Relevant bibliographies by topics / Aldose reductase

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Aldose reductase'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 July 2025

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Journal articles on the topic "Aldose reductase"

1

Sato, S. "Rat kidney aldose reductase and aldehyde reductase and polyol production in rat kidney." American Journal of Physiology-Renal Physiology 263, no. 5 (1992): F799—F805. http://dx.doi.org/10.1152/ajprenal.1992.263.5.f799.

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Mounting evidence indicates that aldose reductase catalyzed reduction of excess glucose to sorbitol initiates the onset of certain diabetic complications. However, the kidney contains a large amount of aldehyde reductase, another NADPH-dependent reductase. The study was designed to assess the importance of these reductases to sugar alcohol (polyol) production in the kidney. To study the ability to reduce aldoses to polyols, both aldose and aldehyde reductases were purified from rat kidneys. Incubation studies with purified enzymes clearly demonstrated the polyol formation by both enzymes. Gala
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Lee, Jung-Kul, Sang-Yong Kim, Yeon-Woo Ryu, Jin-Ho Seo, and Jung-Hoe Kim. "Purification and Characterization of a Novel Erythrose Reductase from Candida magnoliae." Applied and Environmental Microbiology 69, no. 7 (2003): 3710–18. http://dx.doi.org/10.1128/aem.69.7.3710-3718.2003.

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ABSTRACT Erythritol biosynthesis is catalyzed by erythrose reductase, which converts erythrose to erythritol. Erythrose reductase, however, has never been characterized in terms of amino acid sequence and kinetics. In this study, NAD(P)H-dependent erythrose reductase was purified to homogeneity from Candida magnoliae KFCC 11023 by ion exchange, gel filtration, affinity chromatography, and preparative electrophoresis. The molecular weights of erythrose reductase determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography were 38,800 and 79,000, resp
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Balestri, Francesco, Giulio Poli, Lucia Piazza, et al. "Dissecting the Activity of Catechins as Incomplete Aldose Reductase Differential Inhibitors through Kinetic and Computational Approaches." Biology 11, no. 9 (2022): 1324. http://dx.doi.org/10.3390/biology11091324.

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The inhibition of aldose reductase is considered as a strategy to counteract the onset of both diabetic complications, upon the block of glucose conversion in the polyol pathway, and inflammation, upon the block of 3-glutathionyl-4-hydroxynonenal reduction. To ameliorate the outcome of aldose reductase inhibition, minimizing the interference with the detoxifying role of the enzyme when acting on toxic aldehydes, “differential inhibitors”, i.e., molecules able to inhibit the enzyme depending on the substrate the enzyme is working on, has been proposed. Here we report the characterization of dif
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Pastel, Emilie, Jean-Christophe Pointud, Gaëlle Loubeau та ін. "Aldose Reductases Influence Prostaglandin F2α Levels and Adipocyte Differentiation in Male Mouse and Human Species". Endocrinology 156, № 5 (2015): 1671–84. http://dx.doi.org/10.1210/en.2014-1750.

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Aldose reductases (AKR1B) are widely expressed oxidoreductases whose physiological function remains elusive. Some isoforms are genuine prostaglandin F2α (PGF2α) synthases, suggesting they might influence adipose homeostasis because PGF2α inhibits adipogenesis. This was shown by Akr1b7 gene ablation in the mouse, which resulted in increased adiposity related to a lower PGF2α content in fat. Yet humans have no ortholog gene for Akr1b7, so the role of aldose reductases in human adipose homeostasis remains to be explored. We analyzed expression of genes encoding human and mouse aldose reductase is
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Verduyn, C., R. Van Kleef, J. Frank, H. Schreuder, J. P. Van Dijken, and W. A. Scheffers. "Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis." Biochemical Journal 226, no. 3 (1985): 669–77. http://dx.doi.org/10.1042/bj2260669.

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Xylose reductase from the xylose-fermenting yeast Pichia stipitis was purified to electrophoretic and spectral homogeneity via ion-exchange, affinity and high-performance gel chromatography. The enzyme was active with various aldose substrates, such as DL-glyceraldehyde, L-arabinose, D-xylose, D-ribose, D-galactose and D-glucose. Hence the xylose reductase of Pichia stipitis is an aldose reductase (EC 1.1.1.21). Unlike all aldose reductases characterized so far, the enzyme from this yeast was active with both NADPH and NADH as coenzyme. The activity with NADH was approx. 70% of that with NADPH
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CROSAS, Bernat, David J. HYNDMAN, Oriol GALLEGO, et al. "Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism." Biochemical Journal 373, no. 3 (2003): 973–79. http://dx.doi.org/10.1042/bj20021818.

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Aldo–keto reductases (AKRs) are NAD(P)H-dependent oxidoreductases that catalyse the reduction of a variety of carbonyl compounds, such as carbohydrates, aliphatic and aromatic aldehydes and steroids. We have studied the retinal reductase activity of human aldose reductase (AR), human small-intestine (HSI) AR and pig aldehyde reductase. Human AR and HSI AR were very efficient in the reduction of all-trans-, 9-cis- and 13-cis-retinal (kcat/Km=1100–10300 mM−1·min−1), constituting the first cytosolic NADP(H)-dependent retinal reductases described in humans. Aldehyde reductase showed no activity wi
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Smardo, F. L., M. B. Burg, and A. Garcia-Perez. "Kidney aldose reductase gene transcription is osmotically regulated." American Journal of Physiology-Cell Physiology 262, no. 3 (1992): C776—C782. http://dx.doi.org/10.1152/ajpcell.1992.262.3.c776.

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Cells generally adapt to long-term hypertonic stress by accumulating organic osmolytes. PAP-HT25 renal medullary cells in hypertonic medium accumulate sorbitol through a reaction catalyzed by aldose reductase and betaine through osmotically regulated transport. Hypertonicity increases aldose reductase protein synthesis rate by elevating its mRNA abundance. To test whether the rise in aldose reductase mRNA is due to enhanced transcription, PAP-HT25 cells adapted to isotonic medium were switched to hypertonic medium, and transcription rate was measured by nuclear run-on. Aldose reductase transcr
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Kador, P. F., J. H. Kinoshita, D. R. Brittain, D. J. Mirrlees, C. M. Sennitt, and D. Stribling. "Purified rat lens aldose reductase. Polyol production in vitro and its inhibition by aldose reductase inhibitors." Biochemical Journal 240, no. 1 (1986): 233–37. http://dx.doi.org/10.1042/bj2400233.

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The production of polyols in vitro by highly purified aldose reductase (EC 1.1.1.21) was monitored by g.l.c. In the presence of NADPH aldose reductase reduced glucose, galactose and xylose to the respective polyols sorbitol, galactitol and xylitol. The rates of formation of these polyols closely mirrored the Km values for the substrates obtained from kinetic measurements that monitored the rate of disappearance of NADPH. No polyol production occurred in the absence of purified aldose of purified aldose reductase, and analysis by g.l.c. revealed only the presence of unchanged monosaccharides. A
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Cowley, B. D., J. D. Ferraris, D. Carper, and M. B. Burg. "In vivo osmoregulation of aldose reductase mRNA, protein, and sorbitol in renal medulla." American Journal of Physiology-Renal Physiology 258, no. 1 (1990): F154—F161. http://dx.doi.org/10.1152/ajprenal.1990.258.1.f154.

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Sorbitol accumulates in renal medullary cells by synthesis from glucose in a reaction catalyzed by aldose reductase. Medullary sodium and urea are high and vary with urinary concentration. Sorbitol varies similarly, consistent with its role as a compatible intracellular organic osmolyte. We measured renal medullary sodium, urea, sorbitol, aldose reductase (protein and activity), and aldose reductase mRNA in rats treated to change medullary sodium and urea. In untreated Brattleboro rats all measurements were low and increased after 7 days of treatment with arginine vasopressin. In contrast, whe
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Sands, J. M., and D. C. Schrader. "Acute changes in intracellular ions or pH and regulation of aldose reductase activity." Journal of the American Society of Nephrology 2, no. 2 (1991): 212–18. http://dx.doi.org/10.1681/asn.v22212.

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Sorbitol production in the renal medulla increases in dehydrated rats, indicating that aldose reductase activity varies with the state of hydration. This response could be due to an increased synthesis of the enzyme (Moriyama T et al. J Biol Chem 1989:264:16810-16814) and/or a change in aldose reductase activity caused by acute changes in intracellular ionic composition, ionic strength, osmolality, or pH. Aldose reductase activity in tubules dissected from kidneys of control rats and rats undergoing water diuresis was measured, and the tubules were permeabilized so that changes in intracellula
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Dissertations / Theses on the topic "Aldose reductase"

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柯子斌 and Chi-bun Ko. "Regulation of aldose reductase gene." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1997. http://hub.hku.hk/bib/B3123589X.

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Ko, Chi-bun. "Regulation of aldose reductase gene /." Hong Kong : University of Hong Kong, 1997. http://sunzi.lib.hku.hk/hkuto/record.jsp?B18716404.

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MISURI, LIVIA. "STRATEGIES IN ALDOSE REDUCTASE INHIBITION." Doctoral thesis, Università di Siena, 2018. http://hdl.handle.net/11365/1053534.

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Aldose reductase (AKR1B1) is an enzyme involved in the etiology of secondary diabetic complications and inflammation and it has at the same time a central role in cell detoxification. In this work different approaches were applied in order to find novel inhibitors of AKR1B1 from natural sources. To reach this purpose, two different strategies have been used. The first method is aimed to limit the massive convertion of glucose to sorbitol, typical of hyperglicemic condition, leaving the detoxifying role of the enzyme unaffected (intra-site inhibition of aldose reductase). The role of the
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BARTH, PATRICK. "Aldose reductase et aldehyde reductase : purification et quelques proprietes." Université Louis Pasteur (Strasbourg) (1971-2008), 1989. http://www.theses.fr/1989STR13171.

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L'aldose reductase (e. C. 1. 1. 1. 21) et l'aldehyde reductase (e. C. 1. 1. 1. 2) sont des enzymes ubiquitaires appartenant a la famille des aldo/ceto-reductases. Ces enzymes monomeriques utilisent le nadph comme cofacteur et catalysent la reduction de nombreux aldehydes aliphatiques ou aromatiques. L'aldose reductase se distingue de l'aldehyde reductase par sa capacite a reduire en outre une grande variete d'aldoses. Toutefois, ces deux enzymes presentent des proprietes physicochimiques extremement voisines, et leurs sequences en acides amines sont fortement homologues. Le role physiologique
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曹德良 and De-liang Cao. "Over-expression of aldose reductase and a novel aldose reductase-like gene in human primary liver cancers." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1996. http://hub.hku.hk/bib/B31234616.

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Cao, De-liang. "Over-expression of aldose reductase and a novel aldose reductase-like gene in human primary liver cancers /." Hong Kong : University of Hong Kong, 1996. http://sunzi.lib.hku.hk/hkuto/record.jsp?B17506438.

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何存邦 and Tsun-bond Horace Ho. "Aldose reductase deficient mice develop nephrogenic diabetesinsipidus." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2000. http://hub.hku.hk/bib/B31222663.

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Oder, Daniel O. "Generation of Human Aldose Reductase Mutants of Cys298." Youngstown State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=ysu1443087374.

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Zivkovic, DaVena. "Enzymatic Characterization of Aldose Reductase and Its Inhibitors." Youngstown State University / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=ysu1472069987.

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Ho, Tsun-bond Horace. "Aldose reductase deficient mice develop nephrogenic diabetes insipidus /." Hong Kong : University of Hong Kong, 2000. http://sunzi.lib.hku.hk/hkuto/record.jsp?B21949074.

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Books on the topic "Aldose reductase"

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Smolander, Maria. Electrochemical aldose detection with PQQ-dependent aldose dehydrogenase. Technical Research Centre of Finland, 1995.

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1931-, Sakamoto N., ed. Current concepts of aldose reductase and its inhibitions: Proceedings of the Japan-US Aldose Reductase Workshop, Nagoya, Japan, 16-17 November 1989. Excerpta Medica, 1990.

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Dvornik, Dushan. Aldose reductase inhibition: An approach to the prevention of diabetic complications. McGraw-Hill, 1987.

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International Workshop on the Enzymology and Molecular Biology of the Carbonyl Metabolism. Enzymology and molecular biology of carbonyl metabolism 3. Plennum Press, 1991.

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Henry, Weiner, Flynn T. Geoffrey, and International Workshop on the Enzymology and Molecular Biology of the Carbonyl Metabolism (1988 : Gifu-shi, Japan), eds. Enzymology and molecular biology of carbonyl metabolism 2: Aldehyde dehydrogenase, alcohol dehydrogenase, and aldo-keto reductase : proceedings of the fourth international workshop, held in Gifu, Japan, July 4-8, 1988. Liss, 1989.

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Abdillahi, Mariane Lul. Molecular and Cellular Signaling Mechanisms Elucidating Aldose Reductase Mediated Ischemia-Reperfusion Injury in the Myocardium. [publisher not identified], 2012.

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1931-, Sakamoto N., ed. Polyol pathway and its role in diabetic complications: Proceedings of the International Symposium on Polyol Pathway and Its Role in Diabetic Complications, Kashikojima, Japan, 28-30 October 1986. Excerpta Medica, 1988.

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Dvornik, Dushan. Aldose Reductase Inhibition: An Approach to the Prevention of Diabetic Complications. Biomedical Info Corp, 1987.

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(Editor), N. Sakamoto, J. H. Kinoshita (Editor), P. F. Kador (Editor), and N. Hotta (Editor), eds. Current Concepts of Aldose Reductase and Its Inhibitions (International congress series). Elsevier, 1990.

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Weiner, Henry. Enzymology and Molecular Biology of Carbonyl Metabolism 6. Springer, 2013.

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Book chapters on the topic "Aldose reductase"

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Sato, Sanai, Katsumi Sugiyama, and Deborah Carper. "Aldose Reductase as Dihydrodiol Dehydrogenase." In Advances in Experimental Medicine and Biology. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5871-2_56.

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Schomburg, Dietmar, and Dörte Stephan. "Aldose-6-phosphate reductase (NADPH)." In Enzyme Handbook 10. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-57756-7_48.

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Sarges, Reinhard, and Peter J. Oates. "Aldose reductase inhibitors: Recent developments." In Progress in Drug Research / Fortschritte der Arzneimittelforschung / Progrès des recherches pharmaceutiques. Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7147-1_5.

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Abdillahi, Mariane, and Ravichandran Ramasamy. "Aldose Reductase and Diabetic Cardiovascular Disease." In Diabetic Cardiomyopathy. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9317-4_8.

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Cohen, Margo Panush. "Aldose Reductase and the Vascular System." In The Polyol Paradigm and Complications of Diabetes. Springer New York, 1987. http://dx.doi.org/10.1007/978-1-4612-4670-1_6.

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Bhatnagar, Aruni, Si-Qi Liu, Sanjay Srivastava, Kota V. Ramana, and Satish K. Srivastava. "Aldose Reductase and the Stress Response." In ACS Symposium Series. American Chemical Society, 2003. http://dx.doi.org/10.1021/bk-2003-0865.ch014.

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Cohen, M. P. "General aspects of aldose reductase inhibition." In Pharmacology of Diabetes, edited by C. E. Mogensen and E. Standl. De Gruyter, 1990. http://dx.doi.org/10.1515/9783110850321-014.

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Dowling, Thomas G., John F. O’ Rourke, and Keith F. Tipton. "Sepiapterin Reductase and ALR2 (“Aldose Reductase”) from Bovine Brain." In Advances in Experimental Medicine and Biology. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2904-0_33.

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Fujii, Junichi, Motoko Takahashi, Rieko Hamaoka, Yoshimi Kawasaki, Nobuko Miyazawa, and Naoyuki Taniguchi. "Physiological Relevance of Aldehyde Reductase and Aldose Reductase Gene Expression." In Advances in Experimental Medicine and Biology. Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4735-8_52.

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Cohen, Margo Panush. "Aldose Reductase and Complications of the Eye." In The Polyol Paradigm and Complications of Diabetes. Springer New York, 1987. http://dx.doi.org/10.1007/978-1-4612-4670-1_3.

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Conference papers on the topic "Aldose reductase"

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Saxena, Ashish, Ravinder Tammali, Aramati BM Reddy, Satish K. Srivastava, and Kota V. Ramana. "Abstract 1384: Prevention of angiogenesis by aldose reductase inhibition." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1384.

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Li, Yang, and Bing Ma. "Study on Aldose Reductase Inhibitors Based on Quinoxalin Structure." In 2018 International Workshop on Bioinformatics, Biochemistry, Biomedical Sciences (BBBS 2018). Atlantis Press, 2018. http://dx.doi.org/10.2991/bbbs-18.2018.29.

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Aleksić, Mara, Jelena Rupar, N. Vučković, L. Kováčiková, A. Boháč, and V. Dobričić. "ELECTROCHEMICAL BEHAVIOR AND INTERACTION OF THE NEWLY SYNTHESIZED POTENTIAL ALDOSE REDUCTASE INHIBITOR WITH HUMAN SERUM ALBUMIN IN THE PRESENCE OF POLYSORBATE 80." In 17th International Conference on Fundamental and Applied Aspects of Physical Chemistry. Society of Physical Chemists of Serbia, 2024. https://doi.org/10.46793/phys.chem24i.203a.

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Albumin is the most abundant protein in blood plasma and has a great ability to bind numerous molecules. Since inhibition of the enzyme aldose reductase can be used in the treatment of diabetes, it is important to investigate the interaction between albumin and aldose reductase inhibitors (ARI). The aim of this work is to investigate the electrochemical behavior of the newly synthesized potential ARI and to examine the possibility of studying the interaction of ARI with human serum albumin (HSA) by voltammetry. The reduction of ARI is an irreversible, diffusion-controlled process. The applicat
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Hallur, Raghavendra, Anushka Sahay, Sarwan Bradosty, and Faiyaz Shaikh. "Inhibitory Effects of a Specific Phytochemical Combination on Carbohydrate Metabolism, Lipid Digestion, and Free Radicals: An in Vitro Study." In 5th International Conference on Biomedical and Health Sciences. Cihan University-Erbil, 2024. http://dx.doi.org/10.24086/biohs2024/paper.1247.

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Abstract—Context: Diabetes, characterized by insulin insufficiency/resistance and oxidative stress, is a global health concern. Traditional plant combinations offer potential as oral diabetes therapy due to their multifaceted pharmacological properties. Aims: This study evaluated the antidiabetic, antilipidemic, and antioxidant potential of a phytochemical combination comprising Salacia extracts (Salacia chinensis and Salacia oblonga), Curcumin, and Piperine. Settings and Design: In vitro experiments assessed the inhibitory activity of the phytochemical combination on key enzymes related to ca
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Elangovan, Manivannan, Ns Hari Narayana Moorthy, and Karthikeyan Chandra Bose. "Structural Insight into the interaction of flavonoids with aldose reductase." In 7th International Electronic Conference on Medicinal Chemistry. MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11497.

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Hedayati, B. Keshavarz, R. Parra-Hernandez, E. M. Laxdal, N. J. Dimopoulos, P. Alexiou, and V. J. Demopoulos. "An improved neural network ensemble model of Aldose Reductase inhibitory activity." In 2012 International Joint Conference on Neural Networks (IJCNN 2012 - Brisbane). IEEE, 2012. http://dx.doi.org/10.1109/ijcnn.2012.6252798.

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Patra, J. C., R. W. S. Cheong, P. K. Meher, and G. Chakraborty. "Determination of QSAR of aldose reductase inhibitors using an RBF network." In 2008 IEEE International Conference on Systems, Man and Cybernetics (SMC). IEEE, 2008. http://dx.doi.org/10.1109/icsmc.2008.4811535.

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Patra, J. C., L. Li, and P. K. Meher. "Support vector machine application in drug discovery of aldose reductase inhibitors." In 2008 IEEE International Conference on Systems, Man and Cybernetics (SMC). IEEE, 2008. http://dx.doi.org/10.1109/icsmc.2008.4811538.

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Yang, Shaoqi, Xiangyu Qin, Tianwei Luo, Xin Hao, and Changjin Zhu. "Novel Nitro Derivatives of Benzothiadiazine 1,1-Dioxide as Aldose Reductase Inhibitors." In 2015 International Conference on Industrial Technology and Management Science. Atlantis Press, 2015. http://dx.doi.org/10.2991/itms-15.2015.260.

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Ramana, Kota V., Ravinder Tammali, Sharad S. Singhal, Sanjay Awasthi, and Satish K. Srivastava. "Abstract 3233: Inhibition of aldose reductase prevents lung cancer cell growthin vitroandin vivo." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3233.

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Reports on the topic "Aldose reductase"

1

Shapiro, Paul S. Mechanistic Basis for Use of Aldose Reductase Inhibitors to Treat Breast Cancer. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada408682.

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Adeniji, Adegoke. Pharmacological Characterization of a Novel Bifunctional Aldo-Keto Reductase 1C3 Inhibitor and Androgen Receptor Antagonist. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada591193.

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