Aspartátaminotransferáza (Slovak Wikipedia)

Analysis of information sources in references of the Wikipedia article "Aspartátaminotransferáza" in Slovak language version.

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20nih.gov

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19doi.org

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1worldcat.org

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1gpnotebook.co.uk

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doi.org

dx.doi.org

The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Protein Eng., March 1994, s. 405–412. DOI: 10.1093/protein/7.3.405. PMID 7909946.
Transaminase activity in human blood.. The Journal of Clinical Investigation, January 1955, s. 126–31. DOI: 10.1172/jci103055. PMID 13221663.
A note on the spectrometric assay of glutamic-oxalaceticñnn transaminase in human blood serum.. The Journal of Clinical Investigation, January 1955, s. 131–3. DOI: 10.1172/JCI103055. PMID 13221664.
Serum glutamic oxaloacetic transaminase activity in human acute transmural myocardial infarction.. Science, 24 September 1954, s. 497–9. DOI: 10.1126/science.120.3117.497. PMID 13195683.
GIANNINI, E. G.. Liver enzyme alteration: a guide for clinicians. Canadian Medical Association Journal, 2005-02-01, s. 367–379. ISSN 0820-3946. DOI: 10.1503/cmaj.1040752. PMID 15684121.
Kirsch JF; Eichele G; Ford G. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol, 1984, s. 497–525. DOI: 10.1016/0022-2836(84)90333-4. PMID 6143829.
Recent topics in pyridoxal 5'-phosphate enzyme studies. Annu Rev Biochem, 1990, s. 87–110. DOI: 10.1146/annurev.bi.59.070190.000511. PMID 2197992.
Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei. Biochem J, 1991, s. 149–54. DOI: 10.1042/bj2780149. PMID 1909112.
An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. J Biochem, 1996, s. 135–44. DOI: 10.1093/oxfordjournals.jbchem.a021198. PMID 8907187.
Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. J Bacteriol, 1977, s. 429–40. DOI: 10.1128/JB.130.1.429-440.1977. PMID 15983.
X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J Mol Biol, 1992, s. 495–517. DOI: 10.1016/0022-2836(92)90935-D. PMID 1593633.
Rhee S; Silva MM; Hyde CC. Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate. J Biol Chem, 1997, s. 17293–302. DOI: 10.1074/jbc.272.28.17293. PMID 9211866.
Kamitori S; Hirotsu K; Higuchi T. Three-dimensional structure of aspartate aminotransferase from Escherichia coli at 2.8 A resolution. J Biochem, 1988, s. 317–8. DOI: 10.1093/oxfordjournals.jbchem.a122464. PMID 3071527.
Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase. Biochemistry, 1991, s. 1980–1985. DOI: 10.1021/bi00221a035. PMID 1993208.
Domain closure in mitochondrial aspartate aminotransferase. J Mol Biol, 1992, s. 197–213. DOI: 10.1016/0022-2836(92)90691-C. PMID 1522585.
Dual substrate recognition of aminotransferases. The Chemical Record, 2005, s. 160–172. DOI: 10.1002/tcr.20042. PMID 15889412.
Mechanism of racemization of amino acids by aspartate aminotransferase. Eur J Biochem, 1992, s. 563–569. DOI: 10.1111/j.1432-1033.1992.tb16584.x. PMID 1735441.
The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis. Biochemistry, 1996, s. 5280–5291. DOI: 10.1021/bi952138d. PMID 8611515.
Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis. J Biol Chem, 2003, s. 9481–9488. DOI: 10.1074/jbc.M209235200. PMID 12488449.

gpnotebook.co.uk

GPnotebook > reference range (AST) Retrieved on Dec 7, 2009 Archivované 7 január 2017 na Wayback Machine

nih.gov

ncbi.nlm.nih.gov

The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Protein Eng., March 1994, s. 405–412. DOI: 10.1093/protein/7.3.405. PMID 7909946.
Transaminase activity in human blood.. The Journal of Clinical Investigation, January 1955, s. 126–31. DOI: 10.1172/jci103055. PMID 13221663.
A note on the spectrometric assay of glutamic-oxalaceticñnn transaminase in human blood serum.. The Journal of Clinical Investigation, January 1955, s. 131–3. DOI: 10.1172/JCI103055. PMID 13221664.
Serum glutamic oxaloacetic transaminase activity in human acute transmural myocardial infarction.. Science, 24 September 1954, s. 497–9. DOI: 10.1126/science.120.3117.497. PMID 13195683.
GIANNINI, E. G.. Liver enzyme alteration: a guide for clinicians. Canadian Medical Association Journal, 2005-02-01, s. 367–379. ISSN 0820-3946. DOI: 10.1503/cmaj.1040752. PMID 15684121.
Kirsch JF; Eichele G; Ford G. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol, 1984, s. 497–525. DOI: 10.1016/0022-2836(84)90333-4. PMID 6143829.
Recent topics in pyridoxal 5'-phosphate enzyme studies. Annu Rev Biochem, 1990, s. 87–110. DOI: 10.1146/annurev.bi.59.070190.000511. PMID 2197992.
Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei. Biochem J, 1991, s. 149–54. DOI: 10.1042/bj2780149. PMID 1909112.
An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. J Biochem, 1996, s. 135–44. DOI: 10.1093/oxfordjournals.jbchem.a021198. PMID 8907187.
Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. J Bacteriol, 1977, s. 429–40. DOI: 10.1128/JB.130.1.429-440.1977. PMID 15983.
X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J Mol Biol, 1992, s. 495–517. DOI: 10.1016/0022-2836(92)90935-D. PMID 1593633.
Rhee S; Silva MM; Hyde CC. Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate. J Biol Chem, 1997, s. 17293–302. DOI: 10.1074/jbc.272.28.17293. PMID 9211866.
Kamitori S; Hirotsu K; Higuchi T. Three-dimensional structure of aspartate aminotransferase from Escherichia coli at 2.8 A resolution. J Biochem, 1988, s. 317–8. DOI: 10.1093/oxfordjournals.jbchem.a122464. PMID 3071527.
Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase. Biochemistry, 1991, s. 1980–1985. DOI: 10.1021/bi00221a035. PMID 1993208.
Domain closure in mitochondrial aspartate aminotransferase. J Mol Biol, 1992, s. 197–213. DOI: 10.1016/0022-2836(92)90691-C. PMID 1522585.
Dual substrate recognition of aminotransferases. The Chemical Record, 2005, s. 160–172. DOI: 10.1002/tcr.20042. PMID 15889412.
Mechanism of racemization of amino acids by aspartate aminotransferase. Eur J Biochem, 1992, s. 563–569. DOI: 10.1111/j.1432-1033.1992.tb16584.x. PMID 1735441.
The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis. Biochemistry, 1996, s. 5280–5291. DOI: 10.1021/bi952138d. PMID 8611515.
Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis. J Biol Chem, 2003, s. 9481–9488. DOI: 10.1074/jbc.M209235200. PMID 12488449.
Gaze DC. The role of existing and novel cardiac biomarkers for cardioprotection. Current Opinion in Investigational Drugs, 2007, s. 711–7. PMID 17729182.

rnceus.com

AST/ALT [online]. . Dostupné online.

web.archive.org

GPnotebook > reference range (AST) Retrieved on Dec 7, 2009 Archivované 7 január 2017 na Wayback Machine

worldcat.org

GIANNINI, E. G.. Liver enzyme alteration: a guide for clinicians. Canadian Medical Association Journal, 2005-02-01, s. 367–379. ISSN 0820-3946. DOI: 10.1503/cmaj.1040752. PMID 15684121.