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확산 지배 효소 (Korean Wikipedia)

Analysis of information sources in references of the Wikipedia article "확산 지배 효소" in Korean language version.

refsWebsite
Global rank Korean rank
14doi.org
2nd place
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13nih.gov
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4th place
3harvard.edu
18th place
27th place
2worldcat.org
5th place
11th place
1jstor.org
26th place
70th place
1arxiv.org
69th place
54th place

arxiv.org

doi.org

dx.doi.org

  • Bar-Even, Arren; Noor, Elad; Savir, Yonatan; Liebermeister, Wolfram; Davidi, Dan; Tawfik, Dan S; Milo, Ron (2011). “The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters”. 《Biochemistry》 50 (21): 4402–10. doi:10.1021/bi2002289. PMID 21506553. 
  • Alberty, Robert A.; Hammes, Gordon G. (1958). “Application of the Theory of Diffusion-controlled Reactions to Enzyme Kinetics”. 《Journal of Physical Chemistry》 62 (2): 154–9. doi:10.1021/j150560a005. 
  • Eigen, Manfred; Hammes, Gordon G. (2006). 〈Elementary Steps in Enzyme Reactions (as Studied by Relaxation Spectrometry)〉. Nord, F. F. 《Advances in Enzymology and Related Areas of Molecular Biology》. 1–38쪽. doi:10.1002/9780470122709.ch1. ISBN 978-0-470-12270-9. OCLC 777630506. 
  • Koenig, Seymour H.; Brown, Rodney D. (1972). “H2CO3 as Substrate for Carbonic Anhydrase in the Dehydration of HCO3−”. 《Proceedings of the National Academy of Sciences of the United States of America》 69 (9): 2422–5. Bibcode:1972PNAS...69.2422K. doi:10.1073/pnas.69.9.2422. JSTOR 61783. PMC 426955. PMID 4627028. 
  • Riggs, Arthur D; Bourgeois, Suzanne; Cohn, Melvin (1970). “The lac represser-operator interaction”. 《Journal of Molecular Biology》 53 (3): 401–17. doi:10.1016/0022-2836(70)90074-4. PMID 4924006. 
  • Kirschner, Kasper; Gallego, Ernesto; Schuster, Inge; Goodall, David (1971). “Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase”. 《Journal of Molecular Biology》 58 (1): 29–50. doi:10.1016/0022-2836(71)90230-0. PMID 4326080. 
  • Chou, Kuo Chen; Zhou, Guo Ping (1982). “Role of the protein outside active site on the diffusion-controlled reaction of enzymes”. 《Journal of the American Chemical Society》 104 (5): 1409–1413. doi:10.1021/ja00369a043. 
  • Payens, T.A.J (1983). “Why are enzymes so large?”. 《Trends in Biochemical Sciences》 8 (2): 46. doi:10.1016/0968-0004(83)90382-1. 
  • Zhou, Guozhi; Wong, Ming-Tat; Zhou, Guo-Qiang (1983). “Diffusion-controlled reactions of enzymes”. 《Biophysical Chemistry》 18 (2): 125–32. doi:10.1016/0301-4622(83)85006-6. PMID 6626685. 
  • Zhou, Guo-Qiang; Zhong, Wei-Zhu (1982). “Diffusion-Controlled Reactions of Enzymes”. 《European Journal of Biochemistry》 128 (2–3): 383–7. doi:10.1111/j.1432-1033.1982.tb06976.x. PMID 7151785. 
  • Garcia-Viloca, M; Gao, Jiali; Karplus, Martin; Truhlar, Donald G (2004). “How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations”. 《Science》 303 (5655): 186–95. Bibcode:2004Sci...303..186G. doi:10.1126/science.1088172. PMID 14716003. 
  • Olsson, Mats H. M; Siegbahn, Per E. M; Warshel, Arieh (2004). “Simulations of the Large Kinetic Isotope Effect and the Temperature Dependence of the Hydrogen Atom Transfer in Lipoxygenase”. 《Journal of the American Chemical Society》 126 (9): 2820–8. doi:10.1021/ja037233l. PMID 14995199. 
  • Jevtic, S; Anders, J (2017). “A qualitative quantum rate model for hydrogen transfer in soybean lipoxygenase”. 《The Journal of Chemical Physics》 147 (11): 114108. arXiv:1612.03773. Bibcode:2017JChPh.147k4108J. doi:10.1063/1.4998941. PMID 28938801. 
  • Domnik, Lilith; Merrouch, Meriem; Goetzl, Sebastian; Jeoung, Jae-Hun; Léger, Christophe; Dementin, Sébastien; Fourmond, Vincent; Dobbek, Holger (2017년 11월 27일). “CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2”. 《Angewandte Chemie International Edition》 (영어) 56 (48): 15466–15469. doi:10.1002/anie.201709261. ISSN 1521-3773. PMID 29024326. 

harvard.edu

adsabs.harvard.edu

jstor.org

nih.gov

ncbi.nlm.nih.gov

  • Bar-Even, Arren; Noor, Elad; Savir, Yonatan; Liebermeister, Wolfram; Davidi, Dan; Tawfik, Dan S; Milo, Ron (2011). “The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters”. 《Biochemistry》 50 (21): 4402–10. doi:10.1021/bi2002289. PMID 21506553. 
  • Koenig, Seymour H.; Brown, Rodney D. (1972). “H2CO3 as Substrate for Carbonic Anhydrase in the Dehydration of HCO3−”. 《Proceedings of the National Academy of Sciences of the United States of America》 69 (9): 2422–5. Bibcode:1972PNAS...69.2422K. doi:10.1073/pnas.69.9.2422. JSTOR 61783. PMC 426955. PMID 4627028. 
  • Chou, Kuo-Chen; Jiang, Shou-Ping (1974). “Studies on the rate of diffusion-controlled reactions of enzymes. Spatial factor and force field factor”. 《Scientia Sinica》 27 (5): 664–80. PMID 4219062. 
  • Chou, Kuo-Chen (1976). “The kinetics of the combination reaction between enzyme and substrate”. 《Scientia Sinica》 19 (4): 505–28. PMID 824728. 
  • Li, TT; Chou, KC (1976). “The quantitative relations between diffusion-controlled reaction rate and characteristic parameters in enzyme-substrate reaction systems. I. Neutral substrates”. 《Scientia Sinica》 19 (1): 117–36. PMID 1273571. 
  • Riggs, Arthur D; Bourgeois, Suzanne; Cohn, Melvin (1970). “The lac represser-operator interaction”. 《Journal of Molecular Biology》 53 (3): 401–17. doi:10.1016/0022-2836(70)90074-4. PMID 4924006. 
  • Kirschner, Kasper; Gallego, Ernesto; Schuster, Inge; Goodall, David (1971). “Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase”. 《Journal of Molecular Biology》 58 (1): 29–50. doi:10.1016/0022-2836(71)90230-0. PMID 4326080. 
  • Zhou, Guozhi; Wong, Ming-Tat; Zhou, Guo-Qiang (1983). “Diffusion-controlled reactions of enzymes”. 《Biophysical Chemistry》 18 (2): 125–32. doi:10.1016/0301-4622(83)85006-6. PMID 6626685. 
  • Zhou, Guo-Qiang; Zhong, Wei-Zhu (1982). “Diffusion-Controlled Reactions of Enzymes”. 《European Journal of Biochemistry》 128 (2–3): 383–7. doi:10.1111/j.1432-1033.1982.tb06976.x. PMID 7151785. 
  • Garcia-Viloca, M; Gao, Jiali; Karplus, Martin; Truhlar, Donald G (2004). “How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations”. 《Science》 303 (5655): 186–95. Bibcode:2004Sci...303..186G. doi:10.1126/science.1088172. PMID 14716003. 
  • Olsson, Mats H. M; Siegbahn, Per E. M; Warshel, Arieh (2004). “Simulations of the Large Kinetic Isotope Effect and the Temperature Dependence of the Hydrogen Atom Transfer in Lipoxygenase”. 《Journal of the American Chemical Society》 126 (9): 2820–8. doi:10.1021/ja037233l. PMID 14995199. 
  • Jevtic, S; Anders, J (2017). “A qualitative quantum rate model for hydrogen transfer in soybean lipoxygenase”. 《The Journal of Chemical Physics》 147 (11): 114108. arXiv:1612.03773. Bibcode:2017JChPh.147k4108J. doi:10.1063/1.4998941. PMID 28938801. 
  • Domnik, Lilith; Merrouch, Meriem; Goetzl, Sebastian; Jeoung, Jae-Hun; Léger, Christophe; Dementin, Sébastien; Fourmond, Vincent; Dobbek, Holger (2017년 11월 27일). “CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2”. 《Angewandte Chemie International Edition》 (영어) 56 (48): 15466–15469. doi:10.1002/anie.201709261. ISSN 1521-3773. PMID 29024326. 

worldcat.org

  • Eigen, Manfred; Hammes, Gordon G. (2006). 〈Elementary Steps in Enzyme Reactions (as Studied by Relaxation Spectrometry)〉. Nord, F. F. 《Advances in Enzymology and Related Areas of Molecular Biology》. 1–38쪽. doi:10.1002/9780470122709.ch1. ISBN 978-0-470-12270-9. OCLC 777630506. 
  • Domnik, Lilith; Merrouch, Meriem; Goetzl, Sebastian; Jeoung, Jae-Hun; Léger, Christophe; Dementin, Sébastien; Fourmond, Vincent; Dobbek, Holger (2017년 11월 27일). “CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2”. 《Angewandte Chemie International Edition》 (영어) 56 (48): 15466–15469. doi:10.1002/anie.201709261. ISSN 1521-3773. PMID 29024326.