yamamoto E, Sumigama S, Iwase A, Okada M, Shibata K, Ando H, Ino K, Kikkawa F, Mizutani S. Gene regulation and physiological function of placental leucine aminopeptidase/oxytocinase during pregnancy. Biochim. Biophys. Acta. 2005, 1751 (1): 19–25. PMID 15894523. doi:10.1016/j.bbapap.2005.04.006. 
  • Mizutani S, Yokosawa H, Tomoda Y. Degradation of oxytocin by the human placenta: effect of selective inhibitors. Acta Endocrinol. 1992, 127 (1): 76–80. PMID 1355623. doi:10.1530/acta.0.1270076. 
  • Meisenberg G, Simmons WH. Amastatin potentiates the behavioral effects of vasopressin and oxytocin in mice. Peptides. 1984, 5 (3): 535–9. PMID 6540873. doi:10.1016/0196-9781(84)90083-4. 
  • Stancampiano R, Melis MR, Argiolas A. Proteolytic conversion of oxytocin by brain synaptic membranes: role of aminopeptidases and endopeptidases. Peptides. 1991, 12 (5): 1119–25. PMID 1800950. doi:10.1016/0196-9781(91)90068-z. 
  • Itoh C, Watanabe M, Nagamatsu A, Soeda S, Kawarabayashi T, Shimeno H. Two molecular species of oxytocinase (L-cystine aminopeptidase) in human placenta: purification and characterization. Biol. Pharm. Bull. 1997, 20 (1): 20–4. PMID 9013800. doi:10.1248/bpb.20.20. 

nih.gov

ncbi.nlm.nih.gov

  • Tsujimoto M, Hattori A. The oxytocinase subfamily of M1 aminopeptidases. Biochim. Biophys. Acta. 2005, 1751 (1): 9–18. PMID 16054015. doi:10.1016/j.bbapap.2004.09.011. 
  • Nomura S, Ito T, Yamamoto E, Sumigama S, Iwase A, Okada M, Shibata K, Ando H, Ino K, Kikkawa F, Mizutani S. Gene regulation and physiological function of placental leucine aminopeptidase/oxytocinase during pregnancy. Biochim. Biophys. Acta. 2005, 1751 (1): 19–25. PMID 15894523. doi:10.1016/j.bbapap.2005.04.006. 
  • Mizutani S, Yokosawa H, Tomoda Y. Degradation of oxytocin by the human placenta: effect of selective inhibitors. Acta Endocrinol. 1992, 127 (1): 76–80. PMID 1355623. doi:10.1530/acta.0.1270076. 
  • Klimek, Marek. Comparative analysis of ACTH and oxytocinase plasma concentration during pregnancy. Neuro Endocrinology Letters. August 2005, 26 (4): 337–341. ISSN 0172-780X. PMID 16136013. 
  • Meisenberg G, Simmons WH. Amastatin potentiates the behavioral effects of vasopressin and oxytocin in mice. Peptides. 1984, 5 (3): 535–9. PMID 6540873. doi:10.1016/0196-9781(84)90083-4. 
  • Stancampiano R, Melis MR, Argiolas A. Proteolytic conversion of oxytocin by brain synaptic membranes: role of aminopeptidases and endopeptidases. Peptides. 1991, 12 (5): 1119–25. PMID 1800950. doi:10.1016/0196-9781(91)90068-z. 
  • Itoh C, Watanabe M, Nagamatsu A, Soeda S, Kawarabayashi T, Shimeno H. Two molecular species of oxytocinase (L-cystine aminopeptidase) in human placenta: purification and characterization. Biol. Pharm. Bull. 1997, 20 (1): 20–4. PMID 9013800. doi:10.1248/bpb.20.20. 

worldcat.org

  • Klimek, Marek. Comparative analysis of ACTH and oxytocinase plasma concentration during pregnancy. Neuro Endocrinology Letters. August 2005, 26 (4): 337–341. ISSN 0172-780X. PMID 16136013.