Books on the topic 'Enzyme inhibition'

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1

Graham, MacGregor, Sever Peter S, International Symposium on ACE Inhibition (1st : 1989 : London, England), and International Symposium on ACE Inhibition (2nd : 1991 : London, England), eds. Current advances in ACE inhibition. Edinburgh: Churchill Livingstone, 1989.

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2

Lu, Chuang, and Albert P. Li, eds. Enzyme Inhibition in Drug Discovery and Development. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2009. http://dx.doi.org/10.1002/9780470538951.

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3

1930-, Smith H. J., and Simons Claire, eds. Enzymes and their inhibition: Drug development. Boca Raton: CRC Press, 2005.

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4

F, Cleland John G., ed. The Clinician's guide to ACE inhibition. Edinburgh: Churchill Livingstone, 1993.

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5

(Australia), Materials Research Laboratories, ed. Inhibition of EEL acetylcholinesterase by nerve agents: A stopped-flow study. Ascot Vale, Vic: Dept. of Defence, Materials Research Laboratories, 1985.

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6

1932-, Sonnenblick Edmund H., Laragh John H. 1924-, and Lesch Michael, eds. New frontiers in cardiovascular therapy: Focus on angiotensin converting enzyme inhibition. Princeton: Excerpta Medica, 1989.

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7

Ahlström, Marie. Cytochrome P450, metabolism and inhibition: Computational and experimental studies. Göteborg: Göteborg University, 2007.

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8

Chuang, Lu, and Li A. P, eds. Enzyme inhibition in drug discovery and development: The good and the bad. Hoboken, N.J: John Wiley, 2009.

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9

M, Dowsett, ed. Aromatase inhibition: Then, now, and tomorrow. London: Parthenon Pub. Group, 1994.

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10

A, MacGregor G., and Sever Peter S, eds. Current advances in ACE inhibition 2: Proceedings of an Internationalsymposium, Queen Elizabeth II Conference Centre, London, UK 17-21 February 1991. Edinburgh: Churchill Livingstone, 1991.

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11

Jonker, Geert Jan. Angiotensin converting enzyme inhibition in the diagnosis of renovascular hypertension: Experiments in conscious dogs. Groningen: Van Denderen, 1993.

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12

David, Caldwell, MacGregor Graham, and Sever Peter S, eds. Current advances in ACE inhibition 2: Proceedings of an international symposium, Queen Elizabeth II Conference Centre, London, UK, 17-21 February, 1991. Edinburgh: Churchill Livingstone, 1991.

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13

1943-, Greenwald Robert A., Golub Lorne M, and New York Academy of Sciences., eds. Inhibition of matrix metalloproteinases: Therapeutic potential. New York, N.Y: New York Academy of Sciences, 1994.

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14

Larsson, Lars-Johan. Structure and function of [alpha] ₂ macroglobulin: A unique proteinase inhibitor in plasma. Uppsala: Dept. of Veterinary Medical Chemistry, Faculty of Veterinary Medicine, Swedish University of Agricultural Sciences, 1987.

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15

Pekkarinen, Anja. The serine proteinases of Fusarium grown on cereal proteins and in barley grain and their inhibition by barley proteins. Espoo [Finland]: VTT Technical Research Centre of Finland, 2003.

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16

International FOIPAN Symposium. (1988 Shizuoka, Japan). Therapeutic basis of synthetic protease inhibitor: Proceedings of the International FOIPAN Symposium held as a Satellite of the 7th International Symposium on Gastrointestinal Hormones, November 4, 1988, Shizuoka, Japan. Edited by Kanno Tomio 1933-, Miyoshi A, Biomedical Research Foundation (Japan), and International Symposium on Gastrointestinal Hormones. (7th : 1988 : Shizuoka, Japan). Tokyo: Biomedical Research Foundation, 1989.

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17

Iqbal, Choudhary Muhammad, ed. Biological inhibitors. Amsterdam: Harwood Academic Publishers, 1996.

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18

Sharma, Rakesh, ed. Enzyme Inhibition and Bioapplications. InTech, 2012. http://dx.doi.org/10.5772/1963.

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19

Sharma, Rakesh R. Enzyme inhibition and bioapplications. 2012.

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20

(Editor), Graham A. MacGregor, and Peter S. Sever (Editor), eds. Current Advances Ace Inhibition 2 (Current Advances in ACE Inhibition). Churchill Livingstone, 1997.

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21

Baskar, G., K. Sathish Kumar, and K. Tamilarasan, eds. Enzyme Inhibition - Environmental and Biomedical Applications. BENTHAM SCIENCE PUBLISHERS, 2020. http://dx.doi.org/10.2174/97898114608211200101.

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22

Brodie, Alasdair. Aromatase Inhibitors (Journal of Enzyme Inhibition). Harwood Academic (Medical, Reference and Social Sc, 1990.

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23

Baskar, G., K. Sathish Kumar, and K. Tamilarasan. Enzyme Inhibition - Environmental and Biomedical Applications. Bentham Science Publishers, 2020.

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24

Baskar, G., K. Sathish Kumar, and K. Tamilarasan. Enzyme Inhibition - Environmental and Biomedical Applications. Bentham Science Publishers, 2020.

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25

Baskar, G., K. Sathish Kumar, and K. Tamilarasan. Enzyme Inhibition - Environmental and Biomedical Applications. Bentham Science Publishers, 2020.

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26

(Editor), W. Jonat, and R. J. Santen (Editor), eds. Aromatase Inhibition - Present and Future. Taylor & Francis Ltd, 1991.

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27

Li, Albert P., and Chuang Lu. Enzyme Inhibition in Drug Discovery and Development. Wiley & Sons, Incorporated, John, 2010.

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28

Tang, Sishi. Computer modeling of enzyme catalysis and inhibition. 2006.

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29

Baici, Antonio. Kinetics of Enzyme-Modifier Interactions: Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms. Baici Antonio, 2015.

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30

Baici, Antonio. Kinetics of Enzyme-Modifier Interactions: Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms. Springer, 2016.

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31

Baici, Antonio. Kinetics of Enzyme-Modifier Interactions: Selected Topics in the Theory and Diagnosis of Inhibition and Activation Mechanisms. Springer London, Limited, 2015.

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32

Rashwan, Hesham. Studies on inhibition of GMP synthetase and MTA phosphorylase. 1986.

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33

Rosenthal, J. Focus on Angiotensin-Converting Enzyme Inhibition (Clinical Physiology and Biochemistry,). S. Karger AG (Switzerland), 1990.

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34

Bonomo, Robert A., and Marcelo E. Tolmasky. Enzyme-Mediated Resistance to Antibiotics: Mechanisms, Dissemination, and Prospects for Inhibition. Wiley & Sons, Limited, John, 2014.

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35

(Editor), Robert A. Bonomo, and Marcelo E. Tolmasky (Editor), eds. Enzyme-Mediated Resistance to Antibiotics: Mechanisms, Dissemination, and Prospects for Inhibition. ASM Press, 2007.

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36

Enzyme-mediated resistance to antibiotics: Mechanisms, dissemination, and prospects for inhibition. Washington, DC: ASM Press, 2007.

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37

Wasson, Diana H. Identification and characterization of a heat stable protease in arrowtooth flounder (Atheresthes stomias) and methods of inhibition in surimi. 1992.

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38

Li, Albert P., and Chuang Lu. Enzyme Inhibition in Drug Discovery and Development: The Good and the Bad. Wiley & Sons, Incorporated, John, 2010.

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39

Li, Albert P., and Chuang Lu. Enzyme Inhibition in Drug Discovery and Development: The Good and the Bad. Wiley & Sons, Limited, John, 2010.

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40

Bearne, Stephen Lewis *. Enzyme inhibition by phosphonates and protein modification by dicarboxylic acid bis (methyl phosphates). 1991.

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41

Piyachomkwan, Kuakoon. Apparent inhibition of Pacific whiting surimi-associated protease by whey protein concentrate. 1993.

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42

Yuan, Yanqiu. Targeting the bacterial cell wall: Structural insight into peptidoglycan glycosyltransferases and moenomycin inhibition. 2008.

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43

Leung, Eric. A novel technique for lychee enzyme inhibition and the conservation of its color and flavo. 2003.

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44

Struzebecher. Recent Developments in the Field of Thrombin Inhibitors: A special issue of the journal Enzyme Inhibition. Routledge, 1995.

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45

Mitsuya, H. Inhibitors of Reverse Transciptase and Viral Protease: A special issue of the Journal of Enzyme Inhibition (Drug Targeting and Delivery). Routledge, 1992.

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46

van Dorp, Eveline L. A., Douglas Eleveld, Erik Olofsen, and Jaap Vuyk. Drug distribution and elimination in anaesthetic practice. Edited by Michel M. R. F. Struys. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199642045.003.0012.

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An understanding of pharmacokinetics is vital for the practice of anaesthesia. Drugs are, after administration, distributed throughout the body to the effect site (mostly the brain) to exert their effects. This can be influenced by differences in protein binding, systemic blood flow, and concomitant medication. Elimination of drugs from the body is through two main routes: either unchanged through the kidneys or through metabolism by the liver (and consecutive excretion through the kidneys). This process depends on the amount of hepatic blood flow and the amount of hepatic extraction. This in turn depends on the amount of protein binding and the intrinsic hepatic clearance. The cytochrome P450 enzyme family also plays an important role in drug elimination. Individual differences in enzyme activity can lead to differences in drug effect and clearances. Changes in enzyme activity by enzyme induction and inhibition can also be of influence on drug clearance. Compartmental, non-compartmental, and physiologically based models, and various statistical approaches to estimate these models, may be used to analyze the distribution and elimination of anaesthetic agents.
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47

Wheeler, Laurie Ann. Urinary D-glucaric acid excretion as an index of hepatic enzyme induction/inhibition in the phenobarbital or vitamin D r treated guinea pig. 1985.

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48

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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49

Sada, Nagisa, and Tsuyoshi Inoue. Lactate Dehydrogenase. Edited by Detlev Boison. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190497996.003.0029.

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Glucose is transported into neurons and used as an energy source. It is also transported into astrocytes, a type of glial cell, and converted to lactate, which is then released to neurons and used as another energy source. The latter is called the astrocyte-neuron lactate shuttle. Although the lactate shuttle is a metabolic pathway, it also plays important roles in neuronal activities and brain functions. We recently reported that this metabolic pathway is involved in the antiepileptic effects of the ketogenic diet. Lactate dehydrogenase (LDH) is a metabolic enzyme that mediates the lactate shuttle, and its inhibition hyperpolarizes neurons and suppresses seizures. This enzyme is also a molecular target of stiripentol, a clinically used antiepileptic drug for Dravet syndrome. This review provides an overview of electrical regulation by the astrocyte-neuron lactate shuttle, and then introduces LDH as a metabolic target against epilepsy.
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50

Enzyme Inhibitor from Marine Organisms. MDPI, 2020. http://dx.doi.org/10.3390/books978-3-03943-784-9.

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