트라이오스 인산 이성질화효소 (Korean Wikipedia)

Analysis of information sources in references of the Wikipedia article "트라이오스 인산 이성질화효소" in Korean language version.

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doi.org

dx.doi.org

  • Orosz F, Oláh J, Ovádi J (December 2006). “Triosephosphate isomerase deficiency: facts and doubts”. 《IUBMB Life》 58 (12): 703–15. doi:10.1080/15216540601115960. PMID 17424909. 
  • Albery WJ, Knowles JR (December 1976). “Free-energy profile of the reaction catalyzed by triosephosphate isomerase”. 《Biochemistry》 15 (25): 5627–31. doi:10.1021/bi00670a031. PMID 999838. 
  • Rose IA, Fung WJ, Warms JV (May 1990). “Proton diffusion in the active site of triosephosphate isomerase”. 《Biochemistry》 29 (18): 4312–7. doi:10.1021/bi00470a008. PMID 2161683. 
  • Alber T, Banner DW, Bloomer AC, Petsko GA, Phillips D, Rivers PS, Wilson IA (June 1981). “On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase”. 《Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences》 293 (1063): 159–71. doi:10.1098/rstb.1981.0069. PMID 6115415. 
  • Nickbarg EB, Davenport RC, Petsko GA, Knowles JR (August 1988). “Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism”. 《Biochemistry》 27 (16): 5948–60. doi:10.1021/bi00416a019. PMID 2847777. 
  • Komives EA, Chang LC, Lolis E, Tilton RF, Petsko GA, Knowles JR (March 1991). “Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95”. 《Biochemistry》 30 (12): 3011–9. doi:10.1021/bi00226a005. PMID 2007138. 
  • Knowles JR (March 1991). “Enzyme catalysis: not different, just better”. 《Nature》 350 (6314): 121–4. doi:10.1038/350121a0. PMID 2005961. 
  • Harris TK, Cole RN, Comer FI, Mildvan AS (November 1998). “Proton transfer in the mechanism of triosephosphate isomerase”. 《Biochemistry》 37 (47): 16828–38. doi:10.1021/bi982089f. PMID 9843453. 
  • Lambeir AM, Opperdoes FR, Wierenga RK (October 1987). “Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes”. 《European Journal of Biochemistry》 168 (1): 69–74. doi:10.1111/j.1432-1033.1987.tb13388.x. PMID 3311744. 
  • Lolis E, Petsko GA (July 1990). “Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis”. 《Biochemistry》 29 (28): 6619–25. doi:10.1021/bi00480a010. PMID 2204418. 
  • Creighton DJ, Hamilton DS (March 2001). “Brief history of glyoxalase I and what we have learned about metal ion-dependent, enzyme-catalyzed isomerizations”. 《Archives of Biochemistry and Biophysics》 387 (1): 1–10. doi:10.1006/abbi.2000.2253. PMID 11368170. 
  • Lodi PJ, Chang LC, Knowles JR, Komives EA (March 1994). “Triosephosphate isomerase requires a positively charged active site: the role of lysine-12”. 《Biochemistry》 33 (10): 2809–14. doi:10.1021/bi00176a009. PMID 8130193. 

nih.gov

ncbi.nlm.nih.gov

  • Orosz F, Oláh J, Ovádi J (December 2006). “Triosephosphate isomerase deficiency: facts and doubts”. 《IUBMB Life》 58 (12): 703–15. doi:10.1080/15216540601115960. PMID 17424909. 
  • Albery WJ, Knowles JR (December 1976). “Free-energy profile of the reaction catalyzed by triosephosphate isomerase”. 《Biochemistry》 15 (25): 5627–31. doi:10.1021/bi00670a031. PMID 999838. 
  • Rose IA, Fung WJ, Warms JV (May 1990). “Proton diffusion in the active site of triosephosphate isomerase”. 《Biochemistry》 29 (18): 4312–7. doi:10.1021/bi00470a008. PMID 2161683. 
  • Alber T, Banner DW, Bloomer AC, Petsko GA, Phillips D, Rivers PS, Wilson IA (June 1981). “On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase”. 《Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences》 293 (1063): 159–71. doi:10.1098/rstb.1981.0069. PMID 6115415. 
  • Nickbarg EB, Davenport RC, Petsko GA, Knowles JR (August 1988). “Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism”. 《Biochemistry》 27 (16): 5948–60. doi:10.1021/bi00416a019. PMID 2847777. 
  • Komives EA, Chang LC, Lolis E, Tilton RF, Petsko GA, Knowles JR (March 1991). “Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95”. 《Biochemistry》 30 (12): 3011–9. doi:10.1021/bi00226a005. PMID 2007138. 
  • Knowles JR (March 1991). “Enzyme catalysis: not different, just better”. 《Nature》 350 (6314): 121–4. doi:10.1038/350121a0. PMID 2005961. 
  • Harris TK, Cole RN, Comer FI, Mildvan AS (November 1998). “Proton transfer in the mechanism of triosephosphate isomerase”. 《Biochemistry》 37 (47): 16828–38. doi:10.1021/bi982089f. PMID 9843453. 
  • Lambeir AM, Opperdoes FR, Wierenga RK (October 1987). “Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes”. 《European Journal of Biochemistry》 168 (1): 69–74. doi:10.1111/j.1432-1033.1987.tb13388.x. PMID 3311744. 
  • Lolis E, Petsko GA (July 1990). “Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis”. 《Biochemistry》 29 (28): 6619–25. doi:10.1021/bi00480a010. PMID 2204418. 
  • Creighton DJ, Hamilton DS (March 2001). “Brief history of glyoxalase I and what we have learned about metal ion-dependent, enzyme-catalyzed isomerizations”. 《Archives of Biochemistry and Biophysics》 387 (1): 1–10. doi:10.1006/abbi.2000.2253. PMID 11368170. 
  • Lodi PJ, Chang LC, Knowles JR, Komives EA (March 1994). “Triosephosphate isomerase requires a positively charged active site: the role of lysine-12”. 《Biochemistry》 33 (10): 2809–14. doi:10.1021/bi00176a009. PMID 8130193.