Relevant bibliographies by topics / Glycolytic enzymes

Academic literature on the topic 'Glycolytic enzymes'

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Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "Glycolytic enzymes"

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Parkhouse, Wade S. "Regulation of skeletal muscle metabolism by enzyme binding." Canadian Journal of Physiology and Pharmacology 70, no. 1 (January 1, 1992): 150–56. http://dx.doi.org/10.1139/y92-022.

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The random diffusion mechanism is usually assumed in analyzing the energetics of specific pathways despite the findings that enzymes associate with each other and (or) with various membranous and contractile elements of the cell. Successive glycolytic enzymes have been shown to associate in the cytosol as enzyme complexes or bind to the thin filaments. Furthermore, the degree of glycolytic enzyme interactions have been shown to change with altered rates of carbon flux through the pathway. In particular, the proportions of aldolase, phosphofructokinase, and glyceraldehyde phosphate dehydrogenase bound to the contractile proteins have been found to increase with increased rates of glycolysis. In addition, decreasing pH and ionic strength are also associated with an increase in glycolytic enzyme interactions. The kinetics displayed by interacting enzymes generally serve to enhance their catalytic efficiencies. The associations of the glycolytic enzymes serve to enhance metabolite transfer rates, increase the local concentrations of intermediates, and provide for regulation of activity via effectors. Therefore these interactions provide an additional mechanism for regulating glycolytic flux in skeletal muscle.Key words: glycolysis, skeletal muscle, enzymes, binding.
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Ayna, Adnan, and Peter C. E. Moody. "Activity of fructose-1,6-bisphosphatase from Campylobacter jejuni." Biochemistry and Cell Biology 98, no. 4 (August 2020): 518–24. http://dx.doi.org/10.1139/bcb-2020-0021.

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The glycolytic pathway of the enteric pathogen Campylobacter jejuni is incomplete; the absence of phosphofructokinase means that the suppression of futile cycling at this point in the glycolytic–gluconeogenic pathway might not be required, and therefore the mechanism for controlling pathway flux is likely to be quite different or absent. In this study, the characteristics of fructose-1,6-bisphosphatase (FBPase) of C. jejuni are described and the regulation of this enzyme is compared with the equivalent enzymes from organisms capable of glycolysis. The enzyme is insensitive to AMP inhibition, unlike other type I FBPases. Campylobacter jejuni FBPase also shows limited sensitivity to other glycolytic and gluconeogenic intermediates. The allosteric cooperative control of the enzyme’s activity found in type I FBPases appears to have been lost.
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Simoneau, Jean-Aimé, and David E. Kelley. "Altered glycolytic and oxidative capacities of skeletal muscle contribute to insulin resistance in NIDDM." Journal of Applied Physiology 83, no. 1 (July 1, 1997): 166–71. http://dx.doi.org/10.1152/jappl.1997.83.1.166.

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Simoneau, Jean-Aimé, and David E. Kelley. Altered glycolytic and oxidative capacities of skeletal muscle contribute to insulin resistance in NIDDM. J. Appl. Physiol. 83(1): 166–171, 1997.—The insulin resistance of skeletal muscle in glucose-tolerant obese individuals is associated with reduced activity of oxidative enzymes and a disproportionate increase in activity of glycolytic enzymes. Because non-insulin-dependent diabetes mellitus (NIDDM) is a disorder characterized by even more severe insulin resistance of skeletal muscle and because many individuals with NIDDM are obese, the present study was undertaken to examine whether decreased oxidative and increased glycolytic enzyme activities are also present in NIDDM. Percutaneous biopsy of vatus lateralis muscle was obtained in eight lean (L) and eight obese (O) nondiabetic subjects and in eight obese NIDDM subjects and was assayed for marker enzymes of the glycolytic [phosphofructokinase, glyceraldehyde phosphate dehydrogenase, hexokinase (HK)] and oxidative pathways [citrate synthase (CS), cytochrome- c oxidase], as well as for a glycogenolytic enzyme (glycogen phosphorylase) and a marker of anaerobic ATP resynthesis (creatine kinase). Insulin sensitivity was measured by using the euglycemic clamp technique. Activity for glycolytic enzymes (phosphofructokinase, glyceraldehye phosphate dehydrogenase, HK) was highest in subjects with subjects with NIDDM, following the order of NIDDM > O > L, whereas maximum velocity for oxidative enzymes (CS, cytochrome- c oxidase) was lowest in subjects with NIDDM. The ratio between glycolytic and oxidative enzyme activities within skeletal muscle correlated negatively with insulin sensitivity. The HK/CS ratio had the strongest correlation ( r = −0.60, P < 0.01) with insulin sensitivity. In summary, an imbalance between glycolytic and oxidative enzyme capacities is present in NIDDM subjects and is more severe than in obese or lean glucose-tolerant subjects. The altered ratio between glycolytic and oxidative enzyme activities found in skeletal muscle of individuals with NIDDM suggests that a dysregulation between mitochondrial oxidative capacity and capacity for glycolysis is an important component of the expression of insulin resistance.
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Jo, Min-Sik, Hyun-Woo Yang, Joo-Hoo Park, Jae-Min Shin, and Il-Ho Park. "Glycolytic reprogramming is involved in tissue remodeling on chronic rhinosinusitis." PLOS ONE 18, no. 2 (February 16, 2023): e0281640. http://dx.doi.org/10.1371/journal.pone.0281640.

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Background Glycolytic reprogramming is a key feature of chronic inflammatory disease. Extracellular matrix (ECM) produced by myofibroblasts plays an important role in tissue remodeling of nasal mucosa in chronic rhinosinusitis (CRS). This study aimed to determine whether glycolytic reprogramming contributes to myofibroblast differentiation and ECM production in nasal fibroblasts. Methods Primary nasal fibroblasts were isolated from the nasal mucosa of patients with CRS. Glycolytic reprogramming was assessed by measuring the extracellular acidification and oxygen consumption rates in nasal fibroblast, with and without transforming growth factor beta 1 (TGF-β1) treatment. Expression of glycolytic enzymes and ECM components was measured by real-time polymerase chain reaction, western blotting, and immunocytochemical staining. Gene set enrichment analysis was performed using whole RNA-sequencing data of nasal mucosa of healthy donors and patients with CRS. Result Glycolysis of nasal fibroblasts stimulated with TGF-B1 was upregulated along with glycolytic enzymes. Hypoxia-inducing factor (HIF)-1α was a high-level regulator of glycolysis, and increased HIF-1α expression promoted glycolysis of nasal fibroblasts, and inhibition of HIF-1α down-regulated myofibroblasts differentiation and ECM production. Conclusion This study suggests that inhibition of the glycolytic enzyme and HIF-1α in nasal fibroblasts regulates myofibroblast differentiation and ECM generation associated with nasal mucosa remodeling.
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van den Brink, Joost, André B. Canelas, Walter M. van Gulik, Jack T. Pronk, Joseph J. Heijnen, Johannes H. de Winde, and Pascale Daran-Lapujade. "Dynamics of Glycolytic Regulation during Adaptation of Saccharomyces cerevisiae to Fermentative Metabolism †." Applied and Environmental Microbiology 74, no. 18 (July 18, 2008): 5710–23. http://dx.doi.org/10.1128/aem.01121-08.

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ABSTRACT The ability of baker's yeast (Saccharomyces cerevisiae) to rapidly increase its glycolytic flux upon a switch from respiratory to fermentative sugar metabolism is an important characteristic for many of its multiple industrial applications. An increased glycolytic flux can be achieved by an increase in the glycolytic enzyme capacities (V max) and/or by changes in the concentrations of low-molecular-weight substrates, products, and effectors. The goal of the present study was to understand the time-dependent, multilevel regulation of glycolytic enzymes during a switch from fully respiratory conditions to fully fermentative conditions. The switch from glucose-limited aerobic chemostat growth to full anaerobiosis and glucose excess resulted in rapid acceleration of fermentative metabolism. Although the capacities (V max) of the glycolytic enzymes did not change until 45 min after the switch, the intracellular levels of several substrates, products, and effectors involved in the regulation of glycolysis did change substantially during the initial 45 min (e.g., there was a buildup of the phosphofructokinase activator fructose-2,6-bisphosphate). This study revealed two distinct phases in the upregulation of glycolysis upon a switch to fermentative conditions: (i) an initial phase, in which regulation occurs completely through changes in metabolite levels; and (ii) a second phase, in which regulation is achieved through a combination of changes in V max and metabolite concentrations. This multilevel regulation study qualitatively explains the increase in flux through the glycolytic enzymes upon a switch of S. cerevisiae to fermentative conditions and provides a better understanding of the roles of different regulatory mechanisms that influence the dynamics of yeast glycolysis.
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Kondoh, Hiroshi, Matilde E. Lleonart, Jesus Gil, Jing Wang, Paolo Degan, Gordon Peters, Dolores Martinez, Amancio Carnero, and David Beach. "Glycolytic Enzymes Can Modulate Cellular Life Span." Cancer Research 65, no. 1 (January 1, 2005): 177–85. http://dx.doi.org/10.1158/0008-5472.177.65.1.

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Abstract An unbiased screen for genes that can immortalize mouse embryonic fibroblasts identified the glycolytic enzyme phosphoglycerate mutase (PGM). A 2-fold increase in PGM activity enhances glycolytic flux, allows indefinite proliferation, and renders cells resistant to ras-induced arrest. Glucosephosphate isomerase, another glycolytic enzyme, displays similar activity and, conversely, depletion of PGM or glucosephosphate isomerase with short interfering RNA triggers premature senescence. Immortalized mouse embryonic fibroblasts and mouse embryonic stem cells display higher glycolytic flux and more resistance to oxidative damage than senescent cells. Because wild-type p53 down-regulates PGM, mutation of p53 can facilitate immortalization via effects on PGM levels and glycolysis.
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Winther, Sally, Marie S. Isidor, Astrid L. Basse, Nina Skjoldborg, Amanda Cheung, Bjørn Quistorff, and Jacob B. Hansen. "Restricting glycolysis impairs brown adipocyte glucose and oxygen consumption." American Journal of Physiology-Endocrinology and Metabolism 314, no. 3 (March 1, 2018): E214—E223. http://dx.doi.org/10.1152/ajpendo.00218.2017.

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During thermogenic activation, brown adipocytes take up large amounts of glucose. In addition, cold stimulation leads to an upregulation of glycolytic enzymes. Here we have investigated the importance of glycolysis for brown adipocyte glucose consumption and thermogenesis. Using siRNA-mediated knockdown in mature adipocytes, we explored the effect of glucose transporters and glycolytic enzymes on brown adipocyte functions such as consumption of glucose and oxygen. Basal oxygen consumption in brown adipocytes was equally dependent on glucose and fatty acid oxidation, whereas isoproterenol (ISO)-stimulated respiration was fueled mainly by fatty acids, with a significant contribution from glucose oxidation. Knockdown of glucose transporters in brown adipocytes not only impaired ISO-stimulated glycolytic flux but also oxygen consumption. Diminishing glycolytic flux by knockdown of the first and final enzyme of glycolysis, i.e., hexokinase 2 (HK2) and pyruvate kinase M (PKM), respectively, decreased glucose uptake and ISO-stimulated oxygen consumption. HK2 knockdown had a more severe effect, which, in contrast to PKM knockdown, could not be rescued by supplementation with pyruvate. Hence, brown adipocytes rely on glucose consumption and glycolytic flux to achieve maximum thermogenic output, with glycolysis likely supporting thermogenesis not only by pyruvate formation but also by supplying intermediates for efferent metabolic pathways.
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Jung, Da-Woon, Woong-Hee Kim, and Darren R. Williams. "Chemical genetics and its application to moonlighting in glycolytic enzymes." Biochemical Society Transactions 42, no. 6 (November 17, 2014): 1756–61. http://dx.doi.org/10.1042/bst20140201.

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Glycolysis is an ancient biochemical pathway that breaks down glucose into pyruvate to produce ATP. The structural and catalytic properties of glycolytic enzymes are well-characterized. However, there is growing appreciation that these enzymes participate in numerous moonlighting functions that are unrelated to glycolysis. Recently, chemical genetics has been used to discover novel moonlighting functions in glycolytic enzymes. In the present mini-review, we introduce chemical genetics and discuss how it can be applied to the discovery of protein moonlighting. Specifically, we describe the application of chemical genetics to uncover moonlighting in two glycolytic enzymes, enolase and glyceraldehyde dehydrogenase. This led to the discovery of moonlighting roles in glucose homoeostasis, cancer progression and diabetes-related complications. Finally, we also provide a brief overview of the latest progress in unravelling the myriad moonlighting roles for these enzymes.
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Chowdhury, Shomeek, Stephen Hepper, Mudassir K. Lodi, Milton H. Saier, and Peter Uetz. "The Protein Interactome of Glycolysis in Escherichia coli." Proteomes 9, no. 2 (April 6, 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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Lloyd, Pamela G., and Christopher D. Hardin. "Role of microtubules in the regulation of metabolism in isolated cerebral microvessels." American Journal of Physiology-Cell Physiology 277, no. 6 (December 1, 1999): C1250—C1262. http://dx.doi.org/10.1152/ajpcell.1999.277.6.c1250.

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We used13C-labeled substrates and nuclear magnetic resonance spectroscopy to examine carbohydrate metabolism in vascular smooth muscle of freshly isolated pig cerebral microvessels (PCMV). PCMV utilized [2-13C]glucose mainly for glycolysis, producing [2-13C]lactate. Simultaneously, PCMV utilized the glycolytic intermediate [1-13C]fructose 1,6-bisphosphate (FBP) mainly for gluconeogenesis, producing [1-13C]glucose with only minor [3-13C]lactate production. The dissimilarity in metabolism of [2-13C]FBP derived from [2-13C]glucose breakdown and metabolism of exogenous [1-13C]FBP demonstrates that carbohydrate metabolism is compartmented in PCMV. Because glycolytic enzymes interact with microtubules, we disrupted microtubules with vinblastine. Vinblastine treatment significantly decreased [2-13C]lactate peak intensity (87.8 ± 3.7% of control). The microtubule-stabilizing agent taxol also reduced [2-13C]lactate peak intensity (90.0 ± 2.4% of control). Treatment with both agents further decreased [2-13C]lactate production (73.3 ± 4.0% of control). Neither vinblastine, taxol, or the combined drugs affected [1-13C]glucose peak intensity (gluconeogenesis) or disrupted the compartmentation of carbohydrate metabolism. The similar effects of taxol and vinblastine, drugs that have opposite effects on microtubule assembly, suggest that they produce their effects on glycolytic rate by competing with glycolytic enzymes for binding, not by affecting the overall assembly state of the microtubule network. Glycolysis, but not gluconeogenesis, may be regulated in part by glycolytic enzyme-microtubule interactions.
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Dissertations / Theses on the topic "Glycolytic enzymes"

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Crowhurst, Georgina Sheila Ellen. "Studies with hyperthermophilic archaeal glycolytic enzymes." Thesis, University of Exeter, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324719.

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Duncan, John Andrew Carleton University Dissertation Biology. "Glycolytic enzyme binding and metabolic control." Ottawa, 1988.

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Yuan, Meng. "A study of regulatory mechanisms of glycolytic and gluconeogenic enzymes." Thesis, University of Edinburgh, 2016. http://hdl.handle.net/1842/25725.

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Many diseases correlate with abnormal glucose metabolism in cells and organisms. For instance, the human M2 isoform of the glycolytic enzyme pyruvate kinase (M2PYK) plays an important role in metabolic reprogramming of tumour cells whereby aerobic glycolysis or the ‘Warburg effect’ supports cell proliferation by accumulating necessary biomass. By contrast, gluconeogenesis may play an important role, as observed in certain types of trypanosomatid parasites (e.g. the amastigote form of Leishmania major) where anabolism is essential for infectious properties. Hence, these glucose metabolising enzymes are important potential drug targets for cancer and trypanosomiasis. However, many aspects of their regulatory mechanisms are still poorly understood. This thesis describes biochemical and structural studies on M2PYK and on L. major fructose-1,6-bisphosphatase (LmFBPase), providing insights into allosteric mechanisms and structure-based drug design for both enzymes. Human PYKs and LmFBPase were expressed and purified from Escherichia coli, and their kinetics were fully characterised. It was shown that certain amino acids regulate the activity of M2PYK allosterically, but in opposite ways, with some being inhibitors and others activators. X-ray crystallographic structures and biophysical data of M2PYK complexes with alanine, phenylalanine, serine or tryptophan reveal an R-/T-state oscillating model of M2PYK involving a 11° rotation of each subunit. In addition, M2PYK was demonstrated to be a redox-sensitive enzyme. Reducing reagents were shown to help maintain the tetramer and prevent its dissociation, and thereby to activate M2PYK, whereas oxidation and nitrosylation reagents functioned in the opposite sense. Nitrosylation assays showed that the main nitrosylated residue is Cys326 of M2PYK, which is located on the tetramer interface. Dynamics and modulator effects of PYKs were further studied by hydrogen–deuterium exchange by mass spectrometry. These observations highlight the important effects of amino acids on M2PYK regulation. M1PYK by contrast, was demonstrated to be a constitutively fully active pyruvate kinase, with minor effects from modulators. The gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is a potential drug target against leishmaniasis. Here we present biochemical and structural studies for LmFBPase, by characterising its activity in a metal-dependent reaction, as well as its inhibition by AMP. The crystal structure of LmFBPase is a homotetramer, composed of monomers with alternating α/β/α/β/α ‘club sandwich’ topologies. In comparison with previously revealed LmFBPase structures, the AMP-complexed structure shows a rotated form of the tetramer. Comparisons of the structures reveal an ‘unlock-androtate’ allosteric mechanism in which AMP binding causes a series of structural changes culminating in an incomplete and non-productive active site. The structure of the effector site of LmFBPase shows a different conformation from human FBPases, thereby offering a potential specific target for Leishmania.
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Bawa, Simranjot. "Exploring the molecular mechanisms of Drosophila dTRIM32 implicated in pathogenesis of Limb-Girdle Muscular Dystrophy 2H." Thesis, Kansas State University, 2017. http://hdl.handle.net/2097/38243.

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Master of Science
Biochemistry and Molecular Biophysics Interdepartmental Program
Erika Rae Geisbrecht
The E3 ubiquitin ligase TRIM32 is a member of tripartite motif (TRIM) family of proteins involved in various processes including differentiation, cell growth, muscle regeneration and cancer. TRIM32 is conserved between vertebrates (humans, mouse) and invertebrates (Drosophila). The N-terminus of this protein is characterized by a RING domain, B-box domain, and Coiled-Coil region, while the C-terminus contains six NHL repeats. In humans, mutations that cluster in the NHL domains of TRIM32 result in the muscle disorders Limb-Girdle Muscular Dystrophy type 2H (LGMD2H) and Sarcotubular Myopathy (STM). Mutations in the B-box region cause Bardet-Biedl Syndrome (BBS), a clinically separate disorder that affects multiple parts of the body. A comprehensive genetic analysis in vertebrate models is complicated by the ubiquitous expression of TRIM32 and neurogenic defects in TRIM32-/- mutant mice that are independent of the muscle pathology associated with LGMD2H. The model organism Drosophila melanogaster possesses a TRIM32 [dTRIM32/Thin (Tn)/Abba] homolog highly expressed in muscle tissue. We previously showed that dTRIM32 is localized to Z-disk of the sarcomere and is required for myofibril stability. Muscles form correctly in Drosophila tn mutants, but exhibit a degenerative muscle phenotype once contraction ensues. Mutant or RNAi knockdown larvae are also defective in locomotion, which mimics clinical features associated with loss of TRIM32 in LGMD2H patients. It is predicted that mutations in the NHL domain either affect protein structure or are involved in protein-protein interactions. However, the molecular mechanism by which these mutations affect the interaction properties of dTRIM32 is not understood. Biochemical pulldown assays using the bait fusion protein GST-dTRIM32-NHL identified numerous dTRIM32 binding proteins in larval muscle tissue. Many key glycolytic enzymes were present in the dTRIM32 pulldowns and not in control experiments. Glycolytic genes are expressed in the developing Drosophila musculature and are required for myoblast fusion. Strikingly, many glycolytic proteins are also found at the Z-disk, consistent with dTRIM32 localization. Our biochemical and genetic studies provide evidence that there is direct interaction between dTRIM32 and glycolytic proteins (Aldolase and PGLYM). dTRIM32 also regulates glycolytic enzyme levels and protein localization at their sites of action. These data together suggest a role for dTRIM32 in coordinating glycolytic enzyme function, possibly for localized ATP production or to maintain muscle mass via glycolytic intermediates.
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Shanmuganathan, Anupama. "An Analysis of Glycolytic Enzymes in the Cellular Response to Metal Toxicity." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/biology_diss/63.

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Metal toxicity is implicated in neurotoxicity, nephrotoxicity, aging and cancer. Protein oxidation resulting from oxidative stress is now known to be involved in metal toxicity. However, proteomic responses to metal induced oxidative stress have not been characterized. By using the yeast as a model, we characterized these changes occurring in response to sub-lethal doses of metals. Several proteins involved in protein synthesis, ribosome assembly decreased while antioxidant defenses, proteins involved in sulfur metabolism, and glutathione synthesis and ubiquitin increased following metal exposure. We also show that metals induced temporal and targeted protein oxidation independent of protein abundance. Among the targets were glycolytic enzymes and heat-shock proteins. As a consequence, glycolytic enzyme activities decreased whereas the levels and activities of the enzymes of the alternative pathway for glucose metabolism, pentose phosphate pathway (PPP) increased. True to prediction, we also found increased flow through the PPP as measured by elevated levels of NADPH and glutathione. NADPH and glutathione are crucial for maintaining the redox balance in the cell. Thus, rerouting of glucose metabolism into PPP is considered to be beneficial to the organism. Among the oxidation targets is a glycolytic protein, glyceraldehyde 3-phosphate dehydrogenase (GAPDH) that is required for apoptosis in neuronal cells. We show that not only is GAPDH required for metal induced apoptosis in yeast but also the levels of GAPDH transcript and protein increase in the cytosol and the nucleus in an isoform specific fashion. Such changes strongly implicate the role of GAPDH in yeast apoptosis. This work provides evidence for the involvement of targeted protein oxidation in metal toxicity, shows the overlaps and differences in the mechanism of copper and cadmium toxicity, allows comprehension of how metabolic processes respond to metal stress and explores the potential of GAPDH as a sensor of oxidative stress and mediator for apoptosis.
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Abdulla, Sheera. "Biochemical characterisation of unusual glycolytic enzymes from the human intestinal parasite Blastocystis hominis." Thesis, University of Exeter, 2016. http://hdl.handle.net/10871/23933.

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Blastocystis is an important parasite that infects humans and a wide range of animals like rats, birds, reptiles, etc. infecting a sum of 60% of world population. It belongs to the Stramenopiles, a Heterologous group that includes for example the Phythophthora infestans the responsible for the Irish potato famine. Previous work had reported the presence of an unusual fusion protein that is composed of two of the main glycolytic enzymes; Triosephosphate isomerase-glyceraldehyde-3-phosphate dehydrogenase (TPI-GAPDH). Little is known about this protein. Blastocystis TPI-GAPDH and Blastocystis enolase were both characterized biochemically and biophysically in this project. The phylogenetic relationships of those two proteins among other members of either Stramenopiles, or other members of the kingdom of life were examined and found to be grouping within the chromalveolates. Our studies revealed that those two proteins, Blastocystis enolase and Blastocystis TPI-GAPDH, had a peptide signal targeting them to the mitochondria. This was an unusual finding knowing that text books always referred to the glycolytic pathway as a canonical cytoplasmic pathway. Structural studies had also been conducted to unravel the unknown structure of the fusion protein Blastocystis TPI-GAPDH. X-ray crystallography had been conducted to solve the protein structure and the protein was found to be a tetrameric protein composed of a central tetrameric GAPDH protein flanked with two dimmers of TPI protein. Solving its structure would be the starting point towards reviling the role that TPI-GAPDH might play in Blastocystis and other organisms that it was found in as well. Although a fusion protein, the individual components of the fusion were found to contain all features deemed essential for function for TPI and GAPDH and contain all expected protein motifs for these enzymes.
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Peshavaria, Mina. "Structure and regulation of the human muscle-specific enolase gene." Thesis, University of Southampton, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.295627.

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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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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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Lautru, Sylvie. "Purification and characterization of the glycolytic enzymes hexokinase and pyruvate kinase from Eurosta solidaginis." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0035/MQ27053.pdf.

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Books on the topic "Glycolytic enzymes"

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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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Armstrong, Neil, Alan R. Barker, and Alison M. McManus. Muscle metabolism during exercise. Edited by Neil Armstrong and Willem van Mechelen. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780198757672.003.0006.

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Ethical considerations and the lack, until recently, of accessible non-invasive techniques of interrogating exercising muscles have limited research into developmental muscle metabolism during exercise. Current evidence supports an anaerobic/aerobic energy metabolism interplay in exercise in which children present a relatively higher oxidative capacity than adolescents or adults. There is a progressive increase in anaerobic glycolytic flux with age at least into adolescence and, possibly into young adulthood. Independent effects of biological maturation on muscle metabolism during exercise remain to be empirically proven. An amalgam of findings from muscle fibre profiles, muscle enzymes activity, muscle energy stores, substrate utilization, phosphocreatine re-synthesis, and pulmonary oxygen uptake contribute to a plausible model of an age- and sex-specific developing metabolic profile but the precise mechanisms require further clarification. There is a persuasive argument that muscle fibre recruitment patterns are a fundamental component of age- (and perhaps sex-) related differences.
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Zhao, Zhizhuang. Regulation of phosphofructokinase by reversible inactivation. 1990.

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Brito-Arias, Marco. Enzymes Involved in Glycolysis, Fatty Acid and Amino Acid Biosynthesis: Active Site Mechanisms and Inhibition. Bentham Science Publishers, 2020.

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Brito-Arias, Marco. Enzymes Involved in Glycolysis, Fatty Acid and Amino Acid Biosynthesis: Active Site Mechanisms and Inhibition. Bentham Science Publishers, 2020.

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Brito-Arias, Marco. Enzymes Involved in Glycolysis, Fatty Acid and Amino Acid Biosynthesis: Active Site Mechanisms and Inhibition. Bentham Science Publishers, 2020.

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Smerage, Jeffrey. Activated Transcription of the Glycolytic Enzyme Genes of Saccharomyces Cerevisiae: The Chromatin Structures of TP11 and Mechanisms of RAP1P Mediated Activation. Dissertation Discovery Company, 2018.

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Smerage, Jeffrey. Activated Transcription of the Glycolytic Enzyme Genes of Saccharomyces Cerevisiae: The Chromatin Structures of TP11 and Mechanisms of RAP1P Mediated Activation. Creative Media Partners, LLC, 2018.

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Veech, Richard L., and M. Todd King. Alzheimer’s Disease. Edited by Detlev Boison. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190497996.003.0026.

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Deficits in cerebral glucose utilization in Alzheimer’s disease (AD) arise decades before cognitive impairment and accumulation of amyloid plaques and neurofibrillary tangles in brain. Addressing this metabolic deficit has greater potential in treating AD than targeting later disease processes – an approach that has failed consistently in the clinic. Cerebral glucose utilization requires numerous enzymes, many of which have been shown to decline in AD. Perhaps the most important is pyruvate dehydrogenase (PDH), which links glycolysis with the Krebs cycle and aerobic metabolism, and whose activity is greatly suppressed in AD. The unique metabolism of ketone bodies allows them to bypass the block at pyruvate dehydrogenase and restore brain metabolism. Recent studies in mouse genetic models of AD and in a human Alzheimer’s patient showed the potential of ketones in maintaining brain energetics and function. Oral ketone bodies might be a promising avenue for treatment of Alzheimer’s disease.
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Gapdh Biological Properties And Diversity. Springer, 2012.

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Book chapters on the topic "Glycolytic enzymes"

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Benkovic, S. J., and K. J. Schray. "The Anomeric Specificity of Glycolytic Enzymes." In Advances in Enzymology - and Related Areas of Molecular Biology, 139–64. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122891.ch4.

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Ueda, T., and A. Ikemoto. "4.1 Cytoplasmic Glycolytic Enzymes. Synaptic Vesicle-Associated Glycolytic ATP-Generating Enzymes: Coupling to Neurotransmitter Accumulation." In Handbook of Neurochemistry and Molecular Neurobiology, 241–59. Boston, MA: Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-30411-3_10.

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Watson, Herman C. "Structural and Functional Properties of Consecutive Enzymes in the Glycolytic Pathway." In The Enzyme Catalysis Process, 55–68. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-1607-8_5.

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Nakanishi, N., K. Ozawa, and S. Yamada. "Enzymes of the glycolytic pathway — phosphofructokinase, pyruvate kinase and lactate dehydrogenase." In Dynamic Aspects of Dental Pulp, 203–20. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0421-7_13.

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Sorbi, S., M. Mortilla, S. Piacentini, G. Tesco, S. Latorraca, B. Nacmias, S. Tonini, and L. Amaducci. "Lactate production and glycolytic enzymes in sporadic and familial Alzheimer’s disease." In Key Topics in Brain Research, 195–99. Vienna: Springer Vienna, 1990. http://dx.doi.org/10.1007/978-3-7091-3396-5_19.

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Sorbi, S., M. Mortilla, S. Piacentini, G. Tesco, S. Tonini, and L. Amaducci. "Lactate Production and Glycolytic Enzymes in Skin Cultured Cells from Alzheimer’s Disease Patients." In Biological Markers of Alzheimer’s Disease, 163–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-46690-8_17.

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Lanfredi, Guilherme, Guiherme Reis-de-Oliveira, Veronica M. Saia-Cereda, Paul C. Guest, Daniel Martins-de-Souza, and Vitor M. Faça. "Selective Reaction Monitoring Mass Spectrometry for Quantitation of Glycolytic Enzymes in Postmortem Brain Samples." In Advances in Experimental Medicine and Biology, 205–12. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-52479-5_16.

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Stocchi, Vilberto, Beatrice Biagiarelli, Linda Masat, Francesco Palma, Fulvio Palma, Giovanni Piccoli, Luigi Cucchiarini, and Mauro Magnani. "Free Radicals Promote “In Vitro” a Different Intracellular Decay of Rabbit Reticulocyte and Erythrocyte Glycolytic Enzymes." In Advances in Experimental Medicine and Biology, 217–23. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5985-2_20.

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Sheedy, R. J., and F. M. Clarke. "Predicting Interaction Sites between Glycolytic Enzymes and Cytoskeletal Proteins Employing the Concepts of the Molecular Recognition Theory." In Results and Problems in Cell Differentiation, 155–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-540-46560-7_11.

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Sullivan, David, Norma Slepecky, and Nicholas Fuda. "Analysis of Co-Localization of Glycolytic Enzymes in Flight Muscle and its Relation to Muscle Function in Drosophila." In Technological and Medical Implications of Metabolic Control Analysis, 223–31. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-011-4072-0_25.

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Conference papers on the topic "Glycolytic enzymes"

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Yu, Jiaquan, Ashley M. Weichmann, Alexandria Craig, Wei Huang, Dawn R. Church, Farideh Mehraein, Laurie L. Parker, David J. Beebe, George Wilding, and Hirak S. Basu. "Abstract 4968: “Moonlighting Functions” of glycolytic enzymes relate to human prostate cancer invasion." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4968.

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de Oliveira Melo, MN, A. Clavelland Ochioni, P. Zancan, A. Passos Oliveira, R. Garrett, S. Baumgartner, and C. Holandino. "Viscum album ethanolic extract promotes MDA-MB-231 cell death by glycolytic enzymes inhibition." In GA – 70th Annual Meeting 2022. Georg Thieme Verlag KG, 2022. http://dx.doi.org/10.1055/s-0042-1759148.

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Kataria, Nalini, Ashish Joshi, and Anil Kumar Kataria. "Assessment of Environmental Temperature Dependencies of Glycolytic Cycle Enzymes in Marwari Goat from Arid Tract." In Annual International Conference on Advances in Veterinary Science Research. Global, 2015. http://dx.doi.org/10.5176/2382-5685_vetsci15.28.

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Dong, Jiabin, Dengfeng Li, Hyejin Kim, Hong Wang, Zhi Zheng, Ziwei Zhang, Na Ye, Haiying Chen, Jia Zhou, and Qiang Shen. "Abstract LB-299: Glucose metabolism modulator HJC0152 differentially regulates glycolytic enzymes to suppress breast carcinogenesis." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-lb-299.

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Tompa, Peter, Jorg Bar, and Jozsef Batke. "Quantitative Characterization Of The Interactions Of Some Glycolytic Enzymes: An Application Of The Fluorescence Anisotropy Measurement." In 1988 Los Angeles Symposium--O-E/LASE '88, edited by Joseph R. Lakowicz. SPIE, 1988. http://dx.doi.org/10.1117/12.945379.

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Sanchez, Tino Wilson, Jian-Ying Zhang, Liping Dai, Susanne Montgomery, Colwick Wilson, Guangyu Zhang, Saied Mirshahidi, Nathan Wall, and Carlos A. Casiano. "Abstract 3895: Immunoproteomic profiling in African American men with prostate cancer: Evidence for an autoimmune response to glycolytic enzymes." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3895.

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Sanchez, Tino Wilson, Jitian Li, Liping Dai, Saied Mirshahidi, Guangyu Zhang, Nathan Wall, Colwick Wilson, Susanne Montgomery, Jianying Zhang, and Carlos Casiano. "Abstract B05: Immunoproteomic profiling in African American men with prostate cancer: Evidence for an autoimmune response to glycolytic enzymes." In Abstracts: Eighth AACR Conference on The Science of Health Disparities in Racial/Ethnic Minorities and the Medically Underserved; November 13-16, 2015; Atlanta, Georgia. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7755.disp15-b05.

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Alamoudi, Aliaa A., Afnan A. Alqarni, Ghada Ajabnoor, Aleksandra Niedwiecki, Matthias Rath, Steve M. Harakeh, and Ahmed M. Al-Abd. "Abstract 5430: Evaluating a novel phytobiologic mixture against breast cancer cell lines: Effect on glycolytic enzymes and EMT gene expression profile." In 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.am2018-5430.

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Jain, Aditi, James C. K. Lai, Golam MI Chowdhury, Kevin Behar, and Alok Bhushan. "Abstract 923: Interrelations between roles of phospholipase C-gamma 1 inhibition, mTOR and glycolytic enzymes in growth and survival of glioblastoma cells." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-923.

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

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Reports on the topic "Glycolytic enzymes"

1

Peak, M. J., J. G. Peak, F. J. Stevens, J. Blamey, X. Mai, Z. H. Zhou, and 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), December 1993. http://dx.doi.org/10.2172/10124321.

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Doichev, Kostadin, Veselina Georgieva, Elitsa Boteva, and 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, June 2021. http://dx.doi.org/10.7546/crabs.2021.06.06.

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