{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T04:12:38Z","timestamp":1793333558991,"version":"4.5.0"},"reference-count":241,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,9,12]],"date-time":"2021-09-12T00:00:00Z","timestamp":1631404800000},"content-version":"am","delay-in-days":285,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100004097","name":"Fondation ARC pour la Recherche sur le Cancer","doi-asserted-by":"publisher","award":["PJA20181208080"],"award-info":[{"award-number":["PJA20181208080"]}],"id":[{"id":"10.13039\/501100004097","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004099","name":"Ligue Contre le Cancer","doi-asserted-by":"publisher","award":["TAZK20115"],"award-info":[{"award-number":["TAZK20115"]}],"id":[{"id":"10.13039\/501100004099","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical Pharmacology"],"published-print":{"date-parts":[[2020,12]]},"DOI":"10.1016\/j.bcp.2020.114213","type":"journal-article","created":{"date-parts":[[2020,9,2]],"date-time":"2020-09-02T20:51:21Z","timestamp":1599079881000},"page":"114213","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":116,"special_numbering":"C","title":["Cellular toxicity of the metabolic inhibitor 2-deoxyglucose and associated resistance mechanisms"],"prefix":"10.1016","volume":"182","author":[{"given":"Clotilde","family":"Laussel","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S\u00e9bastien","family":"L\u00e9on","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bcp.2020.114213_b0005","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.1600200","article-title":"Fundamentals of cancer metabolism","volume":"2","author":"DeBerardinis","year":"2016","journal-title":"Sci Adv."},{"key":"10.1016\/j.bcp.2020.114213_b0010","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1038\/sj.onc.1209597","article-title":"Glycolysis inhibition for anticancer treatment","volume":"25","author":"Pelicano","year":"2006","journal-title":"Oncogene"},{"key":"10.1016\/j.bcp.2020.114213_b0015","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1089\/ars.2007.1714","article-title":"Differential Toxic Mechanisms of 2-Deoxy-D-Glucose versus 2-Fluorodeoxy-D -Glucose in Hypoxic and Normoxic Tumor Cells","volume":"9","author":"Kurtoglu","year":"2007","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.bcp.2020.114213_b0020","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1002\/iub.1251","article-title":"The wonders of 2-deoxy-D-glucose","volume":"66","author":"Xi","year":"2014","journal-title":"IUBMB Life"},{"key":"10.1016\/j.bcp.2020.114213_b0025","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/0016-0032(52)90482-1","article-title":"2-Desoxyl-D-glucose as an inhibitor of anaerobic glycolysis in tumor tissue","volume":"254","author":"Woodward","year":"1952","journal-title":"J. Frankl. Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0030","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/0016-0032(52)90853-3","article-title":"The influence of 2-Desoxy-D-glucose on the growth of embryonic chicken-heart fibroblasts in tissue culture","volume":"253","author":"Ely","year":"1952","journal-title":"J. Frankl. Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0035","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/0016-0032(52)90177-4","article-title":"2-desoxy-d-glucose as an inhibitor in the aerobic glucose metabolism of yeast","volume":"254","author":"Woodward","year":"1952","journal-title":"J. Frankl. Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0040","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/0016-0032(52)90852-1","article-title":"2-Desoxy-D-glucose as an antagonist of glucose in yeast fermentation","volume":"253","author":"Cramer","year":"1952","journal-title":"J. Frankl. Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0045","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1016\/0016-0032(53)91167-3","article-title":"Carbohydrate analogs as antagonists of glucose in carbohydrate metabolism of yeast","volume":"256","author":"Woodward","year":"1953","journal-title":"J. Frankl. Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0050","first-page":"599","article-title":"The effect of 2-desoxy-D-glucose on glycolysis and respiration of tumor and normal tissues","volume":"14","author":"Woodward","year":"1954","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0055","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/0016-0032(54)90946-1","article-title":"2-deoxy-d-glucose as an inhibitor of cancerous growth in animals","volume":"258","author":"Ely","year":"1954","journal-title":"J. Frankl. Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0060","doi-asserted-by":"crossref","first-page":"579","DOI":"10.3181\/00379727-89-21881","article-title":"2-Deoxyglucose\u2013A Metabolic Block for Glucose","volume":"89","author":"Wick","year":"1955","journal-title":"Exp. Biol. Med."},{"key":"10.1016\/j.bcp.2020.114213_b0065","doi-asserted-by":"crossref","first-page":"124","DOI":"10.3181\/00379727-99-24268","article-title":"Animal Responses to 2-Deoxy-D-Glucose Administration","volume":"99","author":"Landau","year":"1958","journal-title":"Exp. Biol. Med."},{"key":"10.1016\/j.bcp.2020.114213_b0070","first-page":"485","article-title":"Certain metabolic and pharmacologic effects in cancer patients given infusions of 2-deoxy-D-glucose","volume":"21","author":"Landau","year":"1958","journal-title":"J. Natl. Cancer Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0075","article-title":"The Effect of Glucose Analogues on the Metabolism of Human Leukemic Cells","author":"Laszlo","year":"1958","journal-title":"JNCI J. Natl. Cancer Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0080","first-page":"267","article-title":"Effects of glucose analogues (2-deoxy-D-glucose, 2-deoxy-D-galactose) on experimental tumors","volume":"24","author":"Laszlo","year":"1960","journal-title":"J. Natl. Cancer Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0085","doi-asserted-by":"crossref","DOI":"10.1093\/femsyr\/fow080","article-title":"Saccharomyces cerevisiae metabolism in ecological context","volume":"16","author":"Jouhten","year":"2016","journal-title":"FEMS Yeast Res."},{"key":"10.1016\/j.bcp.2020.114213_b0090","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1111\/1574-6976.12065","article-title":"Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae","volume":"38","author":"Conrad","year":"2014","journal-title":"FEMS Microbiol Rev."},{"key":"10.1016\/j.bcp.2020.114213_b0095","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/BF00265579","article-title":"Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression","volume":"154","author":"Zimmermann","year":"1977","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.bcp.2020.114213_b0100","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1007\/BF00131900","article-title":"Starch hydrolysis by derepressed mutants of Schwanniomyces castellii","volume":"5","author":"Dhawale","year":"1983","journal-title":"Biotechnol. Lett."},{"key":"10.1016\/j.bcp.2020.114213_b0105","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1007\/BF00410439","article-title":"Starch utilization by yeasts: mutants resistant of carbon catabolite repression","volume":"8","author":"McCann","year":"1984","journal-title":"Curr. Genet."},{"key":"10.1016\/j.bcp.2020.114213_b0110","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1385\/ABAB:77:1-3:211","article-title":"2-Deoxyglucose as a Selective Agent for Derepressed Mutants of Pichia stipitis","volume":"77","author":"Sreenath","year":"1999","journal-title":"Appl. Biochem. Biotechnol."},{"key":"10.1016\/j.bcp.2020.114213_b0115","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1002\/j.2050-0416.1992.tb01119.x","article-title":"Improving yeast fermentation performance (Cambridge prize lecture)","volume":"98","author":"D\u2019Amore","year":"1992","journal-title":"J. Inst. Brew."},{"key":"10.1016\/j.bcp.2020.114213_b0120","first-page":"161","article-title":"The Use of Catabolite Derepression as a Means of Improving the Fermentation Rate of Brewing Yeast Strains","volume":"44","author":"Jones","year":"1986","journal-title":"J. Am. Soc. Brew. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0125","doi-asserted-by":"crossref","first-page":"4279","DOI":"10.1128\/AEM.67.9.4279-4285.2001","article-title":"Improved Properties of Baker\u2019s Yeast Mutants Resistant to 2-Deoxy-d-Glucose","volume":"67","author":"Rinc\u00f3n","year":"2001","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.bcp.2020.114213_b0130","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1002\/bit.260220314","article-title":"Selective isolation of depressed mutants of an \u03b1-amylase yeast by the use of 2-deoxyglucose: COMMUNICATIONS TO THE EDITOR","volume":"22","author":"van Uden","year":"1980","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.bcp.2020.114213_b0135","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1002\/jobm.3620290202","article-title":"Isolation and characterization of mutants of Trichosporon adeninovorans resistant to 2-deoxy-D-glucose","volume":"29","author":"B\u00fcttner","year":"1989","journal-title":"J. Basic Microbiol."},{"key":"10.1016\/j.bcp.2020.114213_b0140","doi-asserted-by":"crossref","first-page":"1950","DOI":"10.1128\/EC.00256-06","article-title":"Regulation of the nucleocytoplasmic distribution of Snf1-Gal83 protein kinase","volume":"5","author":"Hedbacker","year":"2006","journal-title":"Eukaryot Cell."},{"key":"10.1016\/j.bcp.2020.114213_b0145","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/BF00315774","article-title":"The expression of a specific 2-deoxyglucose-6P phosphatase prevents catabolite repression mediated by 2-deoxyglucose in yeast","volume":"28","author":"Randez-Gil","year":"1995","journal-title":"Curr Genet."},{"key":"10.1016\/j.bcp.2020.114213_b0150","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1016\/S0926-6593(66)80094-2","article-title":"Repression by glucose of alcohol dehydrogenase, malate dehydrogenase, isocitrate lyase and malate synthase in yeast","volume":"118","author":"Witt","year":"1966","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0155","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1128\/jb.158.1.29-35.1984","article-title":"Saccharomyces cerevisiae mutants provide evidence of hexokinase PII as a bifunctional enzyme with catalytic and regulatory domains for triggering carbon catabolite repression","volume":"158","author":"Entian","year":"1984","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0160","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1093\/genetics\/115.2.247","article-title":"Mutations causing constitutive invertase synthesis in yeast: genetic interactions with snf mutations","volume":"115","author":"Neigeborn","year":"1987","journal-title":"Genetics"},{"key":"10.1016\/j.bcp.2020.114213_b0165","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/0304-4165(64)90046-7","article-title":"Metabolic Studies with 2-Deoxyhexoses. II. Resistance to 2- Deoxyglucose in a Yeast Mutant","volume":"86","author":"Heredia","year":"1964","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0170","doi-asserted-by":"crossref","first-page":"3049","DOI":"10.1158\/1535-7163.MCT-07-0310","article-title":"Under normoxia, 2-deoxy-D-glucose elicits cell death in select tumor types not by inhibition of glycolysis but by interfering with N-linked glycosylation","volume":"6","author":"Kurtoglu","year":"2007","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.bcp.2020.114213_b0175","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1534\/genetics.114.169060","article-title":"Genetic analysis of resistance and sensitivity to 2-deoxyglucose in Saccharomyces cerevisiae","volume":"198","author":"McCartney","year":"2014","journal-title":"Genetics"},{"key":"10.1016\/j.bcp.2020.114213_b0180","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/0005-2736(68)90123-5","article-title":"Transport and transport-associated phosphorylation of 2-deoxy-d-glucose in yeast","volume":"163","author":"Van Steveninck","year":"1968","journal-title":"Biochim. Biophys. Acta BBA - Biomembr."},{"key":"10.1016\/j.bcp.2020.114213_b0185","doi-asserted-by":"crossref","first-page":"G153","DOI":"10.1152\/ajpgi.1996.270.1.G153","article-title":"2-Deoxyglucose transport and metabolism in Caco-2 cells","volume":"270","author":"Bissonnette","year":"1996","journal-title":"Am. J. Physiol.-Gastrointest. Liver Physiol."},{"key":"10.1016\/j.bcp.2020.114213_b0190","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1002\/j.2040-4603.2012.tb00424.x","article-title":"Role of monosaccharide transport proteins in carbohydrate assimilation, distribution, metabolism, and homeostasis","volume":"2","author":"Cura","year":"2012","journal-title":"Compr. Physiol."},{"key":"10.1016\/j.bcp.2020.114213_b0195","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1007\/BF01869146","article-title":"2-Deoxyglucose transport by intestinal epithelial cells isolated from the chick","volume":"27","author":"Kimmich","year":"1976","journal-title":"J. Membr. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0200","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/S0969-8051(98)00038-9","article-title":"The importance of glucose transport activity as the rate-limiting step of 2-deoxyglucose uptake in tumor cells in vitro","volume":"25","author":"Waki","year":"1998","journal-title":"Nucl. Med. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0205","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/0304-4165(77)90295-1","article-title":"Uptake and phosphorylation of 2-deoxy-D-glucose by wild type and respiration-deficient baker\u2019s yeast","volume":"497","author":"Meredith","year":"1977","journal-title":"Biochim. Biophys. Acta BBA - Gen. Subj."},{"key":"10.1016\/j.bcp.2020.114213_b0210","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0021-9258(18)70358-X","article-title":"Studies of tissue permeability. V. The penetration and phosphorylation of 2-deoxyglucose in the rat diaphragm","volume":"234","author":"Kipnis","year":"1959","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0215","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/0304-4165(77)90310-5","article-title":"Metabolic effects of 2-deoxy-D-glucose in isolated fat cells","volume":"496","author":"Chandramouli","year":"1977","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0220","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1016\/S0021-9258(18)65384-0","article-title":"Substrate specificity of brain hexokinase","volume":"210","author":"Sols","year":"1954","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0225","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1016\/S0021-9258(18)64988-9","article-title":"Localization of the primary metabolic block produced by 2-deoxyglucose","volume":"224","author":"Wick","year":"1957","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0230","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/0016-0032(55)90108-3","article-title":"Phosphorylation of 2-deoxy-D-glucose by yeast hexokinase: Competition between 2-deoxy-d-glucose and glucose","volume":"259","author":"Woodward","year":"1955","journal-title":"J. Frankl. Inst."},{"key":"10.1016\/j.bcp.2020.114213_b0235","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1128\/jb.111.2.419-429.1972","article-title":"Inhibition by 2-deoxy-D-glucose of synthesis of glycoprotein enzymes by protoplasts of Saccharomyces: relation to inhibition of sugar uptake and metabolism","volume":"111","author":"Kuo","year":"1972","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0240","doi-asserted-by":"crossref","first-page":"1588","DOI":"10.1135\/cccc19671588","article-title":"Metabolism of 2-deoxy-D-glucose by baker\u2019s yeast. I. Isolation and identification of phosphorylated esters of 2-deoxy-D-glucose","volume":"32","author":"Biely","year":"1967","journal-title":"Collect. Czechoslov. Chem. Commun."},{"key":"10.1016\/j.bcp.2020.114213_b0245","doi-asserted-by":"crossref","first-page":"2217","DOI":"10.1111\/j.1471-4159.1993.tb03508.x","article-title":"Synthesis of deoxyglucose-1-phosphate, deoxyglucose-1,6-bisphosphate, and other metabolites of 2-deoxy-D-[14C]glucose in rat brain in vivo: influence of time and tissue glucose level","volume":"60","author":"Dienel","year":"1993","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bcp.2020.114213_b0250","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1111\/j.1471-4159.1958.tb12625.x","article-title":"The effects of 2-deoxy-D-glucose on metabolism of slices of cerebral cortex incubated in vitro","volume":"3","author":"Tower","year":"1958","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bcp.2020.114213_b0255","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1016\/0300-9084(92)90070-U","article-title":"The inhibition of bovine heart hexokinase by 2-deoxy-D-glucose-6-phosphate: characterization by 31P NMR and metabolic implications","volume":"74","author":"Chen","year":"1992","journal-title":"Biochimie"},{"key":"10.1016\/j.bcp.2020.114213_b0260","first-page":"221","article-title":"Impact of 2-deoxy-D-glucose on the target metabolome profile of a human endometrial cancer cell line","volume":"34","author":"Urakami","year":"2013","journal-title":"Biomed. Res. Tokyo Jpn."},{"key":"10.1016\/j.bcp.2020.114213_b0265","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/2049-3002-2-9","article-title":"Decoding the dynamics of cellular metabolism and the action of 3-bromopyruvate and 2-deoxyglucose using pulsed stable isotope-resolved metabolomics","volume":"2","author":"Pietzke","year":"2014","journal-title":"Cancer Metab."},{"key":"10.1016\/j.bcp.2020.114213_b0270","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1016\/S0021-9258(18)62356-7","article-title":"Control mechanisms of adenine nucleotide metabolism of ascites tumor cells","volume":"246","author":"Yushok","year":"1971","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0275","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/0006-291X(59)90008-7","article-title":"An acceptor effect in glycolysis","volume":"1","author":"van Eys","year":"1959","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bcp.2020.114213_b0280","first-page":"71","article-title":"Selective depletion of tumor ATP by 2-deoxyglucose and insulin, detected by 31P magnetic resonance spectroscopy","volume":"52","author":"Karczmar","year":"1992","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0285","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1042\/BJ20141562","article-title":"Novel actions of 2-deoxy-D-glucose: protection against Shiga toxins and changes in cellular lipids","volume":"470","author":"Kavaliauskiene","year":"2015","journal-title":"Biochem. J."},{"key":"10.1016\/j.bcp.2020.114213_b0290","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/0034-5687(94)90027-2","article-title":"Glycolysis vs. respiration as ATP source for the shape of quiescent cardiomyocytes","volume":"97","author":"Uchida","year":"1994","journal-title":"Respir. Physiol."},{"key":"10.1016\/j.bcp.2020.114213_b0295","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1038\/nature11066","article-title":"AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress","volume":"485","author":"Jeon","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.bcp.2020.114213_b0300","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1111\/j.1432-1033.1974.tb03828.x","article-title":"Nucleoside-diphosphate derivatives of 2-deoxy-D-glucose in animal cells","volume":"49","author":"Schmidt","year":"1974","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0305","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0305-0491(83)90312-7","article-title":"2-deoxyglucose as a substrate for glutathione regeneration in human and ruminant red blood cells","volume":"75","author":"Suzuki","year":"1983","journal-title":"Comp. Biochem. Physiol. Part B Comp. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0310","doi-asserted-by":"crossref","first-page":"1887","DOI":"10.1016\/S0021-9258(18)64100-6","article-title":"The effects of 2-deoxyglucose on the growth and metabolism of cultured human cells","volume":"236","author":"Barban","year":"1961","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0315","doi-asserted-by":"crossref","first-page":"4920","DOI":"10.1016\/S0021-9258(19)43652-1","article-title":"A multiple role for the coenzyme in the mechanism of action of 6-phosphogluconate dehydrogenase. The oxidative decarbosylation of 2-deoxy-6-phosphogluconate","volume":"248","author":"Rippa","year":"1973","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0320","doi-asserted-by":"crossref","first-page":"17807","DOI":"10.1073\/pnas.0803090105","article-title":"A catabolic block does not sufficiently explain how 2-deoxy-D-glucose inhibits cell growth","volume":"105","author":"Ralser","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bcp.2020.114213_b0325","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/B978-0-12-066150-3.50010-7","article-title":"Interactions between Regulatory Parameters","author":"Atkinson","year":"1977","journal-title":"Cell. Energy Metab. Its Regul., Elsevier"},{"key":"10.1016\/j.bcp.2020.114213_b0330","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/0304-4165(64)90045-5","article-title":"Metabolic Studies with 2-Deoxyhexoses. I. Mechanisms of Inhibition of Growth and Fermentation in Baker\u2019s Yeast","volume":"86","author":"Heredia","year":"1964","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0335","doi-asserted-by":"crossref","first-page":"3735","DOI":"10.1128\/JB.180.15.3735-3740.1998","article-title":"Cell wall architecture in yeast: new structure and new challenges","volume":"180","author":"Lipke","year":"1998","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0340","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1128\/jb.90.4.1032-1035.1965","article-title":"Effect of 2-deoxyglucose on Schizosaccharomyces pombe","volume":"90","author":"Megnet","year":"1965","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0345","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1128\/jb.95.3.1169-1172.1968","article-title":"Lysis of yeast cell walls induced by 2-deoxyglucose at their sites of glucan synthesis","volume":"95","author":"Johnson","year":"1968","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0350","doi-asserted-by":"crossref","first-page":"3303","DOI":"10.1099\/00221287-130-12-3303","article-title":"The Action of 2-Deoxy-D-glucose on the Incorporation of Glucose into (1->3)-\u03b2-Glucan in Stationary Phase Cultures of Candida albicans","volume":"130","author":"Gale","year":"1984","journal-title":"Microbiology"},{"key":"10.1016\/j.bcp.2020.114213_b0355","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.aaw8000","article-title":"The induction of HAD-like phosphatases by multiple signaling pathways confers resistance to the metabolic inhibitor 2-deoxyglucose","volume":"12","author":"Defenouill\u0117re","year":"2019","journal-title":"Sci Signal."},{"key":"10.1016\/j.bcp.2020.114213_b0360","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/0304-4165(66)90379-5","article-title":"The formation of uridine diphosphate-2-deoxy-D-glucose in yeast","volume":"121","author":"Biely","year":"1966","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0365","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/0304-4165(68)90281-X","article-title":"The formation of guanosine diphosphate-2-deoxy-D-glucose in yeast","volume":"156","author":"Biely","year":"1968","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0370","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/0304-4165(68)90310-3","article-title":"Incorporation of 2-deoxy-D-glucose into glycogen","volume":"158","author":"Biely","year":"1968","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0375","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/0304-4165(71)90145-0","article-title":"Transglycosylic reactions of nucleotides of 2-deoxy-sugars. II. 2-Deoxyglucose incorporation into glycogen","volume":"252","author":"Zemek","year":"1971","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0380","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1111\/j.1432-1033.1993.tb18368.x","article-title":"Non-cooperative effects of glucose and 2-deoxyglucose on their metabolism in Saccharomyces cerevisiae studied by 1H-NMR and 13C-NMR spectroscopy","volume":"218","author":"Herve","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0385","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/0304-4165(75)90236-6","article-title":"Uridine diphosphate 2-deoxyglucose","volume":"381","author":"Druzhinina","year":"1975","journal-title":"Biochim. Biophys. Acta BBA - Gen. Subj."},{"key":"10.1016\/j.bcp.2020.114213_b0390","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/1357-2725(95)00110-7","article-title":"Incorporation of 2-deoxy-d-glucose into glycogen. Implications for measurement of tissue-specific glucose uptake and utilisation","volume":"28","author":"Colwell","year":"1996","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0395","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1128\/jb.109.1.81-88.1972","article-title":"Studies on the diversity of inositol-containing yeast phospholipids: incorporation of 2-deoxyglucose into lipid","volume":"109","author":"Steiner","year":"1972","journal-title":"J Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0400","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/0005-2760(73)90098-2","article-title":"Incorporation of 2-deoxy-d-glucose into glycolipids of normal and SV40-transformed hamster cells","volume":"296","author":"Steiner","year":"1973","journal-title":"Biochim. Biophys. Acta BBA - Lipids Lipid Metab."},{"key":"10.1016\/j.bcp.2020.114213_b0405","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1038\/nrm.2017.107","article-title":"Sphingolipids and their metabolism in physiology and disease","volume":"19","author":"Hannun","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0410","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/0006-291X(74)91027-4","article-title":"Incorporation of [14C]-2 deoxy-D-glucose into the lipids of normal cells as compared to virus-transformed cells","volume":"61","author":"Steiner","year":"1974","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bcp.2020.114213_b0415","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1104\/pp.54.3.368","article-title":"myo -Inositol 1-Phosphate Synthase Inhibition and Control of Uridine Diphosphate-d-glucuronic Acid Biosynthesis in Plants","volume":"54","author":"Loewus","year":"1974","journal-title":"Plant Physiol."},{"key":"10.1016\/j.bcp.2020.114213_b0420","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/0003-9861(77)90243-0","article-title":"Studies on the effect of 5-thio-d-glucose and 2-deoxy-d-glucose on myo-inositol metabolism","volume":"181","author":"Burton","year":"1977","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bcp.2020.114213_b0425","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1111\/j.1432-1033.1978.tb12630.x","article-title":"Formation of 2-deoxyglucose-containing lipid-linked oligosaccharides. Interference with glycosylation of glycoproteins","volume":"90","author":"Datema","year":"1978","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0430","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/0042-6822(73)90127-X","article-title":"Effect of 2-deoxy-d-glucose on the multiplication of semliki forest virus and the reversal of the block by mannose","volume":"54","author":"Kaluza","year":"1973","journal-title":"Virology"},{"key":"10.1016\/j.bcp.2020.114213_b0435","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.4049\/jimmunol.1004085","article-title":"2-deoxy D-glucose prevents cell surface expression of NKG2D ligands through inhibition of N-linked glycosylation","volume":"188","author":"Andresen","year":"2012","journal-title":"J. Immunol."},{"key":"10.1016\/j.bcp.2020.114213_b0440","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1111\/j.1432-1033.1975.tb04157.x","article-title":"Mechanism of 2-deoxy-D-glucose inhibition of cell-wall polysaccharide and glycoprotein biosyntheses in Saccharomyces cerevisiae","volume":"54","author":"Kratky","year":"1975","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0445","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/0005-2736(74)90218-1","article-title":"Metabolism of 2-deoxy-D-glucose by baker\u2019s yeast. VI. A study on cell wall mannan","volume":"352","author":"Biely","year":"1974","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0450","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1128\/jb.107.1.121-129.1971","article-title":"Effect of 2-deoxyglucose on cell wall formation in Saccharomyces cerevisiae and its relation to cell growth inhibition","volume":"107","author":"Biely","year":"1971","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0455","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1128\/jb.98.2.744-748.1969","article-title":"Inhibitory effect of 2-deoxy-d-glucose on the formation of the cell wall in yeast protoplasts","volume":"98","author":"Farkas","year":"1969","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0460","doi-asserted-by":"crossref","first-page":"5794","DOI":"10.1128\/AAC.01126-12","article-title":"Activation of the unfolded protein response by 2-deoxy-D-glucose inhibits Kaposi\u2019s sarcoma-associated herpesvirus replication and gene expression","volume":"56","author":"Leung","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bcp.2020.114213_b0465","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1271\/bbb.120812","article-title":"Comparative Analysis of the Expression Patterns of UPR-Target Genes Caused by UPR-Inducing Compounds","volume":"77","author":"Shinjo","year":"2013","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0470","first-page":"393","article-title":"Complex regulation of heat shock- and glucose-responsive genes in human cells","volume":"8","author":"Watowich","year":"1988","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0475","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1007\/s00280-010-1391-0","article-title":"2-Deoxy-D-glucose activates autophagy via endoplasmic reticulum stress rather than ATP depletion","volume":"67","author":"Xi","year":"2011","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.bcp.2020.114213_b0480","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1016\/j.bcp.2013.02.037","article-title":"Endoplasmic reticulum stress induced by 2-deoxyglucose but not glucose starvation activates AMPK through CaMKK\u03b2 leading to autophagy","volume":"85","author":"Xi","year":"2013","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.bcp.2020.114213_b0485","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1158\/1535-7163.MCT-14-0315","article-title":"2-Deoxy-Glucose Downregulates Endothelial AKT and ERK via Interference with N-Linked Glycosylation, Induction of Endoplasmic Reticulum Stress, and GSK3 Activation","volume":"15","author":"Kovacs","year":"2016","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.bcp.2020.114213_b0490","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.ceb.2017.01.005","article-title":"AMPK signalling in health and disease","volume":"45","author":"Carling","year":"2017","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0495","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.apsb.2015.06.002","article-title":"Regulation of AMP-activated protein kinase by natural and synthetic activators","volume":"6","author":"Hardie","year":"2016","journal-title":"Acta Pharm. Sin. B."},{"key":"10.1016\/j.bcp.2020.114213_b0500","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1126\/science.1191241","article-title":"Signaling Kinase AMPK Activates Stress-Promoted Transcription via Histone H2B Phosphorylation","volume":"329","author":"Bungard","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.bcp.2020.114213_b0505","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1007\/s10549-015-3386-3","article-title":"Combined inhibition of glycolysis and AMPK induces synergistic breast cancer cell killing","volume":"151","author":"Wu","year":"2015","journal-title":"Breast Cancer Res. Treat."},{"key":"10.1016\/j.bcp.2020.114213_b0510","article-title":"2-Deoxy-D-Glucose Treatment of Endothelial Cells Induces Autophagy by Reactive Oxygen Species-Mediated Activation of the AMP-Activated Protein Kinase","volume":"6","author":"Wang","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bcp.2020.114213_b0515","doi-asserted-by":"crossref","first-page":"3627","DOI":"10.1038\/onc.2014.301","article-title":"Differential effects of AMPK agonists on cell growth and metabolism","volume":"34","author":"Vincent","year":"2015","journal-title":"Oncogene"},{"key":"10.1016\/j.bcp.2020.114213_b0520","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.cmet.2006.05.005","article-title":"Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome","volume":"3","author":"Cool","year":"2006","journal-title":"Cell Metab."},{"key":"10.1016\/j.bcp.2020.114213_b0525","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1038\/s41598-017-01801-5","article-title":"Combined treatment with Metformin and 2-deoxy glucose induces detachment of viable MDA-MB-231 breast cancer cells in vitro","volume":"7","author":"Bizjak","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bcp.2020.114213_b0530","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1016\/j.molcel.2017.05.032","article-title":"AMPK: Mechanisms of Cellular Energy Sensing and Restoration of Metabolic Balance","volume":"66","author":"Garcia","year":"2017","journal-title":"Mol. Cell."},{"key":"10.1016\/j.bcp.2020.114213_b0535","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1038\/s41556-018-0205-1","article-title":"mTOR as a central hub of nutrient signalling and cell growth","volume":"21","author":"Kim","year":"2019","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0540","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1126\/science.1063518","article-title":"Mammalian TOR: a homeostatic ATP sensor","volume":"294","author":"Dennis","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.bcp.2020.114213_b0545","doi-asserted-by":"crossref","first-page":"2465","DOI":"10.1158\/0008-5472.CAN-09-2782","article-title":"Targeting cancer cell metabolism: the combination of metformin and 2-deoxyglucose induces p53-dependent apoptosis in prostate cancer cells","volume":"70","author":"Ben Sahra","year":"2010","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0550","doi-asserted-by":"crossref","first-page":"1743","DOI":"10.1002\/pros.20837","article-title":"Therapeutic starvation and autophagy in prostate cancer: a new paradigm for targeting metabolism in cancer therapy","volume":"68","author":"DiPaola","year":"2008","journal-title":"Prostate"},{"key":"10.1016\/j.bcp.2020.114213_b0555","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1038\/ncb1547","article-title":"Insulin signalling to mTOR mediated by the Akt\/PKB substrate PRAS40","volume":"9","author":"Vander Haar","year":"2007","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0560","doi-asserted-by":"crossref","first-page":"2453","DOI":"10.1158\/0008-5472.CAN-08-2872","article-title":"Silencing of Elongation Factor-2 Kinase Potentiates the Effect of 2-Deoxy-D-Glucose against Human Glioma Cells through Blunting of Autophagy","volume":"69","author":"Wu","year":"2009","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0565","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1002\/mc.20425","article-title":"Modulation of the activities of AMP-activated protein kinase, protein kinase B, and mammalian target of rapamycin by limiting energy availability with 2-deoxyglucose","volume":"47","author":"Jiang","year":"2008","journal-title":"Mol. Carcinog."},{"key":"10.1016\/j.bcp.2020.114213_b0570","doi-asserted-by":"crossref","first-page":"23225","DOI":"10.1074\/jbc.M109.005280","article-title":"The Glycolytic Inhibitor 2-Deoxyglucose Activates Multiple Prosurvival Pathways through IGF1R","volume":"284","author":"Zhong","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0575","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1158\/1535-7163.MCT-07-0559","article-title":"2-Deoxyglucose induces Akt phosphorylation via a mechanism independent of LKB1\/AMP-activated protein kinase signaling activation or glycolysis inhibition","volume":"7","author":"Zhong","year":"2008","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.bcp.2020.114213_b0580","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0168793","article-title":"2-Deoxyglucose Suppresses ERK Phosphorylation in LKB1 and Ras Wild-Type Non-Small Cell Lung Cancer Cells","volume":"11","author":"Sun","year":"2016","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bcp.2020.114213_b0585","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/sj.bjc.6600547","article-title":"Evaluation of 2-deoxy-D-glucose as a chemotherapeutic agent: mechanism of cell death","volume":"87","author":"Aft","year":"2002","journal-title":"Br. J. Cancer."},{"key":"10.1016\/j.bcp.2020.114213_b0590","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1038\/bjc.1998.708","article-title":"2-Deoxy-D-glucose preferentially kills multidrug-resistant human KB carcinoma cell lines by apoptosis","volume":"78","author":"Bell","year":"1998","journal-title":"Br. J. Cancer."},{"key":"10.1016\/j.bcp.2020.114213_b0595","doi-asserted-by":"crossref","first-page":"12759","DOI":"10.1074\/jbc.M212392200","article-title":"Inhibition of glucose metabolism sensitizes tumor cells to death receptor-triggered apoptosis through enhancement of death-inducing signaling complex formation and apical procaspase-8 processing","volume":"278","author":"Mu\u00f1oz-Pinedo","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0600","doi-asserted-by":"crossref","first-page":"6796","DOI":"10.1158\/0008-5472.CAN-11-0759","article-title":"2-Deoxyglucose Induces Noxa-Dependent Apoptosis in Alveolar Rhabdomyosarcoma","volume":"71","author":"Ramirez-Peinado","year":"2011","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0605","doi-asserted-by":"crossref","unstructured":"R.R. McCartney, M.C. Schmidt, Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit., J. Biol. Chem. 276 (2001) 36460\u201336466, doi: 10.1074\/jbc.M104418200.","DOI":"10.1074\/jbc.M104418200"},{"key":"10.1016\/j.bcp.2020.114213_b0610","doi-asserted-by":"crossref","first-page":"8839","DOI":"10.1073\/pnas.1533136100","article-title":"Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases","volume":"100","author":"Hong","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U A."},{"key":"10.1016\/j.bcp.2020.114213_b0615","doi-asserted-by":"crossref","first-page":"3909","DOI":"10.1128\/MCB.23.11.3909-3917.2003","article-title":"Yeast Pak1 kinase associates with and activates Snf1","volume":"23","author":"Nath","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0620","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1016\/S0960-9822(03)00459-7","article-title":"Elm1p is one of three upstream kinases for the Saccharomyces cerevisiae SNF1 complex","volume":"13","author":"Sutherland","year":"2003","journal-title":"Curr. Biol. CB."},{"key":"10.1016\/j.bcp.2020.114213_b0625","doi-asserted-by":"crossref","first-page":"31052","DOI":"10.1074\/jbc.M113.503763","article-title":"Ptc1 protein phosphatase 2C contributes to glucose regulation of SNF1\/AMP-activated protein kinase (AMPK) in Saccharomyces cerevisiae","volume":"288","author":"Ruiz","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0630","doi-asserted-by":"crossref","unstructured":"A. Ruiz, X. Xu, M. Carlson, Roles of two protein phosphatases, Reg1-Glc7 and Sit4, and glycogen synthesis in regulation of SNF1 protein kinase, Proc. Natl. Acad. Sci. U A. 108 (2011) 6349\u201354. https:\/\/doi.org\/1102758108 [pii] 10.1073\/pnas.1102758108.","DOI":"10.1073\/pnas.1102758108"},{"key":"10.1016\/j.bcp.2020.114213_b0635","doi-asserted-by":"crossref","first-page":"5939","DOI":"10.1002\/j.1460-2075.1995.tb00282.x","article-title":"REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharomyces cerevisiae","volume":"14","author":"Tu","year":"1995","journal-title":"EMBO J."},{"key":"10.1016\/j.bcp.2020.114213_b0640","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1074\/jbc.M707957200","article-title":"Access denied: Snf1 activation loop phosphorylation is controlled by availability of the phosphorylated threonine 210 to the PP1 phosphatase","volume":"283","author":"Rubenstein","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0645","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.cmet.2011.09.009","article-title":"ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase","volume":"14","author":"Mayer","year":"2011","journal-title":"Cell Metab."},{"key":"10.1016\/j.bcp.2020.114213_b0650","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1126\/science.1200094","article-title":"AMPK Is a Direct Adenylate Charge-Regulated Protein Kinase","volume":"332","author":"Oakhill","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.bcp.2020.114213_b0655","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1038\/nature09932","article-title":"Structure of mammalian AMPK and its regulation by ADP","volume":"472","author":"Xiao","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.bcp.2020.114213_b0660","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1083\/jcb.201109113","article-title":"A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis","volume":"196","author":"Becuwe","year":"2012","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0665","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1038\/nrd4145","article-title":"Metabolic targets for cancer therapy","volume":"12","author":"Galluzzi","year":"2013","journal-title":"Nat. Rev. Drug. Discov."},{"key":"10.1016\/j.bcp.2020.114213_b0670","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1002\/pros.21172","article-title":"Targeting tumor metabolism with 2-deoxyglucose in patients with castrate-resistant prostate cancer and advanced malignancies","volume":"70","author":"Stein","year":"2010","journal-title":"Prostate"},{"key":"10.1016\/j.bcp.2020.114213_b0675","first-page":"5794","article-title":"Inhibitory effect of 2-deoxy-D-glucose on liver tumor growth in rats","volume":"52","author":"Cay","year":"1992","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0680","first-page":"380","article-title":"Inhibition of established rat fibrosarcoma growth by the glucose antagonist 2-deoxy-D-glucose","volume":"102","author":"Kern","year":"1987","journal-title":"Surgery."},{"key":"10.1016\/j.bcp.2020.114213_b0685","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1158\/0008-5472.CAN-03-3294","article-title":"2-deoxy-D-glucose increases the efficacy of adriamycin and paclitaxel in human osteosarcoma and non-small cell lung cancers in vivo","volume":"64","author":"Maschek","year":"2004","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0690","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21010234","article-title":"2-Deoxy-d-Glucose and Its Analogs: From Diagnostic to Therapeutic Agents","volume":"21","author":"Pajak","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bcp.2020.114213_b0695","doi-asserted-by":"crossref","first-page":"7023","DOI":"10.1158\/0008-5472.CAN-05-0453","article-title":"2-Deoxyglucose as an Energy Restriction Mimetic Agent: Effects on Mammary Carcinogenesis and on Mammary Tumor Cell Growth In vitro","volume":"65","author":"Zhu","year":"2005","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0700","doi-asserted-by":"crossref","unstructured":"F. Li, M.C. Simon, Cancer Cells Don\u2019t Live Alone: Metabolic Communication within Tumor Microenvironments, Dev. Cell. (2020) S1534580720304974, doi: 10.1016\/j.devcel.2020.06.018.","DOI":"10.1016\/j.devcel.2020.06.018"},{"key":"10.1016\/j.bcp.2020.114213_b0705","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1007\/s00280-003-0724-7","article-title":"Greater cell cycle inhibition and cytotoxicity induced by 2-deoxy-d-glucose in tumor cells treated under hypoxic vs aerobic conditions","volume":"53","author":"Maher","year":"2004","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.bcp.2020.114213_b0710","doi-asserted-by":"crossref","first-page":"5542","DOI":"10.1021\/bi002426w","article-title":"Hypersensitization of tumor cells to glycolytic inhibitors","volume":"40","author":"Liu","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2020.114213_b0715","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.1016\/S0006-2952(02)01456-9","article-title":"Hypoxia increases tumor cell sensitivity to glycolytic inhibitors: a strategy for solid tumor therapy (Model C)","volume":"64","author":"Liu","year":"2002","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.bcp.2020.114213_b0720","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1158\/0008-5472.613.65.2","article-title":"Inhibition of glycolysis in cancer cells: a novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia","volume":"65","author":"Xu","year":"2005","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2020.114213_b0725","doi-asserted-by":"crossref","first-page":"2799","DOI":"10.1167\/iovs.08-1751","article-title":"Targeting hypoxia, a novel treatment for advanced retinoblastoma","volume":"49","author":"Boutrid","year":"2008","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.bcp.2020.114213_b0730","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0024102","article-title":"Efficient Elimination of Cancer Cells by Deoxyglucose-ABT-263\/737 Combination Therapy","volume":"6","author":"Yamaguchi","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bcp.2020.114213_b0735","doi-asserted-by":"crossref","first-page":"20071","DOI":"10.1073\/pnas.1206360109","article-title":"Combination of glycolysis inhibition with chemotherapy results in an antitumor immune response","volume":"109","author":"Beneteau","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U A."},{"key":"10.1016\/j.bcp.2020.114213_b0740","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1007\/s00280-012-2045-1","article-title":"A phase I dose-escalation trial of 2-deoxy-D-glucose alone or combined with docetaxel in patients with advanced solid tumors","volume":"71","author":"Raez","year":"2013","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.bcp.2020.114213_b0745","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.canlet.2013.03.020","article-title":"Differential sensitivities of glioblastoma cell lines towards metabolic and signaling pathway inhibitions","volume":"336","author":"Kennedy","year":"2013","journal-title":"Cancer Lett."},{"key":"10.1016\/j.bcp.2020.114213_b0750","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.ecl.2016.06.008","article-title":"Metformin: From Research to Clinical Practice","volume":"45","author":"Tan","year":"2016","journal-title":"Endocrinol. Metab. Clin. North Am."},{"key":"10.1016\/j.bcp.2020.114213_b0755","doi-asserted-by":"crossref","first-page":"2355","DOI":"10.1172\/JCI40671","article-title":"Metformin inhibits hepatic gluconeogenesis in mice independently of the LKB1\/AMPK pathway via a decrease in hepatic energy state","volume":"120","author":"Foretz","year":"2010","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bcp.2020.114213_b0760","doi-asserted-by":"crossref","first-page":"2350","DOI":"10.1158\/1535-7163.MCT-11-0497","article-title":"Dual inhibition of tumor energy pathway by 2-deoxyglucose and metformin is effective against a broad spectrum of preclinical cancer models","volume":"10","author":"Cheong","year":"2011","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.bcp.2020.114213_b0765","first-page":"99","article-title":"Induction of Apoptosis by a Combination of 2-Deoxyglucose and Metformin in Esophageal Squamous Cell Carcinoma by Targeting Cancer Cell Metabolism","volume":"44","author":"Shafaee","year":"2019","journal-title":"Iran. J. Med. Sci."},{"key":"10.1016\/j.bcp.2020.114213_b0770","first-page":"4812","article-title":"Targeting cancer cell metabolism: The combination of metformin and 2-Deoxyglucose regulates apoptosis in ovarian cancer cells via p38 MAPK\/JNK signaling pathway","volume":"8","author":"Zhu","year":"2016","journal-title":"Am. J. Transl. Res."},{"key":"10.1016\/j.bcp.2020.114213_b0775","doi-asserted-by":"crossref","unstructured":"S. Mathews Samuel, N.J. Satheesh, S. Ghosh, D. B\u00fcsselberg, Y. Majeed, H. Ding, C.R. Triggle, Treatment with a Combination of Metformin and 2-Deoxyglucose Upregulates Thrombospondin-1 in Microvascular Endothelial Cells: Implications in Anti-Angiogenic Cancer Therapy, Cancers. 11 (2019) 1737, doi: 10.3390\/cancers11111737.","DOI":"10.3390\/cancers11111737"},{"key":"10.1016\/j.bcp.2020.114213_b0780","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.lfs.2015.08.002","article-title":"The anti-angiogenic action of 2-deoxyglucose involves attenuation of VEGFR2 signaling and MMP-2 expression in HUVECs","volume":"139","author":"Chuang","year":"2015","journal-title":"Life Sci."},{"key":"10.1016\/j.bcp.2020.114213_b0785","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1002\/jcb.25629","article-title":"2-Deoxy Glucose Modulates Expression and Biological Activity of VEGF in a SIRT-1 Dependent Mechanism: REGULATION OF VEGF BY 2-DG","volume":"118","author":"Kunhiraman","year":"2017","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0790","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0013699","article-title":"Antiangiogenic Activity of 2-Deoxy-D-Glucose","volume":"5","author":"Merchan","year":"2010","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bcp.2020.114213_b0795","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1007\/s00280-013-2193-y","article-title":"Conversion of 2-deoxyglucose-induced growth inhibition to cell death in normoxic tumor cells","volume":"72","author":"Liu","year":"2013","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.bcp.2020.114213_b0800","doi-asserted-by":"crossref","first-page":"463","DOI":"10.2307\/3575919","article-title":"Energetics of Cellular Repair Processes in a Respiratory-Deficient Mutant of Yeast","volume":"92","author":"Jain","year":"1982","journal-title":"Radiat. Res."},{"key":"10.1016\/j.bcp.2020.114213_b0805","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1016\/0360-3016(87)90293-8","article-title":"Modification of the radiation induced damage by 2-deoxy-D-glucose in organ cultures of human cerebral gliomas","volume":"13","author":"Dwarakanath","year":"1987","journal-title":"Int. J. Radiat. Oncol. Biol. Phys."},{"key":"10.1016\/j.bcp.2020.114213_b0810","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/0360-3016(85)90117-8","article-title":"Effects of 2-deoxy-D-glucose on glycolysis, proliferation kinetics and radiation response of human cancer cells","volume":"11","author":"Jain","year":"1985","journal-title":"Int. J. Radiat. Oncol. Biol. Phys."},{"key":"10.1016\/j.bcp.2020.114213_b0815","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/S0360-3016(96)85017-6","article-title":"Improving cancer radiotherapy with 2-deoxy-d-glucose: phase I\/II clinical trials on human cerebral gliomas","volume":"35","author":"Mohanti","year":"1996","journal-title":"Int. J. Radiat. Oncol."},{"issue":"Suppl 1","key":"10.1016\/j.bcp.2020.114213_b0820","doi-asserted-by":"crossref","first-page":"S21","DOI":"10.4103\/0973-1482.55136","article-title":"Clinical studies for improving radiotherapy with 2-deoxy-D-glucose: present status and future prospects","volume":"5","author":"Dwarakanath","year":"2009","journal-title":"J. Cancer Res. Ther."},{"key":"10.1016\/j.bcp.2020.114213_b0825","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1007\/s00066-005-1320-z","article-title":"Optimizing cancer radiotherapy with 2-deoxy-d-glucose dose escalation studies in patients with glioblastoma multiforme","volume":"181","author":"Singh","year":"2005","journal-title":"Strahlenther. Onkol. Organ Dtsch. Rontgengesellschaft Al."},{"key":"10.1016\/j.bcp.2020.114213_b0830","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1111\/j.1471-4159.1977.tb10649.x","article-title":"The [14C]deoxyglucose method for the measurement of local cerebral glucose utilization: theory, procedure, and normal values in the conscious and anesthetized albino rat","volume":"28","author":"Sokoloff","year":"1977","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bcp.2020.114213_b0835","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1080\/02841850802482486","article-title":"2-[18 f]-2-deoxy-d-glucose (fdg) uptake in human tumor cells is related to the expression of glut-1 and hexokinase II","volume":"49","author":"Ong","year":"2008","journal-title":"Acta Radiol."},{"key":"10.1016\/j.bcp.2020.114213_b0840","first-page":"661","article-title":"PET: the merging of biology and imaging into molecular imaging","volume":"41","author":"Phelps","year":"2000","journal-title":"J. Nucl. Med. Off. Publ. Soc. Nucl. Med."},{"key":"10.1016\/j.bcp.2020.114213_b0845","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1007\/s00280-006-0207-8","article-title":"Efficacy of 2-halogen substituted d-glucose analogs in blocking glycolysis and killing \u201chypoxic tumor cells\u201d","volume":"58","author":"Lampidis","year":"2006","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.bcp.2020.114213_b0850","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/0300-9084(96)88129-6","article-title":"Reciprocal effects of 2-fluoro-2-deoxy-d-glucose and glucose on their metabolism in Saccharomyces cerevisiae studied by multi-nuclear NMR spectroscopy","volume":"77","author":"Tran-Dinh","year":"1995","journal-title":"Biochimie"},{"key":"10.1016\/j.bcp.2020.114213_b0855","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1111\/j.1432-1033.1980.tb04799.x","article-title":"Fluoroglucose-Inhibition of Protein Glycosylation in vivo. Inhibition of Mannose and Glucose Incorporation into Lipid-Linked Oligosaccharides","volume":"109","author":"Datema","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0860","doi-asserted-by":"crossref","first-page":"79885","DOI":"10.18632\/oncotarget.13089","article-title":"Cellular effects of fluorodeoxyglucose: Global changes in the lipidome and alteration in intracellular transport","volume":"7","author":"Kavaliauskiene","year":"2016","journal-title":"Oncotarget."},{"key":"10.1016\/j.bcp.2020.114213_b0865","first-page":"817","article-title":"Retinoblastoma treatment: impact of the glycolytic inhibitor 2-deoxy-d-glucose on molecular genomics expression in LH(BETA)T(AG) retinal tumors","volume":"6","author":"Pi\u00f1a","year":"2012","journal-title":"Clin. Ophthalmol. Auckl. NZ."},{"key":"10.1016\/j.bcp.2020.114213_b0870","doi-asserted-by":"crossref","unstructured":"W. Priebe, R. Zielinski, I. Fokt, E. Felix, V. Radjendirane, J. Arumugam, M. Tai Khuong, M. Krasinski, S. Skora, EXTH-07. design and evaluation of WP1122, an inhibitor of glycolysis with increased cns uptake., Neuro-Oncol. 20 (2018) vi86\u2013vi86, doi: 10.1093\/neuonc\/noy148.356.","DOI":"10.1093\/neuonc\/noy148.356"},{"key":"10.1016\/j.bcp.2020.114213_b0875","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1016\/0006-3002(61)90561-3","article-title":"Mechanism of resistance to 2-deoxy-d-glucose in HeLa cells","volume":"47","author":"Barban","year":"1961","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0880","doi-asserted-by":"crossref","first-page":"2881","DOI":"10.1016\/S0021-9258(18)62264-1","article-title":"Studies on the uptake of hexose phosphates. I. 2-Deoxyglucose and 2-deoxyglucose 6-phosphate","volume":"246","author":"Dietz","year":"1971","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b0885","doi-asserted-by":"crossref","unstructured":"F. Veana, A.C. Flores-Gallegos, A.M. Gonzalez-Montemayor, M. Michel-Michel, L. Lopez-Lopez, P. Aguilar-Zarate, J.A. Ascacio-Vald\u00e9s, R. Rodr\u00edguez-Herrera, Invertase: An Enzyme with Importance in Confectionery Food Industry, in: M. Kuddus (Ed.), Enzym. Food Technol., Springer Singapore, Singapore, 2018, pp. 187\u2013212, doi: 10.1007\/978-981-13-1933-4_10.","DOI":"10.1007\/978-981-13-1933-4_10"},{"key":"10.1016\/j.bcp.2020.114213_b0890","doi-asserted-by":"crossref","first-page":"2870","DOI":"10.1128\/jb.170.6.2870-2872.1988","article-title":"Saccharomyces cerevisiae acquires resistance to 2-deoxyglucose at a very high frequency","volume":"170","author":"Heredia","year":"1988","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0895","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1093\/molbev\/msq184","article-title":"Expansion of Hexose Transporter Genes Was Associated with the Evolution of Aerobic Fermentation in Yeasts","volume":"28","author":"Lin","year":"2011","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.bcp.2020.114213_b0900","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1008484","article-title":"Spontaneous mutations that confer resistance to 2-deoxyglucose act through Hxk2 and Snf1 pathways to regulate gene expression and HXT endocytosis","volume":"16","author":"Soncini","year":"2020","journal-title":"PLoS Genet."},{"key":"10.1016\/j.bcp.2020.114213_b0905","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1099\/13500872-141-2-441","article-title":"Hexokinase activity is affected in mutants of Kluyveromyces lactis resistant to glucose repression","volume":"141","author":"Goffrini","year":"1995","journal-title":"Microbiology"},{"key":"10.1016\/j.bcp.2020.114213_b0910","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1093\/genetics\/158.2.541","article-title":"RAG4 gene encodes a glucose sensor in Kluyveromyces lactis","volume":"158","author":"Betina","year":"2001","journal-title":"Genetics"},{"key":"10.1016\/j.bcp.2020.114213_b0915","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0081412","article-title":"Identification of Glucose Transporters in Aspergillus nidulans","volume":"8","author":"dos Reis","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bcp.2020.114213_b0920","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1128\/jb.171.1.53-58.1989","article-title":"Deoxyglucose-resistant mutants of Neurospora crassa: isolation, mapping, and biochemical characterization","volume":"171","author":"Allen","year":"1989","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0925","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/0014-5793(90)81154-G","article-title":"2-Deoxy-D-glucose resistant yeast with altered sugar transport activity","volume":"269","author":"Novak","year":"1990","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bcp.2020.114213_b0930","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.1099\/00221287-140-10-2617","article-title":"Glucose-transport-deficient mutants of Schizosaccharomyces pombe: phenotype, genetics and use for genetic complementation","volume":"140","author":"Milbradt","year":"1994","journal-title":"Microbiology"},{"key":"10.1016\/j.bcp.2020.114213_b0935","doi-asserted-by":"crossref","first-page":"2475","DOI":"10.1271\/bbb.69.2475","article-title":"Isolation and Characterization of Glucose Derepressed Invertase Mutants from Schizosaccharomyces pombe","volume":"69","author":"Kig","year":"2005","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b0940","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1128\/JB.180.3.674-679.1998","article-title":"std1, a Gene Involved in Glucose Transport in Schizosaccharomyces pombe","volume":"180","author":"Mehta","year":"1998","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b0945","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1038\/nsmb.1452","article-title":"Fission yeast SWI\/SNF and RSC complexes show compositional and functional differences from budding yeast","volume":"15","author":"Monahan","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0950","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1007\/BF00268666","article-title":"Resistance to 2-deoxyglucose in yeast: a direct selection of mutants lacking glucose-phosphorylating enzymes","volume":"157","author":"Lobo","year":"1977","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.bcp.2020.114213_b0955","first-page":"235","article-title":"A Kluyveromyces marxianus 2-deoxyglucose-resistant mutant with enhanced activity of xylose utilization","volume":"18","author":"Suprayogi","year":"2015","journal-title":"Int. Microbiol. Off. J. Span. Soc. Microbiol."},{"key":"10.1016\/j.bcp.2020.114213_b0960","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1186\/1471-2164-13-239","article-title":"Yeast glucose pathways converge on the transcriptional regulation of trehalose biosynthesis","volume":"13","author":"Apweiler","year":"2012","journal-title":"BMC Genomics"},{"key":"10.1016\/j.bcp.2020.114213_b0965","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/0003-9861(77)90544-6","article-title":"Physiological role of glucose-phosphorylating enzymes in Saccharomyces cerevisiae","volume":"182","author":"Lobo","year":"1977","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bcp.2020.114213_b0970","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/0006-3002(58)90245-2","article-title":"Substrate specificity and some other properties of baker\u2019s yeast hexokinase","volume":"30","author":"Sols","year":"1958","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b0975","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1007\/BF00337871","article-title":"Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast","volume":"178","author":"Entian","year":"1980","journal-title":"Mol. Gen. Genet. MGG."},{"key":"10.1016\/j.bcp.2020.114213_b0980","first-page":"4046","article-title":"Effects of null mutations in the hexokinase genes of Saccharomyces cerevisiae on catabolite repression","volume":"6","author":"Ma","year":"1986","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b0985","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1007\/BF00383509","article-title":"Cloning and restriction analysis of the hexokinase PII gene of the yeast Saccharomyces cerevisiae","volume":"194","author":"Fr\u00f6hlich","year":"1984","journal-title":"Mol. Gen. Genet. MGG."},{"key":"10.1016\/j.bcp.2020.114213_b0990","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1128\/MMBR.00012-16","article-title":"The Expanding Landscape of Moonlighting Proteins in Yeasts","volume":"80","author":"Gancedo","year":"2016","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.bcp.2020.114213_b0995","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/S0014-5793(98)00872-2","article-title":"The hexokinase 2 protein participates in regulatory DNA-protein complexes necessary for glucose repression of the SUC2 gene in Saccharomyces cerevisiae","volume":"434","author":"Herrero","year":"1998","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bcp.2020.114213_b1000","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/S0014-5793(98)00289-0","article-title":"Hexokinase PII has a double cytosolic-nuclear localisation in Saccharomyces cerevisiae","volume":"425","author":"Randez-Gil","year":"1998","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bcp.2020.114213_b1005","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1042\/bj3550625","article-title":"The hexokinase 2 protein regulates the expression of the GLK1, HXK1 and HXK2 genes of Saccharomyces cerevisiae","volume":"355","author":"Rodr\u00edguez","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.bcp.2020.114213_b1010","doi-asserted-by":"crossref","first-page":"6243","DOI":"10.1074\/jbc.M114.595074","article-title":"Protein Kinase Ymr291w\/Tda1 Is Essential for Glucose Signaling in Saccharomyces cerevisiae on the Level of Hexokinase Isoenzyme ScHxk2 Phosphorylation*","volume":"290","author":"Kaps","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b1015","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1042\/BJ20100663","article-title":"Functional domains of yeast hexokinase 2","volume":"432","author":"Pel\u00e1ez","year":"2010","journal-title":"Biochem. J."},{"key":"10.1016\/j.bcp.2020.114213_b1020","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1016\/S0021-9258(19)68278-5","article-title":"Genetic evidence for a role of hexokinase isozyme PII in carbon catabolite repression in Saccharomyces cerevisiae","volume":"257","author":"Entian","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b1025","first-page":"5643","article-title":"The residual enzymatic phosphorylation activity of hexokinase II mutants is correlated with glucose repression in Saccharomyces cerevisiae","volume":"9","author":"Ma","year":"1989","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b1030","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1111\/j.1432-1033.1991.tb16149.x","article-title":"Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinases PI and PII","volume":"199","author":"Rose","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b1035","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1099\/13500872-145-3-703","article-title":"Novel alleles of yeast hexokinase PII with distinct effects on catalytic activity and catabolite repression of SUC2","volume":"145","author":"Hohmann","year":"1999","journal-title":"Microbiology"},{"key":"10.1016\/j.bcp.2020.114213_b1040","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/0014-5793(77)81014-4","article-title":"Characterization of a phosphatase specific for 2-deoxyglucose-6-phosphate in a yeast mutant","volume":"83","author":"Martin","year":"1977","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bcp.2020.114213_b1045","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1002\/yea.320111303","article-title":"DOGR1 and DOGR2: two genes from Saccharomyces cerevisiae that confer 2-deoxyglucose resistance when overexpressed","volume":"11","author":"Randez-Gil","year":"1995","journal-title":"Yeast"},{"key":"10.1016\/j.bcp.2020.114213_b1050","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1002\/yea.320100907","article-title":"Molecular characterization of a gene that confers 2-deoxyglucose resistance in yeast","volume":"10","author":"Sanz","year":"1994","journal-title":"Yeast"},{"key":"10.1016\/j.bcp.2020.114213_b1055","doi-asserted-by":"crossref","first-page":"18678","DOI":"10.1074\/jbc.M115.657916","article-title":"Functional Diversity of Haloacid Dehalogenase Superfamily Phosphatases from Saccharomyces cerevisiae: biochemical, structural, and evolutionary insights","volume":"290","author":"Kuznetsova","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b1060","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1128\/jb.173.6.2045-2052.1991","article-title":"Extragenic suppressors of yeast glucose derepression mutants leading to constitutive synthesis of several glucose-repressible enzymes","volume":"173","author":"Schuller","year":"1991","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bcp.2020.114213_b1065","first-page":"5034","article-title":"Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein","volume":"9","author":"Celenza","year":"1989","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b1070","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/b97215","article-title":"Membrane trafficking of yeast transporters: mechanisms and physiological control of downregulation","volume":"9","author":"Haguenauer-Tsapis","year":"2004","journal-title":"Top. Curr. Genet."},{"key":"10.1016\/j.bcp.2020.114213_b1075","doi-asserted-by":"crossref","first-page":"1811","DOI":"10.1083\/jcb.201610094","article-title":"Multilevel regulation of an alpha-arrestin by glucose depletion controls hexose transporter endocytosis","volume":"216","author":"Hovsepian","year":"2017","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b1080","doi-asserted-by":"crossref","first-page":"14973","DOI":"10.1074\/jbc.M116.733923","article-title":"Regulation of the Yeast Hxt6 Hexose Transporter by the Rod1 alpha-Arrestin, the Snf1 Protein Kinase, and the Bmh 2 14\u20133-3 Protein","volume":"291","author":"Llopis-Torregrosa","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b1085","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20030515","article-title":"AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking","volume":"20","author":"O\u2019Donnell","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bcp.2020.114213_b1090","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1128\/MCB.01183-14","article-title":"2-Deoxyglucose impairs Saccharomyces cerevisiae growth by stimulating Snf1-regulated and alpha-arrestin-mediated trafficking of hexose transporters 1 and 3","volume":"35","author":"O\u2019Donnell","year":"2015","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b1095","doi-asserted-by":"crossref","unstructured":"J. Shinoda, Y. Kikuchi, Rod1, an arrestin-related protein, is phosphorylated by Snf1-kinase in Saccharomyces cerevisiae, Biochem Biophys Res Commun. 364 (2007) 258\u2013263. https:\/\/doi.org\/S0006-291X(07)02129-8 [pii] 10.1016\/j.bbrc.2007.09.134.","DOI":"10.1016\/j.bbrc.2007.09.134"},{"key":"10.1016\/j.bcp.2020.114213_b1100","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1016\/j.molcel.2013.01.035","article-title":"AMPK-dependent degradation of TXNIP upon energy stress leads to enhanced glucose uptake via GLUT1","volume":"49","author":"Wu","year":"2013","journal-title":"Mol. Cell."},{"key":"10.1016\/j.bcp.2020.114213_b1105","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1007\/BF00382091","article-title":"Isolation and characterization of a pleiotropic glucose repression resistant mutant of Saccharomyces cerevisiae","volume":"193","author":"Bailey","year":"1984","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.bcp.2020.114213_b1110","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/BF00267449","article-title":"Glycolytic enzymes and intermediates in carbon catabolite repression mutants of Saccharomyces cerevisiae","volume":"177","author":"Entian","year":"1980","journal-title":"Mol. Gen. Genet. MGG."},{"key":"10.1016\/j.bcp.2020.114213_b1115","doi-asserted-by":"crossref","first-page":"3230","DOI":"10.1091\/mbc.e03-03-0135","article-title":"Grr1-dependent inactivation of Mth1 mediates glucose-induced dissociation of Rgt1 from HXT gene promoters","volume":"14","author":"Flick","year":"2003","journal-title":"Mol. Biol. Cell."},{"key":"10.1016\/j.bcp.2020.114213_b1120","doi-asserted-by":"crossref","first-page":"8994","DOI":"10.1128\/MCB.24.20.8994-9005.2004","article-title":"Regulation and recognition of SCFGrr1 targets in the glucose and amino acid signaling pathways","volume":"24","author":"Spielewoy","year":"2004","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.bcp.2020.114213_b1125","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.bbamcr.2004.09.027","article-title":"A hitchhiker\u2019s guide to the cullin ubiquitin ligases: SCF and its kin","volume":"1695","author":"Willems","year":"2004","journal-title":"Biochim. Biophys. Acta BBA - Mol. Cell Res."},{"key":"10.1016\/j.bcp.2020.114213_b1130","doi-asserted-by":"crossref","unstructured":"J.A. Benanti, S.K. Cheung, M.C. Brady, D.P. Toczyski, A proteomic screen reveals SCFGrr1 targets that regulate the glycolytic-gluconeogenic switch, Nat Cell Biol. 9 (2007) 1184\u20131191. https:\/\/doi.org\/ncb1639 [pii] 10.1038\/ncb1639.","DOI":"10.1038\/ncb1639"},{"key":"10.1016\/j.bcp.2020.114213_b1135","doi-asserted-by":"crossref","first-page":"ra64","DOI":"10.1126\/scisignal.2005000","article-title":"Phosphoproteomic analysis identifies proteins involved in transcription-coupled mRNA decay as targets of Snf1 signaling","volume":"7","author":"Braun","year":"2014","journal-title":"Sci. Signal."},{"key":"10.1016\/j.bcp.2020.114213_b1140","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/S0021-9258(18)93917-7","article-title":"Studies on the mechanism of resistance to 2-deoxy-D-glucose in mammalian cell cultures","volume":"237","author":"Barban","year":"1962","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b1145","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/0006-3002(62)91065-X","article-title":"Induced resistance to 2-deoxy-d-glucose in cell cultures","volume":"65","author":"Barban","year":"1962","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bcp.2020.114213_b1150","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/0304-4165(66)90064-X","article-title":"Differential action of hormones on induced resistance to 2-deoxy-d-glucose in mammalian cell cultures","volume":"115","author":"Barban","year":"1966","journal-title":"Biochim. Biophys. Acta BBA - Gen. Subj."},{"key":"10.1016\/j.bcp.2020.114213_b1155","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0014-4827(67)90204-2","article-title":"The correlation of resistance to 2-deoxyglucose with alkaline phosphatase levels in a human cell line","volume":"47","author":"Morrow","year":"1967","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bcp.2020.114213_b1160","doi-asserted-by":"crossref","first-page":"36149","DOI":"10.1074\/jbc.M605449200","article-title":"Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family","volume":"281","author":"Kuznetsova","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2020.114213_b1165","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1042\/BJ20100174","article-title":"HDHD1, which is often deleted in X-linked ichthyosis, encodes a pseudouridine-5\u2019-phosphatase","volume":"431","author":"Preumont","year":"2010","journal-title":"Biochem. J."},{"key":"10.1016\/j.bcp.2020.114213_b1170","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1002\/jcp.1040710105","article-title":"Patterns of resistance to 2-deoxy-D-glucose in pig kidney cells","volume":"71","author":"Bailey","year":"1968","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.bcp.2020.114213_b1175","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1158\/1535-7163.MCT-06-0407","article-title":"Hypoxia-inducible factor-1 confers resistance to the glycolytic inhibitor 2-deoxy-D-glucose","volume":"6","author":"Maher","year":"2007","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.bcp.2020.114213_b1180","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.semcdb.2015.09.008","article-title":"Research into cancer metabolomics: towards a clinical metamorphosis","volume":"43","author":"Olivares","year":"2015","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.bcp.2020.114213_b9005","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/0042-6822(73)90340-1","article-title":"Effects of 2-deoxy-d-glucose on herpes simplex virus replication","volume":"52","author":"Courtney","year":"1973","journal-title":"Virology"},{"key":"10.1016\/j.bcp.2020.114213_b9010","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1042\/bj1840113","article-title":"Interference with glycosylation of glycoproteins. Inhibition of formation of lipid-linked oligosaccharides in vivo","volume":"184","author":"Datema","year":"1979","journal-title":"Biochem J."},{"key":"10.1016\/j.bcp.2020.114213_b9015","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/0042-6822(78)90250-7","article-title":"Effects of glucosamine, 2-deoxyglucose, and tunicamycin on glycosylation, sulfation, and assembly of influenza viral proteins","volume":"84","author":"Nakamura","year":"1978","journal-title":"Virology"},{"key":"10.1016\/j.bcp.2020.114213_b9020","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1111\/j.1432-1033.1976.tb10955.x","article-title":"Interference of nucleoside diphosphate derivatives of 2-deoxy-D-glucose with the glycosylation of virus-specific glycoproteins in vivo","volume":"70","author":"Schmidt","year":"1976","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bcp.2020.114213_b9025","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1128\/jvi.32.2.412-419.1979","article-title":"Inhibition of Rous sarcoma virus replication by 2-deoxyglucose and tunicamycin: identification of an unglycosylated env gene product","volume":"32","author":"Stohrer","year":"1979","journal-title":"J. Virol."}],"container-title":["Biochemical Pharmacology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006295220304494?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006295220304494?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T13:12:45Z","timestamp":1757769165000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006295220304494"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,12]]},"references-count":241,"alternative-id":["S0006295220304494"],"URL":"https:\/\/doi.org\/10.1016\/j.bcp.2020.114213","relation":{},"ISSN":["0006-2952"],"issn-type":[{"value":"0006-2952","type":"print"}],"subject":[],"published":{"date-parts":[[2020,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cellular toxicity of the metabolic inhibitor 2-deoxyglucose and associated resistance mechanisms","name":"articletitle","label":"Article Title"},{"value":"Biochemical Pharmacology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bcp.2020.114213","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"114213"}}