テルモリシン (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "テルモリシン" in Japanese language version.

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4,730th place
2,757th place

doi.org

  • Tajima M, Urabe I. et al. (1976). “Role of calcium ions in the thermostability of thermolysin and Bacillus subtilis var. amylosacchariticus neutral protease”. Eur. J. Biochem. 64 (1): 243-247. doi:10.1111/j.1432-1033.1976.tb10293.x. PMID 819262. 
  • Trusek-Holownia A. (2003). “Synthesis of ZAlaPheOMe, the precursor of bitter dipeptide in the two-phase ethyl acetate-water system catalysed by thermolysin”. J. Biotechnol. 102 (2): 153-163. doi:10.1016/S0168-1656(03)00024-5. PMID 12697393. 
  • Yasukawa K, Kusano M, Inouye K. (2007). “A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli”. Protein Eng. Des. Sel. 20 (8): 375-383. doi:10.1093/protein/gzm031. PMID 17616558. 
  • Inouye K, Kusano M. et al. (2007). “Engineering, expression, purification, and production of recombinant thermolysin”. Biotechnol. Annu. Rev.. Biotechnology Annual Review 13: 43-64. doi:10.1016/S1387-2656(07)13003-9. ISBN 978-0-444-53032-5. PMID 17875473. 
  • Holmes MA and Matthews BW. (1982). “Structure of thermolysin refined at 1.6 A resolution”. J. Mol. Biol. 160 (4): 623-639. doi:10.1016/0022-2836(82)90319-9. PMID 7175940. 
  • Eijsink VG, Veltman OR, et al. (1995). “Structural determinants of the stability of thermolysin-like proteinases”. Nat. Struct. Biol. 2 (5): 374-379. doi:10.1038/nsb0595-374. PMID 7664094. 
  • Dahlquist FW, Long JW and Bigbee WL (1976). “Role of Calcium in the thermal stability of thermolysin”. Biochemistry 15 (5): 1103-1111. doi:10.1021/bi00650a024. PMID 814920. 
  • Yagasaki, Makoto; Hashimoto, Shin-ichi (November 2008). “Synthesis and application of dipeptides; current status and perspectives”. Applied Microbiology and Biotechnology 81 (1): 13-22. doi:10.1007/s00253-008-1590-3. PMID 18795289. 

nih.gov

pubmed.ncbi.nlm.nih.gov

  • Tajima M, Urabe I. et al. (1976). “Role of calcium ions in the thermostability of thermolysin and Bacillus subtilis var. amylosacchariticus neutral protease”. Eur. J. Biochem. 64 (1): 243-247. doi:10.1111/j.1432-1033.1976.tb10293.x. PMID 819262. 
  • Trusek-Holownia A. (2003). “Synthesis of ZAlaPheOMe, the precursor of bitter dipeptide in the two-phase ethyl acetate-water system catalysed by thermolysin”. J. Biotechnol. 102 (2): 153-163. doi:10.1016/S0168-1656(03)00024-5. PMID 12697393. 
  • Yasukawa K, Kusano M, Inouye K. (2007). “A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli”. Protein Eng. Des. Sel. 20 (8): 375-383. doi:10.1093/protein/gzm031. PMID 17616558. 
  • Inouye K, Kusano M. et al. (2007). “Engineering, expression, purification, and production of recombinant thermolysin”. Biotechnol. Annu. Rev.. Biotechnology Annual Review 13: 43-64. doi:10.1016/S1387-2656(07)13003-9. ISBN 978-0-444-53032-5. PMID 17875473. 
  • Holmes MA and Matthews BW. (1982). “Structure of thermolysin refined at 1.6 A resolution”. J. Mol. Biol. 160 (4): 623-639. doi:10.1016/0022-2836(82)90319-9. PMID 7175940. 
  • Matthews BW, Weaver LH and Kester WR. (1974). “The conformation of thermolysin”. J. Biol. Chem. 249 (24): 8030-8044. PMID 4214815. 
  • Eijsink VG, Veltman OR, et al. (1995). “Structural determinants of the stability of thermolysin-like proteinases”. Nat. Struct. Biol. 2 (5): 374-379. doi:10.1038/nsb0595-374. PMID 7664094. 
  • Dahlquist FW, Long JW and Bigbee WL (1976). “Role of Calcium in the thermal stability of thermolysin”. Biochemistry 15 (5): 1103-1111. doi:10.1021/bi00650a024. PMID 814920. 
  • Yagasaki, Makoto; Hashimoto, Shin-ichi (November 2008). “Synthesis and application of dipeptides; current status and perspectives”. Applied Microbiology and Biotechnology 81 (1): 13-22. doi:10.1007/s00253-008-1590-3. PMID 18795289. 

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