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For: Huang L, He R, Luo W, Zhu YS, Li J, Tan T, Zhang X, Hu Z, Luo D. Aldo-Keto Reductase Family 1 Member B10 Inhibitors: Potential Drugs for Cancer Treatment. Recent Pat Anticancer Drug Discov 2016;11:184-96. [PMID: 26844556 DOI: 10.2174/1574892811888160304113346] [Cited by in Crossref: 25] [Cited by in F6Publishing: 29] [Article Influence: 5.0] [Reference Citation Analysis]
Number Citing Articles
1 Silva TA, Azevedo H. Comparative bioinformatics analysis of prognostic and differentially expressed genes in non-muscle and muscle invasive bladder cancer. J Proteomics 2020;229:103951. [PMID: 32860965 DOI: 10.1016/j.jprot.2020.103951] [Reference Citation Analysis]
2 Seliger JM, Cicek SS, Witt LT, Martin HJ, Maser E, Hintzpeter J. Selective Inhibition of Human AKR1B10 by n-Humulone, Adhumulone and Cohumulone Isolated from Humulus lupulus Extract. Molecules 2018;23:E3041. [PMID: 30469331 DOI: 10.3390/molecules23113041] [Cited by in Crossref: 6] [Cited by in F6Publishing: 5] [Article Influence: 1.5] [Reference Citation Analysis]
3 Malila Y, Uengwetwanit T, Thanatsang KV, Arayamethakorn S, Srimarut Y, Petracci M, Soglia F, Rungrassamee W, Visessanguan W. Insights Into Transcriptome Profiles Associated With Wooden Breast Myopathy in Broilers Slaughtered at the Age of 6 or 7 Weeks. Front Physiol 2021;12:691194. [PMID: 34262480 DOI: 10.3389/fphys.2021.691194] [Reference Citation Analysis]
4 DiStefano JK, Davis B. Diagnostic and Prognostic Potential of AKR1B10 in Human Hepatocellular Carcinoma. Cancers (Basel). 2019;11. [PMID: 30959792 DOI: 10.3390/cancers11040486] [Cited by in Crossref: 22] [Cited by in F6Publishing: 25] [Article Influence: 7.3] [Reference Citation Analysis]
5 Jung Y, Lee EH, Lee CG, Rhee K, Jung W, Choi Y, Pan C, Kang K. AKR1B10-inhibitory Selaginella tamariscina extract and amentoflavone decrease the growth of A549 human lung cancer cells in vitro and in vivo. Journal of Ethnopharmacology 2017;202:78-84. [DOI: 10.1016/j.jep.2017.03.010] [Cited by in Crossref: 23] [Cited by in F6Publishing: 20] [Article Influence: 4.6] [Reference Citation Analysis]
6 Amai K, Fukami T, Ichida H, Watanabe A, Nakano M, Watanabe K, Nakajima M. Quantitative analysis of mRNA expression levels of aldo-keto reductase and short-chain dehydrogenase/reductase isoforms in human livers. Drug Metab Pharmacokinet 2020;35:539-47. [PMID: 33036882 DOI: 10.1016/j.dmpk.2020.08.004] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.5] [Reference Citation Analysis]
7 Rajak S, Gupta P, Anjum B, Raza S, Tewari A, Ghosh S, Tripathi M, Singh BK, Sinha RA. Role of AKR1B10 and AKR1B8 in the pathogenesis of non-alcoholic steatohepatitis (NASH) in mouse. Biochim Biophys Acta Mol Basis Dis 2021;:166319. [PMID: 34954342 DOI: 10.1016/j.bbadis.2021.166319] [Reference Citation Analysis]
8 Kabir A, Endo S, Toyooka N, Fukuoka M, Kuwata K, Kamatari YO. Evaluation of compound selectivity of aldo-keto reductases using differential scanning fluorimetry. J Biochem 2017;161:215-22. [PMID: 28003428 DOI: 10.1093/jb/mvw063] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
9 Dai T, Ye L, Yu H, Li K, Li J, Liu R, Lu X, Deng M, Li R, Liu W, Yang Y, Wang G. Regulation Network and Prognostic Significance of Aldo-Keto Reductase (AKR) Superfamily Genes in Hepatocellular Carcinoma. J Hepatocell Carcinoma 2021;8:997-1021. [PMID: 34513744 DOI: 10.2147/JHC.S323743] [Reference Citation Analysis]
10 Hara A, Endo S, Matsunaga T, Soda M, El-Kabbani O, Yashiro K. Inhibition of aldo-keto reductase family 1 member B10 by unsaturated fatty acids. Arch Biochem Biophys 2016;609:69-76. [PMID: 27665999 DOI: 10.1016/j.abb.2016.09.010] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 1.0] [Reference Citation Analysis]
11 Endo S, Matsunaga T, Nishinaka T. The Role of AKR1B10 in Physiology and Pathophysiology. Metabolites 2021;11:332. [PMID: 34063865 DOI: 10.3390/metabo11060332] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
12 Kabir A, Honda RP, Kamatari YO, Endo S, Fukuoka M, Kuwata K. Effects of ligand binding on the stability of aldo-keto reductases: Implications for stabilizer or destabilizer chaperones. Protein Sci 2016;25:2132-41. [PMID: 27595938 DOI: 10.1002/pro.3036] [Cited by in Crossref: 15] [Cited by in F6Publishing: 14] [Article Influence: 2.5] [Reference Citation Analysis]
13 Hara A, Endo S, Matsunaga T, Soda M, Yashiro K, El-kabbani O. Long-chain fatty acids inhibit human members of the aldo-keto reductase 1C subfamily. The Journal of Biochemistry 2017;162:371-9. [DOI: 10.1093/jb/mvx041] [Cited by in Crossref: 6] [Cited by in F6Publishing: 5] [Article Influence: 1.2] [Reference Citation Analysis]
14 Endo S, Xia S, Suyama M, Morikawa Y, Oguri H, Hu D, Ao Y, Takahara S, Horino Y, Hayakawa Y, Watanabe Y, Gouda H, Hara A, Kuwata K, Toyooka N, Matsunaga T, Ikari A. Synthesis of Potent and Selective Inhibitors of Aldo-Keto Reductase 1B10 and Their Efficacy against Proliferation, Metastasis, and Cisplatin Resistance of Lung Cancer Cells. J Med Chem 2017;60:8441-55. [PMID: 28976752 DOI: 10.1021/acs.jmedchem.7b00830] [Cited by in Crossref: 10] [Cited by in F6Publishing: 10] [Article Influence: 2.0] [Reference Citation Analysis]
15 Sinreih M, Štupar S, Čemažar L, Verdenik I, Frković Grazio S, Smrkolj Š, Rižner TL. STAR and AKR1B10 are down-regulated in high-grade endometrial cancer. J Steroid Biochem Mol Biol 2017;171:43-53. [PMID: 28232277 DOI: 10.1016/j.jsbmb.2017.02.015] [Cited by in Crossref: 14] [Cited by in F6Publishing: 13] [Article Influence: 2.8] [Reference Citation Analysis]
16 Soares CT, Fachin LRV, Trombone APF, Rosa PS, Ghidella CC, Belone AFF. Potential of AKR1B10 as a Biomarker and Therapeutic Target in Type 2 Leprosy Reaction. Front Med (Lausanne) 2018;5:263. [PMID: 30320113 DOI: 10.3389/fmed.2018.00263] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 0.8] [Reference Citation Analysis]
17 Liu R, Zheng S, Yang CY, Yu Y, Peng S, Ge Q, Lin Q, Li Q, Shi W, Shao Y. Prognostic value of aldo-keto reductase family 1 member B10 (AKR1B10) in digestive system cancers: A meta-analysis. Medicine (Baltimore) 2021;100:e25454. [PMID: 33832153 DOI: 10.1097/MD.0000000000025454] [Reference Citation Analysis]
18 Fang CY, Lin YH, Chen CL. Overexpression of AKR1B10 predicts tumor recurrence and short survival in oral squamous cell carcinoma patients. J Oral Pathol Med 2019;48:712-9. [PMID: 31237374 DOI: 10.1111/jop.12891] [Cited by in Crossref: 4] [Cited by in F6Publishing: 7] [Article Influence: 1.3] [Reference Citation Analysis]
19 Ko HH, Peng HH, Cheng SJ, Kuo MY. Increased salivary AKR1B10 level: Association with progression and poor prognosis of oral squamous cell carcinoma. Head Neck 2018;40:2642-7. [PMID: 30430672 DOI: 10.1002/hed.25370] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 1.3] [Reference Citation Analysis]
20 Yao Y, Wang X, Zhou D, Li H, Qian H, Zhang J, Jiang L, Wang B, Lin Q, Zhu X. Loss of AKR1B10 promotes colorectal cancer cells proliferation and migration via regulating FGF1-dependent pathway. Aging (Albany NY) 2020;12:13059-75. [PMID: 32615540 DOI: 10.18632/aging.103393] [Cited by in Crossref: 5] [Cited by in F6Publishing: 6] [Article Influence: 2.5] [Reference Citation Analysis]
21 Ko HH, Cheng SL, Lee JJ, Chen HM, Kuo MY, Cheng SJ. Expression of AKR1B10 as an independent marker for poor prognosis in human oral squamous cell carcinoma. Head Neck 2017;39:1327-32. [PMID: 28301069 DOI: 10.1002/hed.24759] [Cited by in Crossref: 12] [Cited by in F6Publishing: 13] [Article Influence: 2.4] [Reference Citation Analysis]
22 Tatsuta T, Nakasato A, Sugawara S, Hosono M. Transcriptomic alterations in malignant pleural mesothelioma cells in response to long‑term treatment with bullfrog sialic acid‑binding lectin. Mol Med Rep 2021;23:467. [PMID: 33880588 DOI: 10.3892/mmr.2021.12106] [Reference Citation Analysis]
23 Gao Y, Xu D, Li H, Xu J, Pan Y, Liao X, Qian J, Hu Y, Yu G. Avasimibe Dampens Cholangiocarcinoma Progression by Inhibiting FoxM1-AKR1C1 Signaling. Front Oncol 2021;11:677678. [PMID: 34127944 DOI: 10.3389/fonc.2021.677678] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
24 Singh M, Kapoor A, Bhatnagar A. Physiological and Pathological Roles of Aldose Reductase. Metabolites 2021;11:655. [PMID: 34677370 DOI: 10.3390/metabo11100655] [Reference Citation Analysis]
25 Aftab Q, Mesnil M, Ojefua E, Poole A, Noordenbos J, Strale PO, Sitko C, Le C, Stoynov N, Foster LJ, Sin WC, Naus CC, Chen VC. Cx43-Associated Secretome and Interactome Reveal Synergistic Mechanisms for Glioma Migration and MMP3 Activation. Front Neurosci 2019;13:143. [PMID: 30941001 DOI: 10.3389/fnins.2019.00143] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 2.3] [Reference Citation Analysis]
26 Rivas A, Pequerul R, Barracco V, Domínguez M, López S, Jiménez R, Parés X, Alvarez R, Farrés J, de Lera AR. Synthesis of C11-to-C14 methyl-shifted all-trans-retinal analogues and their activities on human aldo-keto reductases. Org Biomol Chem 2020;18:4788-801. [PMID: 32530010 DOI: 10.1039/d0ob01084g] [Cited by in Crossref: 1] [Article Influence: 0.5] [Reference Citation Analysis]
27 Ruiz FX, Parés X, Farrés J. Perspective on the Structural Basis for Human Aldo-Keto Reductase 1B10 Inhibition. Metabolites 2021;11:865. [PMID: 34940623 DOI: 10.3390/metabo11120865] [Reference Citation Analysis]
28 Mazzio E, Badisa R, Mack N, Cassim S, Zdralevic M, Pouyssegur J, Soliman KFA. Whole-transcriptome Analysis of Fully Viable Energy Efficient Glycolytic-null Cancer Cells Established by Double Genetic Knockout of Lactate Dehydrogenase A/B or Glucose-6-Phosphate Isomerase. Cancer Genomics Proteomics 2020;17:469-97. [PMID: 32859627 DOI: 10.21873/cgp.20205] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
29 Shehzad MT, Hameed A, al-Rashida M, Imran A, Uroos M, Asari A, Mohamad H, Islam M, Iftikhar S, Shafiq Z, Iqbal J. Exploring antidiabetic potential of adamantyl-thiosemicarbazones via aldose reductase (ALR2) inhibition. Bioorganic Chemistry 2019;92:103244. [DOI: 10.1016/j.bioorg.2019.103244] [Cited by in Crossref: 6] [Cited by in F6Publishing: 4] [Article Influence: 2.0] [Reference Citation Analysis]
30 Seliger JM, Misuri L, Maser E, Hintzpeter J. The hop-derived compounds xanthohumol, isoxanthohumol and 8-prenylnaringenin are tight-binding inhibitors of human aldo-keto reductases 1B1 and 1B10. J Enzyme Inhib Med Chem 2018;33:607-14. [PMID: 29532688 DOI: 10.1080/14756366.2018.1437728] [Cited by in Crossref: 12] [Cited by in F6Publishing: 12] [Article Influence: 3.0] [Reference Citation Analysis]
31 Zhou Z, Zhao Y, Gu L, Niu X, Lu S. Inhibiting proliferation and migration of lung cancer using small interfering RNA targeting on Aldo-keto reductase family 1 member B10. Mol Med Rep 2018;17:2153-60. [PMID: 29207124 DOI: 10.3892/mmr.2017.8173] [Cited by in Crossref: 4] [Cited by in F6Publishing: 8] [Article Influence: 0.8] [Reference Citation Analysis]