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1

service), ScienceDirect (Online, ed. Structure, function and regulation of Tor complexes from yeasts to mammals. Amsterdam: Elsevier/Academic Press, 2010.

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2

Labrou, Nikolaos, ed. Therapeutic Enzymes: Function and Clinical Implications. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-7709-9.

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3

Stöcker, Walter, and Klaudia Brix. Proteases: Structure and function. Wien: Springer, 2013.

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4

Park, Kwan-Hwa. Carbohydrate-active enzymes: Structure, function and applications. Cambridge: Woodhead Publishing Ltd, 2008.

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5

Agricultural Biotechnology Symposium on "Carbohydrate-Active Enzymes: Structure, Function, and Applications" (2008 Seoul National University). Carbohydrate-active enzymes: Structure, function and applications. Boca Raton: CRC Press, 2008.

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6

Jono, Viviana. High-efficiency paper additives based on enzyme recognition functions. Ottawa: National Library of Canada, 2002.

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7

Roussel, Marc R. Functional equation methods in steady-state enzyme kinetics. Ottawa: National Library of Canada, 1990.

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8

Mu, Wanmeng, Wenli Zhang, and Qiuming Chen, eds. Novel enzymes for functional carbohydrates production. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-33-6021-1.

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9

Linder, Markus. Structure-function relationships in fungal cellulose-binding domains. Espoo, Finland: VTT, Technical Research Centre of Finland, 1996.

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10

Microbial production of food ingredients, enzymes and nutraceuticals. [S.l.]: Woodhead Publishing Limited, 2013.

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11

Moreira, Susana. Carbohydrate binding modules: Functions and applications. Hauppauge, N.Y: Nova Science Publisher's, 2009.

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12

Koivula, Anu. Structure-function studies of two polysaccharide-degrading enzymes: Bacillus strearothermophilus Ü-amylase and trichoderma reesei cellobiohydrolase II. Espoo: VTT, Technical Research Centre of Finland, 1996.

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13

Davidovich, Chen. Targeting Functional Centers of the Ribosome. Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg, 2011.

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14

International Meeting on the Function of Thiamin Diphosphate Enzymes (1990 Blaubeuren, Germany). Biochemistry and physiology of thiamin diphosphate enzymes: Proceedings of the International Meeting on the Function of Thiamin Diphosphate Enzymes, held in Blaubeuren, October 1990. Weinheim: VCH, 1991.

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15

Valkonen, Mari. Functional studies of the secretory pathway of filamentous fungi: The effect of unfolded protein response on protein production. Espoo [Finland]: VTT Technical Research Centre of Finland, 2003.

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16

Georgiev, Bojidor. Serpins and protein kinase inhibitors: Novel functions, structural features and molecular mechanisms. New York: Nova Science Publishers, 2010.

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17

L, Schramm Vern, and Wedler Frederick C, eds. Manganese in metabolism and enzyme function. Orlando: Academic Press, 1986.

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18

Manganese in Metabolism and Enzyme Function. Elsevier, 1986. http://dx.doi.org/10.1016/b978-0-12-629050-9.x5001-7.

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19

Evered, David, and Geralyn Lawrenson. Environmental Chemicals, Enzyme Function and Human Disease. Wiley & Sons, Incorporated, John, 2009.

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20

Sliz, Piotr. Structure, function and interactions of enzyme IIA from the phosphoenolpyruvate: Lactose phosphotransferase system. 2000.

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21

Computational Strategies Towards Improved Protein Function Prophecy Of Xylanases From Thermomyces Lanuginosus. Springer, 2012.

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22

Clarke, Andrew. Temperature and reaction rate. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780199551668.003.0007.

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All other things being equal, physiological reaction rate increases roughly exponentially with temperature. Organisms that have adapted over evolutionary time to live at different temperatures can have enzyme variants that exhibit similar kinetics at the temperatures to which they have adapted to operate. Within species whose distribution covers a range of temperatures, there may be differential expression of enzyme variants with different kinetics across the distribution. Enzymes adapted to different optimum temperatures differ in their amino acid sequence and thermal stability. The Gibbs energy of activation tends to be slightly lower in enzyme variants adapted to lower temperatures, but the big change is a decrease in the enthalpy of activation, with a corresponding change in the entropy of activation, both associated with a more open, flexible structure. Despite evolutionary adjustments to individual enzymes involved in intermediary metabolism (ATP regeneration), many whole-organism processes operate faster in tropical ectotherms compared with temperate or polar ectotherms. Examples include locomotion (muscle power output), ATP regeneration (mitochondrial function), nervous conduction and growth.
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23

Skeletal muscle and hepatic enzyme adaptation to physical training under beta-adrenergic blockade in the rat. 1985.

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24

Skeletal muscle and hepatic enzyme adaptation to physical training under beta-adrenergic blockade in the rat. 1987.

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25

Kortgen, Andreas, and Michael Bauer. The effect of acute hepatic failure on drug handling in the critically ill. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0197.

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Impaired hepatic function is a common event in intensive care unit patients and as the liver plays a central role in drug metabolism and excretion this may lead to profound changes in pharmacokinetics. Underlying mechanisms are altered enzyme function of phase I and phase II metabolism, altered transporter protein function together with cholestasis and hepatic perfusion disorders. Moreover, multidrug therapy may lead to induction and inhibition of these enzymes and transporter proteins. In addition, changes in plasma protein binding and volumes of distribution of drugs are common. Altogether, these changes may not only lead to sometimes unpredictable plasma levels of xenobiotics, but also to drug-induced liver injury when hepatocellular accumulation of noxious substances occurs. Concomitant renal dysfunction may further complicate this situation. Pharmacodynamic alterations might also occur. In conclusion, the clinician must carefully evaluate medication given to patients with hepatic failure. Therapeutic drug monitoring should be performed wherever available to guide therapy.
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26

Relationships between structure and function of Cytochrome P-450: Experiments, calculations, models. Berlin: Akademie Verlag, 1992.

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27

Frawley, Geoff. Mucopolysaccharidoses. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199764495.003.0064.

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The mucopolysaccharidoses (MPS) are a group of seven chronic progressive diseases caused by deficiencies of 11 different lysosomal enzymes required for the catabolism of glycosaminoglycans (GAGs). Hurler syndrome (MPS IH) is an autosomal recessive storage disorder caused by a deficiency of α‎-L-iduronidase. Hunter syndrome (MPS II) is an X-linked recessive disorder of metabolism involving the enzyme iduronate-2-sulfatase. Many of the MPS clinical manifestations have potential anesthetic implications. Significant airway issues are particularly common due to thickening of the soft tissues, enlarged tongue, short immobile neck, and limited mobility of the cervical spine and temporomandibular joints. Spinal deformities, hepatosplenomegaly, airway granulomatous tissue, and recurrent lung infections may inhibit pulmonary function. Odontoid dysplasia and radiographic subluxation of C1 on C2 is common and may cause anterior dislocation of the atlas and spinal cord compression.
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28

K, Hopsu-Havu Väinö, Järvinen M, Kirschke Heidrun, and International Conference on Proteolysis and Protein Turnover (11th : 1996 : Turku, Finland), eds. Proteolysis in cell functions. Amsterdam: IOS Press, 1997.

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29

(Editor), Julio Polaina, and Andrew P. MacCabe (Editor), eds. Industrial Enzymes: Structure, Function and Applications. Springer, 2007.

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30

Labrou, Nikolaos. Therapeutic Enzymes: Function and Clinical Implications. Springer, 2019.

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31

Taylor, Christopher, and Sally Connolly. Gastrointestinal disease and nutrition. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780198702948.003.0007.

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This chapter discusses the common gastrointestinal and nutritional consequences of cystic fibrosis (CF) including hepato-biliary disease. The pathophysiology of obstructive gut disease (meconium ileus and distal ileal obstruction) is discussed with reference to CFTR dysfunction. The diagnosis and management of gastro-oesophageal reflux, an increasingly common problem in both children and adults with CF, is also considered in some depth. A new section on eosinophilic gut disease has been added. The importance of nutrition in maintaining lung function is emphasized with a section on pancreatic enzyme physiology and guidance on optimizing pancreatic enzyme replacement therapy. An investigation plan to exclude concomitant gut disease for a child with poor weight gain is given, together with a section on invasive nutritional support. The diagnosis of hepatic disease and biliary complications is considered together with suggested treatments and a long-term monitoring plan
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32

How Enzymes Work: From Structure to Function. Jenny Stanford Publishing, 2015.

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33

Federico, Antonio, and Silvia Palmeri. Oligosaccharidoses. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0057.

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Oligosaccharidoses are a group of lysosomal diseases, also called glycoproteinoses, biochemically characterized by storage of protein-bound oligosaccharides within lysosomes and excretion with urine of corresponding sugars. Storage of oligosaccharides results from absence or defective function of a specific lysosomal enzyme. Classification includes α‎ and β‎ mannosidosis, fucosidosis, sialidosis types I and II, Schindler disease, and aspartylglycosaminuria. Galactosialidosis characterized by deficiency of β‎-galactosidase and α‎-neuraminidase with presence in patient urine of oligosaccharides has been included among oligosaccharidoses but may be better classified as a lysosomal enzyme protection defect disease in relation to its primary defect of cathepsine A-protective protein. The clinical spectrum of the diseases vary widely, as is common in lysosomal storage disorders. Patients frequently have neurological symptoms, but in rare cases presenting in adulthood symptoms may be very subtle. Psychiatric presentations have been described in adults. For adult cases, no treatments are available except for supportive care.
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34

Plesner, Liselotte, Terence L. Kirley, and Aileen F. Knowles. Ecto-Atpases: Recent Progress on Structure and Function. Springer, 2012.

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35

Ecto-ATPases: Recent Progress on Structure and Function. Springer, 2011.

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36

Huber, Robert, and Hermann Eggerer. Structural and Functional Aspects of Enzyme Catalysis. Springer, 2011.

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37

Activation And Detoxification Enzymes Functions And Implications. Springer, 2011.

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38

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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39

Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism. John Wiley & Sons, 1997.

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40

Venom phospholipase A2 enzymes: Structure, function, and mechanism. Chichester: John Wiley, 1997.

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41

Waldek, Stephen. Fabry disease. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0338_update_001.

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Fabry disease is a rare X-linked lysosomal storage disorder in which deficiency of alpha-galactosidase A leads to accumulation of substrate, mostly globotriaosylceramide (Gb3), which causes a progressive, multiorgan disease affecting predominantly the kidneys, skin, heart, and nervous system. Painful peripheral (‘acral’) neuropathy is characteristic. Proteinuria and estimated glomerular filtration rate (eGFR) are strongly associated with risk of progression, but this may be reduced by treatment with angiotensin-converting enzyme inhibitors as well as by enzyme replacement therapy (ERT). ERT was approved in 2001; it improves pain and other neuropathic symptoms, and well-being, and has been proven to clear deposits of Gb3 from tissues, at variable speeds. There is limited randomized controlled trial data but protective effects have been proven for renal outcomes, death, and better outcomes in some other organ systems. Renal function may be protected if ERT is commenced before there is heavy proteinuria or substantial loss of GFR. It is recommended to start ERT as soon as the diagnosis is made in those with very low or absent enzyme. For those with intermediate levels it is recommended to commence treatment only when signs or symptoms appear. Proteinuria and eGFR give most information from a renal point of view, but renal biopsy is also useful for confirming the renal diagnosis and staging the disease as well as monitoring progress in selected cases. Management should include regular screening for complications including myocardial and neurological assessments. It is likely that registries will show progressive rises in median survival with this condition.
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42

Chen, Chang-Hwei. Activation and Detoxification Enzymes: Functions and Implications. Springer, 2014.

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43

Hester, Charles K. Mitogen-Activated Protein Kinases: Activation, Functions and Regulation. Nova Science Publishers, Incorporated, 2019.

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44

Adam, Nikhil. Amylases: Properties, Functions and Uses. Nova Science Publishers, Incorporated, 2019.

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45

Evolution of catalytic function. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory, 1987.

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46

Vimalesvaran, Kavitha, and Michael Marber. Myocardial Remodelling after Myocardial Infarction. Oxford University Press, 2014. http://dx.doi.org/10.1093/med/9780199653461.003.0031.

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This chapter focuses on myocardial remodelling, a process that affects the heart’s shape, structure, and function, following myocardial injury (MI). Post-MI remodelling can be divided into three phases, with the first phase 0–72 hours beginning at the time of ischaemic injury, the second phase 72 hours to 6 weeks, and the third and last phase 6 weeks and beyond. During post-infarction remodelling, hypertrophy is an adaptive response that compensates for the increased load, reduces the effect of progressive dilatation, and balances contractile function. The chapter discusses the factors involved in ventricular remodelling and its association with heart failure progression. The effects of therapies designed to prevent or attenuate post-infarction left ventricular remodelling, with reference to the pathophysiological mechanisms involved, are then considered. Therapies specifically discussed include angiotensin-converting enzyme (ACE) inhibitors, angiotensin receptor blockers (ARBs), β‎-adrenoreceptor blockers, and aldosterone receptor antagonists.
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47

E, Vermeulen N. P., ed. Glutathione S-transferases: Structure, function and clinical implications. London: Taylor & Francis, 1996.

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48

Glutathione S-Transferases: Structure, Function and Clinical Implications. CRC, 1996.

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49

Bramham, Kate, and Catherine Nelson-Piercy. Pregnancy in patients with chronic kidney disease and on dialysis. Edited by Norbert Lameire and Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0295_update_001.

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Chronic kidney disease (CKD) affects a small but increasing minority of women becoming pregnant. It is associated with additional risks depending on pre-pregnancy glomerular filtration rate, proteinuria, and hypertension. Some drugs are contraindicated in pregnancy. These are powerful reasons for counselling all women of childbearing age about pregnancy in CKD. With minor CKD the main issue is moderately increased risk of pregnancy-associated hypertension and pre-eclampsia. More advanced CKD is associated with reduced fertility, progressively increased risk of pre-term delivery and a significant chance of permanent loss of maternal renal function. Distinguishing pre-eclampsia from the natural effects of pregnancy on manifestations of CKD can be challenging. Blood pressure targets may be modified during pregnancy and angiotensin converting enzyme inhibitors and angiotensin receptor blockers are contraindicated. Dialysis may be initiated if pregnancy occurs at advanced levels of CKD. Pregnancy may also occur in patients on dialysis, usually in women with some residual native renal function. More intensive dialysis may improve outcomes.
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50

Agúndez, José A., and Kathrin Klein, eds. Functional Polymorphisms of Xenobiotics Metabolizing Enzymes (XME). Frontiers Media SA, 2013. http://dx.doi.org/10.3389/978-2-88919-142-0.

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