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Artículos de revistas sobre el tema "ALANINE:GLYOXYLATE AMINOTRANSFERASE"

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Publicado: 11 de marzo de 2023

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1

Orzechowski, S., J. Socha-Hanc, and A. Paszkowski. "Alanine aminotransferase and glycine aminotransferase from maize (Zea mays L.) leaves." Acta Biochimica Polonica 46, no. 2 (1999): 447–57. http://dx.doi.org/10.18388/abp.1999_4176.

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Alanine aminotransferase (AlaAT, EC 2.6.1.2) and glycine aminotransferase (GlyAT, EC 2.6.1.4), two different enzymes catalyzing transamination reactions with L-alanine as the amino-acid substrate, were examined in maize in which alanine participates substantially in nitrogen transport. Preparative PAGE of a partially purified preparation of aminotransferases from maize leaves gave 6 fractions differing in electrophoretic mobility. The fastest migrating fraction I represents AlaAT specific for L-alanine as amino donor and 2-oxoglutarate as amino acceptor. The remaining fractions showed three am
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2

Han, Qian, Cihan Yang, Jun Lu, Yinai Zhang, and Jianyong Li. "Metabolism of Oxalate in Humans: A Potential Role Kynurenine Aminotransferase/Glutamine Transaminase/Cysteine Conjugate Betalyase Plays in Hyperoxaluria." Current Medicinal Chemistry 26, no. 26 (2019): 4944–63. http://dx.doi.org/10.2174/0929867326666190325095223.

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Hyperoxaluria, excessive urinary oxalate excretion, is a significant health problem worldwide. Disrupted oxalate metabolism has been implicated in hyperoxaluria and accordingly, an enzymatic disturbance in oxalate biosynthesis can result in the primary hyperoxaluria. Alanine-glyoxylate aminotransferase-1 and glyoxylate reductase, the enzymes involving glyoxylate (precursor for oxalate) metabolism, have been related to primary hyperoxalurias. Some studies suggest that other enzymes such as glycolate oxidase and alanine-glyoxylate aminotransferase-2 might be associated with primary hyperoxaluria
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3

Pey, Angel L., Armando Albert, and Eduardo Salido. "Protein Homeostasis Defects of Alanine-Glyoxylate Aminotransferase: New Therapeutic Strategies in Primary Hyperoxaluria Type I." BioMed Research International 2013 (2013): 1–15. http://dx.doi.org/10.1155/2013/687658.

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Alanine-glyoxylate aminotransferase catalyzes the transamination between L-alanine and glyoxylate to produce pyruvate and glycine using pyridoxal 5′-phosphate (PLP) as cofactor. Human alanine-glyoxylate aminotransferase is a peroxisomal enzyme expressed in the hepatocytes, the main site of glyoxylate detoxification. Its deficit causes primary hyperoxaluria type I, a rare but severe inborn error of metabolism. Single amino acid changes are the main type of mutation causing this disease, and considerable effort has been dedicated to the understanding of the molecular consequences of such missens
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4

Donini, Stefano, Manuela Ferrari, Chiara Fedeli, et al. "Recombinant production of eight human cytosolic aminotransferases and assessment of their potential involvement in glyoxylate metabolism." Biochemical Journal 422, no. 2 (2009): 265–72. http://dx.doi.org/10.1042/bj20090748.

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PH1 (primary hyperoxaluria type 1) is a severe inborn disorder of glyoxylate metabolism caused by a functional deficiency of the peroxisomal enzyme AGXT (alanine-glyoxylate aminotransferase), which converts glyoxylate into glycine using L-alanine as the amino-group donor. Even though pre-genomic studies indicate that other human transaminases can convert glyoxylate into glycine, in PH1 patients these enzymes are apparently unable to compensate for the lack of AGXT, perhaps due to their limited levels of expression, their localization in an inappropriate cell compartment or the scarcity of the
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5

Sakuraba, Haruhiko. "Studies on Avian Peroxisomal Alanine : Glyoxylate Aminotransferase." Journal of the Kyushu Dental Society 45, no. 3 (1991): 390–408. http://dx.doi.org/10.2504/kds.45.390.

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6

Takada, Y., and T. Noguchi. "Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates." Biochemical Journal 231, no. 1 (1985): 157–63. http://dx.doi.org/10.1042/bj2310157.

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Alanine: glyoxylate aminotransferase (EC 2.6.1.44), which is involved in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates in Saccharomyces cerevisiae, was highly purified and characterized. The enzyme had Mr about 80 000, with two identical subunits. It was highly specific for L-alanine and glyoxylate and contained pyridoxal 5′-phosphate as cofactor. The apparent Km values were 2.1 mM and 0.7 mM for L-alanine and glyoxylate respectively. The activity was low (10 nmol/min per mg of protein) with glucose as sole carbon source, but was remarkab
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7

夏, 敬明. "Introduction and Research Progress of Alanine-Glyoxylate Aminotransferase." Open Journal of Nature Science 06, no. 05 (2018): 409–15. http://dx.doi.org/10.12677/ojns.2018.65053.

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8

Rumsby, G., T. Weir, and C. T. Samuell. "A Semiautomated Alanine: Glyoxylate Aminotransferase Assay for the Tissue Diagnosis of Primary Hyperoxaluria Type 1." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 34, no. 4 (1997): 400–404. http://dx.doi.org/10.1177/000456329703400411.

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We have developed a sensitive assay for the measurement of alanine:glyoxylate aminotransferase (EC 2.6.1.44) activity in human liver. The assay is partly automated, and takes into consideration the sensitivity of the reaction to pH and to glyoxylate concentration. It is less subject to interference from other enzymes utilizing glyoxylate and to chemical interference from glyoxylate itself and can therefore be used without correction for cross-over by glutamate:glyoxylate aminotransferase (EC 2.6.1.4). The assay allows clear discrimination between normal and affected livers and is sufficiently
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9

COOPER, Arthur J. L., Boris F. KRASNIKOV, Etsuo OKUNO та Thomas M. JEITNER. "l-Alanine–glyoxylate aminotransferase II of rat kidney and liver mitochondria possesses cysteine S-conjugate β-lyase activity: a contributing factor to the nephrotoxicity/hepatotoxicity of halogenated alkenes?" Biochemical Journal 376, № 1 (2003): 169–78. http://dx.doi.org/10.1042/bj20030988.

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Several halogenated alkenes are metabolized in part to cysteine S-conjugates, which are mitochondrial toxicants of kidney and, to a lesser extent, other organs. Toxicity is due to cysteine S-conjugate β-lyases, which convert the cysteine S-conjugate into pyruvate, ammonia and a reactive sulphur-containing fragment. A section of the human population is exposed to halogenated alkenes. To understand the health effects of such exposure, it is important to identify cysteine S-conjugate β-lyases that contribute to mitochondrial damage. Mitochondrial aspartate aminotransferase [Cooper, Bruschi, Iriar
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10

Kontani, Yasuhide, Masae Kaneko, Mariko Kikugawa, Shigeko Fujimoto, and Nanaya Tamaki. "Identity of D-3-aminoisobutyrate-pyruvate aminotransferase with alanine-glyoxylate aminotransferase 2." Biochimica et Biophysica Acta (BBA) - General Subjects 1156, no. 2 (1993): 161–66. http://dx.doi.org/10.1016/0304-4165(93)90131-q.

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11

Holbrook, Joanna D., Graeme M. Birdsey, Ziheng Yang, Michael W. Bruford, and Christopher J. Danpure. "Molecular Adaptation of Alanine : Glyoxylate Aminotransferase Targeting in Primates." Molecular Biology and Evolution 17, no. 3 (2000): 387–400. http://dx.doi.org/10.1093/oxfordjournals.molbev.a026318.

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12

Ikeda, Mitsunori, Hiroaki Kanouchi, and Yohsuke Minatogawa. "Characterization of Peroxisomal Targeting Signals on Alanine : Glyoxylate Aminotransferase." Biological & Pharmaceutical Bulletin 31, no. 1 (2008): 131–34. http://dx.doi.org/10.1248/bpb.31.131.

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13

Holmes, R. P., C. H. Hurst, D. G. Assimos, and H. O. Goodman. "Glucagon increases urinary oxalate excretion in the guinea pig." American Journal of Physiology-Endocrinology and Metabolism 269, no. 3 (1995): E568—E574. http://dx.doi.org/10.1152/ajpendo.1995.269.3.e568.

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Factors that influence hepatic oxalate synthesis are poorly defined. Hormones are important regulators of hepatic metabolism and could potentially be involved. The effects of hyperglucagonemia were examined in guinea pigs injected with either saline or pharmacological doses of glucagon for 4 days. Glucagon treatment increased mean urinary oxalate excretion by 77% in male and 34% in female animals. The levels of hepatic peroxisomal enzymes involved in oxalate synthesis declined with glucagon treatment, but experiments with isolated peroxisomes indicated that oxalate synthesis in vitro was unaff
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14

Kah, A., D. Dörnemann, and H. Senger. "Isolation and Purification to Apparent Homogeneity of 4,5-Dioxovalerate Aminotransferase from Scenedesmus obliquus Mutant C-2 A′." Zeitschrift für Naturforschung C 43, no. 7-8 (1988): 563–71. http://dx.doi.org/10.1515/znc-1988-7-813.

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In the present paper the purification of a specific 4,5-dioxovalerate transaminase from pigment mutant C-2 A′ of the unicellular green alga Scenedesmus obliquus to apparent homogeneity is described. The newly isolated enzyme ʟ-glutamate: 4,5-dioxovalerate aminotransferase is not identical with ʟ-alanine: 4,5-dioxovalerate aminotransferase (EC 2.6.1.43) and ʟ-alanine: glyoxylate aminotransferase (EC 2.6.1.44). A procedure for the purification is described and the resulting homogeneous protein is characterized by its Kᴍ-values for oxo-substrates and amino donors, its pyridoxal phosphate requirem
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15

Han, Qian, Seong Ryul Kim, Haizhen Ding, and Jianyong Li. "Evolution of two alanine glyoxylate aminotransferases in mosquito." Biochemical Journal 397, no. 3 (2006): 473–81. http://dx.doi.org/10.1042/bj20060469.

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In the mosquito, transamination of 3-HK (3-hydroxykynurenine) to XA (xanthurenic acid) is catalysed by an AGT (alanine glyoxylate aminotransferase) and is the major branch pathway of tryptophan metabolism. Interestingly, malaria parasites hijack this pathway to use XA as a chemical signal for development in the mosquito. Here, we report that the mosquito has two AGT isoenzymes. One is the previously cloned AeHKT [Aedes aegypti HKT (3-HK transaminase)] [Han, Fang and Li (2002) J. Biol. Chem. 277, 15781–15787], similar to hAGT (human AGT), which primarily catalyses 3-HK to XA in mosquitoes, and
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16

Rumsby, G., R. Jones, C. J. Danpure, and C. T. Samuell. "Taql polymorphism at the alanine: glyoxylate aminotransferase (AGXT) gene locus." Human Molecular Genetics 1, no. 5 (1992): 350. http://dx.doi.org/10.1093/hmg/1.5.350-a.

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17

Okuno, Etsuo, Takaya Ishikawa, Jun Kawai, and Ryo Kido. "Alanine: Glyoxylate aminotransferase activities in liver of Suncus murinus (insectivora)." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 90, no. 4 (1988): 773–78. http://dx.doi.org/10.1016/0305-0491(88)90333-1.

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18

Allsop, Jennifer, Patricia R. Jennings, and Christopher J. Danpure. "A new micro-assay for human liver alanine : Glyoxylate aminotransferase." Clinica Chimica Acta 170, no. 2-3 (1987): 187–93. http://dx.doi.org/10.1016/0009-8981(87)90127-6.

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19

Schlösser, Thomas, Cornelia Gätgens, Ulrike Weber, and K. Peter Stahmann. "Alanine : glyoxylate aminotransferase ofSaccharomyces cerevisiae–encoding geneAGX1 and metabolic significance." Yeast 21, no. 1 (2004): 63–73. http://dx.doi.org/10.1002/yea.1058.

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20

Kobayashi, Shigeru, Sueko Hayashi, Satoko Fujiwara, and Tomoo Noguchi. "Identity of alanine: glyoxylate aminotransferase with alanine: 2-oxoglutarate aminotrasferase in rat liver cytosol." Biochimie 71, no. 4 (1989): 471–75. http://dx.doi.org/10.1016/0300-9084(89)90177-6.

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21

Han, Qian, and Jianyong Li. "Comparative characterization ofAedes3-hydroxykynurenine transaminase/alanine glyoxylate transaminase andDrosophilaserine pyruvate aminotransferase." FEBS Letters 527, no. 1-3 (2002): 199–204. http://dx.doi.org/10.1016/s0014-5793(02)03229-5.

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22

Satriano, Letizia, Monika Lewinska, Colm O. Rourke, et al. "THU-491-The role of alanine glyoxylate aminotransferase in hepatocellular carcinoma." Journal of Hepatology 70, no. 1 (2019): e377. http://dx.doi.org/10.1016/s0618-8278(19)30738-8.

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23

Wang, Bing-Jun, Jing-Ming Xia, Qian Wang, Jiang-Long Yu, Zhiyin Song, and Huabin Zhao. "Diet and Adaptive Evolution of Alanine-Glyoxylate Aminotransferase Mitochondrial Targeting in Birds." Molecular Biology and Evolution 37, no. 3 (2019): 786–98. http://dx.doi.org/10.1093/molbev/msz266.

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Abstract Adaptations to different diets represent a hallmark of animal diversity. The diets of birds are highly variable, making them an excellent model system for studying adaptive evolution driven by dietary changes. To test whether molecular adaptations to diet have occurred during the evolution of birds, we examined a dietary enzyme alanine-glyoxylate aminotransferase (AGT), which tends to target mitochondria in carnivorous mammals, peroxisomes in herbivorous mammals, and both mitochondria and peroxisomes in omnivorous mammals. A total of 31 bird species were examined in this study, which
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24

Lage, Melissa D., Adrianne M. C. Pittman, Alessandro Roncador, Barbara Cellini, and Chandra L. Tucker. "Allele-specific Characterization of Alanine: Glyoxylate Aminotransferase Variants Associated with Primary Hyperoxaluria." PLoS ONE 9, no. 4 (2014): e94338. http://dx.doi.org/10.1371/journal.pone.0094338.

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25

Hayashi, Sueko, Haruhiko Sakuraba, and Tomoo Noguchi. "Response of hepatic alanine: Glyoxylate aminotransferase 1 to hormone differs among mammalia." Biochemical and Biophysical Research Communications 165, no. 1 (1989): 372–76. http://dx.doi.org/10.1016/0006-291x(89)91080-2.

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26

Zhao, Chaohui Lisa, Yiang Hui, Li Juan Wang, et al. "Alanine-glyoxylate aminotransferase 1 (AGXT1) is a novel marker for hepatocellular carcinomas." Human Pathology 80 (October 2018): 76–81. http://dx.doi.org/10.1016/j.humpath.2018.05.025.

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27

Kukreja, Anjli, Melissa Lasaro, Christian Cobaugh, et al. "Systemic Alanine Glyoxylate Aminotransferase mRNA Improves Glyoxylate Metabolism in a Mouse Model of Primary Hyperoxaluria Type 1." Nucleic Acid Therapeutics 29, no. 2 (2019): 104–13. http://dx.doi.org/10.1089/nat.2018.0740.

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28

Ishikawa, K., E. aneko, and A. Ichiyama. "Pyridoxal 5'-Phosphate Binding of a Recombinant Rat Serine: Pyruvate/Alanine: Glyoxylate Aminotransferase." Journal of Biochemistry 119, no. 5 (1996): 970–78. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021337.

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29

Liu, Yang, Huihui Xu, Xinpu Yuan, Stephen J. Rossiter, and Shuyi Zhang. "Multiple Adaptive Losses of Alanine-Glyoxylate Aminotransferase Mitochondrial Targeting in Fruit-Eating Bats." Molecular Biology and Evolution 29, no. 6 (2012): 1507–11. http://dx.doi.org/10.1093/molbev/mss013.

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30

Caplin, Ben, Zhen Wang, Anna Slaviero, et al. "Alanine-Glyoxylate Aminotransferase-2 Metabolizes Endogenous Methylarginines, Regulates NO, and Controls Blood Pressure." Arteriosclerosis, Thrombosis, and Vascular Biology 32, no. 12 (2012): 2892–900. http://dx.doi.org/10.1161/atvbaha.112.254078.

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31

NISHIJIMA, SAORI, KIMIO SUGAYA, MAKOTO MOROZUMI, TADASHI HATANO, and YOSHIHIDE OGAWA. "Hepatic Alanine-glyoxylate Aminotransferase Activity and Oxalate Metabolism in Vitamin B6 Deficient Rats." Journal of Urology 169, no. 2 (2003): 683–86. http://dx.doi.org/10.1016/s0022-5347(05)63992-4.

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32

Craigen, W. J. "Persistent glycolic aciduria in a healthy child with normal alanine-glyoxylate aminotransferase activity." Journal of Inherited Metabolic Disease 19, no. 6 (1996): 793–94. http://dx.doi.org/10.1007/bf01799176.

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33

Danpure, C. J. "Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine: glyoxylate aminotransferase." Biochimie 75, no. 3-4 (1993): 309–15. http://dx.doi.org/10.1016/0300-9084(93)90091-6.

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34

Nakatani, Toshihide, Yukihiko Kawasaki, Yohsuke Minatogawa, Etsuo Okuno, and Ryo Kido. "Peroxisome localized human hepatic alanine-glyoxylate aminotransferase and its application to clinical diagnosis." Clinical Biochemistry 18, no. 5 (1985): 311–16. http://dx.doi.org/10.1016/s0009-9120(85)80039-4.

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35

Oda, Toshiaki, Takuji Mizuno, Kouichi Ito, Tsuneyoshi Funai, Arata Ichiyama, and Satoshi Miura. "Peroxisomal and Mitochondrial Targeting of Serine : Pyruvate/Alanine: Glyoxylate Aminotransferase in Rat Liver." Cell Biochemistry and Biophysics 32, no. 1-3 (2000): 277–81. http://dx.doi.org/10.1385/cbb:32:1-3:277.

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36

Oatey, Paru B., Michael J. Lumb, and Christopher J. Danpure. "Molecular Basis of the Variable Mitochondrial and Peroxisomal Localisation of Alanine-Glyoxylate Aminotransferase." European Journal of Biochemistry 241, no. 2 (1996): 374–85. http://dx.doi.org/10.1111/j.1432-1033.1996.00374.x.

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37

Danpure, C. J., and P. R. Jennings. "Enzymatic heterogeneity in primary hyperoxaluria type 1 (hepatic peroxisomal alanine: Glyoxylate aminotransferase deficiency)." Journal of Inherited Metabolic Disease 11, S2 (1988): 205–7. http://dx.doi.org/10.1007/bf01804236.

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38

Hameed, Mohammed, Kashif Eqbal, Beena Nair, Alexander Woywodt, and Aimun Ahmed. "Late Diagnosis of Primary Hyperoxaluria by Crystals in the Bone Marrow!" Nephrology @ Point of Care 1, no. 1 (2015): napoc.2015.1467. http://dx.doi.org/10.5301/napoc.2015.14679.

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Primary hyperoxaluria type 1 (PH1) is a rare, inherited, autosomal recessive, metabolic disorder caused by a deficiency of peroxisomal alanine-glyoxylate aminotransferase (AGT). We describe here a case of a 57-year-old man with End Stage Renal Disease, where the late age of presentation of PH T1 due to marked heterogeneity of disease expression caused a delay in diagnosis, and we discuss the causes of the poor outcome typical of this condition
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39

Horváth, V. Andy P., and Ronald J. A. Wanders. "Re-Evaluation of Conditions Required for Measurement of True Alanine:Glyoxylate Aminotransferase Activity in Human Liver: Implications for the Diagnosis of Hyperoxaluria Type I." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 31, no. 4 (1994): 361–66. http://dx.doi.org/10.1177/000456329403100410.

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In this paper we studied the glyoxylate-dependent transamination of L-alanine and L-glutamate in human liver homogenates in order to develop a reliable method for the determination of true alanine:glyoxylate aminotransferase activity in liver homogenates from patients suspected to suffer from hyperoxaluria type I. Measurements were made according to two protocols described in literature in control human liver homogenates which were either untreated or treated with an antiserum raised against purified alanine:glyoxylate aminotransferase. The results obtained show that enzyme activity can best b
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40

Li, Yueyan, Rui Zheng, Guofeng Xu, et al. "Generation and characterization of a novel rat model of primary hyperoxaluria type 1 with a nonsense mutation in alanine-glyoxylate aminotransferase gene." American Journal of Physiology-Renal Physiology 320, no. 3 (2021): F475—F484. http://dx.doi.org/10.1152/ajprenal.00514.2020.

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Primary hyperoxaluria type 1 is a severe inherited disorder that results in recurrent urolithiasis and renal failure. We generated an alanine-glyoxylate aminotransferase ( Agxt) Q84X nonsense mutant rat model that displayed an early onset of hyperoxaluria, spontaneous renal CaOx precipitation, bladder stone, and kidney injuries. Our results suggest an interaction of renal CaOx crystals with the activation of inflammation-, fibrosis-, and necroptosis-related pathways. In all, the AgxtQ84X rat strain has broad applicability in mechanistic studies and the development of innovative therapeutics.
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41

Chen, Wen-Chi, Hsin-Ping Liu, Hsi-Chin Wu, et al. "Preliminary Study of Ethylene Glycol-Induced Alanine-Glyoxylate Aminotransferase 2 Expression in Rat Kidney." Current Urology 3, no. 3 (2009): 129–35. http://dx.doi.org/10.1159/000253370.

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42

Lhotta, K., G. Rumsby, W. Vogel, H. Pernthaler, H. Feichtinger, and P. Konig. "Primary hyperoxaluria type 1 caused by peroxisome-to-mitochondrion mistargeting of alanine : glyoxylate aminotransferase." Nephrology Dialysis Transplantation 11, no. 11 (1996): 2296–98. http://dx.doi.org/10.1093/oxfordjournals.ndt.a027152.

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43

Lee, In Sook Matsui, Morimitu Nishikimi, Masaya Inoue, Yasuteru Muragaki, and Akira Ooshima. "Specific Expression of Alanine-Glyoxylate Aminotransferase 2 in the Epithelial Cells of Henle’s Loop." Nephron 83, no. 2 (1999): 184–85. http://dx.doi.org/10.1159/000045507.

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44

Albert, Armando, Cristina Yunta, Rocío Arranz, et al. "Structure of GroEL in Complex with an Early Folding Intermediate of Alanine Glyoxylate Aminotransferase." Journal of Biological Chemistry 285, no. 9 (2010): 6371–76. http://dx.doi.org/10.1074/jbc.m109.062471.

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45

LUMB, Michael J., P. Edward PURDUE, and Christopher J. DANPURE. "Molecular evolution of alanine/glyoxylate aminotransferase 1 intracellular targeting. Analysis of the feline gene." European Journal of Biochemistry 221, no. 1 (1994): 53–62. http://dx.doi.org/10.1111/j.1432-1033.1994.tb18714.x.

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46

Danpure, C. J., P. R. Jennings, and R. W. E. Watts. "Primary Hyperoxaluria Type 1 and Hepatic Alanine: Glyoxylate Aminotransferase, a Study of Five Cases." Clinical Science 72, s16 (1987): 23P. http://dx.doi.org/10.1042/cs072023pa.

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47

Danpure, Christopher J. "Variable peroxisomal and mitochondrial targeting of alanine: Glyoxylate aminotransferase in mammalian evolution and disease." BioEssays 19, no. 4 (1997): 317–26. http://dx.doi.org/10.1002/bies.950190409.

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48

Danpure, Christopher J., Patricia R. Jennings, Richard J. Penketh, Pauline J. Wise, Penelope J. Cooper, and Charles H. Rodeck. "Fetal liver alanine: Glyoxylate aminotransferase and the prenatal diagnosis of primary hyperoxaluria type 1." Prenatal Diagnosis 9, no. 4 (1989): 271–81. http://dx.doi.org/10.1002/pd.1970090406.

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49

Chung, Eunsook, Kyoung Mi Kim, Jee Eun Heo, Chang-Woo Cho, Seon-Woo Lee, and Jai-Heon Lee. "Molecular characterization of mungbean peroxisomal alanine glyoxylate aminotransferase gene induced by low temperature stress." Genes & Genomics 31, no. 1 (2009): 11–18. http://dx.doi.org/10.1007/bf03191133.

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Naidu, S., A. B. Moser, C. J. Danpure, L. Civitello, and H. W. Moser. "New defect in peroxisome biogenesis with leukodystrophy, oxaluria, and normal hepatic alanine: Glyoxylate aminotransferase." Pediatric Neurology 11, no. 2 (1994): 144. http://dx.doi.org/10.1016/0887-8994(94)90375-1.

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