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Artykuły w czasopismach na temat „Stearoyl CoA desaturase”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 25 kwietnia 2022

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1

Oatman, Nicole, Julie Reisz, Angelo D’Alessandro, and Biplab Dasgupta. "TAMI-55. THE EVOLUTIONARY ENIGMA OF FATTY ACID DESATURATION IN GLIOBLASTOMA." Neuro-Oncology 22, Supplement_2 (November 2020): ii225. http://dx.doi.org/10.1093/neuonc/noaa215.942.

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Abstract Fatty acid desaturation is an enzymatic reaction in which a double bond is introduced into an acyl chain. Of the four functionally distinct desaturase subfamilies, the First Desaturase Family of enzymes introduce the first double bond into a saturated fatty acid, resulting in the synthesis of monounsaturated fatty acids (MUFA). MUFA are essential components of membrane and storage lipids and exert a profound influence on the fluidity of biological membranes. A disequilibrium in saturated to unsaturated fatty acid ratio alters cell growth, differentiation and response to external stimu

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2

Oatman, Nicole, and Biplab Dasgupta. "DDRE-15. THE EVOLUTIONARY ENIGMA OF FATTY ACID DESATURATION IN GLIOBLASTOMA." Neuro-Oncology Advances 3, Supplement_1 (March 1, 2021): i9. http://dx.doi.org/10.1093/noajnl/vdab024.037.

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Abstract Fatty acid desaturation is an enzymatic reaction in which a double bond is introduced into an acyl chain. Of the four functionally distinct desaturase subfamilies, the First Desaturase Family of enzymes introduce the first double bond into a saturated fatty acid, resulting in the synthesis of monounsaturated fatty acids (MUFA). MUFA are essential components of membrane and storage lipids and exert a profound influence on the fluidity of biological membranes. A disequilibrium in saturated to unsaturated fatty acid ratio alters cell growth, differentiation and response to external stimu

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3

Kawashima, Y., N. Uy-Yu, and H. Kozuka. "Sex-related differences in the enhancing effects of perfluoro-octanoic acid on stearoyl-CoA desaturase and its influence on the acyl composition of phospholipid in rat liver. Comparison with clofibric acid and tiadenol." Biochemical Journal 263, no. 3 (November 1, 1989): 897–904. http://dx.doi.org/10.1042/bj2630897.

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The effects of the peroxisome proliferators clofibric acid (p-chlorophenoxyisobutyric acid), tiadenol [2,2′-(decamethylenedithio)diethanol] and perfluoro-octanoic acid (PFOA) on hepatic stearoyl-CoA desaturation in male and female rats were compared. Treatment of male rats with the three peroxisome proliferators increased markedly the activity of stearoyl-CoA desaturase. Administration of clofibric acid or tiadenol to female rats increased greatly the hepatic activity of stearoyl-CoA desaturase, the extent of the increases being slightly less pronounced than those of male rats. In contrast wit

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4

Kikuchi, Kohtaro, and Hidekazu Tsukamoto. "Stearoyl-CoA desaturase and tumorigenesis." Chemico-Biological Interactions 316 (January 2020): 108917. http://dx.doi.org/10.1016/j.cbi.2019.108917.

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5

Lu, He, Xin Qin, Jing Zhang, Shuang Zhang, Yu Zhu, and Wei Hua Wu. "Molecular target analysis of stearoyl-CoA desaturase genes of protozoan parasites." Acta Parasitologica 63, no. 1 (March 26, 2018): 48–54. http://dx.doi.org/10.1515/ap-2018-0006.

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AbstractProtozoan parasites can synthesize polyunsaturated fatty acids. They possess stearoyl-CoA desaturase to convert stearate into oleate and linoleate. Stearoyl-CoA desaturase are the key enzymes required for the synthesis of unsaturated fatty acids. It seems attractive to evaluate the possibility of using unsaturated fatty acid biosynthesis pathways as drug targets. In this study, the authors investigate codon usage bias, base composition variations and protein sequence in ten available complete stearoyl-CoA desaturase gene sequences fromToxoplasma gondii,Neospora caninumetc. The results

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6

Hao, Pan, Xia Cui, Jing Liu, Muzi Li, Yong Fu, and Qun Liu. "Identification and characterization of stearoyl-CoA desaturase in Toxoplasma gondii." Acta Biochimica et Biophysica Sinica 51, no. 6 (May 29, 2019): 615–26. http://dx.doi.org/10.1093/abbs/gmz040.

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Abstract Few information of the function of stearoyl-coenzyme A (CoA) desaturase (SCD) in apicomplaxan parasite has been obtained. In this study, we retrieved a putative fatty acyl-CoA desaturase (TGGT1_238950) by a protein alignment with Plasmodium falciparum SCD in ToxoDB. A typical Δ9-desaturase domain was revealed in this protein. The putative desaturase was tagged with HA endogenously in Toxoplasma gondii, and the endoplasmic reticulum localization of the putative desaturase was revealed, which was consistent with the fatty acid desaturases in other organisms. Therefore, the TGGT1_238950

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7

Ntambi, James M., Makoto Miyazaki, and Agnieszka Dobrzyn. "Regulation of stearoyl-CoA desaturase expression." Lipids 39, no. 11 (November 2004): 1061–65. http://dx.doi.org/10.1007/s11745-004-1331-2.

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8

Ntambi, James M., Youngjin Choi, Yeonhwa Park, Jeffrey M. Peters, and Michael W. Pariza. "Effects of Conjugated Linoleic Acid (CLA) on Immune Responses, Body Composition and Stearoyl-CoA Desaturase." Canadian Journal of Applied Physiology 27, no. 6 (December 1, 2002): 617–27. http://dx.doi.org/10.1139/h02-036.

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Conjugated linoleic acid (CLA) has shown a wide range of biologically beneficial effects; reduction of incidence and severity of animal carcinogenesis, reduction of the adverse effects of immune stimulation, reduction of severity of atherosclerosis, growth promotion in young rats, and modulation of stearoyl-CoA desaturase (SCD). One of the most interesting aspects of CLA is its ability to reduce body fat while enhancing lean body mass which is associated with the trans-10,cis-12 isomer of CLA. The effects of CLA are unique characteristics that have not been observed with other polyunsaturated

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9

Sæther, Thomas, Thien N. Tran, Helge Rootwelt, Bjørn O. Christophersen та Trine B. Haugen. "Expression and Regulation of Δ5-Desaturase, Δ6-Desaturase, Stearoyl-Coenzyme A (CoA) Desaturase 1, and Stearoyl-CoA Desaturase 2 in Rat Testis". Biology of Reproduction 69, № 1 (1 липня 2003): 117–24. http://dx.doi.org/10.1095/biolreprod.102.014035.

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10

Murphy, D. J., I. E. Woodrow, and K. D. Mukherjee. "Substrate specificities of the enzymes of the oleate desaturase system from photosynthetic tissue." Biochemical Journal 225, no. 1 (January 1, 1985): 267–70. http://dx.doi.org/10.1042/bj2250267.

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In the microsomal fraction from young pea (Pisum sativum L.) leaves, the oleoyl moieties from oleoyl-CoA are principally transferred to the sn-2 position of phosphatidylcholine by oleoyl-CoA:1-acyl-lysophosphatidylcholine acyltransferase. The major product of this acyl transfer is 1-palmitoyl(stearoyl)-2-oleoyl phosphatidylcholine. The 1-palmitoyl(stearoyl)-2-oleoyl phosphatidylcholine is subsequently converted into 1-palmitoyl(stearoyl)-2-linoleoyl phosphatidylcholine by the oleate desaturase complex without equilibrating with the bulk membrane phosphatidylcholine pool. Hence, both the acyl t

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11

Kucharski, Mirosław, and Urszula Kaczor. "Stearoyl-CoA desaturase – the lipid metabolism regulator." Postępy Higieny i Medycyny Doświadczalnej 68 (March 27, 2014): 334–42. http://dx.doi.org/10.5604/17322693.1095856.

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12

Hodson, Leanne, and Barbara A. Fielding. "Stearoyl-CoA desaturase: rogue or innocent bystander?" Progress in Lipid Research 52, no. 1 (January 2013): 15–42. http://dx.doi.org/10.1016/j.plipres.2012.08.002.

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13

Tebbey, Paul W., and Thomas M. Buttke. "Stearoyl-CoA desaturase gene expression in lymphocytes." Biochemical and Biophysical Research Communications 186, no. 1 (July 1992): 531–36. http://dx.doi.org/10.1016/s0006-291x(05)80840-x.

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14

Ntambi, James M., and Makoto Miyazaki. "Recent insights into stearoyl-CoA desaturase-1." Current Opinion in Lipidology 14, no. 3 (June 2003): 255–61. http://dx.doi.org/10.1097/00041433-200306000-00005.

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15

Ntambi, James M. "The regulation of stearoyl-CoA desaturase (SCD)." Progress in Lipid Research 34, no. 2 (January 1995): 139–50. http://dx.doi.org/10.1016/0163-7827(94)00010-j.

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16

Cai, Yuanheng, Xiao-Hong Yu, Jin Chai, Chang-Jun Liu та John Shanklin. "A conserved evolutionary mechanism permits Δ9 desaturation of very-long-chain fatty acyl lipids". Journal of Biological Chemistry 295, № 32 (11 червня 2020): 11337–45. http://dx.doi.org/10.1074/jbc.ra120.014258.

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Δ9 fatty acyl desaturases introduce a cis–double bond between C9 and C10 of saturated fatty acyl chains. From the crystal structure of the mouse stearoyl-CoA desaturase (mSCD1) it was proposed that Tyr-104, a surface residue located at the distal end of the fatty acyl binding pocket plays a key role in specifying 18C selectivity. We created mSCD1-Y104G to test the hypothesis that eliminating this bulky side chain would create an opening and permit the substrate's methyl end to protrude through the enzyme into the lipid bilayer, facilitating the desaturation of very-long-chain (VLC) substrates.

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17

O’Neill, Lucas M., Chang-An Guo, Fang Ding, Yar Xin Phang, Zhaojin Liu, Sohel Shamsuzzaman, and James M. Ntambi. "Stearoyl-CoA Desaturase-2 in Murine Development, Metabolism, and Disease." International Journal of Molecular Sciences 21, no. 22 (November 16, 2020): 8619. http://dx.doi.org/10.3390/ijms21228619.

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Stearoyl-CoA Desaturase-2 (SCD2) is a member of the Stearoyl-CoA Desaturase (SCD) family of enzymes that catalyze the rate-limiting step in monounsaturated fatty acid (MUFA) synthesis. The MUFAs palmitoleoyl-CoA (16:1n7) and oleoyl-CoA (18:1n9) are the major products of SCD2. Palmitoleoyl-CoA and oleoyl-CoA have various roles, from being a source of energy to signaling molecules. Under normal feeding conditions, SCD2 is ubiquitously expressed and is the predominant SCD isoform in the brain. However, obesogenic diets highly induce SCD2 in adipose tissue, lung, and kidney. Here we provide a comp

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18

Paton, Chad M., and James M. Ntambi. "Biochemical and physiological function of stearoyl-CoA desaturase." American Journal of Physiology-Endocrinology and Metabolism 297, no. 1 (July 2009): E28—E37. http://dx.doi.org/10.1152/ajpendo.90897.2008.

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A key and highly regulated enzyme that is required for the biosynthesis of monounsaturated fatty acids is stearoyl-CoA desaturase (SCD), which catalyzes the D9- cis desaturation of a range of fatty acyl-CoA substrates. The preferred substrates are palmitoyl- and stearoyl-CoA, which are converted into palmitoleoyl- and oleoyl-CoA respectively. Oleate is the most abundant monounsaturated fatty acid in dietary fat and is therefore readily available. Studies of mice that have a naturally occurring mutation in the SCD-1 gene isoform as well as a mouse model with a targeted disruption of the SCD gen

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19

Cohen, Paul, James M. Ntambi, and Jeffrey M. Friedman. "Stearoyl-CoA Desaturase-1 and the Metabolic Syndrome." Current Drug Targets - Immune, Endocrine & Metabolic Disorders 3, no. 4 (December 1, 2003): 271–80. http://dx.doi.org/10.2174/1568008033340117.

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20

Williams, Noelle S., Stephen Gonzales, Jacinth Naidoo, Giomar Rivera-Cancel, Sukesh Voruganti, Prema Mallipeddi, Panayotis C. Theodoropoulos, et al. "Tumor-Activated Benzothiazole Inhibitors of Stearoyl-CoA Desaturase." Journal of Medicinal Chemistry 63, no. 17 (August 5, 2020): 9773–86. http://dx.doi.org/10.1021/acs.jmedchem.0c00899.

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Attie, Alan D., Matthew T. Flowers, Jessica B. Flowers, Albert K. Groen, Folkert Kuipers, and James M. Ntambi. "Stearoyl-CoA Desaturase Deficiency, Hypercholesterolemia, Cholestasis, and Diabetes." Nutrition Reviews 65 (June 28, 2008): S35—S38. http://dx.doi.org/10.1111/j.1753-4887.2007.tb00326.x.

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Attie, Alan D., Matthew T. Flowers, Jessica B. Flowers, Albert K. Groen, Folkert Kuipers, and James M. Ntambi. "Stearoyl-CoA Desaturase Deficiency, Hypercholesterolemia, Cholestasis, and Diabetes." Nutrition Reviews 65, no. 6 (June 1, 2007): 35–38. http://dx.doi.org/10.1301/nr.2007.jun.s35-s38.

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23

Man, Weng Chi, Makoto Miyazaki, Kiki Chu, and James M. Ntambi. "Membrane Topology of Mouse Stearoyl-CoA Desaturase 1." Journal of Biological Chemistry 281, no. 2 (November 7, 2005): 1251–60. http://dx.doi.org/10.1074/jbc.m508733200.

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Liu, Gang. "Stearoyl-CoA desaturase inhibitors: update on patented compounds." Expert Opinion on Therapeutic Patents 19, no. 9 (August 19, 2009): 1169–91. http://dx.doi.org/10.1517/13543770903061311.

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Vincent, Benjamin M., Daniel F. Tardiff, Jeff S. Piotrowski, Rebecca Aron, Matthew C. Lucas, Chee Yeun Chung, Helene Bacherman та ін. "Inhibiting Stearoyl-CoA Desaturase Ameliorates α-Synuclein Cytotoxicity". Cell Reports 25, № 10 (грудень 2018): 2742–54. http://dx.doi.org/10.1016/j.celrep.2018.11.028.

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Kamal, Shagufta, Ayesha Saleem, Saima Rehman, Ismat Bibi, and Hafiz M. N. Iqbal. "Protein engineering: Regulatory perspectives of stearoyl CoA desaturase." International Journal of Biological Macromolecules 114 (July 2018): 692–99. http://dx.doi.org/10.1016/j.ijbiomac.2018.03.171.

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Li, Chun Sing, Liette Belair, Jocelyne Guay, Renata Murgasva, Wayne Sturkenboom, Yeeman K. Ramtohul, Lei Zhang, and Zheng Huang. "Thiazole analog as stearoyl-CoA desaturase 1 inhibitor." Bioorganic & Medicinal Chemistry Letters 19, no. 17 (September 2009): 5214–17. http://dx.doi.org/10.1016/j.bmcl.2009.07.015.

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Koeberle, Andreas, Konstantin Löser, and Maria Thürmer. "Stearoyl-CoA desaturase-1 and adaptive stress signaling." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1861, no. 11 (November 2016): 1719–26. http://dx.doi.org/10.1016/j.bbalip.2016.08.009.

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Shen, Jiemin, Gang Wu, Ah-Lim Tsai, and Ming Zhou. "Structure and Function of Mammalian Stearoyl-COA Desaturase." Biophysical Journal 114, no. 3 (February 2018): 426a. http://dx.doi.org/10.1016/j.bpj.2017.11.2361.

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Petroff, Anna B., Rebecca L. Weir, Charles R. Yates, Joseph D. Ng, and Jerome Baudry. "Sequential Dynamics of Stearoyl-CoA Desaturase-1(SCD1)/Ligand Binding and Unbinding Mechanism: A Computational Study." Biomolecules 11, no. 10 (September 30, 2021): 1435. http://dx.doi.org/10.3390/biom11101435.

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Stearoyl-CoA desaturase-1 (SCD1 or delta-9 desaturase, D9D) is a key metabolic protein that modulates cellular inflammation and stress, but overactivity of SCD1 is associated with diseases, including cancer and metabolic syndrome. This transmembrane endoplasmic reticulum protein converts saturated fatty acids into monounsaturated fatty acids, primarily stearoyl-CoA into oleoyl-CoA, which are critical products for energy metabolism and membrane composition. The present computational molecular dynamics study characterizes the molecular dynamics of SCD1 with substrate, product, and as an apoprote

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31

Miyazaki, Makoto, Francisco Enrique Gomez та James M. Ntambi. "Lack of stearoyl-CoA desaturase-1 function induces a palmitoyl-CoA Δ6 desaturase and represses the stearoyl-CoA desaturase-3 gene in the preputial glands of the mouse". Journal of Lipid Research 43, № 12 (16 вересня 2002): 2146–54. http://dx.doi.org/10.1194/jlr.m200271-jlr200.

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NAKASHIMA, Shigeru, Yutong ZHAO та Yoshinori NOZAWA. "Molecular cloning of Δ9 fatty acid desaturase from the protozoan Tetrahymena thermophila and its mRNA expression during thermal membrane adaptation". Biochemical Journal 317, № 1 (1 липня 1996): 29–34. http://dx.doi.org/10.1042/bj3170029.

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In response to a decrease in its growth temperature, the protozoan Tetrahymena is known to increase the level of unsaturated fatty acids in its membrane phospholipids so as to maintain the correct physical state (fluidity) of the membranes. In this organism, synthesis of unsaturated fatty acids is initiated by Δ9 acyl-CoA desaturase. Our previous studies have shown that, during cold adaptation, the activity of microsomal palmitoyl- and stearoyl-CoA desaturase increases, reaching a maximal level at 2 h after a temperature down-shift to 15 °C. Two hypotheses have been proposed to explain this in

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33

Milanesi, E., L. Nicoloso, and P. Crepaldi. "Stearoyl CoA desaturase gene polymorphism in Italian cattle breeds." Italian Journal of Animal Science 6, sup1 (January 2007): 167. http://dx.doi.org/10.4081/ijas.2007.1s.167.

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Moioli, B., L. Orrù, G. Catillo, G. B. Congiu, and F. Napolitano. "Partial sequencing of Stearoyl-CoA desaturase gene in buffalo." Italian Journal of Animal Science 4, sup2 (January 2005): 25–27. http://dx.doi.org/10.4081/ijas.2005.2s.25.

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Dobrzyn, Pawel, Tomasz Bednarski, and Agnieszka Dobrzyn. "Metabolic reprogramming of the heart through stearoyl-CoA desaturase." Progress in Lipid Research 57 (January 2015): 1–12. http://dx.doi.org/10.1016/j.plipres.2014.11.003.

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Savino, Angela Maria, Orianne Olivares, Shani Barel, Lev Yakimov, Ifat Geron, Hila Fishman, Inbal Mor, et al. "Stearoyl-CoA Desaturase (SCD) Enhances Central Nervous System Leukemia." Blood 132, Supplement 1 (November 29, 2018): 389. http://dx.doi.org/10.1182/blood-2018-99-114749.

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Abstract Background: Central nervous system (CNS) involvement by acute lymphoblastic leukemia (ALL) is a major clinical concern. Leukemic cells can be found in the CNS at diagnosis (1-2%) or, more frequently, at relapse (30%). Very little is known about the pathogenesis and therefore there are no targeted therapies. Prophylactic CNS-directed conventional intrathecal chemotherapy or irradiation are required for relapse-free survival. However, they are associated with substantial rates of short and long term toxicity. Therefore, elucidation of molecular mechanisms and pathways mediating leukemia

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37

Dobrzyn, Agnieszka, and Pawel Dobrzyn. "Inhibition of stearoyl-CoA desaturase by cyclic amine derivatives." Expert Opinion on Therapeutic Patents 18, no. 4 (April 2008): 457–60. http://dx.doi.org/10.1517/13543776.18.4.457.

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Bai, Yonghong, Jason G. McCoy, Elena J. Levin, Pablo Sobrado, Kanagalaghatta R. Rajashankar, Brian G. Fox, and Ming Zhou. "X-ray structure of a mammalian stearoyl-CoA desaturase." Nature 524, no. 7564 (June 22, 2015): 252–56. http://dx.doi.org/10.1038/nature14549.

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NERGİS, Hazniye, Seyrani KONCAGÜL, and Selahaddin KİRAZ. "Hereford ırkı sığırlarda stearoyl-CoA desaturase (SCD) gen polimorfizmi." Harran Tarım ve Gıda Bilimleri Dergisi 23, no. 2 (June 18, 2019): 247–53. http://dx.doi.org/10.29050/harranziraat.487490.

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Sampath, Harini, and James M. Ntambi. "Role of stearoyl-CoA desaturase in human metabolic disease." Future Lipidology 3, no. 2 (April 2008): 163–73. http://dx.doi.org/10.2217/17460875.3.2.163.

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UMEKI, Shigenobu, and Yoshiniri NOZAWA. "Effect of Local Anesthetics on Stearoyl-CoA Desaturase ofTetrahymenaMicrosomes." Biological Chemistry Hoppe-Seyler 367, no. 1 (January 1986): 61–66. http://dx.doi.org/10.1515/bchm3.1986.367.1.61.

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Fenner, Annette. "Stearoyl-CoA desaturase: a novel therapeutic target for RCC." Nature Reviews Urology 10, no. 7 (May 21, 2013): 370. http://dx.doi.org/10.1038/nrurol.2013.116.

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Zhang, Chun-Lei, Xue-Yuan Gao, Ru-Ying Shao, Yan-Hong Wang, Xing-Tang Fang, and Hong Chen. "Stearoyl-CoA Desaturase (SCD) Gene Polymorphism in Goat Breeds." Biochemical Genetics 48, no. 9-10 (July 14, 2010): 822–28. http://dx.doi.org/10.1007/s10528-010-9363-y.

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Koltun, Dmitry O., Natalya I. Vasilevich, Eric Q. Parkhill, Andrei I. Glushkov, Timur M. Zilbershtein, Elena I. Mayboroda, Melanie A. Boze, et al. "Orally bioavailable, liver-selective stearoyl-CoA desaturase (SCD) inhibitors." Bioorganic & Medicinal Chemistry Letters 19, no. 11 (June 2009): 3050–53. http://dx.doi.org/10.1016/j.bmcl.2009.04.004.

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Wang, Jian, Lan Yu, He Wang, Yunling Gao, James P. Schrementi, Regina K. Porter, David A. Yurek, et al. "Identification and Characterization of Hamster Stearoyl-CoA Desaturase Isoforms." Lipids 43, no. 3 (December 15, 2007): 197–205. http://dx.doi.org/10.1007/s11745-007-3139-0.

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Liu, Xueqing, Makoto Miyazaki, Matthew T. Flowers, Harini Sampath, Minghui Zhao, Kiki Chu, Chad M. Paton, Diane Seohee Joo, and James M. Ntambi. "Loss of Stearoyl-CoA Desaturase-1 Attenuates Adipocyte Inflammation." Arteriosclerosis, Thrombosis, and Vascular Biology 30, no. 1 (January 2010): 31–38. http://dx.doi.org/10.1161/atvbaha.109.195636.

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Liu, Lulu, Yu Wang, Xiaojuan Liang, Xiao Wu, Jiali Liu, Shulin Yang, Cong Tao, et al. "Stearoyl-CoA Desaturase Is Essential for Porcine Adipocyte Differentiation." International Journal of Molecular Sciences 21, no. 7 (April 1, 2020): 2446. http://dx.doi.org/10.3390/ijms21072446.

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Fat deposition, which influences pork production, meat quality and growth efficiency, is an economically important trait in pigs. Numerous studies have demonstrated that stearoyl-CoA desaturase (SCD), a key enzyme that catalyzes the conversion of saturated fatty acids into monounsaturated fatty acids, is associated with fatty acid composition in pigs. As SCD was observed to be significantly induced in 3T3-L1 preadipocytes differentiation, we hypothesized that it plays a role in porcine adipocyte differentiation and fat deposition. In this study, we revealed that SCD is highly expressed in adip

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ZHANG, Lin, Lan GE, Tai TRAN, Kurt STENN, and Stephen M. PROUTY. "Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element." Biochemical Journal 357, no. 1 (June 25, 2001): 183–93. http://dx.doi.org/10.1042/bj3570183.

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Stearoyl-CoA desaturase is the rate-limiting enzyme in the production of mono-unsaturated fatty acids. We have recently cloned and characterized the human Scd cDNA and SCD (the stearoyl-CoA desaturase structural gene) on chromosome 10, as well as the non-transcribed pseudogene on chromosome 17. In order to further define SCD regulation and function, we have isolated and characterized the promoter of the structural gene. Screening of chromosome-10-specific libraries resulted in the isolation of 4.1kb of SCD sequence upstream of the translation start site. Binding sites for transcription factors

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Li, Weihua, Huimin Bai, Shiping Liu, Dongyan Cao, Hongying Wu, Keng Shen, Yanhong Tai, and Jiaxin Yang. "Targeting stearoyl-CoA desaturase 1 to repress endometrial cancer progression." Oncotarget 9, no. 15 (January 24, 2018): 12064–78. http://dx.doi.org/10.18632/oncotarget.24304.

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Dobrzyn, A. "The Role of Stearoyl-CoA Desaturase in Body Weight Regulation." Trends in Cardiovascular Medicine 14, no. 2 (February 2004): 77–81. http://dx.doi.org/10.1016/j.tcm.2003.12.005.

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