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Libros sobre el tema "Glycolysis"

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

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1

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

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2

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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3

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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4

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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5

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

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6

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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7

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

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8

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

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9

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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10

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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11

Persson, Lars-Olof. Phase partitioning in analysis of weak heterogeneous enzyme: Enzyme interactions and in protein purification ; applications on Calvin-cycle enzymes from spinach chloroplasts and glycolytic enzymes from bakers' yeast. Lund: Univ., 1989.

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12

Ferreira, Rita, Pedro Fontes Oliveira y Rita Nogueira-Ferreira. Glycolysis. Elsevier Science & Technology Books, 2022.

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13

Lithaw, Paul N. Glycolysis: Regulation, Processes and Diseases. Nova Science Publishers, Incorporated, 2015.

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14

Castilho, Alexandra. Glyco-Engineering: Methods and Protocols. Springer New York, 2016.

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15

Hung, Shang-Cheng y Medel Manuel L. Zulueta. Glycochemical Synthesis: Strategies and Applications. Wiley & Sons, Incorporated, John, 2016.

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16

Hung, Shang-Cheng y Medel Manuel L. Zulueta. Glycochemical Synthesis: Strategies and Applications. Wiley & Sons, Limited, John, 2016.

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17

Witczak, Zbigniew J. y Roman Bielski. Coupling and Decoupling of Diverse Molecular Units in Glycosciences. Springer, 2017.

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18

Hung, Shang-Cheng y Medel Manuel L. Zulueta. Glycochemical Synthesis: Strategies and Applications. Wiley & Sons, Limited, John, 2016.

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19

Witczak, Zbigniew J. y Roman Bielski. Coupling and Decoupling of Diverse Molecular Units in Glycosciences. Springer, 2018.

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20

Kuhns, William y Inka Brockhausen. Glycoproteins and Human Disease. Springer Berlin / Heidelberg, 2014.

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21

Hung, Shang-Cheng y Medel Manuel L. Zulueta. Glycochemical Synthesis: Strategies and Applications. Wiley & Sons, Incorporated, John, 2016.

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22

Castilho, Alexandra. Glyco-Engineering: Methods and Protocols. Springer New York, 2015.

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23

Kuhns, William y Inka Brockhausen. Glycoproteins and Human Disease. Springer London, Limited, 2013.

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24

Cancer: Between glycolysis and physical constraint. Berlin: Springer, 2004.

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25

Schwartz, Laurent. Cancer - Between Glycolysis and Physical Constraint. Springer London, Limited, 2012.

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26

Ganapathy-Kanniappan, Shanmugasundaram. Advances in GAPDH Protein Analysis: A Functional and Biochemical Approach. Springer, 2018.

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27

Ganapathy-Kanniappan, Shanmugasundaram. Advances in GAPDH Protein Analysis: A Functional and Biochemical Approach. Springer, 2018.

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28

Holst, Otto, Patrick J. Brennan, Anthony P. Moran y Mark von Itzstein. Microbial Glycobiology: Structures, Relevance and Applications. Elsevier Science & Technology Books, 2009.

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29

Aoki-Kinoshita, Kiyoko F. Practical Guide to Using Glycomics Databases. Springer, 2016.

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30

Aoki-Kinoshita, Kiyoko F. Practical Guide to Using Glycomics Databases. Springer, 2017.

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31

Aoki-Kinoshita, Kiyoko F. A Practical Guide to Using Glycomics Databases. Springer, 2018.

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32

Seidler, Norbert W. GAPDH: Biological Properties and Diversity. Springer London, Limited, 2012.

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33

Zhao, Zhizhuang. Regulation of phosphofructokinase by reversible inactivation. 1990.

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34

Glycolysis: Tissue-Specific Metabolic Regulation in Physio-Pathological Conditions. Elsevier Science & Technology, 2023.

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35

Hochachka, Peter W. Living Without Oxygen. Harvard University Press, 2014.

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36

Connett, Richard J. Defining hypoxia: A systems view of Vo2, glycolysis, energetics, and intracellular Po2. 1990.

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37

Avedisian, Lori-Ann. The effect of selected buffering agents on performance in the competitive 1600 meter run. 1995.

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38

Schurr, Avital y Evelyne Gozal, eds. Glycolysis at 75: Is it Time to Tweak the First Elucidated Metabolic Pathway in History? Frontiers Media SA, 2015. http://dx.doi.org/10.3389/978-2-88919-586-2.

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39

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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40

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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41

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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42

Stafstrom, Carl E. y Thomas P. Sutula. 2-Deoxyglucose. Editado por Dominic P. D’Agostino. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190497996.003.0036.

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Metabolic regulation of excitability is increasingly appreciated as a strategy to control seizures and reduce pathogenesis. Inhibiting or bypassing glycolysis may be one way in which the ketogenic diet suppresses seizures. 2-deoxy-D-glucose (2DG) is a glucose analog that partially inhibits glycolysis and has antiseizure effects in several acute and chronic seizure models. The mechanisms underlying the acute and chronic effects of 2DG are being investigated. Preliminary studies provide evidence that the acute anticonvulsant actions of 2DG involve activity-dependent presynaptic suppression of excitatory synaptic transmission during network synchronization. The chronic effects of 2DG entail reduction of the expression of brain-derived neurotrophic factor and its receptor, tyrosine kinase B. Preclinical toxicology studies demonstrate that 2DG has a favorable toxicity profile at doses effective for seizure protection. Currently available preclinical studies support 2DG as a novel first-in-class metabolic treatment for epilepsy with an antiglycolytic mechanism distinct from all other anticonvulsants.
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43

Microbial Glycobiology Structures Relevance And Applications. Academic Press, 2009.

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44

Joseph David Jean Andre Bissonnette. Effects of hypocaloric feeding and high carbohydrate refeeding on in situ muscle function, glycolysis and body composition in adult rats. 1996.

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45

Sherwood, Dennis y Paul Dalby. The bioenergetics of living cells. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198782957.003.0024.

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Living systems create order, and appear to break the Second Law. This chapter explains, and resolves, this apparent paradox, drawing on the concept of coupled reactions (as introduced in Chapters 13 and 16), as mediated by ‘energy currencies’ such as ATP and NADH. The chapter then examines the key energy-capturing systems in biological systems – glycolysis and the citric acid cycle, and also photosynthesis. Topics covered include how energy is captured in the conversion of glucose to pyruvate, the mitochondrial membrane, respiration, electron transport, ATP synthase, chloroplasts and thylakoids, photosystems I and II, and the light-independent reactions of photosynthesis.
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46

Dalbeth, Nicola. Clinical features of gout. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780198748311.003.0005.

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About 60% of the variance in serum urate levels can be explained by inherited genetic factors, but the extent of the contribution of genetic factors to gout in the presence of hyperuricaemia is not known. Genome-wide association studies in Europeans have identified 28 loci controlling serum urate levels, although the molecular basis of the majority of these genetic associations is currently unknown. The SLC2A9 and ABCG2 renal and gut uric acid transporters have very strong effects on urate levels and the risk of gout. Other uric acid transporters (e.g. SLC22A11/OAT478, SLC22A12/URAT1) and a glycolysis gene (GCKR) are associated with urate levels. Environmental exposures such as sugar-sweetened beverages and alcohol interact with urate-associated genetic variants in an unpredictable fashion. Very little is known about the genetic control of gout in the presence of hyperuricaemia, formation of monosodium urate crystals, and the immune response.
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47

Veech, Richard L. y M. Todd King. Alzheimer’s Disease. Editado por 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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48

Madl, Ulrike. Pathophysiology of glucose control. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0258.

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Hyperglycaemia is a frequent phenomenon in critically-ill patients, associated with increased morbidity and mortality. Hyperglycaemia results in cellular glucose overload and toxic adverse effects of glycolysis and oxidative phosphorylation, especially in tissues with insulin-independent glucose uptake, and acute hyperglycaemia can exert a variety of negative effects. It is the main side effect of intensive insulin therapy. Both severe and moderate hypoglycaemia are independent risk factors of mortality in critically-ill patients. Prolonged hypoglycaemia induces neuronal damage, but may also have adverse cardiovascular effects. Several risk factors predispose critically-ill patients to hypoglycaemic events. Rapid glucose fluctuations may induce oxidative stress and lead to vascular damage. Glucose complexity is a marker of endogenous glucose regulation. Association between hyperglycaemia and outcome is weaker in diabetic critically-ill patients than in non-diabetic patients. Pre-admission glucose control in diabetic critically-ill patients plays a role in the response to glucose control and mortality.
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49

Merriman, Tony R. The genetic basis of gout. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199668847.003.0040.

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An individual’s risk of gout is determined by a complex relationship between inherited genetic variants and environmental exposures. Genetic variants that control hyperuricaemia and subsequent progression to clinical gout specify pathogenic pathways that could be therapeutically targeted. Genome-wide association studies (GWAS) have provided novel insights into the pathways leading to hyperuricaemia. GWAS have identified the renal uric acid transporter SLC2A9/GLUT9 and the gut excretory molecule ABCG2, which each have very strong genetic effects in the control of urate levels and risk of gout. Histone deacetylase inhibitors are able to correct the genetically-determined ABCG2 dysfunction. Other renal uric acid transporters, such as SLC22A11/OAT4 and SLC22A12/URAT1 have been confirmed to be genetically associated with urate and the risk of gout. Genes that generate urate during glycolysis (e.g. GCKR) are also implicated. In contrast very little is known about genetic variants that control the progression from hyperuricaemia to gout with the toll-like receptor 4 gene being the only gene with replicated evidence of association.
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50

Gapdh Biological Properties And Diversity. Springer, 2012.

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