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Journal articles on the topic 'UDP-glucose pyrophosphorylase'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Kleczkowski, Leszek A., Matt Geisler, Elisabeth Fitzek, and Malgorzata Wilczynska. "A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases." Biochemical Journal 439, no. 3 (2011): 375–81. http://dx.doi.org/10.1042/bj20110730.

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Plant pyrophosphorylases that are capable of producing UDP-sugars, key precursors for glycosylation reactions, include UDP-glucose pyrophosphorylases (A- and B-type), UDP-sugar pyrophosphorylase and UDP-N-acetylglucosamine pyrophosphorylase. Although not sharing significant homology at the amino acid sequence level, the proteins share a common structural blueprint. Their structures are characterized by the presence of the Rossmann fold in the central (catalytic) domain linked to enzyme-specific N-terminal and C-terminal domains, which may play regulatory functions. Molecular mobility between t

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2

Silva, Elisabete, Ana Rita Marques, Arsénio Mendes Fialho, Ana Teresa Granja, and Isabel Sá-Correia. "Proteins Encoded by Sphingomonas elodea ATCC 31461 rmlA and ugpG Genes, Involved in Gellan Gum Biosynthesis, Exhibit both dTDP- and UDP-Glucose Pyrophosphorylase Activities." Applied and Environmental Microbiology 71, no. 8 (2005): 4703–12. http://dx.doi.org/10.1128/aem.71.8.4703-4712.2005.

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ABSTRACT The commercial gelling agent gellan is a heteropolysaccharide produced by Sphingomonas elodea ATCC 31461. In this work, we carried out the biochemical characterization of the enzyme encoded by the first gene (rmlA) of the rml 4-gene cluster present in the 18-gene cluster required for gellan biosynthesis (gel cluster). Based on sequence homology, the putative rml operon is presumably involved in the biosynthesis of dTDP-rhamnose, the sugar necessary for the incorporation of rhamnose in the gellan repeating unit. Heterologous RmlA was purified as a fused His6-RmlA protein from extracts

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3

Prakash, Ohm, Jana Führing, John Post, et al. "Identification of Leishmania major UDP-Sugar Pyrophosphorylase Inhibitors Using Biosensor-Based Small Molecule Fragment Library Screening." Molecules 24, no. 5 (2019): 996. http://dx.doi.org/10.3390/molecules24050996.

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Leishmaniasis is a neglected disease that is caused by different species of the protozoan parasite Leishmania, and it currently affects 12 million people worldwide. The antileishmanial therapeutic arsenal remains very limited in number and efficacy, and there is no vaccine for this parasitic disease. One pathway that has been genetically validated as an antileishmanial drug target is the biosynthesis of uridine diphosphate-glucose (UDP-Glc), and its direct derivative UDP-galactose (UDP-Gal). De novo biosynthesis of these two nucleotide sugars is controlled by the specific UDP-glucose pyrophosp

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4

Signorini, M., C. Ferrari, E. Mariotti, F. Dallocchio, and C. M. Bergamini. "Inactivation of skeletal-muscle UDP-glucose pyrophosphorylase by reaction with carboxylate-directed reagents." Biochemical Journal 264, no. 3 (1989): 799–804. http://dx.doi.org/10.1042/bj2640799.

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Skeletal-muscle UDP-glucose pyrophosphorylase is inactivated by reaction with 2-ethoxy-N-(ethoxy-carbonyl)-1,2-dihydroquinoline (EEDQ) and 1-(3-dimethylaminopropyl-3-ethylcarbodi-imide (EDAC), two reagents specific for carboxylate groups. The former reagent is a more effective inactivator than EDAC. Although no evidence of reversible enzyme-reagent complexes of the affinity-labelling type was obtained by kinetic analysis of the inactivation, the selective protection of UDP-glucose pyrophosphorylase activity against inactivation by EEDQ in the presence of uridine substrates is indicative of an

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5

Rodríguez-Díaz, Jesús, and María J. Yebra. "Enhanced UDP-glucose and UDP-galactose by homologous overexpression of UDP-glucose pyrophosphorylase in Lactobacillus casei." Journal of Biotechnology 154, no. 4 (2011): 212–15. http://dx.doi.org/10.1016/j.jbiotec.2011.05.015.

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6

Kleczkowski, Leszek A., Françoise Martz, and Malgorzata Wilczynska. "Factors affecting oligomerization status of UDP-glucose pyrophosphorylase." Phytochemistry 66, no. 24 (2005): 2815–21. http://dx.doi.org/10.1016/j.phytochem.2005.09.034.

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7

Kusunoki, M., Y. Kitagawa, H. Naitou та ін. "Left-handed β-helix protein UDP-glucose pyrophosphorylase". Acta Crystallographica Section A Foundations of Crystallography 52, a1 (1996): C110—C111. http://dx.doi.org/10.1107/s0108767396094731.

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8

Chen, Rongzhi, Xiao Zhao, Zhe Shao, Lili Zhu, and Guangcun He. "Multiple isoforms of UDP-glucose pyrophosphorylase in rice." Physiologia Plantarum 129, no. 4 (2007): 725–36. http://dx.doi.org/10.1111/j.1399-3054.2007.00865.x.

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9

Kleczkowski, Leszek A. "Glucose activation and metabolism through UDP-glucose pyrophosphorylase in plants." Phytochemistry 37, no. 6 (1994): 1507–15. http://dx.doi.org/10.1016/s0031-9422(00)89568-0.

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10

Lamerz, Anne-Christin, Sebastian Damerow, Barbara Kleczka, et al. "Deletion of UDP-glucose pyrophosphorylase reveals a UDP-glucose independent UDP-galactose salvage pathway in Leishmania major." Glycobiology 20, no. 7 (2010): 872–82. http://dx.doi.org/10.1093/glycob/cwq045.

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11

HIGUITA, Juan-Carlos, Alberto ALAPE-GIRÓN, Monica THELESTAM, and Abram KATZ. "A point mutation in the UDP-glucose pyrophosphorylase gene results in decreases of UDP-glucose and inactivation of glycogen synthase." Biochemical Journal 370, no. 3 (2003): 995–1001. http://dx.doi.org/10.1042/bj20021320.

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The regulatory role of UDP-glucose in glycogen biogenesis was investigated in fibroblasts containing a point mutation in the UDP-glucose pyrophosphorylase gene and, consequently, chronically low UDP-glucose levels (Qc). Comparisons were made with cells having the intact gene and restored UDP-glucose levels (G3). Glycogen was always very low in Qc cells. [14C]Glucose incorporation into glycogen was decreased and unaffected by insulin in Qc cells, whereas insulin stimulated glucose incorporation by 50% in G3 cells. Glycogen synthase (GS) activity measured in vitro was virtually absent and the a

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12

Nakano, Kenichi, Yasuko Omura, Mitsuo Tagaya, and Toshio Fukui. "UDP-Glucose Pyrophosphorylase from Potato Tuber: Purification and Characterization1." Journal of Biochemistry 106, no. 3 (1989): 528–32. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122886.

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13

Kleczkowski, Leszek A., Matt Geisler, Iwona Ciereszko, and Henrik Johansson. "UDP-Glucose Pyrophosphorylase. An Old Protein with New Tricks." Plant Physiology 134, no. 3 (2004): 912–18. http://dx.doi.org/10.1104/pp.103.036053.

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14

Martínez, Lucila I., Claudia V. Piattoni, Sergio A. Garay, Daniel E. Rodrígues, Sergio A. Guerrero, and Alberto A. Iglesias. "Redox regulation of UDP-glucose pyrophosphorylase from Entamoeba histolytica." Biochimie 93, no. 2 (2011): 260–68. http://dx.doi.org/10.1016/j.biochi.2010.09.019.

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15

Elling, Lothar, and Maria-Regina Kula. "Purification of UDP-glucose pyrophosphorylase from germinated barley (malt)." Journal of Biotechnology 34, no. 2 (1994): 157–63. http://dx.doi.org/10.1016/0168-1656(94)90085-x.

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16

Sharma, Monica, Swati Sharma, Pallab Ray, and Anuradha Chakraborti. "Targeting Streptococcus pneumoniae UDP-glucose pyrophosphorylase (UGPase): in vitro validation of a putative inhibitor." Drug Target Insights 14, no. 1 (2020): 26–33. http://dx.doi.org/10.33393/dti.2020.2103.

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Background: Genome plasticity of Streptococcus pneumoniae is responsible for the reduced efficacy of various antibiotics and capsular polysaccharide based vaccines. Therefore targets independent of capsular types are sought to control the pneumococcal pathogenicity. UcrDP-glucose pyrophosphorylase (UGPase) is one such desired candidate being responsible for the synthesis of UDP-glucose, a sugar-precursor in capsular biosynthesis and metabolic Leloir pathway. Being crucial to pneumococcal pathobiology, the effect of UGPase inhibition on virulence was evaluated in vitro. Methods: A putativ

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17

Flores-Dı́az, Marietta, Alberto Alape-Girón, Bengt Persson, et al. "Cellular UDP-Glucose Deficiency Caused by a Single Point Mutation in the UDP-Glucose Pyrophosphorylase Gene." Journal of Biological Chemistry 272, no. 38 (1997): 23784–91. http://dx.doi.org/10.1074/jbc.272.38.23784.

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18

McCoy, Jason G., Eduard Bitto, Craig A. Bingman, et al. "Structure and Dynamics of UDP–Glucose Pyrophosphorylase from Arabidopsis thaliana with Bound UDP–Glucose and UTP." Journal of Molecular Biology 366, no. 3 (2007): 830–41. http://dx.doi.org/10.1016/j.jmb.2006.11.059.

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19

Sowokinos, J. R., J. P. Spychalla, and S. L. Desborough. "Pyrophosphorylases in Solanum tuberosum (IV. Purification, Tissue Localization, and Physicochemical Properties of UDP-Glucose Pyrophosphorylase)." Plant Physiology 101, no. 3 (1993): 1073–80. http://dx.doi.org/10.1104/pp.101.3.1073.

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20

Katsube, Takuya, Yasuaki Kazuta, Hiroyuki Mori, Kenichi Nakano, Katsuyuki Tanizawa, and Toshio Fukui. "UDP-Glucose Pyrophosphorylase from Potato Tuber: cDNA Cloning and Sequencing1." Journal of Biochemistry 108, no. 2 (1990): 321–26. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a123200.

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21

Soares, Jose Sergio M., Agustina Gentile, Valeria Scorsato, et al. "Oligomerization, Membrane Association, andin VivoPhosphorylation of Sugarcane UDP-glucose Pyrophosphorylase." Journal of Biological Chemistry 289, no. 48 (2014): 33364–77. http://dx.doi.org/10.1074/jbc.m114.590125.

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22

Chivasa, Stephen, Daniel F. A. Tomé, and Antoni R. Slabas. "UDP-Glucose Pyrophosphorylase Is a Novel Plant Cell Death Regulator." Journal of Proteome Research 12, no. 4 (2013): 1743–53. http://dx.doi.org/10.1021/pr3010887.

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23

Elling, Lothar. "Kinetic characterization of UDP-glucose pyrophosphorylase from germinated barley (malt)." Phytochemistry 42, no. 4 (1996): 955–60. http://dx.doi.org/10.1016/0031-9422(96)00089-1.

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24

Kim, Hun, Jongkeun Choi, Truc Kim, et al. "Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase." Molecules and Cells 29, no. 4 (2010): 397–405. http://dx.doi.org/10.1007/s10059-010-0047-6.

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25

Yang, Yueqin, Hariprasad Vankayalapati, Manshu Tang, et al. "Discovery of Novel Inhibitors Targeting Multi-UDP-hexose Pyrophosphorylases as Anticancer Agents." Molecules 25, no. 3 (2020): 645. http://dx.doi.org/10.3390/molecules25030645.

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To minimize treatment toxicities, recent anti-cancer research efforts have switched from broad-based chemotherapy to targeted therapy, and emerging data show that altered cellular metabolism in cancerous cells can be exploited as new venues for targeted intervention. In this study, we focused on, among the altered metabolic processes in cancerous cells, altered glycosylation due to its documented roles in cancer tumorigenesis, metastasis and drug resistance. We hypothesize that the enzymes required for the biosynthesis of UDP-hexoses, glycosyl donors for glycan synthesis, could serve as therap

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26

Boels, Ingeborg C., Ana Ramos, Michiel Kleerebezem, and Willem M. de Vos. "Functional Analysis of the Lactococcus lactis galU and galE Genes and Their Impact on Sugar Nucleotide and Exopolysaccharide Biosynthesis." Applied and Environmental Microbiology 67, no. 7 (2001): 3033–40. http://dx.doi.org/10.1128/aem.67.7.3033-3040.2001.

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ABSTRACT We studied the UDP-glucose pyrophosphorylase (galU) and UDP-galactose epimerase (galE) genes of Lactococcus lactis MG1363 to investigate their involvement in biosynthesis of UDP-glucose and UDP-galactose, which are precursors of glucose- and galactose-containing exopolysaccharides (EPS) in L. lactis. The lactococcal galU gene was identified by a PCR approach using degenerate primers and was found by Northern blot analysis to be transcribed in a monocistronic RNA. The L. lactis galU gene could complement an Escherichia coli galU mutant, and overexpression of this gene in L. lactis unde

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27

Fujita, Ken-Ichi, Teruhiko Tanigawa, Kiyotaka Machida, Toshio Tanaka, and Makoto Taniguchi. "Synthesis of uridine 5′-monophosphate glucose as an inhibitor of UDP-glucose pyrophosphorylase." Journal of Fermentation and Bioengineering 86, no. 2 (1998): 145–48. http://dx.doi.org/10.1016/s0922-338x(98)80052-4.

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28

Yang, Ting, and Maor Bar-Peled. "Identification of a novel UDP-sugar pyrophosphorylase with a broad substrate specificity in Trypanosoma cruzi." Biochemical Journal 429, no. 3 (2010): 533–43. http://dx.doi.org/10.1042/bj20100238.

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The diverse types of glycoconjugates synthesized by trypanosomatid parasites are unique compared with the host cells. These glycans are required for the parasite survival, invasion or evasion of the host immune system. Synthesis of those glycoconjugates requires a constant supply of nucleotide-sugars (NDP-sugars), yet little is known about how these NDP-sugars are made and supplied. In the present paper, we report a functional gene from Trypanosoma cruzi that encodes a nucleotidyltransferase, which is capable of transforming different types of sugar 1-phosphates and NTP into NDP-sugars. In the

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29

Padilla, Leandro, Susanne Morbach, Reinhard Krämer, and Eduardo Agosin. "Impact of Heterologous Expression of Escherichia coli UDP-Glucose Pyrophosphorylase on Trehalose and Glycogen Synthesis in Corynebacterium glutamicum." Applied and Environmental Microbiology 70, no. 7 (2004): 3845–54. http://dx.doi.org/10.1128/aem.70.7.3845-3854.2004.

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ABSTRACT Trehalose is a disaccharide with a wide range of applications in the food industry. We recently proposed a strategy for trehalose production based on improved strains of the gram-positive bacterium Corynebacterium glutamicum. This microorganism synthesizes trehalose through two major pathways, OtsBA and TreYZ, by using UDP-glucose and ADP-glucose, respectively, as the glucosyl donors. In this paper we describe improvement of the UDP-glucose supply through heterologous expression in C. glutamicum of the UDP-glucose pyrophosphorylase gene from Escherichia coli, either expressed alone or

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30

Niewoehner, C. B., and B. Neil. "Mechanism of delayed hepatic glycogen synthesis after an oral galactose load vs. an oral glucose load in adult rats." American Journal of Physiology-Endocrinology and Metabolism 263, no. 1 (1992): E42—E49. http://dx.doi.org/10.1152/ajpendo.1992.263.1.e42.

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We have compared the effects of administration of oral galactose or glucose (1 g/kg) to 24-h fasted rats to examine the mechanism by which galactose regulates its own incorporation into liver glycogen in vivo. Liver glycogen increased to a maximum more slowly after galactose than after glucose administration (0.14 vs. 0.29 mumol.g liver-1.min-1). Glycogen accumulation after the galactose load was 70% of that after the glucose load (149 vs. 214 mumol), and the net increase in liver glycogen represented the same proportion (24 vs. 22%) of added carbohydrate after urinary loss of galactose was ac

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31

De Luca, Claudio, Manfred Lansing, Fabiana Crescenzi, et al. "Overexpression, one-step purification and characterization of UDP-glucose dehydrogenase and UDP-N-acetylglucosamine pyrophosphorylase." Bioorganic & Medicinal Chemistry 4, no. 1 (1996): 131–41. http://dx.doi.org/10.1016/0968-0896(95)00159-x.

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32

Borovkov, Alex Y., Phillip E. McClean, and Gary A. Secor. "Organization and transcription of the gene encoding potato UDP-glucose pyrophosphorylase." Gene 186, no. 2 (1997): 293–97. http://dx.doi.org/10.1016/s0378-1119(96)00724-x.

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33

Führing, Jana, Sebastian Damerow, Roman Fedorov, Julia Schneider, Anja-Katharina Münster-Kühnel, and Rita Gerardy-Schahn. "Octamerization is essential for enzymatic function of human UDP-glucose pyrophosphorylase." Glycobiology 23, no. 4 (2012): 426–37. http://dx.doi.org/10.1093/glycob/cws217.

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34

Zhu, Bao-Hua, Hong-Ping Shi, Guan-Pin Yang, Na-Na Lv, Miao Yang, and Ke-Hou Pan. "Silencing UDP-glucose pyrophosphorylase gene in Phaeodactylum tricornutum affects carbon allocation." New Biotechnology 33, no. 1 (2016): 237–44. http://dx.doi.org/10.1016/j.nbt.2015.06.003.

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35

KOO, Hyun Min, Seok-Won YIM, Chang-Seung LEE, Yu Ryang PYUN, and Yu Sam KIM. "Cloning, Sequencing, and Expression of UDP-Glucose Pyrophosphorylase Gene fromAcetobacter xylinumBRC5." Bioscience, Biotechnology, and Biochemistry 64, no. 3 (2000): 523–29. http://dx.doi.org/10.1271/bbb.64.523.

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36

Steiner, Thomas, Anne-Christin Lamerz, Petra Hess, et al. "Open and Closed Structures of the UDP-glucose Pyrophosphorylase fromLeishmania major." Journal of Biological Chemistry 282, no. 17 (2007): 13003–10. http://dx.doi.org/10.1074/jbc.m609984200.

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37

Othman, R., H. L. Chong, and A. M. H. Zeti. "Cloning and recombinant expression of UDP-glucose pyrophosphorylase from Eucheuma denticulatum." Journal of Biotechnology 150 (November 2010): 483. http://dx.doi.org/10.1016/j.jbiotec.2010.09.736.

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38

Ragheb, Jack A., and Robert P. Dottin. "Structure and sequence of a UDP glucose pyrophosphorylase gene ofDictyostelium discoideum." Nucleic Acids Research 15, no. 9 (1987): 3891–906. http://dx.doi.org/10.1093/nar/15.9.3891.

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39

Entwistle, G., and T. A. Rees. "Enzymic capacities of amyloplasts from wheat (Triticum aestivum) endosperm." Biochemical Journal 255, no. 2 (1988): 391–96. http://dx.doi.org/10.1042/bj2550391.

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Lysates of protoplasts from the endosperm of developing grains of wheat (Triticum aestivum) were fractionated on density gradients of Nycodenz to give amyloplasts. Enzyme distribution on the gradients suggested that: (i) starch synthase and ADP-glucose pyrophosphorylase are confined to the amyloplasts; (ii) pyrophosphate: fructose-6-phosphate 1-phosphotransferase and UDP-glucose pyrophosphorylase are confined to the cytosol; (iii) a significant proportion (23-45%) of each glycolytic enzyme, from phosphoglucomutase to pyruvate kinase inclusive, is in the amyloplast. Starch synthase, ADP-glucose

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40

Goulard, F., M. Diouris, E. Deslandes, and J. Y. Floc'h. "An HPLC method for the assay of UDP-glucose pyrophosphorylase and UDP-glucose-4-epimerase in Solieria chordalis (Rhodophyceae)." Phytochemical Analysis 12, no. 6 (2001): 363–65. http://dx.doi.org/10.1002/pca.604.

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41

Sener, Keriman, Zuojun Shen, David S. Newburg, and Edward L. Jarroll. "Amino sugar phosphate levels in Giardia change during cyst wall formation." Microbiology 150, no. 5 (2004): 1225–30. http://dx.doi.org/10.1099/mic.0.26898-0.

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The parasite Giardia intestinalis exists as a trophozoite (vegetative) that infects the human small intestine, and a cyst (infective) that is shed in host faeces. Cyst viability in the environment depends upon a protective cyst wall, which consists of proteins and a unique β(1-3) GalNAc homopolymer. UDP-GalNAc, the precursor for this polysaccharide, is synthesized from glucose by an enzyme pathway that involves amino sugar phosphate intermediates. Using a novel method of microanalysis by capillary electrophoresis, the levels of amino sugar phosphate intermediates in trophozoites before encystm

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42

Degeest, Bart, Frederik Vaningelgem, Andrew P. Laws, and Luc De Vuyst. "UDP-N-Acetylglucosamine 4-Epimerase Activity Indicates the Presence of N-Acetylgalactosamine in Exopolysaccharides of Streptococcus thermophilus Strains." Applied and Environmental Microbiology 67, no. 9 (2001): 3976–84. http://dx.doi.org/10.1128/aem.67.9.3976-3984.2001.

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ABSTRACT The monomer composition of the exopolysaccharides (EPS) produced byStreptococcus thermophilus LY03 and S. thermophilus Sfi20 were evaluated by high-pressure liquid chromatography with amperometric detection and nuclear magnetic resonance spectroscopy. Both strains produced the same EPS composed of galactose, glucose, and N-acetylgalactosamine. Further, it was demonstrated that the activity of the precursor-producing enzyme UDP-N-acetylglucosamine 4-epimerase, converting UDP-N-acetylglucosamine into UDP-N-acetylgalactosamine, is responsible for the presence of N-acetylgalactosamine in

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43

Reynolds, Thomas H., Yunbae Pak, Thurl E. Harris, Jill Manchester, Eugene J. Barrett, and John C. Lawrence. "Effects of Insulin and Transgenic Overexpression of UDP-glucose Pyrophosphorylase on UDP-glucose and Glycogen Accumulation in Skeletal Muscle Fibers." Journal of Biological Chemistry 280, no. 7 (2004): 5510–15. http://dx.doi.org/10.1074/jbc.m413614200.

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44

Berbis, M., Jose Sanchez-Puelles, F. Canada, and Jesus Jimenez-Barbero. "Structure and Function of Prokaryotic UDP-Glucose Pyrophosphorylase, A Drug Target Candidate." Current Medicinal Chemistry 22, no. 14 (2015): 1687–97. http://dx.doi.org/10.2174/0929867322666150114151248.

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45

Meng, M., M. Geisler, H. Johansson, et al. "UDP-Glucose Pyrophosphorylase is not Rate Limiting, but is Essential in Arabidopsis." Plant and Cell Physiology 50, no. 5 (2009): 998–1011. http://dx.doi.org/10.1093/pcp/pcp052.

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46

Vella, John, and Les Copeland. "UDP-glucose pyrophosphorylase from the plant fraction of nitrogen-fixing soybean nodules." Physiologia Plantarum 78, no. 1 (1990): 140–46. http://dx.doi.org/10.1034/j.1399-3054.1990.780123.x.

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47

Führing, Jana, Johannes T. Cramer, Françoise H. Routier, et al. "Catalytic Mechanism and Allosteric Regulation of UDP-Glucose Pyrophosphorylase from Leishmania major." ACS Catalysis 3, no. 12 (2013): 2976–85. http://dx.doi.org/10.1021/cs4007777.

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48

Coleman, Heather D., Thomas Canam, Kyu-Young Kang, David D. Ellis, and Shawn D. Mansfield. "Over-expression of UDP-glucose pyrophosphorylase in hybrid poplar affects carbon allocation." Journal of Experimental Botany 58, no. 15-16 (2007): 4257–68. http://dx.doi.org/10.1093/jxb/erm287.

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49

Lightcap, Eric S., та Perry A. Frey. "μ-Monothiopyrophosphate as a Substrate for Inorganic Pyrophosphatase and UDP-Glucose Pyrophosphorylase". Archives of Biochemistry and Biophysics 335, № 1 (1996): 183–90. http://dx.doi.org/10.1006/abbi.1996.0496.

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50

Zavala, Agustín, Verónica Kovacec, Gustavo Levín, et al. "Screening assay for inhibitors of a recombinant Streptococcus pneumoniae UDP-glucose pyrophosphorylase." Journal of Enzyme Inhibition and Medicinal Chemistry 32, no. 1 (2017): 203–7. http://dx.doi.org/10.1080/14756366.2016.1247055.

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