Books on the topic 'Methyltransferases'

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1

Margueron, Raphaël, and Daniel Holoch, eds. Histone Methyltransferases. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4.

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2

G, Clarke Steven, and Tamanoi Fuyuhiko, eds. Protein methyltransferases. Amsterdam: Academic Press, 2006.

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3

Jeltsch, Albert, and Renata Z. Jurkowska, eds. DNA Methyltransferases - Role and Function. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43624-1.

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4

Jeltsch, Albert, and Renata Z. Jurkowska, eds. DNA Methyltransferases - Role and Function. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-11454-0.

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5

Ki, Paik Woon, and Kim Sangduk, eds. Protein methylation. Boca Raton, Fla: CRC Press, 1990.

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6

F, Vani͡u︡shin B., ed. Strukturno-funkt͡s︡ionalʹnye osnovy ėnzimaticheskogo metilirovanii͡a︡ DNK. Moskva: VINITI, 1987.

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7

G, Chirikjian Jack, ed. Restriction endonucleases and methylases. New York: Elsevier, 1987.

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8

Leo, Colleen M. Thiopurine methyltransferase pharmacogenetics. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1992.

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9

Fitzpatrick, Teresa. Studies on the serine hydroxymethyltransferase catalysed exchange of the [alpha]-protons of amino acids. Dublin: University College Dublin, 1998.

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10

Henri, Grosjean, ed. DNA and RNA modification enzymes: Structure, mechanism, function, and evolution. Austin, Tex: Landes Bioscience, 2009.

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11

Levac, Dylan. The Catharanthus roseus 16-hydroxytabersonine O-methyltransferase involved in vindoline biosynthesis. St. Catharines, Ont: Brock University, Dept. of Biological Sciences, 2008.

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12

Gill, Kathryn Anne. Huaman liver nicotinamide-N-Methyltransferase: Population studies and enzyme partial purification. Birmingham: University of Birmingham, 1995.

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13

Yarychkivska, Olga. Biology of maintenance and de novo methylation mediated by DNA methyltransferase-1. [New York, N.Y.?]: [publisher not identified], 2017.

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14

Marks, Philip M. H. Expression, purification and characterisation of the novel type 1 1/2 methyltransferase M.AhdI. Portsmouth: University of Portsmouth, Institute of Biomedical and Biomolecular Sciences, 2002.

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15

Pakusch, Anne-Elisabeth. S-Adenosyl-L-methionin:trans-Kaffeoyl-CoA 3-O-Methyltransferase, ein ungewöhnliches Enzym der pflanzlichen Abwehr: Molekulare Charakterisierung und Regulation. [s.l.]: [s.n.], 1991.

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16

Kim, Eun-Joo. Untersuchungen zur Altersabhängigkeit der Catechol-O-Methyltransferase (COMT) sowie der Catachol-Oestrogene bei der Ratte und Einfluss von Piracetam-Behandlung. [s.l.]: [s.n.], 1985.

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17

Protein Methyltransferases. Elsevier, 2006. http://dx.doi.org/10.1016/s1874-6047(06)x8002-2.

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18

Tamanoi, Fuyuhiko, and Steven G. Clarke. Enzymes: Protein Methyltransferases. Elsevier Science & Technology Books, 2011.

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19

Cheng, Xiaodong, and Robert M. Blumenthal. S-Adenosylmethionine-Dependent Methyltransferases. WORLD SCIENTIFIC, 1999. http://dx.doi.org/10.1142/4098.

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20

Margueron, Raphael, and Daniel Holoch. Histone Methyltransferases: Methods and Protocols. Springer, 2022.

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21

Jeltsch, Albert, and Renata Z. Jurkowska. DNA Methyltransferases - Role and Function. Springer International Publishing AG, 2018.

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22

Jeltsch, Albert, and Renata Z. Jurkowska. DNA Methyltransferases - Role and Function. Springer, 2016.

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23

Jeltsch, Albert, and Renata Z. Jurkowska. DNA Methyltransferases - Role and Function. Springer, 2016.

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24

Jeltsch, Albert, and Renata Z. Jurkowska. DNA Methyltransferases - Role and Function. Springer International Publishing AG, 2022.

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25

Structure, Activity, and Function of Protein Methyltransferases. MDPI, 2022. http://dx.doi.org/10.3390/books978-3-0365-3707-8.

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26

Role of DNA Methyltransferases in the Epigenome. MDPI, 2020. http://dx.doi.org/10.3390/books978-3-03928-021-6.

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27

(Editor), Robert M. Blumenthal, ed. S-Adenosylmethionine-Dependent Methyltransferases: Structures and Functions. World Scientific Publishing Company, 2000.

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28

S-Adenosylmethionine-Dependent Methyltransferases: Structures and Functions. World Scientific Publishing Co Pte Ltd, 1999.

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29

The Enzymes, Volume 24: Protein Methyltransferases (The Enzymes). Academic Press, 2006.

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30

(Editor), Fuyuhiko Tamanoi, and Steven Clarke (Editor), eds. The Enzymes, Volume 24: Protein Methyltransferases (The Enzymes). Academic Press, 2006.

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31

Lindquist, Jonathan A. Automethylation: A response to enzyme aging. 1995.

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32

Bhardwaj, Swati. Cytosine DNA Methyltransferases in the Moss, Physcomitrella patens. LAP Lambert Academic Publishing, 2013.

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33

Grosjean, Henri. DNA and RNA Modification Enzymes: Structure, Mechanism, Function and Evolution. Taylor & Francis Group, 2009.

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34

Grosjean, Henri. DNA and RNA Modification Enzymes: Structure, Mechanism, Function and Evolution. Taylor & Francis Group, 2009.

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35

Morell-Ducos, Fausto. COMT and morphine use in cancer pain. Edited by Paul Farquhar-Smith, Pierre Beaulieu, and Sian Jagger. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198834359.003.0082.

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The landmark paper discussed in this chapter is ‘Genetic variation in the catechol-O-methyltransferase (COMT) gene and morphine requirements in cancer patients with pain’, published by Rakvåg et al. in 2008. Genetic variation contributes to differences in pain sensitivity and response to analgesics. Catecholamines are involved in the modulation of pain and are metabolized by catchol-O-methyltransferase (COMT). Genetic variability in the COMT gene may therefore contribute to differences in pain sensitivity and response to analgesics. It has been shown that a polymorphism in the COMT gene, Rs4680 (val158met), influences pain sensitivity and efficacy for morphine in cancer pain treatment. This study investigated whether the variability in other regions in the COMT gene also contributes to the inter-individual variability of morphine efficacy by mapping 11 single nucleotide polymorphisms, constructing haplotypes from them, and then comparing genotypes and haplotypes against pharmacological, demographic, and patient symptom measurements in patients receiving morphine for cancer pain.
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36

Basic Aspects of Catechol-O-Methyltransferase and the Clinical Applications of its Inhibitors. Elsevier, 2010. http://dx.doi.org/10.1016/c2009-0-62373-4.

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37

Nissinen, Erkki. Basic Aspects of Catechol-O-Methyltransferase and the Clinical Applications of Its Inhibitors. Elsevier Science & Technology Books, 2010.

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38

Basic Aspects of Catechol-O-Methyltransferase and the Clinical Applications of Its Inhibitors. Elsevier Science & Technology Books, 2010.

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39

Jugel, Anja. Charakterisierung von DNA Bindungseigenschaften der DNA Methyltransferasen M. BspRI, M. SPR, M.o3T und mutierter Derivate. 1991.

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40

Lerner, Christian Daniel. Strukturbasiertes Design, Synthese und in vitro Bewertung von Bisubstrat-Inhibitoren der Catechol-O-Methyltransferase (COMT). 2003.

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41

Schutz, Peter W., and Sylvia Stockler. Cerebral Creatine Deficiency Disorders. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0065.

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Cerebral creatine deficiency disorders that result in very low levels of creatine in the brain, can cause in intellectual disability, seizures, expressive speech disorder and behavior disorders if not treated in early childhood. CCDDs comprise disorders of creatine synthesis (arginine:glycine [AGAT; MIM 602360]; guanidinoacetate methyltransferase deficiency [GAMT; MIM 601240]) and of creatine transport (SLC6A8 deficiency [SLC6A8; MIM 300036]). Inborn errors of creatine synthesis-but not, as yet, of transport-can be treated by creatine substitution and are thus treatable causes of intellectual disability.
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42

Masjost, Birgit. Structure-based design, synthesis and in vitro evaluation of bisubstrate inhibitors for catechol O-methyltransferase (COMT). 2000.

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43

Didovyk, Andriy. The structural basis of DNA recognition and base extrusion by a DNA cytosine-5 methyltransferase M.HaeIII. 2010.

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44

Park, Lindsay Jane. Characterization of the ionizing radiation-inducible gene O6-methylguanine DNA methyltransferase and its role in radiation responses . 2004.

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45

Yan, Lu. Polymorphisms in the catechol-O-methyltransferase gene ( COMT) affect the risk for chronic post-mastectomy pain syndrome (PMPS). 2006.

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46

Streitberg, Michael. Selektives Screening nach dem guanidinoacetat-methyltransferase (GAMT)-defekt gaschromatographisch-massenspektrometrische Quantitizierung der Guanidinoessigsäure mit deuteriertem intemem Standard (d₂-GAA). 2003.

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47

Weller, Michael, Michael Brada, Tai-Tong Wong, and Michael A. Vogelbaum. Astrocytic tumours: diffuse astrocytoma, anaplastic astrocytoma, glioblastoma, and gliomatosis cerebri. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199651870.003.0003.

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Astrocytic gliomas are primary brain tumours thought to originate from neural stem or progenitor cells. They are assigned grades II, III, or IV by the World Health Organization according to degree of malignancy as defined by histology. The following molecular markers are increasingly used for diagnostic subclassification or clinical decision-making: 1p/19q co-deletion status, O6-methylguanine-DNA methyltransferase (MGMT) promoter methylation status, and isocitrate dehydrogenase 1 and 2 mutation status. Extent of resection is a favourable prognostic factor, but surgery is never curative. Radiotherapy prolongs progression-free survival across all astrocytic glioma entities. Alkylating agent chemotherapy is an active treatment in particular for patients with MGMT promoter-methylated tumours. Anti-angiogenic therapies have failed to improve survival, and the current focus of major clinical trials is on novel targeted agents or on immunotherapy.
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48

Hanneken, Ludger. Einfluss von variationen des erdmagnetfeldes (EMF) auf die aktivität der hydroxyindol-D-methyltransferase und N-acetyltransferase in retina und pinealorgan von hühnerembryonen. 1986.

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49

Trus, Michael. Altering retinoid sensitivity in acute myeloblastic leukemia cells by treatment with the histone deacetylase inhibitor, valproic acid, and the inhibitor of DNA methyltransferase activity, 5-aza-2'-deoxycytidine. 2006.

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50

Hong, Chi-Chen. Influence of genetic polymorphisms in P450 C17[alpha](T27C), catechol-O-methyltransferase (VAL158MET), and activity level of cytochrome P450 1A2 on mammographic density levels and other risk factors for breast cancer. 2004.

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