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Journal articles on the topic 'N-methyltransferase'

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1

Ganzetti, Giulia, Davide Sartini, Anna Campanati, et al. "Nicotinamide N-methyltransferase." Melanoma Research 28, no. 2 (2018): 82–88. http://dx.doi.org/10.1097/cmr.0000000000000430.

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2

Weinshilboum, Richard M., Diane M. Otterness, and Carol L. Szumlanski. "METHYLATION PHARMACOGENETICS: Catechol O-Methyltransferase, Thiopurine Methyltransferase, and Histamine N-Methyltransferase." Annual Review of Pharmacology and Toxicology 39, no. 1 (1999): 19–52. http://dx.doi.org/10.1146/annurev.pharmtox.39.1.19.

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3

Yan, Dongsheng, Yong Zhang, Lifang Niu, Yi Yuan, and Xiaofeng Cao. "Identification and characterization of two closely related histone H4 arginine 3 methyltransferases in Arabidopsis thaliana." Biochemical Journal 408, no. 1 (2007): 113–21. http://dx.doi.org/10.1042/bj20070786.

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Arginine methylation of histone H3 and H4 plays important roles in transcriptional regulation in eukaryotes such as yeasts, fruitflies, nematode worms, fish and mammals; however, less is known in plants. In the present paper, we report the identification and characterization of two Arabidopsis thaliana protein arginine N-methyltransferases, AtPRMT1a and AtPRMT1b, which exhibit high homology with human PRMT1. Both AtPRMT1a and AtPRMT1b methylated histone H4, H2A, and myelin basic protein in vitro. Site-directed mutagenesis of the third arginine (R3) on the N-terminus of histone H4 to lysine (H4
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4

Ashihara, Hiroshi. "Biosynthetic Pathways of Purine and Pyridine Alkaloids in Coffee Plants." Natural Product Communications 11, no. 7 (2016): 1934578X1601100. http://dx.doi.org/10.1177/1934578x1601100742.

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Caffeine (1,3,7- N-trimethylxanthine) and trigonelline (1 N-methylnicotinic acid) are major alkaloids in coffee plants. The key enzymes involved in the biosynthesis of these compounds are very closely related N-methyltransferases belonging to the motif B’ family of methyltransferases. The major biosynthetic pathways of caffeine and trigonelline are summarized in this review, including new evidence obtained from recombinant enzymes. In addition, precursor supply pathways are discussed with newly obtained results. Transgenic plants produced by the modification of the expression of N-methyltransf
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5

Vance, Dennis E., Christopher J. Walkey, and Zheng Cui. "Phosphatidylethanolamine N-methyltransferase from liver." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1348, no. 1-2 (1997): 142–50. http://dx.doi.org/10.1016/s0005-2760(97)00108-2.

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6

Yan, Lan, Diane M. Otterness, Timothy L. Craddock, and Richard M. Weinshilboum. "Mouse Liver Nicotinamide N-Methyltransferase:." Biochemical Pharmacology 54, no. 10 (1997): 1139–49. http://dx.doi.org/10.1016/s0006-2952(97)00325-0.

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7

Nemmara, Venkatesh V., Ronak Tilvawala, Ari J. Salinger, et al. "Citrullination Inactivates Nicotinamide-N-methyltransferase." ACS Chemical Biology 13, no. 9 (2018): 2663–72. http://dx.doi.org/10.1021/acschembio.8b00578.

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8

Futo, Judit, Josh P. Kupferberg, Jonathan Moss, Mark R. Fahey, John E, and Ronald D. Miller. "Vecuronium Inhibits Histamine N-Methyltransferase." Anesthesiology 69, no. 1 (1988): 92–96. http://dx.doi.org/10.1097/00000542-198807000-00014.

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9

Yan, Lan, Diane M. Otterness, and Richard M. Weinshilboum. "Human nicotinamide N-methyltransferase pharmacogenetics." Pharmacogenetics 9, no. 3 (1999): 307–16. http://dx.doi.org/10.1097/00008571-199906000-00005.

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10

Moss, J., K. M. Verburg, and D. P. Henry. "DROPERIDOL INHIBITS HISTAMINE N-METHYLTRANSFERASE." Anesthesiology 63, Supplement (1985): A303. http://dx.doi.org/10.1097/00000542-198509001-00303.

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11

Zhou, Yangsheng, Debashish Ray, Yiwei Zhao, et al. "Structure and Function of Flavivirus NS5 Methyltransferase." Journal of Virology 81, no. 8 (2007): 3891–903. http://dx.doi.org/10.1128/jvi.02704-06.

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ABSTRACT The plus-strand RNA genome of flavivirus contains a 5′ terminal cap 1 structure (m7GpppAmG). The flaviviruses encode one methyltransferase, located at the N-terminal portion of the NS5 protein, to catalyze both guanine N-7 and ribose 2′-OH methylations during viral cap formation. Representative flavivirus methyltransferases from dengue, yellow fever, and West Nile virus (WNV) sequentially generate GpppA → m7GpppA → m7GpppAm. The 2′-O methylation can be uncoupled from the N-7 methylation, since m7GpppA-RNA can be readily methylated to m7GpppAm-RNA. Despite exhibiting two distinct methy
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12

Rivas, Maria Prates, Talita Ferreira Marques Aguiar, Mariana Maschietto, et al. "Hepatoblastomas exhibit marked NNMT downregulation driven by promoter DNA hypermethylation." Tumor Biology 42, no. 12 (2020): 101042832097712. http://dx.doi.org/10.1177/1010428320977124.

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Hepatoblastomas exhibit the lowest mutational burden among pediatric tumors. We previously showed that epigenetic disruption is crucial for hepatoblastoma carcinogenesis. Our data revealed hypermethylation of nicotinamide N-methyltransferase, a highly expressed gene in adipocytes and hepatocytes. The expression pattern and the role of nicotinamide N-methyltransferase in pediatric liver tumors have not yet been explored, and this study aimed to evaluate the effect of nicotinamide N-methyltransferase hypermethylation in hepatoblastomas. We evaluated 45 hepatoblastomas and 26 non-tumoral liver sa
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13

Drozak, Jakub, Lukasz Chrobok, Olga Poleszak, Adam K. Jagielski, and Rafal Derlacz. "Molecular Identification of Carnosine N-Methyltransferase as Chicken Histamine N-Methyltransferase-Like Protein (HNMT-Like)." PLoS ONE 8, no. 5 (2013): e64805. http://dx.doi.org/10.1371/journal.pone.0064805.

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14

Yoshikawa, Takeo, Tadaho Nakamura, and Kazuhiko Yanai. "Histamine N-Methyltransferase in the Brain." International Journal of Molecular Sciences 20, no. 3 (2019): 737. http://dx.doi.org/10.3390/ijms20030737.

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Brain histamine is a neurotransmitter and regulates diverse physiological functions. Previous studies have shown the involvement of histamine depletion in several neurological disorders, indicating the importance of drug development targeting the brain histamine system. Histamine N-methyltransferase (HNMT) is a histamine-metabolising enzyme expressed in the brain. Although pharmacological studies using HNMT inhibitors have been conducted to reveal the direct involvement of HNMT in brain functions, HNMT inhibitors with high specificity and sufficient blood–brain barrier permeability have not be
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15

Loring, Heather S., and Paul R. Thompson. "Kinetic Mechanism of Nicotinamide N-Methyltransferase." Biochemistry 57, no. 38 (2018): 5524–32. http://dx.doi.org/10.1021/acs.biochem.8b00775.

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16

Wong, D. L., C. L. Bildstein, B. L. Siddall, and A. S. Lesage. "NEURAL REGULATION OF PHENYLETHANOLAMINE N-METHYLTRANSFERASE." Clinical Neuropharmacology 15 (1992): 133B. http://dx.doi.org/10.1097/00002826-199202001-00256.

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17

Ridgway, N. D., and D. E. Vance. "Kinetic mechanism of phosphatidylethanolamine N-methyltransferase." Journal of Biological Chemistry 263, no. 32 (1988): 16864–71. http://dx.doi.org/10.1016/s0021-9258(18)37471-4.

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18

Vance, Dennis E. "Physiological roles of phosphatidylethanolamine N-methyltransferase." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1831, no. 3 (2013): 626–32. http://dx.doi.org/10.1016/j.bbalip.2012.07.017.

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19

Ruszkowska, Agnieszka. "METTL16, Methyltransferase-Like Protein 16: Current Insights into Structure and Function." International Journal of Molecular Sciences 22, no. 4 (2021): 2176. http://dx.doi.org/10.3390/ijms22042176.

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Methyltransferase-like protein 16 (METTL16) is a human RNA methyltransferase that installs m6A marks on U6 small nuclear RNA (U6 snRNA) and S-adenosylmethionine (SAM) synthetase pre-mRNA. METTL16 also controls a significant portion of m6A epitranscriptome by regulating SAM homeostasis. Multiple molecular structures of the N-terminal methyltransferase domain of METTL16, including apo forms and complexes with S-adenosylhomocysteine (SAH) or RNA, provided the structural basis of METTL16 interaction with the coenzyme and substrates, as well as indicated autoinhibitory mechanism of the enzyme activ
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20

Ashihara, Hiroshi. "Metabolism of alkaloids in coffee plants." Brazilian Journal of Plant Physiology 18, no. 1 (2006): 1–8. http://dx.doi.org/10.1590/s1677-04202006000100001.

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Coffee beans contain two types of alkaloids, caffeine and trigonelline, as major components. This review describes the distribution and metabolism of these compounds. Caffeine is synthesised from xanthosine derived from purine nucleotides. The major biosynthetic route is xanthosine -> 7-methylxanthosine -> 7-methylxanthine -> theobromine -> caffeine. Degradation activity of caffeine in coffee plants is very low, but catabolism of theophylline is always present. Theophylline is converted to xanthine, and then enters the conventional purine degradation pathway. A recent development i
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21

Gou, Qing, ShuJiao He, and ZeJian Zhou. "Protein arginine N-methyltransferase 1 promotes the proliferation and metastasis of hepatocellular carcinoma cells." Tumor Biology 39, no. 2 (2017): 101042831769141. http://dx.doi.org/10.1177/1010428317691419.

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Hepatocellular carcinoma is the most common subtype of liver cancer. Protein arginine N-methyltransferase 1 was shown to be upregulated in various cancers. However, the role of protein arginine N-methyltransferase 1 in hepatocellular carcinoma progression remains incompletely understood. We investigated the clinical and functional significance of protein arginine N-methyltransferase 1 in a series of clinical hepatocellular carcinoma samples and a panel of hepatocellular carcinoma cell lines. We performed suppression analysis of protein arginine N-methyltransferase 1 using small interfering RNA
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22

Chu, Uyen B., Sevahn K. Vorperian, Kenneth Satyshur, et al. "Noncompetitive Inhibition of Indolethylamine-N-methyltransferase by N,N-Dimethyltryptamine and N,N-Dimethylaminopropyltryptamine." Biochemistry 53, no. 18 (2014): 2956–65. http://dx.doi.org/10.1021/bi500175p.

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23

Shimbhu, Dawan, Kohichi Kojima, and Toshiharu Nagatsu. "A SENSITIVE ASSAY FOR NON-SPECIFIC N-METHYLTRANSFERASE ACTIVITY IN RAT TISSUES BY HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY ELECTROCHEMICAL DETECTION." ASEAN Journal on Science and Technology for Development 19, no. 1 (2017): 63–68. http://dx.doi.org/10.29037/ajstd.318.

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Phenylethanolamine N-methyltransferase (PNMT) and non-specific N -methyltransferase (EC 2.1.1.28) catalyze the N-methylation of aromatic amines. PNMT is specific for phenylethanolamines such as noradrenaline (NA). and catalyzes the step in catecholamine biosynthesis, forming adrenaline (AD) from NA. PNMT activity is high in adrenal gland, whereas non-specific N-methyltransferase is distributed in various tissues such as the lungs. Borchardt et al. first reported a method to detect PNMT activity by high-performance liquid chromatography electrochemical detection (HPLC-EICD), which could demonst
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24

Brosnan, John T., Rene L. Jacobs, Lori M. Stead, and Margaret E. Brosnan. "Methylation demand: a key determinant of homocysteine metabolism." Acta Biochimica Polonica 51, no. 2 (2004): 405–13. http://dx.doi.org/10.18388/abp.2004_3580.

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Elevated plasma homocysteine is a risk factor for cardiovascular disease and Alzheimer's disease. To understand the factors that determine the plasma homocysteine level it is necessary to appreciate the processes that produce homocysteine and those that remove it. Homocysteine is produced as a result of methylation reactions. Of the many methyltransferases, two are, normally, of the greatest quantitative importance. These are guanidinoacetate methyltransferase (that produces creatine) and phosphatidylethanolamine N-methyltransferase (that produces phosphatidylcholine). In addition, methylation
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25

Rowe, P. M., L. S. Wright, and F. L. Siegel. "Calmodulin N-methyltransferase. Partial purification and characterization." Journal of Biological Chemistry 261, no. 15 (1986): 7060–69. http://dx.doi.org/10.1016/s0021-9258(19)62721-3.

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26

Biastoff, Stefan, Wolfgang Brandt, and Birgit Dräger. "Putrescine N-methyltransferase – The start for alkaloids." Phytochemistry 70, no. 15-16 (2009): 1708–18. http://dx.doi.org/10.1016/j.phytochem.2009.06.012.

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27

Ramsden, David B., Rosemary H. Waring, David J. Barlow, and Richard B. Parsons. "Nicotinamide N-Methyltransferase in Health and Cancer." International Journal of Tryptophan Research 10 (January 1, 2017): 117864691769173. http://dx.doi.org/10.1177/1178646917691739.

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Over the past decade, the roles of nicotinamide N-methyltransferase and its product 1-methyl nicotinamide have emerged from playing merely minor roles in phase 2 xenobiotic metabolism as actors in some of the most important scenes of human life. In this review, the structures of the gene, messenger RNA, and protein are discussed, together with the role of the enzyme in many of the common cancers that afflict people today.
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28

Ramsden, David B., Rosemary H. Waring, Richard B. Parsons, David J. Barlow, and Adrian C. Williams. "Nicotinamide N-Methyltransferase: Genomic Connection to Disease." International Journal of Tryptophan Research 13 (January 2020): 117864692091977. http://dx.doi.org/10.1177/1178646920919770.

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Single-nucleotide polymorphisms (SNPs) in and around the nicotinamide N-methyltransferase (NNMT) gene are associated with a range of cancers and other diseases and conditions. The data on these associations have been assembled, and their strength discussed. There is no evidence that the presence of either the major or minor base in any SNP affects the expression of nicotinamide N-methyltransferase. Nevertheless, suggestions have been put forward that some of these SNPs do affect NNMT expression and thus homocysteine metabolism. An alternative idea involving non-coding messenger RNAs (mRNAs) is
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29

Hausmann, Stéphane, Sushuang Zheng, Carme Fabrega, Stewart W. Schneller, Christopher D. Lima, and Stewart Shuman. "Encephalitozoon cuniculimRNA Cap (Guanine N-7) Methyltransferase." Journal of Biological Chemistry 280, no. 21 (2005): 20404–12. http://dx.doi.org/10.1074/jbc.m501073200.

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30

Kennedy, B., H. Elayan, and M. G. Ziegler. "Glucocorticoid hypertension and nonadrenal phenylethanolamine N-methyltransferase." Hypertension 21, no. 4 (1993): 415–19. http://dx.doi.org/10.1161/01.hyp.21.4.415.

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31

Mahmoodi, Niusha, Rajesh K. Harijan, and Vern L. Schramm. "Transition-State Analogues of Phenylethanolamine N-Methyltransferase." Journal of the American Chemical Society 142, no. 33 (2020): 14222–33. http://dx.doi.org/10.1021/jacs.0c05446.

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32

Tai, Tze Chun, David C. Wong-Faull, Robert Claycomb, Jennifer L. Aborn, and Dona Lee Wong. "PACAP-regulated phenylethanolamine N-methyltransferase gene expression." Journal of Neurochemistry 115, no. 5 (2010): 1195–205. http://dx.doi.org/10.1111/j.1471-4159.2010.07005.x.

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33

Iyamu, Iredia D., and Rong Huang. "Mechanisms and inhibitors of nicotinamide N-methyltransferase." RSC Medicinal Chemistry 12, no. 8 (2021): 1254–61. http://dx.doi.org/10.1039/d1md00016k.

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34

Yu, Peter H., Bruce A. Davis, and David A. Durden. "Enzymatic N-methylation of phenelzine catalyzed by phenylethanolamine N-methyltransferase." Progress in Neuro-Psychopharmacology and Biological Psychiatry 15, no. 2 (1991): 307–12. http://dx.doi.org/10.1016/0278-5846(91)90098-l.

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35

Dong, Hongping, Katja Fink, Roland Züst, Siew Pheng Lim, Cheng-Feng Qin, and Pei-Yong Shi. "Flavivirus RNA methylation." Journal of General Virology 95, no. 4 (2014): 763–78. http://dx.doi.org/10.1099/vir.0.062208-0.

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The 5′ end of eukaryotic mRNA contains the type-1 (m7GpppNm) or type-2 (m7GpppNmNm) cap structure. Many viruses have evolved various mechanisms to develop their own capping enzymes (e.g. flavivirus and coronavirus) or to ‘steal’ caps from host mRNAs (e.g. influenza virus). Other viruses have developed ‘cap-mimicking’ mechanisms by attaching a peptide to the 5′ end of viral RNA (e.g. picornavirus and calicivirus) or by having a complex 5′ RNA structure (internal ribosome entry site) for translation initiation (e.g. picornavirus, pestivirus and hepacivirus). Here we review the diverse viral RNA
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36

Gearhart, Debra A., Edward J. Neafsey та Michael A. Collins. "Phenylethanolamine N-methyltransferase has β-carboline 2N-methyltransferase activity: hypothetical relevance to Parkinson’s disease". Neurochemistry International 40, № 7 (2002): 611–20. http://dx.doi.org/10.1016/s0197-0186(01)00115-2.

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37

Kloor, Doris, Katrin Karnahl, and Jost Kömpf. "Characterization of glycineN-methyltransferase from rabbit liver." Biochemistry and Cell Biology 82, no. 3 (2004): 369–74. http://dx.doi.org/10.1139/o04-007.

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The enzymatic properties of glycine N-methyltransferase from rabbit liver and the effects of endogenous adenosine nucleosides, nucleotides and methyltransferase inhibitors were investigated using a photometrical assay to detect sarcosine with o-dianisidine as a dye. After isolation and purification the denatured enzyme showed a two-banded pattern by SDS–PAGE. The enzyme was highly specific for its substrates with a pH-optimum at pH 8.6. Glycine N-methyltransferase exhibits Michaelis-Menten kinetics for its substrates, S-adenosylmethionine and glycine, respectively. The apparent Kmand Vmaxvalue
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38

Pawlik, Grzegorz, Mike F. Renne, Matthijs A. Kol, and Anton I. P. M. de Kroon. "The topology of the ER-resident phospholipid methyltransferase Opi3 of Saccharomyces cerevisiae is consistent with in trans catalysis." Journal of Biological Chemistry 295, no. 8 (2020): 2473–82. http://dx.doi.org/10.1074/jbc.ra119.011102.

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Phospholipid N-methyltransferases (PLMTs) synthesize phosphatidylcholine by methylating phosphatidylethanolamine using S-adenosylmethionine as a methyl donor. Eukaryotic PLMTs are integral membrane enzymes located in the endoplasmic reticulum (ER). Recently Opi3, a PLMT of the yeast Saccharomyces cerevisiae was proposed to perform in trans catalysis, i.e. while localized in the ER, Opi3 would methylate lipid substrates located in the plasma membrane at membrane contact sites. Here, we tested whether the Opi3 active site is located at the cytosolic side of the ER membrane, which is a prerequisi
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39

Ridgway, N. D., Z. Yao, and D. E. Vance. "Phosphatidylethanolamine Levels and Regulation of Phosphatidylethanolamine N- Methyltransferase." Journal of Biological Chemistry 264, no. 2 (1989): 1203–7. http://dx.doi.org/10.1016/s0021-9258(19)85072-x.

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40

Ridgway, N. D., and D. E. Vance. "Purification of phosphatidylethanolamine N-methyltransferase from rat liver." Journal of Biological Chemistry 262, no. 35 (1987): 17231–39. http://dx.doi.org/10.1016/s0021-9258(18)45514-7.

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41

Wong, D. L., and T. C. Tai. "444. Phenylethanolamine N-methyltransferase gene: neural signalling mechanism." Biological Psychiatry 47, no. 8 (2000): S136. http://dx.doi.org/10.1016/s0006-3223(00)00714-9.

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42

TAHARA, Yasutaka, Tomoyuki YAMASHITA, Atsushi SOGABE, Yoshihiro OGAWA, and Yuzo YAMADA. "Zymomonas mobilis mutant defective in phosphatidylethanolamine N-methyltransferase." Agricultural and Biological Chemistry 51, no. 11 (1987): 3179–81. http://dx.doi.org/10.1271/bbb1961.51.3179.

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43

Yeo, E. J., and C. Wagner. "Purification and properties of pancreatic glycine N-methyltransferase." Journal of Biological Chemistry 267, no. 34 (1992): 24669–74. http://dx.doi.org/10.1016/s0021-9258(18)35816-2.

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44

Richardson, Stacie L., Yunfei Mao, Gang Zhang, Pahul Hanjra, Darrell L. Peterson, and Rong Huang. "Kinetic Mechanism of Protein N-terminal Methyltransferase 1." Journal of Biological Chemistry 290, no. 18 (2015): 11601–10. http://dx.doi.org/10.1074/jbc.m114.626846.

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45

Wong, Dona L., Anne Lesage, Brenda Siddall, and John W. Funder. "Glucocorticoid regulation of phenylethanolamine N ‐methyltransferase in vivo." FASEB Journal 6, no. 14 (1992): 3310–15. http://dx.doi.org/10.1096/fasebj.6.14.1426768.

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46

Kitano, Haruna, Takeo Yoshikawa, and Kazuhiko Yanai. "Drug development targeting histamine N-methyltransferase." Proceedings for Annual Meeting of The Japanese Pharmacological Society 92 (2019): 1—P—006. http://dx.doi.org/10.1254/jpssuppl.92.0_1-p-006.

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47

TSVETNITSKY, VADIM, LUMA AUCHI, FRANCIS A. YEBOAH, and WILLIAM A. GIBBONS. "Isozymes of rat brain myelin phospholipid-N-methyltransferase." Biochemical Society Transactions 21, no. 4 (1993): 489S. http://dx.doi.org/10.1042/bst021489s.

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48

Bennett, Matthew R., Mark L. Thompson, Sarah A. Shepherd, et al. "Structure and Biocatalytic Scope of Coclaurine N ‐Methyltransferase." Angewandte Chemie 130, no. 33 (2018): 10760–64. http://dx.doi.org/10.1002/ange.201805060.

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49

Pattanayek, R., M. E. Newcomer, and C. Wagner. "Crystal structure of apo-glycine N-methyltransferase (GNMT)." Protein Science 7, no. 6 (1998): 1326–31. http://dx.doi.org/10.1002/pro.5560070608.

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50

Bennett, Matthew R., Mark L. Thompson, Sarah A. Shepherd, et al. "Structure and Biocatalytic Scope of Coclaurine N ‐Methyltransferase." Angewandte Chemie International Edition 57, no. 33 (2018): 10600–10604. http://dx.doi.org/10.1002/anie.201805060.

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