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Triosa fosfat isomerase (Malay Wikipedia)

Analysis of information sources in references of the Wikipedia article "Triosa fosfat isomerase" in Malay language version.

refsWebsite
Global rank Malay rank
12doi.org
2nd place
8th place
12nih.gov
4th place
14th place

doi.org

  • "Triosephosphate isomerase deficiency: facts and doubts". IUBMB Life. 58 (12): 703–15. December 2006. doi:10.1080/15216540601115960. PMID 17424909.
  • "Free-energy profile of the reaction catalyzed by triosephosphate isomerase". Biochemistry. 15 (25): 5627–31. December 1976. doi:10.1021/bi00670a031. PMID 999838.
  • "Proton diffusion in the active site of triosephosphate isomerase". Biochemistry. 29 (18): 4312–7. May 1990. doi:10.1021/bi00470a008. PMID 2161683.
  • "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. June 1981. doi:10.1098/rstb.1981.0069. PMID 6115415.
  • "Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism". Biochemistry. 27 (16): 5948–60. August 1988. doi:10.1021/bi00416a019. PMID 2847777.
  • "Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95". Biochemistry. 30 (12): 3011–9. March 1991. doi:10.1021/bi00226a005. PMID 2007138.
  • "Enzyme catalysis: not different, just better". Nature. 350 (6314): 121–4. March 1991. doi:10.1038/350121a0. PMID 2005961.
  • "Proton transfer in the mechanism of triosephosphate isomerase". Biochemistry. 37 (47): 16828–38. November 1998. doi:10.1021/bi982089f. PMID 9843453.
  • "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. October 1987. doi:10.1111/j.1432-1033.1987.tb13388.x. PMID 3311744.
  • "Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis". Biochemistry. 29 (28): 6619–25. July 1990. doi:10.1021/bi00480a010. PMID 2204418.
  • "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. March 2001. doi:10.1006/abbi.2000.2253. PMID 11368170.
  • "Triosephosphate isomerase requires a positively charged active site: the role of lysine-12". Biochemistry. 33 (10): 2809–14. March 1994. doi:10.1021/bi00176a009. PMID 8130193.

nih.gov

pubmed.ncbi.nlm.nih.gov

  • "Triosephosphate isomerase deficiency: facts and doubts". IUBMB Life. 58 (12): 703–15. December 2006. doi:10.1080/15216540601115960. PMID 17424909.
  • "Free-energy profile of the reaction catalyzed by triosephosphate isomerase". Biochemistry. 15 (25): 5627–31. December 1976. doi:10.1021/bi00670a031. PMID 999838.
  • "Proton diffusion in the active site of triosephosphate isomerase". Biochemistry. 29 (18): 4312–7. May 1990. doi:10.1021/bi00470a008. PMID 2161683.
  • "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. June 1981. doi:10.1098/rstb.1981.0069. PMID 6115415.
  • "Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism". Biochemistry. 27 (16): 5948–60. August 1988. doi:10.1021/bi00416a019. PMID 2847777.
  • "Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95". Biochemistry. 30 (12): 3011–9. March 1991. doi:10.1021/bi00226a005. PMID 2007138.
  • "Enzyme catalysis: not different, just better". Nature. 350 (6314): 121–4. March 1991. doi:10.1038/350121a0. PMID 2005961.
  • "Proton transfer in the mechanism of triosephosphate isomerase". Biochemistry. 37 (47): 16828–38. November 1998. doi:10.1021/bi982089f. PMID 9843453.
  • "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. October 1987. doi:10.1111/j.1432-1033.1987.tb13388.x. PMID 3311744.
  • "Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis". Biochemistry. 29 (28): 6619–25. July 1990. doi:10.1021/bi00480a010. PMID 2204418.
  • "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. March 2001. doi:10.1006/abbi.2000.2253. PMID 11368170.
  • "Triosephosphate isomerase requires a positively charged active site: the role of lysine-12". Biochemistry. 33 (10): 2809–14. March 1994. doi:10.1021/bi00176a009. PMID 8130193.