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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1946 2
1947 1
1950 1
1953 1
1954 2
1955 1
1956 7
1957 6
1958 17
1959 16
1960 11
1961 20
1962 107
1963 384
1964 505
1965 384
1966 427
1967 493
1968 543
1969 613
1970 601
1971 756
1972 743
1973 800
1974 822
1975 692
1976 531
1977 523
1978 448
1979 503
1980 459
1981 420
1982 472
1983 410
1984 513
1985 530
1986 474
1987 424
1988 443
1989 475
1990 568
1991 518
1992 521
1993 515
1994 551
1995 517
1996 505
1997 552
1998 581
1999 547
2000 578
2001 562
2002 630
2003 709
2004 684
2005 871
2006 955
2007 1142
2008 1193
2009 1215
2010 1277
2011 1466
2012 1587
2013 1772
2014 1860
2015 1883
2016 1918
2017 1962
2018 2020
2019 2080
2020 1668
2021 3
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44,829 results
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[Aspartate aminotransferase--key enzyme in the human systemic metabolism].
Otto-Ślusarczyk D, Graboń W, Mielczarek-Puta M. Otto-Ślusarczyk D, et al. Postepy Hig Med Dosw (Online). 2016 Mar 16;70:219-30. doi: 10.5604/17322693.1197373. Postepy Hig Med Dosw (Online). 2016. PMID: 27117097 Free article. Review. Polish.
Aspartate aminotransferase is an organ-nonspecific enzyme located in many tissues of the human body where it catalyzes reversible reaction of transamination. There are two aspartate aminotransferase isoforms--cytoplasmic (AST1) and mitochondrial (AST2)
Aspartate aminotransferase is an organ-nonspecific enzyme located in many tissues of the human body where it catalyzes reversi
Metabolic effects of an aspartate aminotransferase-inhibitor on two T-cell lines.
Antti H, Sellstedt M. Antti H, et al. PLoS One. 2018 Dec 7;13(12):e0208025. doi: 10.1371/journal.pone.0208025. eCollection 2018. PLoS One. 2018. PMID: 30532126 Free PMC article.
Here two T-cell lines were treated with an inhibitor of aspartate aminotransferase and analyzed with untargeted GC-MS. The interpretation of the data was enhanced by the use of two different cell-lines and supports aspartate aminotransferase as a targe …
Here two T-cell lines were treated with an inhibitor of aspartate aminotransferase and analyzed with untargeted GC-MS. The int …
Isolated elevation of aspartate aminotransferase (AST) in an asymptomatic patient due to macro-AST.
González Raya A, Coca Zúñiga R, Martín Salido E. González Raya A, et al. J Clin Lab Anal. 2019 Feb;33(2):e22690. doi: 10.1002/jcla.22690. Epub 2018 Oct 15. J Clin Lab Anal. 2019. PMID: 30320474 Free PMC article.
BACKGROUND: A rare and benign cause of isolated aspartate aminotransferase (AST) increase is due to the presence of macro aspartate aminotransferase (macro-AST). ...
BACKGROUND: A rare and benign cause of isolated aspartate aminotransferase (AST) increase is due to the presence of macro a
Crystal structure of L-aspartate aminotransferase from Schizosaccharomyces pombe.
Jeong SY, Jin H, Chang JH. Jeong SY, et al. PLoS One. 2019 Aug 29;14(8):e0221975. doi: 10.1371/journal.pone.0221975. eCollection 2019. PLoS One. 2019. PMID: 31465495 Free PMC article.
L-aspartate aminotransferase is a pyridoxal 5'-phosphate-dependent transaminase that catalyzes reversible transfer of an α-amino group from aspartate to α-ketoglutarate or from glutamate to oxaloacetate. ...A structural comparison between two yeast L-aspar
L-aspartate aminotransferase is a pyridoxal 5'-phosphate-dependent transaminase that catalyzes reversible transfer of an α-ami …
Aspartate aminotransferase: an old dog teaches new tricks.
Toney MD. Toney MD. Arch Biochem Biophys. 2014 Feb 15;544:119-27. doi: 10.1016/j.abb.2013.10.002. Epub 2013 Oct 9. Arch Biochem Biophys. 2014. PMID: 24121043 Free PMC article. Review.
Aspartate aminotransferase (AAT) is a prototypical pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes the reversible interconversion of l-aspartate and α-ketoglutarate with oxalacetate and l-glutamate via a ping-pong catalytic cycle in which the pyr
Aspartate aminotransferase (AAT) is a prototypical pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes the reversible
Aspartate aminotransferase isoenzymes.
Panteghini M. Panteghini M. Clin Biochem. 1990 Aug;23(4):311-9. doi: 10.1016/0009-9120(90)80062-n. Clin Biochem. 1990. PMID: 2225456 Review.
Aspartate aminotransferase (AST, EC 2.6.1.1) exists in human tissues as two distinct isoenzymes, one located in the cytoplasm (c-AST), and the other in mitochondria (m-AST). ...
Aspartate aminotransferase (AST, EC 2.6.1.1) exists in human tissues as two distinct isoenzymes, one located in the cytoplasm
Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase.
Marković-Housley Z, Schirmer T, Hohenester E, Khomutov AR, Khomutov RM, Karpeisky MY, Sandmeier E, Christen P, Jansonius JN. Marković-Housley Z, et al. Eur J Biochem. 1996 Mar 15;236(3):1025-32. doi: 10.1111/j.1432-1033.1996.01025.x. Eur J Biochem. 1996. PMID: 8665890 Free article.
The crystal structures of the adducts of mitochondrial aspartate aminotransferase with the monocarboxylic analogue of L-aspartate in the open and closed enzyme conformation were determined at 0.23-nm and 0.25-nm resolution, respectively. ...This is probably d …
The crystal structures of the adducts of mitochondrial aspartate aminotransferase with the monocarboxylic analogue of L-asp
Aspartate aminotransferase isozymes and their clinical significance.
Wada H, Kamiike W. Wada H, et al. Prog Clin Biol Res. 1990;344:853-75. Prog Clin Biol Res. 1990. PMID: 2203064 Review. No abstract available.
[Isolated aspartate aminotransferase elevation in a young, healthy person. Case report].
Kovács F, Varga M, Szabó S, Bertók K. Kovács F, et al. Orv Hetil. 2014 Sep 28;155(39):1558-62. doi: 10.1556/OH.2014.29997. Orv Hetil. 2014. PMID: 25240878 Hungarian.
The authors present diagnostic methods used in a young healthy person who had isolated aspartate aminotransferase elevation. Polyethylene glycol precipitation test, aspartate aminotransferase serum electrophoresis and immunofixation were performed for …
The authors present diagnostic methods used in a young healthy person who had isolated aspartate aminotransferase elevation. P …
Aspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase.
Lowe PN, Rowe AF. Lowe PN, et al. Biochem J. 1985 Dec 15;232(3):689-95. doi: 10.1042/bj2320689. Biochem J. 1985. PMID: 3879173 Free PMC article.
Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. ...Such high rates of aromatic amino acid aminotransferase activity have not been reported before in eukaryotic asp
Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and
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