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Journal articles on the topic 'Neuropathy target esterase'

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Published: 7 July 2024

Last updated: 22 June 2025

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1

GLYNN, Paul. "Neuropathy target esterase." Biochemical Journal 344, no. 3 (1999): 625–31. http://dx.doi.org/10.1042/bj3440625.

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Neuropathy target esterase (NTE) is an integral membrane protein present in all neurons and in some non-neural-cell types of vertebrates. Recent data indicate that NTE is involved in a cell-signalling pathway controlling interactions between neurons and accessory glial cells in the developing nervous system. NTE has serine esterase activity and efficiently catalyses the hydrolysis of phenyl valerate (PV) in vitro, but its physiological substrate is unknown. By sequence analysis NTE has been found to be related neither to the major serine esterase family, which includes acetylcholinesterase, nor to any other known serine hydrolases. NTE comprises at least two functional domains: an N-terminal putative regulatory domain and a C-terminal effector domain which contains the esterase activity and is, in part, conserved in proteins found in bacteria, yeast, nematodes and insects. NTE's effector domain contains three predicted transmembrane segments, and the active-site serine residue lies at the centre of one of these segments. The isolated recombinant domain shows PV hydrolase activity only when incorporated into phospholipid liposomes. NTE's esterase activity appears to be largely redundant in adult vertebrates, but organophosphates which react with NTE in vivo initiate unknown events which lead, after a delay of 1-3 weeks, to a neuropathy with degeneration of long axons. These neuropathic organophosphates leave a negatively charged group covalently attached to the active-site serine residue, and it is suggested that this may cause a toxic gain of function in NTE.

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2

GLYNN, Paul. "Neuropathy target esterase." Biochemical Journal 344, no. 3 (1999): 625. http://dx.doi.org/10.1042/0264-6021:3440625.

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3

Hou, Wei-Yuan, Ding-Xin Long, and Yi-Jun Wu. "Effect of Inhibition of Neuropathy Target Esterase in Mouse Nervous Tissues In Vitro on Phosphatidylcholine and Lysophosphatidylcholine Homeostasis." International Journal of Toxicology 28, no. 5 (2009): 417–24. http://dx.doi.org/10.1177/1091581809340704.

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Neuropathy target esterase has been shown to be a lysophospholipase in mouse. The authors investigate the effect of neuropathy target esterase inhibition in mouse nervous tissues in vitro on the homeostasis of phosphatidylcholine and lysophosphatidylcholine by treating the homogenates with tri-ortho-cresyl phosphate, paraoxon, paraoxon plus mipafox, and phenylmethylsulfonyl fluoride. The activity of neuropathy target esterase is significantly inhibited by phenylmethylsulfonyl fluoride and paraoxon plus mipafox but not by paraoxon alone. Tri-ortho-cresyl phosphate slightly but significantly inhibits neuropathy target esterase activity in brain. The levels of phosphatidylcholine and lysophosphatidylcholine in all 3 nervous tissues are not obviously altered after treatment with tri-ortho-cresyl phosphate, paraoxon, or paraoxon plus mipafox. However, phosphatidylcholine and lysophosphatidylcholine levels are clearly enhanced by phenylmethylsulfonyl fluoride. It is concluded that inhibition of neuropathy target esterase in mouse nervous tissues is not enough to disrupt the homeostasis of phosphatidylcholine and lysophosphatidylcholine and that the upregulation by phenylmethylsulfonyl fluoride may be the consequence of combined inhibition of neuropathy target esterase and other phospholipases.

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4

Glynn, Paul. "Axonal Degeneration and Neuropathy Target Esterase." Archives of Industrial Hygiene and Toxicology 58, no. 3 (2007): 355–58. http://dx.doi.org/10.2478/v10004-007-0029-z.

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Axonal Degeneration and Neuropathy Target EsteraseThis brief review summarises recent observations which suggest a possible mechanism for organophosphate-induced delayed neuropathy (OPIDN). Neuropathy target esterase (NTE) has been shown to deacylate endoplasmic reticulum (ER) membrane phosphatidylcholine (PtdCho). Raised levels of PtdCho are present in the brains of swiss cheese/NTE mutant Drosophila together with abnormal membrane structures, axonal and dendritic degeneration and neural cell loss. Similar vacuolated pathology is found in the brains of mice with brain-specific deletion of the NTE gene and, in old age, these mice show clinical and histopathological features of neuropathy resembling those in wild-type mice chronically dosed with tri-ortho-cresylphosphate. It is suggested that OPIDN results from the loss of NTE's phospholipase activity which in turn causes ER malfunction and perturbation of axonal transport and glial-axonal interactions.

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5

Lush, Michael, David Read, and Paul Glynn. "Molecular cloning of neuropathy target esterase." Toxicology Letters 88 (October 1996): 27. http://dx.doi.org/10.1016/s0378-4274(96)80098-1.

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6

Glynn, Paul. "Neurodegeneration involving neuropathy target esterase (NTE)." Toxicology Letters 164 (September 2006): S9. http://dx.doi.org/10.1016/j.toxlet.2006.06.023.

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7

Glynn, Paul. "Neuropathy target esterase and phospholipid deacylation." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1736, no. 2 (2005): 87–93. http://dx.doi.org/10.1016/j.bbalip.2005.08.002.

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8

Bertoncin, Daniela, Alessandra Russolo, Stefano Caroldi, and Marcello Lotti. "Neuropathy Target Esterase in Human Lymphocytes." Archives of Environmental Health: An International Journal 40, no. 3 (1985): 139–44. http://dx.doi.org/10.1080/00039896.1985.10545905.

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9

Thomas, Thomas C., András Székács, Bruce D. Hammock, Barry W. Wilson, and Mark G. McNamee. "Affinity chromatography of neuropathy target esterase." Chemico-Biological Interactions 87, no. 1-3 (1993): 347–60. http://dx.doi.org/10.1016/0009-2797(93)90063-5.

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10

Seifert, Josef. "A Tentative Mechanism of Solubilization of Neuropathy Target Esterase from Chicken Embryo Brain by Phospholipase A2." Scientific World JOURNAL 8 (2008): 346–49. http://dx.doi.org/10.1100/tsw.2008.51.

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The neuropathy target esterase is a membrane-bound enzyme linked to organophosphate-induced distal neuropathy. Here we report a tentative mechanism of its solubilization from chicken embryo brains by using phospholipase A2. The enzyme was released from brain membranes after degradation of their structural phospholipids initiated by phospholipase A2. L-α-lysophosphatidylcholine, tested as a representative product of phospholipid hydrolysis, was identified as a new efficient detergent for solubilization of the neuropathy target esterase.

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11

Glynn, P., D. J. Read, R. Guo, S. Wylie, and M. K. Johnson. "Synthesis and characterization of a biotinylated organophosphorus ester for detection and affinity purification of a brain serine esterase: neuropathy target esterase." Biochemical Journal 301, no. 2 (1994): 551–56. http://dx.doi.org/10.1042/bj3010551.

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We have synthesized a novel stable precursor, saligenin phosphorotrichloridate, which, on reaction with N-monobiotinyldiamines, generates a series of biotinylated covalent inhibitors of serine esterases. A homologue designated S9B [1-(saligenin cyclic phospho)-9-biotinyldiaminononane] was selected to allow detection and rapid isolation of neuropathy target esterase (NTE). This enzyme is the primary target site for those organophosphorus esters (OPs) which cause delayed neuropathy. NTE comprises about 0.03% of the total protein in brain microsomal fractions and has resisted purification attempts over many years. S9B is a potent progressive inhibitor of NTE esteratic activity (second-order rate constant 1.4 x 10(7) M-1.min-1). Incubation of S9B with brain microsomes led to specific covalent labelling of NTE as determined by detection of a biotinylated 155 kDa polypeptide on Western blots. Specificity of S9B labelling was further demonstrated by inhibition with the neuropathic OP mipafox. Biotinyl-NTE in SDS-solubilized S9B-labelled microsomes was adsorbed on to avidin-Sepharose and subsequently eluted, yielding a fraction enriched approx. 1000-fold in NTE by a single step with recoveries of 30%. Essentially pure NTE was obtained after separation from two endogenous biotinylated polypeptides (120 and 70 kDa) in avidin-Sepharose eluates by preparative SDS/PAGE. Other biotinylated saligenin phosphoramidates derived from the same precursor may be useful for detection and isolation of other serine esterases and proteinases.

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12

Glynn, Paul, David J. Read, Michael J. Lush, Yong Li, and Jane Atkins. "Molecular cloning of neuropathy target esterase (NTE)." Chemico-Biological Interactions 119-120 (May 1999): 513–17. http://dx.doi.org/10.1016/s0009-2797(99)00065-4.

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13

Richardson, Rudy J., Nichole D. Hein, Sanjeeva J. Wijeyesakere, John K. Fink, and Galina F. Makhaeva. "Neuropathy target esterase (NTE): overview and future." Chemico-Biological Interactions 203, no. 1 (2013): 238–44. http://dx.doi.org/10.1016/j.cbi.2012.10.024.

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14

Moretto, Angelo, and Marcello Lotti. "Promotion of Peripheral Axonopathies by Certain Esterase Inhibitors." Toxicology and Industrial Health 9, no. 6 (1993): 1037–46. http://dx.doi.org/10.1177/074823379300900604.

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Certain esterase inhibitors were found to exacerbate the clinical signs of polyneuropathy caused by various neurotoxic compounds and to delay the recovery from nerve crush. This phenomenon is referred to as promotion of axonopathies. The molecular target of promotion has not yet been identified. However, all known promoters are also inhibitors of neuropathy target esterase (NTE), the putative target of organophosphate neuropathy, but it has been shown that the target of promotion is unlikely to be NTE. Available data suggest that promoters might affect a target and a mechanism present in the nervous system that is not activated by axonal lesions. Promotion may be important to understand the physiological mechanism of nerve damage and repair. This finding also implies a changing perspective for the risk assessment of exposures to esterase inhibitors, some of which are used as pesticides and might be promoters.

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15

Kohli, Neeraj, Devesh Srivastava, Jun Sun, Rudy J. Richardson, Ilsoon Lee, and Robert M. Worden. "Nanostructured Biosensor for Measuring Neuropathy Target Esterase Activity." Analytical Chemistry 79, no. 14 (2007): 5196–203. http://dx.doi.org/10.1021/ac0701684.

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16

Pamies, David, Eugenio Villanova, and Miguel Angel Sogorb. "Neuropathy target esterase in mouse embryonic stem cells." Toxicology Letters 189 (September 2009): S65. http://dx.doi.org/10.1016/j.toxlet.2009.06.195.

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17

Borhan, Babak, Ying Ko, Chris Mackay, Barry W. Wilson, Mark J. Kurth, and Bruce D. Hammock. "Development of surrogate substrates for neuropathy target esterase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1250, no. 2 (1995): 171–82. http://dx.doi.org/10.1016/0167-4838(95)00058-3.

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18

Chang, Ping-An, Ding-Xin Long, Yi-Jun Wu, Quan Sun, and Fang-Zhou Song. "Identification and characterization of chicken neuropathy target esterase." Gene 435, no. 1-2 (2009): 45–52. http://dx.doi.org/10.1016/j.gene.2009.01.004.

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19

Moretto, Angelo, and Marcello Lotti. "Organ distribution of neuropathy target esterase in man." Biochemical Pharmacology 37, no. 15 (1988): 3041–43. http://dx.doi.org/10.1016/0006-2952(88)90295-x.

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20

Thomas, Thomas C., András Székács, Scott Rojas, Bruce D. Hammock, Barry W. Wilson, and Mark G. McNamee. "Characterization of neuropathy target esterase using trifluoromethyl ketones." Biochemical Pharmacology 40, no. 12 (1990): 2587–96. http://dx.doi.org/10.1016/0006-2952(90)90575-6.

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21

Maroni, M., and M. L. Bleecker. "Neuropathy target esterase in human lymphocytes and platelets." Journal of Applied Toxicology 6, no. 1 (1986): 1–7. http://dx.doi.org/10.1002/jat.2550060102.

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22

Moretto, Angelo. "A novel probe for characterisation of neuropathy target esterase." Human & Experimental Toxicology 14, no. 11 (1995): 930–31. http://dx.doi.org/10.1177/096032719501401113.

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23

Glynn, Paul. "Neuropathy target esterase (NTE): Molecular characterisation and cellular localisation." Toxicology Letters 88 (October 1996): 9. http://dx.doi.org/10.1016/s0378-4274(96)80030-0.

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24

Vose, Sarah C., Kazutoshi Fujioka, Alex G. Gulevich, Amy Y. Lin, Nina T. Holland, and John E. Casida. "Cellular function of neuropathy target esterase in lysophosphatidylcholine action." Toxicology and Applied Pharmacology 232, no. 3 (2008): 376–83. http://dx.doi.org/10.1016/j.taap.2008.07.015.

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25

Rainier, Shirley, Melanie Bui, Erin Mark, et al. "Neuropathy Target Esterase Gene Mutations Cause Motor Neuron Disease." American Journal of Human Genetics 82, no. 3 (2008): 780–85. http://dx.doi.org/10.1016/j.ajhg.2007.12.018.

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26

van Tienhoven, Marianne, Jane Atkins, Yong Li, and Paul Glynn. "Human Neuropathy Target Esterase Catalyzes Hydrolysis of Membrane Lipids." Journal of Biological Chemistry 277, no. 23 (2002): 20942–48. http://dx.doi.org/10.1074/jbc.m200330200.

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27

Vicedo, J. L., V. Carrera, J. Barril, and E. Vilanova. "Properties of partly preinhibited hen brain neuropathy target esterase." Chemico-Biological Interactions 87, no. 1-3 (1993): 417–23. http://dx.doi.org/10.1016/0009-2797(93)90069-b.

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28

Sigolaeva, Larisa V., Alexander Makower, Arkadi V. Eremenko, et al. "Bioelectrochemical Analysis of Neuropathy Target Esterase Activity in Blood." Analytical Biochemistry 290, no. 1 (2001): 1–9. http://dx.doi.org/10.1006/abio.2000.4822.

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29

Crowell, J. A., R. M. Parker, T. J. Bucci, and J. C. Dacre. "Neuropathy target esterase in hens after sarin and soman." Journal of Biochemical Toxicology 4, no. 1 (1989): 15–20. http://dx.doi.org/10.1002/jbt.2570040104.

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30

Mangas, Iris, Eugenio Vilanova, and Jorge Estévez. "Kinetic interactions of a neuropathy potentiator (phenylmethylsulfonyl fluoride) with the neuropathy target esterase and other membrane bound esterases." Archives of Toxicology 88, no. 2 (2013): 355–66. http://dx.doi.org/10.1007/s00204-013-1135-0.

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31

Milatovic, Dejan, Angelo Moretto, Khaled A. Osman, and Marcello Lotti. "Phenyl Valerate Esterases Other than Neuropathy Target Esterase and the Promotion of Organophosphate Polyneuropathy†." Chemical Research in Toxicology 10, no. 9 (1997): 1045–48. http://dx.doi.org/10.1021/tx960207z.

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32

Makhaeva, G. F., E. V. Rudakova, and R. J. Richardson. "Investigation of the Esterase Status as a Complex Biomarker of Exposure to Organophosphorus Compounds." Biomedical Chemistry: Research and Methods 1, no. 3 (2018): e00028. http://dx.doi.org/10.18097/bmcrm00028.

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Development of biomarkers of human exposures to organophosphorus compounds OPCs and their quantification is a vital component of a system of prediction and early diagnostics of OPC-induced diseases. Our study was focused on investigation of esterase status as a complex biomarker of exposure to OPCs and an aid in accurate diagnosis. We suggest that this complex biomarker should be more effective and informative than standard assays of plasma butyrylcholinesterase (BChE), erythrocyte acetylcholinesterase (RBC AChE), and lymphocyte neuropathy target esterase (NTE). It will help: 1) to assess an exposure as such and to confirm the nonexposure of individuals suspected to have been exposed; 2) to determine if the exposure was to agents expected to produce acute and/or delayed neurotoxicity; 3) to perform dosimetry of the exposure, which provides valuable information for medical treatment. To confirm this hypothesis, we have examined the changes in activity of blood AChE, NTE, BChE and carboxylesterase (CaE) 1 h after i.p. administration of increasing doses of three OPCs with different esterase profiles: the known neuropathic compound O,O-dipropyl-O-dichlorovinyl phosphate (C3H 7O)2P(O)OCH=CCl2 (diPr-DClVP) as the control compound and two model dialkylphosphates (C2H5O)2P(O)OCH(CF3)2 (diEt-PFP) and (C4H9O)2P(O)OCH(CF3)2 (diBu-PFP). The esterases assay was performed in hemolysed blood by spectrophotometric (AChE, BChE, CaE) and biosensor (NTE) methods. Analysis of the obtained dose-dependences for blood esterases inhibition showed that blood BChE and CaE were the most sensitive biomarkers, allowing detection of low doses. Inhibition of blood NTE and AChE can be used to assess the likelihood that an exposure to OPC would produce cholinergic and/or delayed neuropathic effects.

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33

Wu, Shao-Yong, and John E. Casida. "Ethyl Octylphosphonofluoridate and Analogs: Optimized Inhibitors of Neuropathy Target Esterase." Chemical Research in Toxicology 8, no. 8 (1995): 1070–75. http://dx.doi.org/10.1021/tx00050a011.

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34

Read, D. J., Y. Li, M. V. Chao, J. B. Cavanagh, and P. Glynn. "Neuropathy Target Esterase Is Required for Adult Vertebrate Axon Maintenance." Journal of Neuroscience 29, no. 37 (2009): 11594–600. http://dx.doi.org/10.1523/jneurosci.3007-09.2009.

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35

Quistad, G. B., C. Barlow, C. J. Winrow, S. E. Sparks, and J. E. Casida. "Evidence that mouse brain neuropathy target esterase is a lysophospholipase." Proceedings of the National Academy of Sciences 100, no. 13 (2003): 7983–87. http://dx.doi.org/10.1073/pnas.1232473100.

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36

Glynn, P., J. L. Holton, C. C. Nolan, et al. "Neuropathy target esterase: Immunolocalization to neuronal cell bodies and axons." Neuroscience 83, no. 1 (1998): 295–302. http://dx.doi.org/10.1016/s0306-4522(97)00388-6.

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37

Long, Ding-Xin, Ping-An Chang, Yu-Jie Liang, Lin Yang, and Yi-Jun Wu. "Degradation of neuropathy target esterase by the macroautophagic lysosomal pathway." Life Sciences 84, no. 3-4 (2009): 89–96. http://dx.doi.org/10.1016/j.lfs.2008.11.007.

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38

Glynn, Paul. "Neural development and neurodegeneration: two faces of Neuropathy Target Esterase." Progress in Neurobiology 61, no. 1 (2000): 61–74. http://dx.doi.org/10.1016/s0301-0082(99)00043-x.

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39

Sigolaeva, L. V., A. V. Eremenko, A. Makower, G. F. Makhaeva, V. V. Malygin, and I. N. Kurochkin. "A new approach for determination of neuropathy target esterase activity." Chemico-Biological Interactions 119-120 (May 1999): 559–65. http://dx.doi.org/10.1016/s0009-2797(99)00070-8.

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40

Johnson, Martin K. "Sensitivity and selectivity of compounds interacting with neuropathy target esterase." Biochemical Pharmacology 37, no. 21 (1988): 4095–104. http://dx.doi.org/10.1016/0006-2952(88)90101-3.

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41

Sogorb, M. A., S. Viniegra, J. A. Reig, and E. Vilanova. "Partial characterization of neuropathy target esterase and related phenyl valerate esterases from bovine adrenal medulla." Journal of Biochemical Toxicology 9, no. 3 (1994): 145–52. http://dx.doi.org/10.1002/jbt.2570090306.

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42

Matiytsiv, N. P. "SWS/NTE-dependent neuropathy is the model system to study neurodegeneration." Faktori eksperimental'noi evolucii organizmiv 26 (September 1, 2020): 67–71. http://dx.doi.org/10.7124/feeo.v26.1243.

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Today there is many described neurodegenerative D. melanogaster mutants, which characterized by development of degenerative changes in brain. One of them are a swiss cheese (sws) gene mutants. Mutations in this gene causes apoptosis of neurons and hyperwrapping of their somas by the glial cells, reducing of life expectancy and decrease of locomotion. The sws gene is the ortholog of mammal’s neuropathy target esterase (NTE / PNPLA6). NTE is s neuronal, transmembrane protein, that possesses serinesterase activity, and can be the target for neurotoxic organophosphorus compounds activity. Mutations in PNPLA6 gene cause number hereditary neurodegenerative disorders, which nowadays are incurable. The search for therapeutic agents require use of model objects because researches on humans have both methodical and ethical limitations. During two last decades D. melanogaster has proven itself as a good model for study of neurodegenerative diseases. In this review, we described general characteristics of D. melanogaster gene sws, consequences of its mutations and provided evidences of high conservatism of gene product. Keywords: gene swiss cheese, neuropathy target esterase, neurodegeneration, brain, life span.

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43

Makhaeva, Galina F., Vladimir V. Malygin, Nadezhda N. Strakhova, et al. "Biosensor assay of neuropathy target esterase in whole blood as a new approach to OPIDN risk assessment: review of progress." Human & Experimental Toxicology 26, no. 4 (2007): 273–82. http://dx.doi.org/10.1177/0960327106070463.

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Organophosphates (OPs) that inhibit neuropathy target esterase (NTE) with subsequent ageing can produce OP-induced delayed neuropathy (OPIDN). NTE inhibition in lymphocytes can be used as a biomarker of exposure to neuropathic OPs. An electrochemical method was developed to assay NTE in whole blood. The high sensitivity of the tyrosinase carbon-paste biosensors for the phenol produced by hydrolysis of the substrate, phenyl valerate, allowed NTE activity to be measured in diluted samples of whole blood, which cannot be done using the standard colorimetric assay. The biosensor was used to establish correlations of NTE inhibitions in blood with that in lymphocytes and brain after dosing hens with a neuropathic OP. The results of further studies demonstrated that whole blood NTE is a reliable biomarker of neuropathic OPs for up to 96 hours after exposure. These validation results suggest that the biosensor NTE assay for whole blood could be developed to measure human exposure to neuropathic OPs as a predictor of OPIDN. The small blood volume required (100 μL), simplicity of sample preparation and rapid analysis times indicate that the biosensor should be useful in biomonitoring and epidemiological studies. The present paper is an overview of our previous and ongoing work in this area. Human & Experimental Toxicology (2007) 26, 273-282

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44

Thomas, T. C., Y. Ishikawa, M. G. McNamee, and B. W. Wilson. "Correlation of neuropathy target esterase activity with specific tritiated di-isopropyl phosphorofluoridate-labelled proteins." Biochemical Journal 257, no. 1 (1989): 109–16. http://dx.doi.org/10.1042/bj2570109.

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Neuropathy target esterase (NTE) is a membrane-bound carboxylesterase activity that has been proposed as the target site for initiation of organophosphate-induced delayed neuropathy. This activity is identified by its resistance to treatment with Paraoxon and sensitivity to co-incubation with Paraoxon and Mipafox. Sucrose-density-gradient centrifugation of membrane-associated proteins isolated from chick-embryo brains identified three proteins, Mr 161,000, 116,500 and 103,000, that were labelled with [3H]di-isopropyl phosphorofluoridate in an NTE-like manner and that co-migrated with NTE. The 161,000-Mr and 116,500-Mr proteins were identified in both adult and embryo brain. One or both of these proteins may therefore contribute to the activity defined as NTE. In addition, a 61,000-Mr protein was identified that does not comigrate with NTE, but that was labelled with [3H]di-isopropyl phosphorofluoridate in a Paraoxon-resistant and Mipafox-sensitive manner. The effect of Mipafox on labelling, however, was reversibly blocked by co-incubation with Paraoxon. This protein, therefore, is not NTE, but has the necessary inhibitor-sensitivity to be the target site for organophosphate-induced delayed neuropathy.

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45

Akassoglou, K., B. Malester, J. Xu, L. Tessarollo, J. Rosenbluth, and M. V. Chao. "Brain-specific deletion of neuropathy target esterase/swisscheese results in neurodegeneration." Proceedings of the National Academy of Sciences 101, no. 14 (2004): 5075–80. http://dx.doi.org/10.1073/pnas.0401030101.

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46

Pamies, David, David Pamies, Miguel Angel Sogorb, et al. "Effect of neuropathy target esterase inhibition and silencing on NT2 differentiation." Toxicology Letters 211 (June 2012): S106—S107. http://dx.doi.org/10.1016/j.toxlet.2012.03.397.

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47

Kaur, Pushpinder, Geetu Raheja, Surjit Singh, and K. D. Gill. "Purification and characterization of neuropathy target esterase (NTE) from rat brain." Life Sciences 78, no. 25 (2006): 2967–73. http://dx.doi.org/10.1016/j.lfs.2005.11.029.

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48

CHANG, P., D. LONG, and Y. WU. "Molecular cloning and expression of chicken neuropathy target esterase activity domain." Toxicology Letters 174, no. 1-3 (2007): 42–48. http://dx.doi.org/10.1016/j.toxlet.2007.08.011.

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49

Pedro Fernández-Murray, J., and Christopher R. McMaster. "Phosphatidylcholine synthesis and its catabolism by yeast neuropathy target esterase 1." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1771, no. 3 (2007): 331–36. http://dx.doi.org/10.1016/j.bbalip.2006.04.004.

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50

Hufnagel, Robert B., Gavin Arno, Nichole D. Hein, et al. "Neuropathy target esterase impairments cause Oliver–McFarlane and Laurence–Moon syndromes." Journal of Medical Genetics 52, no. 2 (2014): 85–94. http://dx.doi.org/10.1136/jmedgenet-2014-102856.

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