Aspartate transaminase (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Aspartate transaminase" in English language version.

refsWebsite

Global rank English rank

24nih.gov

4^th place

18doi.org

2^nd place

1harvard.edu

18^th place

17^th place

1rnceus.com

low place

1gpnotebook.co.uk

low place

1web.archive.org

1^st place

doi.org

Karmen A, Wroblewski F, Ladue JS (January 1955). "Transaminase activity in human blood". The Journal of Clinical Investigation. 34 (1): 126–131. doi:10.1172/jci103055. PMC 438594. PMID 13221663.
Karmen A (January 1955). "A note on the spectrometric assay of glutamic-oxalacetic transaminase in human blood serum". The Journal of Clinical Investigation. 34 (1): 131–133. doi:10.1172/JCI103055. PMC 438594. PMID 13221664.
Ladue JS, Wroblewski F, Karmen A (September 1954). "Serum glutamic oxaloacetic transaminase activity in human acute transmural myocardial infarction". Science. 120 (3117): 497–499. Bibcode:1954Sci...120..497L. doi:10.1126/science.120.3117.497. PMID 13195683.
Giannini EG, Testa R, Savarino V (February 2005). "Liver enzyme alteration: a guide for clinicians". CMAJ. 172 (3): 367–379. doi:10.1503/cmaj.1040752. PMC 545762. PMID 15684121. Aminotransferase clearance is carried out within the liver by sinusoidal cells. The half-life in the circulation is about 47 hours for ALT, about 17 hours for total AST and, on average, 87 hours for mitochondrial AST.
Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P (April 1984). "Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure". Journal of Molecular Biology. 174 (3): 497–525. doi:10.1016/0022-2836(84)90333-4. PMID 6143829.
Hayashi H, Wada H, Yoshimura T, Esaki N, Soda K (1990). "Recent topics in pyridoxal 5'-phosphate enzyme studies". Annual Review of Biochemistry. 59: 87–110. doi:10.1146/annurev.bi.59.070190.000511. PMID 2197992.
Muriana FJ, Alvarez-Ossorio MC, Relimpio AM (August 1991). "Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei". The Biochemical Journal. 278 (1): 149–154. doi:10.1042/bj2780149. PMC 1151461. PMID 1909112.
Okamoto A, Kato R, Masui R, Yamagishi A, Oshima T, Kuramitsu S (January 1996). "An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8". Journal of Biochemistry. 119 (1): 135–144. doi:10.1093/oxfordjournals.jbchem.a021198. PMID 8907187.
Gelfand DH, Steinberg RA (April 1977). "Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases". Journal of Bacteriology. 130 (1): 429–440. doi:10.1128/JB.130.1.429-440.1977. PMC 235221. PMID 15983.
McPhalen CA, Vincent MG, Jansonius JN (May 1992). "X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase". Journal of Molecular Biology. 225 (2): 495–517. doi:10.1016/0022-2836(92)90935-D. PMID 1593633.
Rhee S, Silva MM, Hyde CC, Rogers PH, Metzler CM, Metzler DE, Arnone A (July 1997). "Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate". The Journal of Biological Chemistry. 272 (28): 17293–17302. doi:10.1074/jbc.272.28.17293. PMID 9211866.
Kamitori S, Hirotsu K, Higuchi T, Kondo K, Inoue K, Kuramitsu S, et al. (September 1988). "Three-dimensional structure of aspartate aminotransferase from Escherichia coli at 2.8 A resolution". Journal of Biochemistry. 104 (3): 317–318. doi:10.1093/oxfordjournals.jbchem.a122464. PMID 3071527.
Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D (February 1991). "Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase". Biochemistry. 30 (7): 1980–1985. doi:10.1021/bi00221a035. PMID 1993208.
McPhalen CA, Vincent MG, Picot D, Jansonius JN, Lesk AM, Chothia C (September 1992). "Domain closure in mitochondrial aspartate aminotransferase". Journal of Molecular Biology. 227 (1): 197–213. doi:10.1016/0022-2836(92)90691-C. PMID 1522585.
Hirotsu K, Goto M, Okamoto A, Miyahara I (2005). "Dual substrate recognition of aminotransferases". Chemical Record. 5 (3): 160–172. doi:10.1002/tcr.20042. PMID 15889412.
Kochhar S, Christen P (February 1992). "Mechanism of racemization of amino acids by aspartate aminotransferase". European Journal of Biochemistry. 203 (3): 563–569. doi:10.1111/j.1432-1033.1992.tb16584.x. PMID 1735441.
Goldberg JM, Kirsch JF (April 1996). "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. 35 (16): 5280–5291. doi:10.1021/bi952138d. PMID 8611515.
Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H (March 2003). "Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis". The Journal of Biological Chemistry. 278 (11): 9481–9488. doi:10.1074/jbc.M209235200. PMID 12488449.

gpnotebook.co.uk

GPnotebook > reference range (AST) Retrieved on Dec 7, 2009 Archived 7 January 2017 at the Wayback Machine

harvard.edu

ui.adsabs.harvard.edu

Ladue JS, Wroblewski F, Karmen A (September 1954). "Serum glutamic oxaloacetic transaminase activity in human acute transmural myocardial infarction". Science. 120 (3117): 497–499. Bibcode:1954Sci...120..497L. doi:10.1126/science.120.3117.497. PMID 13195683.

nih.gov

pubmed.ncbi.nlm.nih.gov

Karmen A, Wroblewski F, Ladue JS (January 1955). "Transaminase activity in human blood". The Journal of Clinical Investigation. 34 (1): 126–131. doi:10.1172/jci103055. PMC 438594. PMID 13221663.
Karmen A (January 1955). "A note on the spectrometric assay of glutamic-oxalacetic transaminase in human blood serum". The Journal of Clinical Investigation. 34 (1): 131–133. doi:10.1172/JCI103055. PMC 438594. PMID 13221664.
Ladue JS, Wroblewski F, Karmen A (September 1954). "Serum glutamic oxaloacetic transaminase activity in human acute transmural myocardial infarction". Science. 120 (3117): 497–499. Bibcode:1954Sci...120..497L. doi:10.1126/science.120.3117.497. PMID 13195683.
Giannini EG, Testa R, Savarino V (February 2005). "Liver enzyme alteration: a guide for clinicians". CMAJ. 172 (3): 367–379. doi:10.1503/cmaj.1040752. PMC 545762. PMID 15684121. Aminotransferase clearance is carried out within the liver by sinusoidal cells. The half-life in the circulation is about 47 hours for ALT, about 17 hours for total AST and, on average, 87 hours for mitochondrial AST.
Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P (April 1984). "Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure". Journal of Molecular Biology. 174 (3): 497–525. doi:10.1016/0022-2836(84)90333-4. PMID 6143829.
Hayashi H, Wada H, Yoshimura T, Esaki N, Soda K (1990). "Recent topics in pyridoxal 5'-phosphate enzyme studies". Annual Review of Biochemistry. 59: 87–110. doi:10.1146/annurev.bi.59.070190.000511. PMID 2197992.
Muriana FJ, Alvarez-Ossorio MC, Relimpio AM (August 1991). "Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei". The Biochemical Journal. 278 (1): 149–154. doi:10.1042/bj2780149. PMC 1151461. PMID 1909112.
Okamoto A, Kato R, Masui R, Yamagishi A, Oshima T, Kuramitsu S (January 1996). "An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8". Journal of Biochemistry. 119 (1): 135–144. doi:10.1093/oxfordjournals.jbchem.a021198. PMID 8907187.
Gelfand DH, Steinberg RA (April 1977). "Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases". Journal of Bacteriology. 130 (1): 429–440. doi:10.1128/JB.130.1.429-440.1977. PMC 235221. PMID 15983.
McPhalen CA, Vincent MG, Jansonius JN (May 1992). "X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase". Journal of Molecular Biology. 225 (2): 495–517. doi:10.1016/0022-2836(92)90935-D. PMID 1593633.
Rhee S, Silva MM, Hyde CC, Rogers PH, Metzler CM, Metzler DE, Arnone A (July 1997). "Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate". The Journal of Biological Chemistry. 272 (28): 17293–17302. doi:10.1074/jbc.272.28.17293. PMID 9211866.
Kamitori S, Hirotsu K, Higuchi T, Kondo K, Inoue K, Kuramitsu S, et al. (September 1988). "Three-dimensional structure of aspartate aminotransferase from Escherichia coli at 2.8 A resolution". Journal of Biochemistry. 104 (3): 317–318. doi:10.1093/oxfordjournals.jbchem.a122464. PMID 3071527.
Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D (February 1991). "Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase". Biochemistry. 30 (7): 1980–1985. doi:10.1021/bi00221a035. PMID 1993208.
McPhalen CA, Vincent MG, Picot D, Jansonius JN, Lesk AM, Chothia C (September 1992). "Domain closure in mitochondrial aspartate aminotransferase". Journal of Molecular Biology. 227 (1): 197–213. doi:10.1016/0022-2836(92)90691-C. PMID 1522585.
Hirotsu K, Goto M, Okamoto A, Miyahara I (2005). "Dual substrate recognition of aminotransferases". Chemical Record. 5 (3): 160–172. doi:10.1002/tcr.20042. PMID 15889412.
Kochhar S, Christen P (February 1992). "Mechanism of racemization of amino acids by aspartate aminotransferase". European Journal of Biochemistry. 203 (3): 563–569. doi:10.1111/j.1432-1033.1992.tb16584.x. PMID 1735441.
Goldberg JM, Kirsch JF (April 1996). "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. 35 (16): 5280–5291. doi:10.1021/bi952138d. PMID 8611515.
Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H (March 2003). "Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis". The Journal of Biological Chemistry. 278 (11): 9481–9488. doi:10.1074/jbc.M209235200. PMID 12488449.
Gaze DC (September 2007). "The role of existing and novel cardiac biomarkers for cardioprotection". Current Opinion in Investigational Drugs. 8 (9): 711–717. PMID 17729182.

ncbi.nlm.nih.gov

Karmen A, Wroblewski F, Ladue JS (January 1955). "Transaminase activity in human blood". The Journal of Clinical Investigation. 34 (1): 126–131. doi:10.1172/jci103055. PMC 438594. PMID 13221663.
Karmen A (January 1955). "A note on the spectrometric assay of glutamic-oxalacetic transaminase in human blood serum". The Journal of Clinical Investigation. 34 (1): 131–133. doi:10.1172/JCI103055. PMC 438594. PMID 13221664.
Giannini EG, Testa R, Savarino V (February 2005). "Liver enzyme alteration: a guide for clinicians". CMAJ. 172 (3): 367–379. doi:10.1503/cmaj.1040752. PMC 545762. PMID 15684121. Aminotransferase clearance is carried out within the liver by sinusoidal cells. The half-life in the circulation is about 47 hours for ALT, about 17 hours for total AST and, on average, 87 hours for mitochondrial AST.
Muriana FJ, Alvarez-Ossorio MC, Relimpio AM (August 1991). "Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei". The Biochemical Journal. 278 (1): 149–154. doi:10.1042/bj2780149. PMC 1151461. PMID 1909112.
Gelfand DH, Steinberg RA (April 1977). "Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases". Journal of Bacteriology. 130 (1): 429–440. doi:10.1128/JB.130.1.429-440.1977. PMC 235221. PMID 15983.

rnceus.com

"AST/ALT". www.rnceus.com.

web.archive.org

GPnotebook > reference range (AST) Retrieved on Dec 7, 2009 Archived 7 January 2017 at the Wayback Machine