Enzym (Swedish Wikipedia)

Analysis of information sources in references of the Wikipedia article "Enzym" in Swedish language version.

refsWebsite

Global rank Swedish rank

31nih.gov

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28doi.org

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6web.archive.org

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3nobelprize.org

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2qmul.ac.uk

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1expasy.org

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1virginia.edu

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1books.google.com

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1kva.se

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1fasebj.org

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1ebi.ac.uk

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1bnf.fr

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1worldcat.org

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1gsu.edu

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1pnas.org

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1molbiolcell.org

low place

1asm.org

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1fass.org

low place

asm.org

mmbr.asm.org

Meighen EA (1 Mars 1991). ”Molecular biology of bacterial bioluminescence”. Microbiol. Rev. 55 (1): sid. 123–42. PMID 2030669. PMC: 372803. http://mmbr.asm.org/cgi/reprint/55/1/123?view=long&pmid=2030669.

bnf.fr

gallica.bnf.fr

Fischer E. (1894). ”Einfluss der Configuration auf die Wirkung der Enzyme”. Ber. Dt. Chem. Ges. 27: sid. 2985–93. doi:10.1002/cber.18940270364. http://gallica.bnf.fr/ark:/12148/bpt6k90736r/f364.chemindefer.

books.google.com

Kühne myntade termen "enzyme" i: W. Kühne (1877) "Über das Verhalten verschiedener organisirter und sog. ungeformter Fermente", Verhandlungen des naturhistorisch-medicinischen Vereins zu Heidelberg, vol. 1, nummer 3, sidorna 190-193. relevanta stycket finns att finna på sidan 190: "Um Missverständnissen vorzubeugen und lästige Umschreibungen zu vermeiden schlägt Vortragender vor, die ungeformten oder nicht organisirten Fermente, deren Wirkung ohne Anwesenheit von Organismen und ausserhalb derselben erfolgen kann, als Enzyme zu bezeichnen." (Översättning: För att förebygga missförstånd och undvika besvärliga omskrivningar, föreslår författaren att man betecknar de oformade eller inte organiserade ferment, vilkas verkning kan ske utan närvaron av organismen och utanför den samma, som Enzyme.)

doi.org

dx.doi.org

Bairoch A. (2000). ”The ENZYME database in 2000” (på engelska) (PDF). Nucleic Acids Res 28 (1): sid. 304–5. doi:10.1093/nar/28.1.304. PMID 10592255. PMC: 102465. Arkiverad från originalet den 1 juni 2011. https://web.archive.org/web/20110601003507/http://www.expasy.org/NAR/enz00.pdf. Läst 12 november 2010. Arkiverad 1 juni 2011 hämtat från the Wayback Machine.
Lilley D (2005). ”Structure, folding and mechanisms of ribozymes” (på engelska). Curr Opin Struct Biol 15 (3): sid. 313–23. doi:10.1016/j.sbi.2005.05.002. PMID 15919196.
Cech T (2000). ”Structural biology. The ribosome is a ribozyme” (på engelska). Science 289 (5481): sid. 878–9. doi:10.1126/science.289.5481.878. PMID 10960319.
Groves JT (1997). ”Artificial enzymes. The importance of being selective” (på engelska). Nature 389 (6649): sid. 329–30. doi:10.1038/38602. PMID 9311771.
Dubos J. (1951). ”Louis Pasteur: Free Lance of Science, Gollancz. Quoted in Manchester K. L. (1995) Louis Pasteur (1822–1895)—chance and the prepared mind”. Trends Biotechnol 13 (12): sid. 511–5. doi:10.1016/S0167-7799(00)89014-9. PMID 8595136.
Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR. (1965). ”Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution”. Nature 22 (206): sid. 757–61. doi:10.1038/206757a0. PMID 5891407.
Anfinsen C.B. (1973). ”Principles that Govern the Folding of Protein Chains”. Science 181 (96): sid. 223–30. doi:10.1126/science.181.4096.223. PMID 4124164.
Dunaway-Mariano D (2008). ”Enzyme function discovery”. Structure 16 (11): sid. 1599–600. doi:10.1016/j.str.2008.10.001. PMID 19000810.
Jaeger KE, Eggert T. (2004). ”Enantioselective biocatalysis optimized by directed evolution”. Curr Opin Biotechnol. 15 (4): sid. 305–13. doi:10.1016/j.copbio.2004.06.007. PMID 15358000.
Shevelev IV, Hubscher U. (2002). ”The 3' 5' exonucleases”. Nat Rev Mol Cell Biol. 3 (5): sid. 364–76. doi:10.1038/nrm804. PMID 11988770.
Zenkin N, Yuzenkova Y, Severinov K. (2006). Transcript-assisted transcriptional proofreading. "313". sid. 518–20. doi:10.1126/science.1127422. PMID 16873663.
Ibba M, Soll D. (2000). ”Aminoacyl-tRNA synthesis”. Annu Rev Biochem. 69: sid. 617–50. doi:10.1146/annurev.biochem.69.1.617. PMID 10966471.
Rodnina MV, Wintermeyer W. (2001). ”Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms”. Annu Rev Biochem. 70: sid. 415–35. doi:10.1146/annurev.biochem.70.1.415. PMID 11395413.
Fischer E. (1894). ”Einfluss der Configuration auf die Wirkung der Enzyme”. Ber. Dt. Chem. Ges. 27: sid. 2985–93. doi:10.1002/cber.18940270364. http://gallica.bnf.fr/ark:/12148/bpt6k90736r/f364.chemindefer.
Koshland D. E. (1958). ”Application of a Theory of Enzyme Specificity to Protein Synthesis”. Proc. Natl. Acad. Sci. 44 (2): sid. 98–104. doi:10.1073/pnas.44.2.98. PMID 16590179.
Vasella A, Davies GJ, Bohm M. (2002). ”Glycosidase mechanisms”. Curr Opin Chem Biol. 6 (5): sid. 619–29. doi:10.1016/S1367-5931(02)00380-0. PMID 12413546.
Neet KE (1995). ”Cooperativity in enzyme function: equilibrium and kinetic aspects”. Meth. Enzymol. 249: sid. 519–67. doi:10.1016/0076-6879(95)49048-5. PMID 7791626.
Changeux JP, Edelstein SJ (2005). ”Allosteric mechanisms of signal transduction”. Science 308 (5727): sid. 1424–8. doi:10.1126/science.1108595. PMID 15933191.
Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, Govindasamy L, Silverman DN and McKenna R. (2005). ”Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II”. Biochemistry 44 (4): sid. 1097–115. doi:10.1021/bi0480279. PMID 15667203.
Törnroth-Horsefield S, Neutze R (2008). ”Opening and closing the metabolite gate”. Proc. Natl. Acad. Sci. U.S.A. 105 (50): sid. 19565–6. doi:10.1073/pnas.0810654106. PMID 19073922. PMC: 2604989. http://www.pnas.org/cgi/pmidlookup?view=long&pmid=19073922.
Hunter T. (1995). ”Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling”. Cell. 80 (2): sid. 225–36. doi:10.1016/0092-8674(95)90405-0. PMID 7834742.
Mackie RI, White BA (1 oktober 1990). ”Recent advances in rumen microbial ecology and metabolism: potential impact on nutrient output”. J. Dairy Sci. "73" (10): ss. 2971–95. doi:10.3168/jds.S0022-0302(90)78986-2. PMID 2178174. http://jds.fass.org/cgi/reprint/73/10/2971.
Zhou, X. B., Chen, C., Li, Z. C. & Zou, X. Y. (2007). ”Using Chou's amphiphilic pseudo-amino acid composition and support vector machine for prediction of enzyme subfamily classes”. Journal of Theoretical Biology 248 (3): sid. 546–551. doi:10.1016/j.jtbi.2007.06.001. PMID 17628605.
Renugopalakrishnan V, Garduno-Juarez R, Narasimhan G, Verma CS, Wei X, Li P. (2005). ”Rational design of thermally stable proteins: relevance to bionanotechnology”. J Nanosci Nanotechnol. 5 (11): sid. 1759–1767. doi:10.1166/jnn.2005.441. PMID 16433409.
Hult K, Berglund P. (2003). ”Engineered enzymes for improved organic synthesis”. Curr Opin Biotechnol. 14 (4): sid. 395–400. doi:10.1016/S0958-1669(03)00095-8. PMID 12943848.
Jiang L, Althoff EA, Clemente FR (2008). ”De novo computational design of retro-aldol enzymes”. Science (journal) 319 (5868): sid. 1387–91. doi:10.1126/science.1152692. PMID 18323453.
Guzmán-Maldonado H, Paredes-López O (1995). ”Amylolytic enzymes and products derived from starch: a review”. Critical reviews in food science and nutrition 35 (5): sid. 373–403. doi:10.1080/10408399509527706. PMID 8573280.
Dulieu C, Moll M, Boudrant J, Poncelet D (2000). ”Improved performances and control of beer fermentation using encapsulated alpha-acetolactate decarboxylase and modeling”. Biotechnology progress 16 (6): sid. 958–65. doi:10.1021/bp000128k. PMID 11101321.

ebi.ac.uk

”The Catalytic Site Atlas”. The European Bioinformatics Institute. Arkiverad från originalet den 3 augusti 2013. https://web.archive.org/web/20130803032349/http://www.ebi.ac.uk/thornton-srv/databases/CSA/. Läst 14 november 2010. .

expasy.org

Bairoch A. (2000). ”The ENZYME database in 2000” (på engelska) (PDF). Nucleic Acids Res 28 (1): sid. 304–5. doi:10.1093/nar/28.1.304. PMID 10592255. PMC: 102465. Arkiverad från originalet den 1 juni 2011. https://web.archive.org/web/20110601003507/http://www.expasy.org/NAR/enz00.pdf. Läst 12 november 2010. Arkiverad 1 juni 2011 hämtat från the Wayback Machine.

fasebj.org

Smith S (1 december 1994). ”The animal fatty acid synthase: one gene, one polypeptide, seven enzymes”. FASEB J. 8 (15): sid. 1248–59. PMID 8001737. http://www.fasebj.org/content/8/15/1248.full.pdf+html. Läst 14 november 2010.

fass.org

jds.fass.org

Mackie RI, White BA (1 oktober 1990). ”Recent advances in rumen microbial ecology and metabolism: potential impact on nutrient output”. J. Dairy Sci. "73" (10): ss. 2971–95. doi:10.3168/jds.S0022-0302(90)78986-2. PMID 2178174. http://jds.fass.org/cgi/reprint/73/10/2971.

gsu.edu

chemistry.gsu.edu

”PDBs for Biochemistry”. Georgia State University. Arkiverad från originalet den 16 juli 2011. https://web.archive.org/web/20110716103545/http://chemistry.gsu.edu/Glactone/PDB/Proteins/Krebs/1pyd.html. Läst 22 januari 2011.

kva.se

”Pristagare Kungl. Vetenskapsakademin: Eduard Buchner”. Kungl. Vetenskapsakademin. Arkiverad från originalet den 3 december 2022. https://web.archive.org/web/20221203002016/https://www.kva.se/prisvinnare/eduard-buchner/. Läst 30 oktober 2018. ”för hans biologiskkemiska undersökningar och upptäckt av den cellfria jäsningen”

molbiolcell.org

Berg JS, Powell BC, Cheney RE (1 April 2001). ”A millennial myosin census”. Mol. Biol. Cell 12 (4): sid. 780–94. PMID 11294886. PMC: 32266. http://www.molbiolcell.org/cgi/content/full/12/4/780.

nih.gov

ncbi.nlm.nih.gov

Bairoch A. (2000). ”The ENZYME database in 2000” (på engelska) (PDF). Nucleic Acids Res 28 (1): sid. 304–5. doi:10.1093/nar/28.1.304. PMID 10592255. PMC: 102465. Arkiverad från originalet den 1 juni 2011. https://web.archive.org/web/20110601003507/http://www.expasy.org/NAR/enz00.pdf. Läst 12 november 2010. Arkiverad 1 juni 2011 hämtat från the Wayback Machine.
Lilley D (2005). ”Structure, folding and mechanisms of ribozymes” (på engelska). Curr Opin Struct Biol 15 (3): sid. 313–23. doi:10.1016/j.sbi.2005.05.002. PMID 15919196.
Cech T (2000). ”Structural biology. The ribosome is a ribozyme” (på engelska). Science 289 (5481): sid. 878–9. doi:10.1126/science.289.5481.878. PMID 10960319.
Groves JT (1997). ”Artificial enzymes. The importance of being selective” (på engelska). Nature 389 (6649): sid. 329–30. doi:10.1038/38602. PMID 9311771.
Dubos J. (1951). ”Louis Pasteur: Free Lance of Science, Gollancz. Quoted in Manchester K. L. (1995) Louis Pasteur (1822–1895)—chance and the prepared mind”. Trends Biotechnol 13 (12): sid. 511–5. doi:10.1016/S0167-7799(00)89014-9. PMID 8595136.
Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR. (1965). ”Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution”. Nature 22 (206): sid. 757–61. doi:10.1038/206757a0. PMID 5891407.
Chen LH, Kenyon GL, Curtin F, Harayama S, Bembenek ME, Hajipour G, Whitman CP (1992). ”4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer”. J. Biol. Chem. 267 (25): sid. 17716–21. PMID 1339435.
Smith S (1 december 1994). ”The animal fatty acid synthase: one gene, one polypeptide, seven enzymes”. FASEB J. 8 (15): sid. 1248–59. PMID 8001737. http://www.fasebj.org/content/8/15/1248.full.pdf+html. Läst 14 november 2010.
Anfinsen C.B. (1973). ”Principles that Govern the Folding of Protein Chains”. Science 181 (96): sid. 223–30. doi:10.1126/science.181.4096.223. PMID 4124164.
Dunaway-Mariano D (2008). ”Enzyme function discovery”. Structure 16 (11): sid. 1599–600. doi:10.1016/j.str.2008.10.001. PMID 19000810.
Jaeger KE, Eggert T. (2004). ”Enantioselective biocatalysis optimized by directed evolution”. Curr Opin Biotechnol. 15 (4): sid. 305–13. doi:10.1016/j.copbio.2004.06.007. PMID 15358000.
Shevelev IV, Hubscher U. (2002). ”The 3' 5' exonucleases”. Nat Rev Mol Cell Biol. 3 (5): sid. 364–76. doi:10.1038/nrm804. PMID 11988770.
Zenkin N, Yuzenkova Y, Severinov K. (2006). Transcript-assisted transcriptional proofreading. "313". sid. 518–20. doi:10.1126/science.1127422. PMID 16873663.
Ibba M, Soll D. (2000). ”Aminoacyl-tRNA synthesis”. Annu Rev Biochem. 69: sid. 617–50. doi:10.1146/annurev.biochem.69.1.617. PMID 10966471.
Rodnina MV, Wintermeyer W. (2001). ”Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms”. Annu Rev Biochem. 70: sid. 415–35. doi:10.1146/annurev.biochem.70.1.415. PMID 11395413.
Koshland D. E. (1958). ”Application of a Theory of Enzyme Specificity to Protein Synthesis”. Proc. Natl. Acad. Sci. 44 (2): sid. 98–104. doi:10.1073/pnas.44.2.98. PMID 16590179.
Vasella A, Davies GJ, Bohm M. (2002). ”Glycosidase mechanisms”. Curr Opin Chem Biol. 6 (5): sid. 619–29. doi:10.1016/S1367-5931(02)00380-0. PMID 12413546.
Neet KE (1995). ”Cooperativity in enzyme function: equilibrium and kinetic aspects”. Meth. Enzymol. 249: sid. 519–67. doi:10.1016/0076-6879(95)49048-5. PMID 7791626.
Changeux JP, Edelstein SJ (2005). ”Allosteric mechanisms of signal transduction”. Science 308 (5727): sid. 1424–8. doi:10.1126/science.1108595. PMID 15933191.
Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, Govindasamy L, Silverman DN and McKenna R. (2005). ”Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II”. Biochemistry 44 (4): sid. 1097–115. doi:10.1021/bi0480279. PMID 15667203.
Törnroth-Horsefield S, Neutze R (2008). ”Opening and closing the metabolite gate”. Proc. Natl. Acad. Sci. U.S.A. 105 (50): sid. 19565–6. doi:10.1073/pnas.0810654106. PMID 19073922. PMC: 2604989. http://www.pnas.org/cgi/pmidlookup?view=long&pmid=19073922.
Hunter T. (1995). ”Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling”. Cell. 80 (2): sid. 225–36. doi:10.1016/0092-8674(95)90405-0. PMID 7834742.
Berg JS, Powell BC, Cheney RE (1 April 2001). ”A millennial myosin census”. Mol. Biol. Cell 12 (4): sid. 780–94. PMID 11294886. PMC: 32266. http://www.molbiolcell.org/cgi/content/full/12/4/780.
Meighen EA (1 Mars 1991). ”Molecular biology of bacterial bioluminescence”. Microbiol. Rev. 55 (1): sid. 123–42. PMID 2030669. PMC: 372803. http://mmbr.asm.org/cgi/reprint/55/1/123?view=long&pmid=2030669.
Mackie RI, White BA (1 oktober 1990). ”Recent advances in rumen microbial ecology and metabolism: potential impact on nutrient output”. J. Dairy Sci. "73" (10): ss. 2971–95. doi:10.3168/jds.S0022-0302(90)78986-2. PMID 2178174. http://jds.fass.org/cgi/reprint/73/10/2971.
Zhou, X. B., Chen, C., Li, Z. C. & Zou, X. Y. (2007). ”Using Chou's amphiphilic pseudo-amino acid composition and support vector machine for prediction of enzyme subfamily classes”. Journal of Theoretical Biology 248 (3): sid. 546–551. doi:10.1016/j.jtbi.2007.06.001. PMID 17628605.
Renugopalakrishnan V, Garduno-Juarez R, Narasimhan G, Verma CS, Wei X, Li P. (2005). ”Rational design of thermally stable proteins: relevance to bionanotechnology”. J Nanosci Nanotechnol. 5 (11): sid. 1759–1767. doi:10.1166/jnn.2005.441. PMID 16433409.
Hult K, Berglund P. (2003). ”Engineered enzymes for improved organic synthesis”. Curr Opin Biotechnol. 14 (4): sid. 395–400. doi:10.1016/S0958-1669(03)00095-8. PMID 12943848.
Jiang L, Althoff EA, Clemente FR (2008). ”De novo computational design of retro-aldol enzymes”. Science (journal) 319 (5868): sid. 1387–91. doi:10.1126/science.1152692. PMID 18323453.
Guzmán-Maldonado H, Paredes-López O (1995). ”Amylolytic enzymes and products derived from starch: a review”. Critical reviews in food science and nutrition 35 (5): sid. 373–403. doi:10.1080/10408399509527706. PMID 8573280.
Dulieu C, Moll M, Boudrant J, Poncelet D (2000). ”Improved performances and control of beer fermentation using encapsulated alpha-acetolactate decarboxylase and modeling”. Biotechnology progress 16 (6): sid. 958–65. doi:10.1021/bp000128k. PMID 11101321.

nobelprize.org

”Eduard Buchner – Biography” (på engelska). Nobelprize.org. https://www.nobelprize.org/prizes/chemistry/1907/buchner/biographical/. Läst 30 oktober 2018.
”Eduard Buchner's 1907 Nobel lecture – Cell-Free Fermentation” (på engelska). Nobelprize.org. https://www.nobelprize.org/prizes/chemistry/1907/buchner/lecture/. Läst 30 oktober 2018.
”The Nobel Prize in Chemistry 1946” (på engelska). Nobelprize.org. https://www.nobelprize.org/prizes/chemistry/1946/. Läst 30 oktober 2018.

pnas.org

Törnroth-Horsefield S, Neutze R (2008). ”Opening and closing the metabolite gate”. Proc. Natl. Acad. Sci. U.S.A. 105 (50): sid. 19565–6. doi:10.1073/pnas.0810654106. PMID 19073922. PMC: 2604989. http://www.pnas.org/cgi/pmidlookup?view=long&pmid=19073922.

qmul.ac.uk

chem.qmul.ac.uk

de Bolster, M.W.G. (1997). ”Glossary of Terms Used in Bioinorganic Chemistry: Cofactor” (på engelska). International Union of Pure and Applied Chemistry. Arkiverad från originalet den 21 januari 2017. https://web.archive.org/web/20170121172848/http://www.chem.qmul.ac.uk/iupac/bioinorg/CD.html#34#34. Läst 12 november 2010.
de Bolster, M.W.G. (1997). ”Glossary of Terms Used in Bioinorganic Chemistry: Coenzyme”. International Union of Pure and Applied Chemistry. Arkiverad från originalet den 21 januari 2017. https://web.archive.org/web/20170121172848/http://www.chem.qmul.ac.uk/iupac/bioinorg/CD.html#33#33. Läst 12 november 2010.

virginia.edu

etext.lib.virginia.edu

Williams, H. S. (1904). A History of Science: in Five Volumes. Volume IV: Modern Development of the Chemical and Biological Sciences. New York: Harper and Brothers. http://etext.lib.virginia.edu/toc/modeng/public/Wil4Sci.html

web.archive.org

Bairoch A. (2000). ”The ENZYME database in 2000” (på engelska) (PDF). Nucleic Acids Res 28 (1): sid. 304–5. doi:10.1093/nar/28.1.304. PMID 10592255. PMC: 102465. Arkiverad från originalet den 1 juni 2011. https://web.archive.org/web/20110601003507/http://www.expasy.org/NAR/enz00.pdf. Läst 12 november 2010. Arkiverad 1 juni 2011 hämtat från the Wayback Machine.
”Pristagare Kungl. Vetenskapsakademin: Eduard Buchner”. Kungl. Vetenskapsakademin. Arkiverad från originalet den 3 december 2022. https://web.archive.org/web/20221203002016/https://www.kva.se/prisvinnare/eduard-buchner/. Läst 30 oktober 2018. ”för hans biologiskkemiska undersökningar och upptäckt av den cellfria jäsningen”
”The Catalytic Site Atlas”. The European Bioinformatics Institute. Arkiverad från originalet den 3 augusti 2013. https://web.archive.org/web/20130803032349/http://www.ebi.ac.uk/thornton-srv/databases/CSA/. Läst 14 november 2010. .
de Bolster, M.W.G. (1997). ”Glossary of Terms Used in Bioinorganic Chemistry: Cofactor” (på engelska). International Union of Pure and Applied Chemistry. Arkiverad från originalet den 21 januari 2017. https://web.archive.org/web/20170121172848/http://www.chem.qmul.ac.uk/iupac/bioinorg/CD.html#34#34. Läst 12 november 2010.
de Bolster, M.W.G. (1997). ”Glossary of Terms Used in Bioinorganic Chemistry: Coenzyme”. International Union of Pure and Applied Chemistry. Arkiverad från originalet den 21 januari 2017. https://web.archive.org/web/20170121172848/http://www.chem.qmul.ac.uk/iupac/bioinorg/CD.html#33#33. Läst 12 november 2010.
”PDBs for Biochemistry”. Georgia State University. Arkiverad från originalet den 16 juli 2011. https://web.archive.org/web/20110716103545/http://chemistry.gsu.edu/Glactone/PDB/Proteins/Krebs/1pyd.html. Läst 22 januari 2011.

worldcat.org

Boyer, Rodney (2002). ”6” (på engelska). Concepts in Biochemistry (2:a upplagan). New York, Chichester, Weinheim, Brisbane, Singapore, Toronto.: John Wiley & Sons, Inc. sid. 137–8. ISBN 0-470-00379-0. OCLC 51720783