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Books on the topic 'GlycoGag'

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Author: Grafiati
Published: 11 March 2023

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1

DiNuzzo, Mauro, and Arne Schousboe, eds. Brain Glycogen Metabolism. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-27480-1.

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2

Savage, Madelyn. The Avian Glycogen body. Salford: University of Salford, 1986.

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3

R, Acharya K., ed. Glycogen phosphorylase b: Description of the protein structure. Singapore: World Scientific, 1991.

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4

Martinez, Ana, Ana Castro, and Miguel Medina, eds. Glycogen Synthase Kinase 3 (GSK-3) and Its Inhibitors. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/0470052171.

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5

Patel, Mona D. Abnormalities in glycogen storage and metabolism in patients with liver-related diseases. Roehampton: University of Surrey Roehampton, 2002.

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6

library, Wiley online, ed. Glycogen synthase kinase 3 (GSK-3) and its inhibitors: Drug discovery and development. Hoboken, N.J: Wiley-Interscience, 2006.

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7

Seal, Leonard Henry. Studies on glycogen in the nervous systems of Haemopis Sanguisuga and Planorbis Corneus. Salford: University of Salford, 1986.

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8

Clement, Nichole S. The effects of the neurotoxin tetrodotoxin on glycogen content in rat soleus muscles. Sudbury, Ont: Laurentian University, 1993.

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9

Wender, Regina. Astrocytic glycogen influences axon function and survival during glucose deprivation in central white matter. [Baltimore, MD]: Society for Neuroscience, 2000.

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10

1863-1902, Johnston Wyatt, ed. The medico-legal significance of the presence of sugar and glycogen in the liver post mortem. [S.l: s.n., 1985.

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11

Filosto, Massimiliano. Advances in diagnosis and management of glycogenosis II. Hauppauge, N.Y: Nova Science Publishers, 2011.

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12

Müller, Rabea Annina. Phosphoinositide-3-kinases p110α and p110β mediate S phase entry in astroglial cells in the marginal zone of rat neocortex. Freiburg: Universität, 2013.

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13

Crowley, John F. Chasing miracles: The Crowley family journey of strength, hope, and joy. New York: Newmarket Press, 2010.

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14

K, Welply Joseph, Jaworski Ernest, and University of California, Los Angeles., eds. Glycobiology: Proceedings of a Smith, Kline & French Laboratories-UCLA Symposium held at Frisco, Colorado, January 14-20, 1989. New York: Wiley-Liss, 1990.

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15

Kurt, Drickamer, ed. Introduction to glycobiology. 3rd ed. Oxford: Oxford University Press, 2011.

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16

Hunnisett, Douglas J. Leptin demonstrates no significant effect on basal or insulin-stimulated 2-deoxyglucose uptake and C14-labelled glucose incorporation into glycogen in L6 myotubes. Ottawa: National Library of Canada, 2000.

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17

Anand, Geeta. The Cure. New York: HarperCollins, 2009.

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18

Michèle, Aubery, ed. Glycans in cell interaction and recognition: Therapeutic aspects. Australia: Harwood Academic, 2001.

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19

1935-, Graucob E., ed. Hematologic cytology of storage diseases. Berlin: Springer-Verlag, 1985.

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20

Carlin, James Irish. The effects of prolonged exercise and the ingestion of alanine and glucose during recovery on plasma carnitine and ketosis. Eugene: Microform Publications, College of Human Development and Performance, University of Oregon, 1986.

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21

Acharya, K. R., D. I. Stuart, K. M. Varvill, and L. N. Johnson. Glycogen PhosphorylaseB. WORLD SCIENTIFIC, 1991. http://dx.doi.org/10.1142/1319.

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22

Cassiman, David, Pascal Laforêt, and Fanny Mochel. Glycogen Storage Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0001.

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Glucose is the body’s major energy source, and carbohydrate serves as fuel—particularly during high-intensity exercise that requires rapid energy release. A deficiency of any of the enzymes involved in the catabolism of glycogen to glucose may cause symptoms, with hypoglycemia and exercise intolerance as the most common presentations. Glycogen storage disorders (GSD) affect muscle, liver, and brain. The most common GSDs affecting muscle are GSD II (Pompe disease) and GSD V (McArdle disease). GSDs affecting mainly the liver are GSD I, III, IV, VI, IX, XI. Most liver-GSDs present during infancy, with symptoms of hypoglycemia, impressive hepatomegaly, and retarded growth. Adult presentations have been reported for GSD Ia, III, IV, and IX.Adult polyglucosan body disease (APBD) is the main GSD affecting primarily the brain and mainly characterized by spastic paraplegia, axonal neuropathy and leukodystrophy. APBD is a subtype of GSD IV and is due to a deficiency of glycogen branching enzyme (GBE). Besides GSD IV, other GSDs have been reported to have CNS effects in some patients—notably GSD II and GSD III.
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23

Wang, Tammy, Jocelyn Wong, and Anita Honkanen. Glycogen Storage Diseases. Edited by Kirk Lalwani, Ira Todd Cohen, Ellen Y. Choi, and Vidya T. Raman. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780190685157.003.0048.

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Glycogen storage diseases result from deficiencies of various enzymes or proteins in the pathways of glycogen metabolism. The reduction in effective glucose storage and/or mobilization results in hypoglycemia and accumulation of glycogen in tissues. Diagnosis can occur at any age, from infancy to adulthood, depending on the pathway affected and the degree of enzyme deficiency. The clinical presentation varies, but the most commonly affected organ systems include the heart, liver, and skeletal muscles. In addition to the morbidity that can occur from dysfunction of these organs, important anesthetic implications include administration of glucose-containing fluids to avoid hypoglycemia, monitoring for acidosis, and caution with use of depolarizing muscle relaxants because of the potential risk of hyperkalemia and rhabdomyolysis. Inheritance is commonly autosomal recessive.
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24

Schousboe, Arne, and Mauro DiNuzzo. Brain Glycogen Metabolism. Springer International Publishing AG, 2020.

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25

Schousboe, Arne, and Mauro DiNuzzo. Brain Glycogen Metabolism. Springer, 2019.

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26

Brown, Angus. Glycogen and Energy Metabolism. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199794591.003.0036.

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This is a digitally enhanced text. Readers can also see the coverage of this topic area in the second edition of Neuroglia. The second edition of Neuroglia was first published digitally in Oxford Scholarship Online and the bibliographic details provided, if cited, will direct people to that version of the text. Readers can also see the coverage of this topic area in the ...
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27

Whelan, W. J., and Margaret P. Cameron. Control of Glycogen Metabolism. Wiley & Sons, Incorporated, John, 2009.

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28

Whelan, W. J., and CIBA Foundation Symposium Staff. Control of Glycogen Metabolism. Wiley & Sons, Limited, John, 2008.

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29

Yu, Guangli, Hongzhi Cao, Hironobu Hojo, Tongzhong Ju, and Chung-Yi Wu. Synthetic Glycomes. Royal Society of Chemistry, The, 2019.

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30

Methods on Glycoconjugates: A Laboratory Manual. Routledge, 1995.

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31

Glycogen supercompensation in female distance runners. 1985.

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32

Stambolic, Vuk. Regulation of glycogen synthase kinase-3. 1997.

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33

Effect of adrenalectomy on diurnal glycogen fluctuation in rats. 1985.

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34

Acharya, K. R., D. I. Stuart, K. M. Varvill, and L. N. Johnson, eds. Glycogen Phosphorylase b: Description of the Protein Structure. World Scientific Publishing Co. Pte. Ltd., 1991. http://dx.doi.org/10.1142/9789814360401.

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35

Stuart, D. I., K. M. Varvill, L. N. Johnson, and K. R. Acharya. Glycogen Phosphorylase-B: Description of the Protein Structure. World Scientific Publishing Company, 1991.

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36

Stuart, D. I., and K. R. Acharya. Glycogen Phosphorylase B: Description of the Protein Structure. World Scientific Publishing Company, 1991.

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37

Luo, Juan. Disruption of glycogen synthase kinase-3[Beta] in mice. 2002.

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38

Abelson, John N., Melvin I. Simon, Gerald W. Hart, and William J. Lennarz. Guide to Techniques in Glycobiology. Elsevier Science & Technology Books, 1994.

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39

(Editor), John N. Abelson, Melvin I. Simon (Editor), William J. Lennarz (Editor), and Gerald W. Hart (Editor), eds. Guide to Techniques in Glycobiology (Methods in Enzymology). Academic Press, 1994.

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40

Wang, Binghe, Ana Martinez, Ana Castro, and Miguel Medina. Glycogen Synthase Kinase 3 and Its Inhibitors: Drug Discovery and Development. Wiley & Sons, Incorporated, John, 2006.

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41

(Editor), Ana Martinez, Ana Castro (Editor), Miguel Medina (Editor), and Binghe Wang (Editor), eds. Glycogen Synthase Kinase 3 (GSK-3) and Its Inhibitors: Drug Discovery and Development (Wiley Series in Drug Discovery and Development). Wiley-Interscience, 2006.

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42

Observations on the glycogen content of certain invertebrates and fishes. [Toronto]: University Library, pub. by the Librarian, 1994.

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43

Carbohydrate feedings and exercise performance: Influence of muscle glycogen availability. 1992.

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44

Glycogen resynthesis following submaximal and supramaximal exhaustive exercise in man. 1986.

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45

Weiss, Pedro L., and Brian D. Faulkner. Glycogen: Structure, Functions in the Body and Role in Disease. Nova Science Publishers, Incorporated, 2013.

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46

Possible mechanism for changes in glycogen metabolism in unloaded soleus muscle. [Washington, D.C: National Aeronautics and Space Administration, 1985.

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47

Leslie G. (Leslie Gifford) Kilborn and J. J. R. (John James Rickard) MacLeod. Observations on the Glycogen Content of Certain Invertebrates and Fishes [microform]. Creative Media Partners, LLC, 2021.

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48

Beattie, R. Mark, Anil Dhawan, and John W.L. Puntis. Carbohydrate intolerance. Oxford University Press, 2011. http://dx.doi.org/10.1093/med/9780198569862.003.0018.

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Carbohydrates in the diet 128Carbohydrate digestion 129Hypolactasia/lactose intolerance 130Congenital sucrase–isomaltase deficiency 130Glucose–galactose malabsorption 131Confirmation of diagnosis of carbohydrate malabsorption 131Carbohydrates make up at least half the energy intake in the diet. The principal carbohydrates are the storage polysaccharides (starch, glycogen and cellulose), the disaccharides lactose and sucrose, and the monosaccharides glucose and fructose....
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49

Wera, S. Purification and Characterisation of the Glycogen-Bound Protein Phosphatase from Rat Liver. Leuven University Press, 1991.

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50

van der Ploeg, Ans T., and Pascal Laforêt. Pompe Disease. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0055.

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Pompe disease, also named acid maltase deficiency and glycogen storage disease type II (GSDII), is a rare autosomal recessive disorder caused by the deficiency of the glycogen-degrading lysosomal enzyme acid α‎-glucosidase. The clinical spectrum of this disease is broad, varying from a lethal infantile-onset generalized myopathy including cardiomyopathy, to late-onset slowly progressive muscle weakness mimicking limb-girdle muscular dystrophy. Respiratory insufficiency is a frequent complication and the main cause of death. The prognosis of Pompe disease has changed considerably with the use of enzyme replacement therapy using recombinant acid α‎-glucosidase (alglucosidase alfa), which has been widely available since 2006. Improvements in survival and major motor achievements can be observed in patients with infantile forms, and recent studies demonstrate improvement of walking distance and stabilization of pulmonary function in late-onset forms. A longer-term study of the safety and efficacy of ERT, based on data gathering across the complete spectrum of Pompe disease via national or international patient registries, is needed in order to formulate more precise guidelines for treatment.
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