Bibliografías temáticas / Glycolysis

Literatura académica sobre el tema "Glycolysis"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 29 de julio de 2024

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Artículos de revistas sobre el tema "Glycolysis"

1

Reiter, Russel J., Ramaswamy Sharma y Sergio Rosales-Corral. "Anti-Warburg Effect of Melatonin: A Proposed Mechanism to Explain its Inhibition of Multiple Diseases". International Journal of Molecular Sciences 22, n.º 2 (14 de enero de 2021): 764. http://dx.doi.org/10.3390/ijms22020764.

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Glucose is an essential nutrient for every cell but its metabolic fate depends on cellular phenotype. Normally, the product of cytosolic glycolysis, pyruvate, is transported into mitochondria and irreversibly converted to acetyl coenzyme A by pyruvate dehydrogenase complex (PDC). In some pathological cells, however, pyruvate transport into the mitochondria is blocked due to the inhibition of PDC by pyruvate dehydrogenase kinase. This altered metabolism is referred to as aerobic glycolysis (Warburg effect) and is common in solid tumors and in other pathological cells. Switching from mitochondrial oxidative phosphorylation to aerobic glycolysis provides diseased cells with advantages because of the rapid production of ATP and the activation of pentose phosphate pathway (PPP) which provides nucleotides required for elevated cellular metabolism. Molecules, called glycolytics, inhibit aerobic glycolysis and convert cells to a healthier phenotype. Glycolytics often function by inhibiting hypoxia-inducible factor-1α leading to PDC disinhibition allowing for intramitochondrial conversion of pyruvate into acetyl coenzyme A. Melatonin is a glycolytic which converts diseased cells to the healthier phenotype. Herein we propose that melatonin’s function as a glycolytic explains its actions in inhibiting a variety of diseases. Thus, the common denominator is melatonin’s action in switching the metabolic phenotype of cells.
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Chowdhury, Shomeek, Stephen Hepper, Mudassir K. Lodi, Milton H. Saier y Peter Uetz. "The Protein Interactome of Glycolysis in Escherichia coli". Proteomes 9, n.º 2 (6 de abril de 2021): 16. http://dx.doi.org/10.3390/proteomes9020016.

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Glycolysis is regulated by numerous mechanisms including allosteric regulation, post-translational modification or protein-protein interactions (PPI). While glycolytic enzymes have been found to interact with hundreds of proteins, the impact of only some of these PPIs on glycolysis is well understood. Here we investigate which of these interactions may affect glycolysis in E. coli and possibly across numerous other bacteria, based on the stoichiometry of interacting protein pairs (from proteomic studies) and their conservation across bacteria. We present a list of 339 protein-protein interactions involving glycolytic enzymes but predict that ~70% of glycolytic interactors are not present in adequate amounts to have a significant impact on glycolysis. Finally, we identify a conserved but uncharacterized subset of interactions that are likely to affect glycolysis and deserve further study.
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3

Connett, R. J. "Glycolytic regulation during an aerobic rest-to-work transition in dog gracilis muscle". Journal of Applied Physiology 63, n.º 6 (1 de diciembre de 1987): 2366–74. http://dx.doi.org/10.1152/jappl.1987.63.6.2366.

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Glycogen phosphorylase activity and several glycolytic intermediates were measured at rest and after 5, 10, 15, 30, 60, and 180 s of twitch stimulation at 4 Hz in fast-frozen samples of gracilis muscle. During an initial burst of glycolysis (0–5 s) only 3-phosphoglycerate and lactate accumulate. These changes are reversed during the period of low glycolytic flux (5–30 s). During a second burst of glycolysis (30–60 s) most glycolytic intermediates increase. The levels of glycogen phosphorylase a changes in parallel with the initial burst of glycolysis but remain at resting levels throughout the second burst. The phosphoglycerate mutase-enolase steps deviate from equilibrium during the initial burst of glycolysis, suggesting a transiently rate-limiting role. Analysis using a model of phosphofructokinase kinetics indicates that combined changes in cytosolic pH (R. J. Connett, J. Appl. Physiol. 63: 2360–2365, 1987) and free [ADP] and [AMP] can account for the initial burst of glycolysis. The second burst of glycolysis requires other regulatory factors. It is concluded that an initial alkalization is a major regulatory factor in the early burst of glycolysis during a rest-to-work transition in red muscle.
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Ghazi, Susan, Marcello Polesel y Andrew M. Hall. "Targeting glycolysis in proliferative kidney diseases". American Journal of Physiology-Renal Physiology 317, n.º 6 (1 de diciembre de 2019): F1531—F1535. http://dx.doi.org/10.1152/ajprenal.00460.2019.

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Glycolytic activity is increased in proliferating cells, leading to the concept that glycolysis could be a therapeutic target in cystic diseases and kidney cancer. Preclinical studies using the glucose analog 2-deoxy-d-glucose have shown promise; however, inhibiting glycolysis in humans is unlikely to be without risks. While proximal tubules are predominantly aerobic, later segments are more glycolytic. Understanding exactly where and why glycolysis is important in the physiology of the distal nephron is thus crucial in predicting potential adverse effects of glycolysis inhibitors. Live imaging techniques could play an important role in the process of characterizing cellular metabolism in the functioning kidney. The goal of this review is to briefly summarize recent findings on targeting glycolysis in proliferative kidney diseases and to highlight the necessity for future research focusing on glycolysis in the healthy kidney.
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Zhan, Huiwang David, Jane Borleis, Chris Janetopoulos y Peter Devreotes. "Abstract 288: Glycolysis is enriched to propagating waves in cell cortex as a new mechanism for cancer progression". Cancer Research 83, n.º 7_Supplement (4 de abril de 2023): 288. http://dx.doi.org/10.1158/1538-7445.am2023-288.

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Abstract Tumors preferentially metabolize glucose anaerobically through glycolysis with lower ATP production efficiency rather than aerobically even when oxygen is available. This was reported by Otto Warburg 100 years ago, yet the mechanism is hitherto not well-understood. Glycolysis is canonically thought to occur only in cytosol; if and how it is regulated by the actin cytoskeletal network is controversial. I found that, in epithelial cells, 6 of the 9 glycolytic enzymes (HK, PFK, ALDO, GAPDH, ENO, and PK, others not tested) are enriched at newly formed LifeAct labeled waves and protrusions, where mitochondria are barely detected by Mito-Tracker. The application of glycolysis inhibitors but not oxidative phosphorylation inhibitors abolishes cell migration. These results indicate that cells rely on the local ATP production from glycolysis enriched in the cortical waves and protrusions to move. We visualized and measured glycolysis production in confocal and TIRF microscopes using a series of biosensors for ATP, NADH/NAD+ ratio, and pyruvate. We then found glycolysis was enhanced by perturbations that increase wave formation such as EGF/Insulin stimulation or recruiting ActA to membrane, and reduced by wave decrease from PI3K inhibition, hyper- and hypo-osmotic shock, or F-actin assembly inhibition. This suggests that enriching glycolytic enzymes on waves results in higher glycolysis production. We do not think the changes of glycolysis by wave perturbations are merely due to direct regulation on glycolytic enzymes by canonical signaling pathways (e.g., Ras-PI3K-AKT), since ActA recruitment or F-actin inhibition does not lead to acute changes in these signaling pathways but mainly causes the assembly or disassembly of the F-actin/glycolytic waves. These findings together lead to our new theory that energy production from glycolysis is enhanced by recruiting the glycolytic enzymes to the waves and protrusions on the cell cortex. This is potentially paradigm-shifting because for many decades glycolysis - one of the two major ways in a cell to produce ATP - has been thought to only occur in cytosol. Interestingly, we also found glycolytic enzymes enriched in F-actin labeled protrusions of Dictyostelium cells, which indicates that this can possibly be an evolutionally conserved mechanism. Additionally, we investigated non-cancer MCF-10A cells (M1) and a series of M1-derived cancer cell lines (M2 - M4) with increased metastatic index and cancer malignancy, and found a sequential increase in actin wave and glycolysis activities from M1 to M4 cells. Cancer cells such as M3 had a larger drop in glycolysis than non-cancer parental M1 cells upon wave inhibition. These results provide a new explanation for the Warburg effect that increased cortical waves in cancer cells will accelerate and improve glycolysis, which will not only greatly contribute to our understanding of cancer but also the design of new interventions. Citation Format: Huiwang David Zhan, Jane Borleis, Chris Janetopoulos, Peter Devreotes. Glycolysis is enriched to propagating waves in cell cortex as a new mechanism for cancer progression [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2023; Part 1 (Regular and Invited Abstracts); 2023 Apr 14-19; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2023;83(7_Suppl):Abstract nr 288.
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6

Qu, Hengdong, Junli Liu, Di Zhang, Ruoyan Xie, Lijuan Wang y Jian Hong. "Glycolysis in Chronic Liver Diseases: Mechanistic Insights and Therapeutic Opportunities". Cells 12, n.º 15 (26 de julio de 2023): 1930. http://dx.doi.org/10.3390/cells12151930.

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Chronic liver diseases (CLDs) cover a spectrum of liver diseases, ranging from nonalcoholic fatty liver disease to liver cancer, representing a growing epidemic worldwide with high unmet medical needs. Glycolysis is a conservative and rigorous process that converts glucose into pyruvate and sustains cells with the energy and intermediate products required for diverse biological activities. However, abnormalities in glycolytic flux during CLD development accelerate the disease progression. Aerobic glycolysis is a hallmark of liver cancer and is responsible for a broad range of oncogenic functions including proliferation, invasion, metastasis, angiogenesis, immune escape, and drug resistance. Recently, the non-neoplastic role of aerobic glycolysis in immune activation and inflammatory disorders, especially CLD, has attracted increasing attention. Several key mediators of aerobic glycolysis, including HIF-1α and pyruvate kinase M2 (PKM2), are upregulated during steatohepatitis and liver fibrosis. The pharmacological inhibition or ablation of PKM2 effectively attenuates hepatic inflammation and CLD progression. In this review, we particularly focused on the glycolytic and non-glycolytic roles of PKM2 in the progression of CLD, highlighting the translational potential of a glycolysis-centric therapeutic approach in combating CLD.
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Chacon-Barahona, Jonathan A., Jeffrey P. MacKeigan y Nathan J. Lanning. "Unique Metabolic Contexts Sensitize Cancer Cells and Discriminate between Glycolytic Tumor Types". Cancers 15, n.º 4 (11 de febrero de 2023): 1158. http://dx.doi.org/10.3390/cancers15041158.

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Cancer cells utilize variable metabolic programs in order to maintain homeostasis in response to environmental challenges. To interrogate cancer cell reliance on glycolytic programs under different nutrient availabilities, we analyzed a gene panel containing all glycolytic genes as well as pathways associated with glycolysis. Using this gene panel, we analyzed the impact of an siRNA library on cellular viability in cells containing only glucose or only pyruvate as the major bioenergetic nutrient source. From these panels, we aimed to identify genes that elicited conserved and glycolysis-dependent changes in cellular bioenergetics across glycolysis-promoting and OXPHOS-promoting conditions. To further characterize gene sets within this panel and identify similarities and differences amongst glycolytic tumor RNA-seq profiles across a pan-cancer cohort, we then used unsupervised statistical classification of RNA-seq profiles for glycolytic cancers and non-glycolytic cancer types. Here, Kidney renal clear cell carcinoma (KIRC); Head and Neck squamous cell carcinoma (HNSC); and Lung squamous cell carcinoma (LUSC) defined the glycolytic cancer group, while Prostate adenocarcinoma (PRAD), Thyroid carcinoma (THCA), and Thymoma (THYM) defined the non-glycolytic cancer group. These groups were defined based on glycolysis scoring from previous studies, where KIRC, HNSC, and LUSC had the highest glycolysis scores, meanwhile, PRAD, THCA, and THYM had the lowest. Collectively, these results aimed to identify multi-omic profiles across cancer types with demonstrated variably glycolytic rates. Our analyses provide further support for strategies aiming to classify tumors by metabolic phenotypes in order to therapeutically target tumor-specific vulnerabilities.
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McDowell, Ruth E., Kulwant S. Aulak, Allaa Almoushref, Celia A. Melillo, Brittany E. Brauer, Jennie E. Newman, Adriano R. Tonelli y Raed A. Dweik. "Platelet glycolytic metabolism correlates with hemodynamic severity in pulmonary arterial hypertension". American Journal of Physiology-Lung Cellular and Molecular Physiology 318, n.º 3 (1 de marzo de 2020): L562—L569. http://dx.doi.org/10.1152/ajplung.00389.2019.

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Group 1 pulmonary hypertension (PH), i.e., pulmonary arterial hypertension (PAH), is associated with a metabolic shift favoring glycolysis in cells comprising the lung vasculature as well as skeletal muscle and right heart. We sought to determine whether this metabolic switch is also detectable in circulating platelets from PAH patients. We used Seahorse Extracellular Flux to measure bioenergetics in platelets isolated from group 1 PH (PAH), group 2 PH, patients with dyspnea and normal pulmonary artery pressures, and healthy controls. We show that platelets from group 1 PH patients exhibit enhanced basal glycolysis and lower glycolytic reserve compared with platelets from healthy controls but do not differ from platelets of group 2 PH or dyspnea patients without PH. Although we were unable to identify a glycolytic phenotype unique to platelets from PAH patients, we found that platelet glycolytic metabolism correlated with hemodynamic severity only in group 1 PH patients, supporting the known link between PAH pathology and altered glycolytic metabolism and extending this association to ex vivo platelets. Pulmonary artery pressure and pulmonary vascular resistance in patients with group 1 PH were directly associated with basal platelet glycolysis and inversely associated with maximal and reserve glycolysis, suggesting that PAH progression reduces the capacity for glycolysis even while demanding an increase in glycolytic metabolism. Therefore, platelets may provide an easy-to-harvest, real-time window into the metabolic shift occurring in the lung vasculature and represent a useful surrogate for interrogating the glycolytic shift central to PAH pathology.
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9

Ma, Yibao, Wei Wang, Michael Idowu, Unsong Oh, Xiang-Yang Wang, Sarah Temkin y Xianjun Fang. "Ovarian Cancer Relies on Glucose Transporter 1 to Fuel Glycolysis and Growth: Anti-Tumor Activity of BAY-876". Cancers 11, n.º 1 (31 de diciembre de 2018): 33. http://dx.doi.org/10.3390/cancers11010033.

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The recent progresses in understanding of cancer glycolytic phenotype have offered new strategies to manage ovarian cancer and other malignancies. However, therapeutic targeting of glycolysis to treat cancer remains unsuccessful due to complex mechanisms of tumor glycolysis and the lack of selective, potent and safe glycolytic inhibitors. Recently, BAY-876 was identified as a new-generation inhibitor of glucose transporter 1 (GLUT1), a GLUT isoform commonly overexpressed but functionally poorly defined in ovarian cancer. Notably, BAY-876 has not been evaluated in any cell or preclinical animal models since its discovery. We herein took advantage of BAY-876 and molecular approaches to study GLUT1 regulation, targetability, and functional relevance to cancer glycolysis. The anti-tumor activity of BAY-876 was evaluated with ovarian cancer cell line- and patient-derived xenograft (PDX) models. Our results show that inhibition of GLUT1 is sufficient to block basal and stress-regulated glycolysis, and anchorage-dependent and independent growth of ovarian cancer cells. BAY-876 dramatically inhibits tumorigenicity of both cell line-derived xenografts and PDXs. These studies provide direct evidence that GLUT1 is causally linked to the glycolytic phenotype in ovarian cancer. BAY-876 is a potent blocker of GLUT1 activity, glycolytic metabolism and ovarian cancer growth, holding promise as a novel glycolysis-targeted anti-cancer agent.
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10

Mao, Na, Honghao Yang, Jie Yin, Yaqian Li, Fuyu Jin, Tian Li, Xinyu Yang et al. "Glycolytic Reprogramming in Silica-Induced Lung Macrophages and Silicosis Reversed by Ac-SDKP Treatment". International Journal of Molecular Sciences 22, n.º 18 (17 de septiembre de 2021): 10063. http://dx.doi.org/10.3390/ijms221810063.

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Glycolytic reprogramming is an important metabolic feature in the development of pulmonary fibrosis. However, the specific mechanism of glycolysis in silicosis is still not clear. In this study, silicotic models and silica-induced macrophage were used to elucidate the mechanism of glycolysis induced by silica. Expression levels of the key enzymes in glycolysis and macrophage activation indicators were analyzed by Western blot, qRT-PCR, IHC, and IF analyses, and by using a lactate assay kit. We found that silica promotes the expression of the key glycolysis enzymes HK2, PKM2, LDHA, and macrophage activation factors iNOS, TNF-α, Arg-1, IL-10, and MCP1 in silicotic rats and silica-induced NR8383 macrophages. The enhancement of glycolysis and macrophage activation induced by silica was reduced by Ac-SDKP or siRNA-Ldha treatment. This study suggests that Ac-SDKP treatment can inhibit glycolytic reprogramming in silica-induced lung macrophages and silicosis.
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Tesis sobre el tema "Glycolysis"

1

Graham, James William Alexander. "Mitochondrial glycolysis in plants". Thesis, University of Oxford, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.445769.

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Hale, R. D. "Glycolysis in Crithidia fasciculata". Thesis, University of Liverpool, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.234866.

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Robinson, Andrew James Cave. "Pyruvate kinase & glycolysis in potato". Thesis, University of Cambridge, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335799.

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Pearce, Amanda K. "Regulation of glycolysis in Saccharomyces cerevisiae". Thesis, University of Aberdeen, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301297.

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This thesis extends the work of Crimmins (1995) on the control of glycolytic flux in yeast by the enzymes 6-phosphofructo-1-kinase and pyruvate kinase (Pyk1p). This study also examines the influence of Pf1kp and Pyk1p upon yeast resistance to the weak acid preservative, benzoic acid. In Saccharomyces cerevisiae, Pyk1p is encoded by PYK1, and the α and β subunits of Pf1kp are encoded by PFK1 and PFK2, respectively. To test the influence of these genes upon glycolytic control, an isogenic set of S. cerevisiae mutants were utilised in which PYK1, PFK1 and PFK2 expression is dependent on the PGK1 promoter. Increased Pf1k levels had little effect upon rates of glucose utilisation or ethanol production during fermentative growth. However, overexpressing Pyk1p resulted in an increased growth rate and an increase in glycolytic flux. This suggests that Pyk1p, but not Pf1kp, exerts some degree of control over the glycolytic flux under these conditions. The effects of reducing Pf1kp and Pyk1p levels were also studied by placing PYK1, PFK1 and PFK2 under the control of the weak PGK1Δuas promoter. The double Pf1kp mutant showed no significant changes in doubling time, ethanol production or glucose consumption. However, a mutant with a 3-fold reduction ion Pyk1p levels displayed slower growth rates and reduced glycolytic flux. In addition, there was an imbalance in the carbon flow in this mutant, with reductions in ethanol and glycerol production evident, along with increased TCA cycle activity. Hence, while Pf1kp levels did not affect cell physiology significantly under the conditions studied, reduced Pyk1p levels seemed to disturb glycolytic flux and carbon flow. Decreased Pf1kp levels caused an increase in the sensitivity of yeast cells to benzoate, whereas the Pyk1p mutant was not affected. This confirmed that benzoic acid specifically inhibits Pf1kp rather than glycolysis in general.
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Tandon, Preeti. "S6K1 mediates oncogenic glycolysis in Pten deficient leukemia". University of Cincinnati / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1320682200.

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Xintaropoulou, Chrysi. "Targeting aerobic glycolysis in breast and ovarian cancer". Thesis, University of Edinburgh, 2017. http://hdl.handle.net/1842/29525.

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Cancer cells, unlike normal tissue, frequently rely on glycolysis for the production of energy and the metabolic intermediates required for their growth regardless of cellular oxygenation levels. This metabolic reconfiguration, termed the Warburg effect, provides a potential strategy to preferentially target tumours from a therapeutic perspective. The present study sought to investigate the glycolytic phenotype of breast and ovarian cancer, and assess the possibility of exploiting several glycolytic targets therapeutically. Initially the growth dependency of breast and ovarian cancer cells on the availability of glucose was established. An array of 10 compounds reported to inhibit key enzymes of the glycolytic pathway were investigated and compared against an extended panel of breast and ovarian cancer cell line models. All inhibitors investigated, targeted against multiple points of the pathway, were shown to block the glycolytic pathway as demonstrated by glucose accumulation in the culture media combined with decreased lactate secretion, and attenuated breast and ovarian cancer cell proliferation in a concentration dependent manner. Furthermore their mechanism of action was investigated by flow cytometric analysis and their antiproliferative effect was associated with induction of apoptosis and G0/G1 cell cycle arrest. The glycolytic inhibitors were further assessed in combination strategies with established chemotherapeutic and targeted agents and several synergistic interactions, characterised by low combination index values, were revealed. Among them, 3PO (a novel PFKFB3 inhibitor) enhanced the effect of cisplatin in both platinum sensitive and platinum resistant ovarian cancer cells suggesting a strategy for treatment of platinum resistant disease. Furthermore robust synergy was identified between IOM-1190 (a novel GLUT1 inhibitor) and metformin, an antidiabetic inhibitor of oxidative phosphorylation, resulting in strong inhibition of breast cancer cell growth. This combination is proposed for the treatment of highly aggressive triple negative breast tumours. An additional objective of this research was to investigate the effect of the oxygen level on sensitivity to glycolysis inhibition. Breast cancer cells were found to be more sensitive to glycolysis inhibition in high oxygen conditions. This enhanced resistance at low oxygen levels was associated with upregulation of the targeted glycolytic enzymes as demonstrated at both the mRNA (by gene expression microarray profiling, Illumina BeadArrays) and protein level (by Western blotting). Manipulation of LDHA (Lactate Dehydrogenase A) by siRNA knockdown provided further evidence that downregulation of this target was sufficient to significantly suppress breast cancer cell proliferation. Finally, the expression of selected glycolytic targets was examined in a clinical tissue microarray set of a large cohort of ovarian tumours using quantitative immunofluorescence technology, AQUA. The role of the glycolytic phenotype in ovarian cancer was suggested and interesting associations between the glycolytic profile and clear cell and endometrioid ovarian cancers revealed. Increased PKM2 (Pyruvate kinase isozyme M2) and LDHA expression were demonstrated in clear cell tumours and also low expression of these enzymes was significantly correlated with improved survival of endometrioid ovarian cancer patients. Taken together the findings of this study support the glycolytic pathway as a legitimate target for further investigation in breast and ovarian cancer treatment.
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Stefansson, G. "Effects of gases on post-mortem glycolysis in meats". Thesis, University of Leeds, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.371847.

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Long, Heidi Sarah. "Glycolysis and the control of pulmonary tone during hypoxia". Thesis, King's College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.250174.

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Shen, Qingwu. "AMP-activated protein kinase, postmortem glycolysis, and PSE meat". Laramie, Wyo. : University of Wyoming, 2007. http://proquest.umi.com/pqdweb?did=1338871331&sid=1&Fmt=2&clientId=18949&RQT=309&VName=PQD.

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Nairn, Jacqueline. "Phosphoglycerate mutases from microorganisms". Thesis, University of Stirling, 1992. http://hdl.handle.net/1893/22851.

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Phosphoglycerate mutase catalyses the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in the glycolytic/gluconeogenic pathways. There are two main types of phosphoglycerate mutase: 2,3-bisphosphoglycerate dependent and 2,3-bisphosphoglycerate independent. The enzyme from Saccharomyces cerevisiae has been extensively studied: the high resolution crystal structure of this tetrameric enzyme, subunit Mr 27,000, is known (Winn et al., 1981), the amino acid sequence has been determined (Fothergill and Harkins, 1982) and the gene encoding the enzyme has been isolated and sequenced (White and Fothergill-Gilmore, 1988). Phosphoglycerate mutase from the fission yeast, Schizosaccharomyces pombe, has been purified and partially characterised (Price et al., 1985; Johnson and Price, 1987). It is monomeric, of Mr 23,000, and the sequences of a number of peptides produced by digestion of this enzyme have been determined (Fothergill and Dunbar. unpublished). Alignment of these sequenced peptides with the sequence of S.cerevisiae phosphoglycerate mutase shows 40% identity and the conservation of a number of residues which are known to be essential to the activity of the S. cerevisia enzyme e. g. His-8, Arg-7, Ser-11. Thr-20 and Arg-59. Attempts were made to isolate and sequence the gene encoding S. pombe phosphoglycerate mutase. The S.cerevisiae phosphoglycerate mutase gene failed to detect gene sequence homologies in the S.pombe genome. An oligonucleotide, designed against part of the S.pombe phosphoglycerate mutase sequence (a stretch which was not homologous to the S. cerevisiae sequence) also failed to detect sequence homologies in the S.pombe genome. Thus under the conditions used, neither the S. cerevisiae gene nor the degenerate oligonucleotide appeared to be a suitable molecular probe to screen the S.pombe cDNA expression library in λgt11 (which was synthesised by V. Simanis). A polyclonal antibody against S.pombe phosphoglycerate mutase was prepared and used to screen the S. pombe cDNA expression library. A number of small identical clones were isolated and sequenced. the cDNA inserts encoded 69 residues and part of this sequence was similar to part of the sequence of phosphoglycerate mutase from other sources. Part of the sequence was also similar to a stretch of fructose-2,6-bisphosphatase sequence (fructose-2,6-bisphosphatase appears to be divergently related to phosphoglycerate mutase, Pilkis et al., 1987). A purification scheme for phosphoglycerate mutase from the prokaryote, Streptomyces coelicolor, has been devised. The N-terminal sequence of this enzyme was determined and confirmed that the gene isolated and sequenced by Peter White, encoded phosphoglycerate mutase from S. coelicolor. The enzyme was shown to be a tetramer with a subunit Mr of 29,000. S. coelicolor phosphoglycerate mutase was also shown to be partially 2,3-bisphosphoglycerate dependent.
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Libros sobre el tema "Glycolysis"

1

N, Lithaw Paul, ed. Glycolysis: Regulation, processes, and diseases. Hauppauge, NY: Nova Science Publishers, 2009.

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Schwartz, Laurent. Cancer — Between Glycolysis and Physical Constraint. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18543-4.

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United States. National Aeronautics and Space Administration., ed. Model of early self-replication based on covalent complementarity for a copolymer of glycerate-3-phosphate and glycerol-3-phosphate. San Diego, CA: Salk Institute for Biological Studies, 1989.

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United States. National Aeronautics and Space Administration., ed. Model of early self-replication based on covalent complementarity for a copolymer of glycerate-3-phosphate and glycerol-3-phosphate. San Diego, CA: Salk Institute for Biological Studies, 1989.

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Sloan, Denis. Glycolysis in the human hepatocellular carcinoma cell line Hep-G2. Sudbury, Ont: Laurentian University, 1993.

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International Workshop on Protein Glycosylation (1990 Braunschweig, Germany). Protein glycosylation: Cellular, biotechnological, and analytical aspects. Weinheim, Federal Republic of Germany: VCH, 1991.

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P, Apte Shireesh y Sarangarajan Rangaprasad, eds. Cellular respiration and carcinogenesis. New York: Springer, 2008.

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P, Apte Shireesh y Sarangarajan Rangaprasad, eds. Cellular respiration and carcinogenesis. New York: Springer, 2008.

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Viau, François. Effects of neural activity on oxidative and glycolytic enzyme activity and myosin heavy chain expression within diaphragm muscle fibers. Sudbury, Ont: Laurentian University, 1999.

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International Symposium on Glycolytic and Mitochondrial Defects in Muscle and Nerve (1995 Osaka, Japan). International Symposium on Glycolytic and Mitochondrial Defects in Muscle and Nerve, Osaka, Japan, July 7-8, 1994 ; Osaka Sun Palace (Expo Park Senti, Suita, Osaka. Editado por Tarui Seiichirō. New York: Wiley, 1995.

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Capítulos de libros sobre el tema "Glycolysis"

1

Sharma, Shobhona, Gotam K. Jarori y Haripalsingh M. Sonawat. "Glycolysis". En Encyclopedia of Malaria, 1–15. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-8757-9_21-1.

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Urich, Klaus. "Glycolysis". En Comparative Animal Biochemistry, 514–61. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-06303-3_14.

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Manji, Husseini K., Jorge Quiroz, R. Andrew Chambers, Anthony Absalom, David Menon, Patrizia Porcu, A. Leslie Morrow et al. "Glycolysis". En Encyclopedia of Psychopharmacology, 560. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1394.

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Peretó, Juli. "Glycolysis". En Encyclopedia of Astrobiology, 996. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1848.

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Chesworth, J. M., T. Stuchbury y J. R. Scaife. "Glycolysis". En An Introduction to Agricultural Biochemistry, 141–47. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-009-1441-4_10.

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Smith, C. A. y E. J. Wood. "Glycolysis". En Energy in Biological Systems, 101–24. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3124-7_5.

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Wagner, Peter, Frank C. Mooren, Hidde J. Haisma, Stephen H. Day, Alun G. Williams, Julius Bogomolovas, Henk Granzier et al. "Glycolysis". En Encyclopedia of Exercise Medicine in Health and Disease, 375. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2451.

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Peretó, Juli. "Glycolysis". En Encyclopedia of Astrobiology, 683. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1848.

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Gooch, Jan W. "Glycolysis". En Encyclopedic Dictionary of Polymers, 896. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13846.

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Fortnagel, Peter. "Glycolysis". En Bacillus subtilis and Other Gram-Positive Bacteria, 171–80. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818388.ch12.

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Actas de conferencias sobre el tema "Glycolysis"

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Demongeot, Jacques y Andrei Doncescu. "Modeling the Glycolysis: An Inverse Problem Approach". En 2009 International Conference on Advanced Information Networking and Applications Workshops (WAINA). IEEE, 2009. http://dx.doi.org/10.1109/waina.2009.135.

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Yin, Junyi y Zhanguo Li. "New Exact Solutions for a Glycolysis Model". En 2015 International Symposium on Energy Science and Chemical Engineering. Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/isesce-15.2015.60.

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Ghosh, S., N. Kedia Mehta, L. E. Gleeson y J. Keane. "Meclizine Induces Aerobic Glycolysis in Human Macrophages and Can Enhance the Glycolytic Response to Mycobacterium Tuberculosis Infection". En American Thoracic Society 2024 International Conference, May 17-22, 2024 - San Diego, CA. American Thoracic Society, 2024. http://dx.doi.org/10.1164/ajrccm-conference.2024.209.1_meetingabstracts.a4868.

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Pankratov, Alexander y Irina Bashkirtseva. "Spatial self-organization in diffusion model of glycolysis". En THE VII INTERNATIONAL YOUNG RESEARCHERS’ CONFERENCE – PHYSICS, TECHNOLOGY, INNOVATIONS (PTI-2020). AIP Publishing, 2020. http://dx.doi.org/10.1063/5.0036616.

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Chandra, Fiona A., Gentian Buzi y John C. Doyle. "Linear control analysis of the autocatalytic glycolysis system". En 2009 American Control Conference. IEEE, 2009. http://dx.doi.org/10.1109/acc.2009.5159925.

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Gagnon, P. A., C. Romanet, O. Boucherat, M. Rouabhia, M. Klein y J. Chakir. "Glycolysis of Airway Fibroblasts Fuels Severe Asthma Phenotype". En American Thoracic Society 2024 International Conference, May 17-22, 2024 - San Diego, CA. American Thoracic Society, 2024. http://dx.doi.org/10.1164/ajrccm-conference.2024.209.1_meetingabstracts.a4332.

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Wolf, Amparo M., Sameer Agnihotri, Diana M. Munoz-Gajadhar, Cynthia Hawkins y Abhijit Guha. "Abstract 40: Developmental profile and regulation of the glycolytic enzyme hexokinase 2 and its association with aerobic glycolysis". En Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-40.

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Bashkirtseva, Irina, Alexander Pankratov y Lev Ryashko. "Analysis of dynamics in the distributed model of glycolysis". En PHYSICS, TECHNOLOGIES AND INNOVATION (PTI-2018): Proceedings of the V International Young Researchers’ Conference. Author(s), 2018. http://dx.doi.org/10.1063/1.5055080.

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Zhao, Ziyan y Adam Zweifach. "Abstract B020: Glycolysis inhibitors are antiproliferative in leukemic cells". En Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; October 26-30, 2017; Philadelphia, PA. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1535-7163.targ-17-b020.

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Lokshin, Anna E., Mounia Alaoui El Azher, Liudmila Velikokhatnaya y Denise Prosser. "Abstract 5142: Elevated glycolysis in pre-malignant ovarian cancer". En Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-5142.

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Informes sobre el tema "Glycolysis"

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Lin, Paul P., Alec J. Jaeger, Tung-Yun Wu, Sharon C. Xu, Abraxa S. Lee, Fanke Gao, Po-Wei Chen y James C. Liao. Construction of a Robust Non-Oxidative Glycolysis in Model Organisms for n-Butanol Production. Office of Scientific and Technical Information (OSTI), abril de 2019. http://dx.doi.org/10.2172/1506427.

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Gilewski, Teresa A. Position Emitter I124 Iododeoxyuridine as a Tracer to Follow DNA Metabolism on Scans and in Tumor Samples in Advanced Breast Cancer: Comparison of 18F 2-Fluror-2-Deoxy-(D)-Glucose, as a Tracer for Glycolysis. Fort Belvoir, VA: Defense Technical Information Center, diciembre de 2005. http://dx.doi.org/10.21236/ada450668.

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DiPaola, Robert S. y Eileen White. The Effect of Glycolytic Modulation on Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, julio de 2010. http://dx.doi.org/10.21236/ada535349.

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Liao, J. C. Role of Glycolytic Intermediates in Global Regulation and Signal Transduction. Final Report. Office of Scientific and Technical Information (OSTI), mayo de 2000. http://dx.doi.org/10.2172/765400.

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Peak, M. J., J. G. Peak, F. J. Stevens, J. Blamey, X. Mai, Z. H. Zhou y M. W. W. Adams. Characterization of the glycolytic enzyme enolase which is abundant in the hyperthermophilic archaeon, Pyrococcus furiosus. Office of Scientific and Technical Information (OSTI), diciembre de 1993. http://dx.doi.org/10.2172/10124321.

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Farmer, W. R. y J. C. Liao. Role of glycolytic intermediate in regulation: Improving lycopene production in Escherichia coli by engineering metabolic control. Office of Scientific and Technical Information (OSTI), junio de 2001. http://dx.doi.org/10.2172/842949.

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Doichev, Kostadin, Veselina Georgieva, Elitsa Boteva y Rumiana Mironova. Modification of DNA with Glucose 6-Phosphate to Examine the Glycolytic Enzyme Phosphoglucose Isomerase for DNA-amadoriase Activity. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, junio de 2021. http://dx.doi.org/10.7546/crabs.2021.06.06.

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