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Artículos de revistas sobre el tema "Major Royal Jelly Protein 1"

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Publicado: 4 de junio de 2021
Última modificación: 15 de febrero de 2022

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1

Kashima, Yuri, Satoshi Kanematsu, Saori Asai, et al. "Identification of a Novel Hypocholesterolemic Protein, Major Royal Jelly Protein 1, Derived from Royal Jelly." PLoS ONE 9, no. 8 (2014): e105073. http://dx.doi.org/10.1371/journal.pone.0105073.

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2

YAMAGUCHI, Kikuji, Shaoyu HE, Zhengyue LI, et al. "Quantification of Major Royal Jelly Protein 1 in Fresh Royal Jelly by Indirect Enzyme-Linked Immunosorbent Assay." Bioscience, Biotechnology, and Biochemistry 77, no. 6 (2013): 1310–12. http://dx.doi.org/10.1271/bbb.130013.

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3

Wang, Xueyu, Jie Dong, Jiangtao Qiao, Gensheng Zhang, and Hongcheng Zhang. "Purification and characteristics of individual major royal jelly protein 1–3." Journal of Apicultural Research 59, no. 5 (2020): 1049–60. http://dx.doi.org/10.1080/00218839.2020.1761071.

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4

Moriyama, Takanori, Aimi Ito, Sumire Omote, Yuri Miura, and Hiroki Tsumoto. "Heat Resistant Characteristics of Major Royal Jelly Protein 1 (MRJP1) Oligomer." PLOS ONE 10, no. 5 (2015): e0119169. http://dx.doi.org/10.1371/journal.pone.0119169.

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5

Shen, Li-rong, Yi-ran Wang, Liang Zhai, et al. "Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody." Journal of Zhejiang University-SCIENCE B 16, no. 2 (2015): 155–66. http://dx.doi.org/10.1631/jzus.b1400223.

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6

Lin, Na, Si Chen, Hong Zhang, Junmin Li, and Linglin Fu. "Quantification of Major Royal Jelly Protein 1 in Fresh Royal Jelly by Ultraperformance Liquid Chromatography–Tandem Mass Spectrometry." Journal of Agricultural and Food Chemistry 66, no. 5 (2018): 1270–78. http://dx.doi.org/10.1021/acs.jafc.7b05698.

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7

Furusawa, Takako, Yasuko Arai, Kenji Kato, and Kenji Ichihara. "Quantitative Analysis of Apisin, a Major Protein Unique to Royal Jelly." Evidence-Based Complementary and Alternative Medicine 2016 (2016): 1–9. http://dx.doi.org/10.1155/2016/5040528.

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Apisin, a protein that is unique to royal jelly (RJ), is known to compose the greater part of the RJ proteins and to exist as a heterooligomer containing major royal jelly protein 1 and apisimin. However, few reports on the methods for quantifying apisin have been published. Thus, we attempted to quantify apisin using HPLC, a widely used analytical technique, as described below. Isoelectric precipitation and size-exclusion chromatography were used to obtain the purified protein, which was identified as apisin by SDS-PAGE and LC-MS analyses. The purified apisin was lyophilized and then used to
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8

Tamura, Shougo, Shizuka Amano, Toru Kono, et al. "Molecular characteristics and physiological functions of major royal jelly protein 1 oligomer." PROTEOMICS 9, no. 24 (2009): 5534–43. http://dx.doi.org/10.1002/pmic.200900541.

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9

Ibarra-Herrera, Celeste C., Mario A. Torres-Acosta, Gonzalo I. Mendoza-Ochoa, Jose M. Aguilar-Yañez, and Marco Rito-Palomares. "Recovery of major royal jelly protein 1 expressed inPichia pastorisin aqueous two-phase systems." Journal of Chemical Technology & Biotechnology 89, no. 7 (2014): 941–47. http://dx.doi.org/10.1002/jctb.4342.

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10

Majtán, Juraj, Elena Kováčová, Katarína Bíliková та Jozef Šimúth. "The immunostimulatory effect of the recombinant apalbumin 1–major honeybee royal jelly protein–on TNFα release". International Immunopharmacology 6, № 2 (2006): 269–78. http://dx.doi.org/10.1016/j.intimp.2005.08.014.

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11

Mandacaru, Samuel C., Luis H. F. do Vale, Siavash Vahidi, et al. "Characterizing the Structure and Oligomerization of Major Royal Jelly Protein 1 (MRJP1) by Mass Spectrometry and Complementary Biophysical Tools." Biochemistry 56, no. 11 (2017): 1645–55. http://dx.doi.org/10.1021/acs.biochem.7b00020.

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12

Zhang, Yifan, Yong Chen, Yiting Cai, et al. "Novel polyclonal antibody-based rapid gold sandwich immunochromatographic strip for detecting the major royal jelly protein 1 (MRJP1) in honey." PLOS ONE 14, no. 2 (2019): e0212335. http://dx.doi.org/10.1371/journal.pone.0212335.

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13

Majtan, Juraj, Pawan Kumar, Tomas Majtan, Andrew F. Walls, and Jaroslav Klaudiny. "Effect of honey and its major royal jelly protein 1 on cytokine and MMP-9 mRNA transcripts in human keratinocytes." Experimental Dermatology 19, no. 8 (2009): e73-e79. http://dx.doi.org/10.1111/j.1600-0625.2009.00994.x.

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14

Cruz, Gabriel C. N., Liudy Garcia, Adelson J. Silva, et al. "Calcium effect and pH-dependence on self-association and structural stability of the Apis mellifera major royal jelly protein 1." Apidologie 42, no. 3 (2011): 252–69. http://dx.doi.org/10.1007/s13592-011-0025-9.

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15

Borutinskaitė, Veronika, Gražina Treigytė, Dalius Matuzevičius, et al. "Proteomic Analysis of Pollen and Blossom Honey from Rape Seed Brassica Napus L." Journal of Apicultural Science 61, no. 1 (2017): 73–92. http://dx.doi.org/10.1515/jas-2017-0006.

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Abstract In the study, honey from oilseed rape Brassica napus L., and both hand-collected (winter rape Visby and Cult) and bee-collected pollen of oilseed rape were analyzed for their proteome content, in order to see if any plant proteins were present to allow the proteo-typing of the oilseed rape honey. Proteins were fractionated by two-dimensional gel electrophoresis (2DE), stained by Coomassie blue and then analyzed by mass spectrometry. All identified proteins were divided into few groups due to their biological function. In 2DE gels with separated proteins from blossom honey, only bee (A
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16

Imjongjirak, Chanprapa, Sirawut Klinbunga, and Siriporn Sittipraneed. "Cloning, Expression and Genomic Organization of Genes Encoding Major Royal Jelly Protein 1 and 2 of the Honey Bee (Apis cerana)." BMB Reports 38, no. 1 (2005): 49–57. http://dx.doi.org/10.5483/bmbrep.2005.38.1.049.

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17

Lazarevska, Sofija, and Petre Makreski. "Insights into the infrared and Raman spectra of fresh and lyophilized royal jelly and protein degradation IR spectroscopy study during heating." Macedonian Journal of Chemistry and Chemical Engineering 34, no. 1 (2015): 87. http://dx.doi.org/10.20450/mjcce.2015.669.

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<p> In terms of chemical composition, a honeybee secretion known as royal jelly (RJ) is very complex product containing water, proteins, carbohydrates, lipids, mineral salts and small amounts of polyphenols, vitamins and enzymes. Despite its chemical diversity, the bands originating from vibrational modes of the present proteins were successfully assigned in 1800–1200 cm<sup>–1</sup> (Raman and IR) region where the interference of bands from other vibrational species is not substantial. The protein bands were attributed to amide I, amide II and amide III modes and their inten
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18

Chakrabarti, Priyadarshini, and Ramesh R. Sagili. "Changes in Honey Bee Head Proteome in Response to Dietary 24-Methylenecholesterol." Insects 11, no. 11 (2020): 743. http://dx.doi.org/10.3390/insects11110743.

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Phytosterols are important micronutrients that are precursors of important molting hormones and help maintain cellular membrane integrity in insects including bees. Previous research has shown that 24-methylenecholesterol is a key phytosterol that enhances honey bee longevity and improves nurse bee physiology. Nurse bees have the ability to selectively transfer this sterol to developing larvae through brood food. This study examines the physiological impacts of 24-methylenecholesterol on nurse bees, by analyzing the protein profiles of nurse bee heads upon dietary sterol manipulation. Dietary
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19

Park, Hee-Geun, Bo-Yeon Kim, Jin-Myung Kim, et al. "Upregulation of Transferrin and Major Royal Jelly Proteins in the Spermathecal Fluid of Mated Honeybee (Apis mellifera) Queens." Insects 12, no. 8 (2021): 690. http://dx.doi.org/10.3390/insects12080690.

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Sperm storage in the spermathecae of honeybee (Apis mellifera) queens is vital for reproduction of honeybees. However, the molecular mechanisms whereby queens store sperm in a viable state over prolonged periods in the spermatheca are not fully understood. Here, we conducted RNA sequencing analysis of the spermathecae in both virgin and mated A. mellifera queens 24 h after mating and observed that the genes encoding transferrin (Tf) and major royal jelly proteins (MRJPs) were differentially expressed in the spermathecae of mated queens. The concentrations of Tf and antioxidant proteins such as
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20

Brudzynski, Katrina, and Calvin Sjaarda. "Honey Glycoproteins Containing Antimicrobial Peptides, Jelleins of the Major Royal Jelly Protein 1, Are Responsible for the Cell Wall Lytic and Bactericidal Activities of Honey." PLOS ONE 10, no. 4 (2015): e0120238. http://dx.doi.org/10.1371/journal.pone.0120238.

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21

Korb, Judith, Karen Meusemann, Denise Aumer, et al. "Comparative transcriptomic analysis of the mechanisms underpinning ageing and fecundity in social insects." Philosophical Transactions of the Royal Society B: Biological Sciences 376, no. 1823 (2021): 20190728. http://dx.doi.org/10.1098/rstb.2019.0728.

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The exceptional longevity of social insect queens despite their lifelong high fecundity remains poorly understood in ageing biology. To gain insights into the mechanisms that might underlie ageing in social insects, we compared gene expression patterns between young and old castes (both queens and workers) across different lineages of social insects (two termite, two bee and two ant species). After global analyses, we paid particular attention to genes of the insulin/insulin-like growth factor 1 signalling (IIS)/target of rapamycin (TOR)/juvenile hormone (JH) network, which is well known to re
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22

MIZUTANI, Yoko, Yoshinao SHIBUYA, Toshiya TAKAHASHI, Takahiko TSUNODA, Tatsuya MORIYAMA, and Mariko SEISHIMA. "Major royal jelly protein 3 as a possible allergen in royal jelly-induced anaphylaxis." Journal of Dermatology 38, no. 11 (2011): 1079–81. http://dx.doi.org/10.1111/j.1346-8138.2010.01179.x.

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23

Park, Min Ji, Bo Yeon Kim, Hee Geun Park, et al. "Major royal jelly protein 2 acts as an antimicrobial agent and antioxidant in royal jelly." Journal of Asia-Pacific Entomology 22, no. 3 (2019): 684–89. http://dx.doi.org/10.1016/j.aspen.2019.05.003.

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24

Hossen, Md Sakib, Taebun Nahar, Siew Hua Gan, and Md Ibrahim Khalil. "Bioinformatics and Therapeutic Insights on Proteins in Royal Jelly." Current Proteomics 16, no. 2 (2019): 84–101. http://dx.doi.org/10.2174/1570164615666181012113130.

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Background: To date, there is no x-ray crystallography or structures from nuclear magnetic resonance (NMR) on royal jelly proteins available in the online data banks. In addition, characterization of proteins in royal jelly is not fully accomplished to date. Although new investigations unravel novel proteins in royal jelly, the majority of a protein family is present in high amounts (80-90%). Objective: In this review, we attempted to predict the three-dimensional structure of royal jelly proteins (especially the major royal jelly proteins) to allow visualization of the four protein surface pr
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25

Albert, Štefan, and Jürgen Schmitz. "Characterization of major royal jelly protein-like DNA sequences inApis dorsata." Journal of Apicultural Research 41, no. 3-4 (2002): 75–82. http://dx.doi.org/10.1080/00218839.2002.11101072.

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26

Kim, Bo Yeon, Kwang Sik Lee, Boknam Jung, et al. "Honeybee (Apis cerana) major royal jelly protein 4 exhibits antimicrobial activity." Journal of Asia-Pacific Entomology 22, no. 1 (2019): 175–82. http://dx.doi.org/10.1016/j.aspen.2018.12.020.

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27

Li, Jian-ke, Mao Feng, Lan Zhang, Zhao-hui Zhang, and Ying-hong Pan. "Proteomics Analysis of Major Royal Jelly Protein Changes under Different Storage Conditions." Journal of Proteome Research 7, no. 8 (2008): 3339–53. http://dx.doi.org/10.1021/pr8002276.

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28

Bilal, Bushra, and M. Kamran Azim. "Nematicidal activity of ‘major royal jelly protein’-containing glycoproteins from Acacia honey." Experimental Parasitology 192 (September 2018): 52–59. http://dx.doi.org/10.1016/j.exppara.2018.07.011.

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29

KOROŠEC, Mojca, and Jasna BERTONCELJ. "Pomen čebeljih pridelkov v humani prehrani." Acta agriculturae Slovenica 115, no. 2 (2020): 223. http://dx.doi.org/10.14720/aas.2020.115.2.632.

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Bee products are a natural source of nutrients and biologically active compounds, which may also be found on the lists of functional ingredients. In our diets, mainly honey is used and to a lesser extent bee pollen and royal jelly. Propolis and bee venom are mainly used in apitherapy due to their therapeutic properties. Regarding the basic nutrients, honey is primarily a source of sugars, while protein and fat contents are considerable in royal jelly and pollen, which also contains dietary fiber. Bee products also contain small amounts of bioactive compounds that have antioxidant, antimicrobia
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30

Okamoto, Iwao, Yoshifumi Taniguchi, Toshio Kunikata, et al. "Major royal jelly protein 3 modulates immune responses in vitro and in vivo." Life Sciences 73, no. 16 (2003): 2029–45. http://dx.doi.org/10.1016/s0024-3205(03)00562-9.

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31

Kim, Bo Yeon. "Antiapoptotic role of major royal jelly protein 8 of honeybee (Apis mellifera) venom." Journal of Asia-Pacific Entomology 24, no. 3 (2021): 666–70. http://dx.doi.org/10.1016/j.aspen.2021.05.014.

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32

Kolayli, Sevgi, Huseyin Sahin, Zehra Can, Oktay Yildiz, Meltem Malkoc, and Alsever Asadov. "A Member of Complementary Medicinal Food." Journal of Evidence-Based Complementary & Alternative Medicine 21, no. 4 (2016): NP43—NP48. http://dx.doi.org/10.1177/2156587215618832.

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This study investigated various chemical and antioxidant properties of Anatolian royal jelly samples. Moisture, pH, total protein, 10-hydroxy-2-decenoic acid (10-HDA) and sugars were analyzed from 18 samples. Total phenolic contents, ferric reducing antioxidant capacity and 2,2-diphenyl-1-picryhydrazyl (DPPH) free radical scavenging activity were measured as antioxidant determinants. 10-HDA contents and total protein content of fresh weight ranged between 1.0% and 3.9%, and 11.4% and 15.8%, respectively. The main sugars detected were glucose and fructose. Maltose, trehalose, and melibiose were
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33

Feng, Mao, Yu Fang, Chuan Ma, et al. "Mechanistic Insight into Royal Protein Inhibiting the Gram-Positive Bacteria." Biomolecules 11, no. 1 (2021): 64. http://dx.doi.org/10.3390/biom11010064.

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Royal jelly (RJ), a natural honeybee product, has a wide range of antibacterial activities. N-glycosylated major royal jelly protein 2 (N-MRJP2), purified from RJ, can inhibit the growth of Paenibacillus larvae (P. larvae, Gram-positive), a contagious etiological agent of the American foulbrood disease of honeybees. However, the inhibitory mechanism is largely unknown. Antibacterial assay and membrane proteome were conducted to investigate the inhibition capacity of RJ from different instar larvae and P. larvae treated by N-MRJP2, respectively. The similar antibacterial efficiency of RJ from d
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34

Abu-Serie, Marwa M., and Noha H. Habashy. "Two purified proteins from royal jelly with in vitro dual anti-hepatic damage potency: Major royal jelly protein 2 and its novel isoform X1." International Journal of Biological Macromolecules 128 (May 2019): 782–95. http://dx.doi.org/10.1016/j.ijbiomac.2019.01.210.

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35

Buttstedt, Anja, Robin FA Moritz, and Silvio Erler. "More than royal food - Major royal jelly protein genes in sexuals and workers of the honeybee Apis mellifera." Frontiers in Zoology 10, no. 1 (2013): 72. http://dx.doi.org/10.1186/1742-9994-10-72.

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36

Minegaki, Naho, Tetsuo Koshizuka, Saeka Nishina, et al. "The Carboxyl-Terminal Penta-Peptide Repeats of Major Royal Jelly Protein 3 Enhance Cell Proliferation." Biological and Pharmaceutical Bulletin 43, no. 12 (2020): 1911–16. http://dx.doi.org/10.1248/bpb.b20-00607.

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37

Hanes, Jozef, and Jozef Šimuth. "Identification and partial characterization of the major royal jelly protein of the honey bee (Apis melliferaL.)." Journal of Apicultural Research 31, no. 1 (1992): 22–26. http://dx.doi.org/10.1080/00218839.1992.11101256.

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38

Bilikova, Katarina, Tatiana Kristof Krakova, Kikuji Yamaguchi, and Yoshihisa Yamaguchi. "Major royal jelly proteins as markers of authenticity and quality of honey / Glavni proteini matične mliječi kao markeri izvornosti i kakvoće meda." Archives of Industrial Hygiene and Toxicology 66, no. 4 (2015): 259–67. http://dx.doi.org/10.1515/aiht-2015-66-2653.

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Until now, the properties of honey have been defined based exclusively on the content of plant components in the nectar of given plant. We showed that apalbumin1, the major royal jelly (RJ) protein, is an authentic and regular component of honey. Apalbumin1 and other RJ proteins and peptides are responsible for the immunostimulatory properties and antibiotic activity of honey. For the quantification of apalbumin1, an enzyme-linked immunosorbent assay (ELISA) was developed using polyclonal anti-apalbumin1 antibody. The method is suitable for honey authenticity determination; moreover it is usef
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39

Zhang, Yan-Zheng, Shuai Wang, Yi-Fan Chen, et al. "Authentication of Apis cerana Honey and Apis mellifera Honey Based on Major Royal Jelly Protein 2 Gene." Molecules 24, no. 2 (2019): 289. http://dx.doi.org/10.3390/molecules24020289.

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In Asia, honey is mainly produced by Apis mellifera and Apis cerana. However, the price of A. cerana honey is usually much higher than A. mellifera honey. Seeing considerable profits, some dishonest companies and beekeepers mislabel A. mellifera honey as A. cerana honey or incorporate A. mellifera honey into A. cerana honey. In the present study, we developed methods to discriminate A. cerana honey from A. mellifera honey based on the MRJP2 (major royal jelly protein 2) gene. Two pairs of species-specific primers were designed. The amplification products of A. cerana and A. mellifera were 212
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40

Kupke, Jens, Johannes Spaethe, Martin J. Mueller, Wolfgang Rössler, and Štefan Albert. "Molecular and biochemical characterization of the major royal jelly protein in bumblebees suggest a non-nutritive function." Insect Biochemistry and Molecular Biology 42, no. 9 (2012): 647–54. http://dx.doi.org/10.1016/j.ibmb.2012.05.003.

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41

Wang, Kang, Heng Chen, Zhe-Guang Lin, et al. "Carbendazim exposure during the larval stage suppresses major royal jelly protein expression in nurse bees (Apis mellifera)." Chemosphere 266 (March 2021): 129011. http://dx.doi.org/10.1016/j.chemosphere.2020.129011.

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42

Drapeau, M. D., S. Albert, R. Kucharski, C. Prusko, and R. Maleszka. "Evolution of the Yellow/Major Royal Jelly Protein family and the emergence of social behavior in honey bees." Genome Research 16, no. 11 (2006): 1385–94. http://dx.doi.org/10.1101/gr.5012006.

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43

Helbing, Sophie, H. Michael G. Lattorff, Robin F. A. Moritz, and Anja Buttstedt. "Comparative analyses of the major royal jelly protein gene cluster in three Apis species with long amplicon sequencing." DNA Research 24, no. 3 (2017): 279–87. http://dx.doi.org/10.1093/dnares/dsw064.

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44

Kim, Bo Yeon, and Byung Rae Jin. "Antimicrobial activity of the C-terminal of the major royal jelly protein 4 in a honeybee (Apis cerana)." Journal of Asia-Pacific Entomology 22, no. 2 (2019): 561–64. http://dx.doi.org/10.1016/j.aspen.2019.04.004.

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45

Shirakawa, Tomohiko, Aki Miyawaki, Takuma Matsubara, et al. "Daily Oral Administration of Protease-Treated Royal Jelly Protects Against Denervation-Induced Skeletal Muscle Atrophy." Nutrients 12, no. 10 (2020): 3089. http://dx.doi.org/10.3390/nu12103089.

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Honeybees produce royal jelly (RJ) from their cephalic glands. Royal jelly is a source of nutrition for the queen honey bee throughout its lifespan and is also involved in fertility and longevity. Royal jelly has long been considered beneficial to human health. We recently observed that RJ delayed impairment of motor function during aging, affecting muscle fiber size. However, how RJ affects skeletal muscle metabolism and the functional component of RJ is as of yet unidentified. We demonstrate that feeding mice with RJ daily prevents a decrease in myofiber size following denervation without af
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46

Bíliková, Katarína, and Jozef Šimúth. "New Criterion for Evaluation of Honey: Quantification of Royal Jelly Protein Apalbumin 1 in Honey by ELISA." Journal of Agricultural and Food Chemistry 58, no. 15 (2010): 8776–81. http://dx.doi.org/10.1021/jf101583s.

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47

Cheng, Yang, Jiadong Cai, Yuanyuan Fu, Congjing Feng, Yue Hao, and Youheng Wei. "Royal jelly attenuates metabolic defects in a Drosophila mutant with elevated TORC1 activity." Biology Open 9, no. 11 (2020): bio054999. http://dx.doi.org/10.1242/bio.054999.

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ABSTRACTTarget of rapamycin complex 1 (TORC1) is a master regulator of cell metabolism, and its dysregulation has been linked to an array of pathologies, including cancer and age-related diseases. Nprl3, a component of GTPase-activating protein towards Rags complex 1 (GATOR1), inhibits TORC1 activity under nutrient scarcity status. The nprl3 mutant exhibits some metabolic defects due to hyper TORC1 activity in Drosophila. Royal jelly (RJ) is a honeybee-secreted product and plays an essential role in caste differentiation that requires TORC1 activity. RJ is also used as a health-benefit food fo
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48

Terao, A., T. Yoneshiro, R. Kaede, et al. "P.231 Uncoupling protein 1 is involved in anti-obesity effects of royal jelly in high fat diet-fed mice." European Neuropsychopharmacology 40 (November 2020): S130—S131. http://dx.doi.org/10.1016/j.euroneuro.2020.09.172.

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49

Ostroverkhova, Nadezhda V., Aksana N. Kucher, Nadezhda P. Babushkina, Olga L. Konusova, and Igor V. Sharakhov. "Variability and Structure of the Repetitive Region of the Major Royal Jelly Protein Gene mrjp3 in Honeybee Apis mellifera of Different Evolutionary Branches." Journal of Molecular Biology Research 8, no. 1 (2018): 122. http://dx.doi.org/10.5539/jmbr.v8n1p122.

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An assessment of the genetic diversity of the microsatellite locus mrjp3 in honeybee of European Apis mellifera subspecies was conducted. Differences in the frequency of alleles for the mrjp3 locus were found in honeybees of different evolutionary branches. Allele "529" was found to be specific for the Apis mellifera mellifera, evolutionary branch M, while alleles "406", "518", and "485" were characteristic of the southern subspecies of bees (A. m. carnica, A. m. carpatica (some researchers consider this breed as a derivative of A. m. carnica), and A. m. caucasica; evolutionary branches C and
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Habashy, Noha H., and Marwa M. Abu-Serie. "Major royal-jelly protein 2 and its isoform X1 are two novel safe inhibitors for hepatitis C and B viral entry and replication." International Journal of Biological Macromolecules 141 (December 2019): 1072–87. http://dx.doi.org/10.1016/j.ijbiomac.2019.09.080.

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