References
1. Fujita T, Kozuka-Hata H, Ao-Kondo H, Kunieda T, Oyama M, Kubo T: Proteomic analysis of the royal jelly and characterization of the functions of its derivation glands in the honeybee. J Proteome Res 2012, 12(1):404–411.
2. Winston ML: The biology of the honey bee. Cambridge, MA 02138 USA: Harvard University Press; 1987.
3. Silici S, Ekmekcioglu O, Eraslan G, Demirtas A: Antioxidative effect of royal jelly in cisplatin-induced testes damage. Urology 2009, 74(3):545–551.
4. Fujiwara S, Imai J, Fujiwara M, Yaeshima T, Kawashima T, Kobayashi K: A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin. J Biol Chem1990, 265(19):11333–11337.
5. Sver L, Orsolic N, Tadic Z, Njari B, Valpotic I, Basic I: A royal jelly as a new potential immunomodulator in rats and mice. Comp Immunol Microbiol Infect Dis 1996, 19(1):31–38.
6. Tamura T, Fujii A, Kuboyama N: Antitumor effects of royal jelly (RJ). Nihon Yakurigaku zasshi 1987, 89(2):73.
7. Albert ?, Klaudiny J: The MRJP/YELLOW protein family of apis mellifera: identification of new members in the EST library. J Insect Physiol 2004, 50(1):51–59.
8. Albert S, Klaudiny J: MRJP9, an ancient protein of the honeybee MRJP family with non-nutritional function. J Apicult Res 2007, 46(2):99–104.
9. Schmitzova J, Klaudiny J, Albert S, Schroder W, Schreckengost W, Hanes J, Judova J, Simuth J: A family of major royal jelly proteins of the honeybee Apis mellifera L. Cell Mol Life Sci 1998, 54(9):1020–1030.
10. Li JK, Feng M, Zhang L, Zhang ZH, Pan YH: Proteomics analysis of major royal jelly protein changes under different storage conditions. J Proteome Res 2008, 7(8):3339–3353.
11. Han B, Li CX, Zhang L, Fang Y, Feng M, Li JK: Novel royal jelly proteins identified by gel-based and gel-free proteomics. J Agr Food Chem 2011, 59(18):10346–10355.
12. Scarselli R, Donadio E, Giuffrida MG, Fortunato D, Conti A, Balestreri E, Felicioli R, Pinzauti M, Sabatini AG, Felicioli A: Towards royal jelly proteome. Proteomics 2005, 5(3):769–776.
13. Okamoto I, Taniguchi Y, Kunikata T, Kohno K, Iwaki K, Ikeda M, Kurimoto M: Major royal jelly protein 3 modulates immune responses in vitro and in vivo. Life Sci 2003, 73(16):2029–2045.
14. Kimura Y, Nagai H, Miyamoto M, Kimura M, Yonekura M: Identification of a royal jelly glycoprotein that carries unique complex-type N-glycans harboring the T-antigen (Galbeta1-3GalNAc) unit. Biosci Biotechnol Biochem 2010, 74(10):2148–2150.
15. Kimura M, Kimura Y, Tsumura K, Okihara K, Sugimoto H, Yamada H, Yonekura M: 350-kDa royal jelly glycoprotein (Apisin), which stimulates proliferation of human monocytes, bears the 1-3galactosylated N-glycan: analysis of the N-glycosylation site. Biosci Biotechnol Biochem 2003, 67(9):2055–2058.
16. Bilikova K, Mirgorodskaya E, Bukovska G, Gobom J, Lehrach H, Simuth J: Towards functional proteomics of minority component of honeybee royal jelly: the effect of post-translational modifications on the antimicrobial activity of apalbumin2. Proteomics 2009, 9(8):2131–2138.
17. Li JK, Wang T, Zhang ZH, Pan YH: Proteomic analysis of royal jelly from three strains of western honeybees (Apis mellifera). J Agric Food Chem 2007, 55(21):8411–8422.
18. Apweiler R, Hermjakob H, Sharon N: On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1999, 1473:4–8.
19. Spiro RG: Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 2002, 12(4):43R–56R.
20. Walsh TC: Posttranslational modification of proteins. Greenwood Village, Colorado 80111 USA: Roberts and Company Publishers; 2006.
21. Lis H, Sharon N: Protein glycosylation. Eur J Biochem 1993, 218(1):1–27.
22. Baas S, Sharrow M, Kotu V, Middleton M, Nguyen K, Flanagan-Steet H, Aoki
K, Tiemeyer M: Sugar-free frosting, a homolog of SAD kinase, drives neural-specific glycan expression in the Drosophila embryo. Development 2011, 138(3):553–563.
23. Rudd PM, Elliott T, Cresswell P, Wilson IA, Dwek RA: Glycosylation and the immune system. Science 2001, 291:5512–2370.
24. Zielinska DF, Gnad FW, Mann M: Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints.Cell 2010, 141(5):897–907.
25. Zhang H, Yi EC, Li XJ, Mallick P, Kelly-Spratt KS, Masselon CD, Camp DG 2nd,Smith RD, Kemp CJ, Aebersold R: High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry. Mol Cell Proteomics 2005, 4(2):144–155.
26. Bause E: Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochemical Journal 1983, 209(2):331.
27. Küster B, Mann M: 18O-Labeling of N-Glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching. Anal Chem 1999, 71(7):1431–1440.
28. Furusawa T, Rakwal R, Nam HW, Shibato J, Agrawal GK, Kim YS, Ogawa Y, Yoshida Y, Kouzuma Y, Masuo Y, Yonekura M: Comprehensive royal jelly (RJ) proteomics using one- and two-dimensional proteomics platforms reveals novel RJ proteins and potential phospho/glycoproteins. J Proteome Res 2008, 7(8):3194–3229.
29. Schonleben S, Sickmann A, Mueller MJ, Reinders J: Proteome analysis of Apis mellifera royal jelly. Anal Bioanal Chem 2007, 389(4):1087–1093.
30. Horton P, Park KJ, Obayashi T, Fujita N, Harade H, Adams-Collier CJ, Nakai K: WoLF PSORT: protein localization predictor. Nucleic Acids Res 2007,35:w585–w587.
31. Petersen TN, Brunak S, Von HG, Nielsen H: SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 2011, 8(10):785–786.
32. Wang DI: Growth rates of young queen and worker honeybee larvae.J Apic Res 1965, 4(1):3–5.
33. Albert S, Bhattacharya D, Klaudiny J, Schmitzov J, Simth J: The family of major royal jelly proteins and its evolution. J Mol Evol 1999, 49(2):290–297.
34. Drapeau MD, Albert S, Kucharski R, Prusko C, Maleszka R: Evolution of the yellow/major royal jelly protein family and the emergence of social behavior in honey bees. Genome Res 2006, 16(11):1385–1394.
35. Garcia L, Saraiva Garcia CH, Calabria LK, Costa Nunes da Cruz G, Sanchez Puentes A, Bao SN, Fontes W, Ricart CA, Salmen Espindola F, Valle de Sousa M: Proteomic analysis of honey bee brain upon ontogenetic and behavioral development. J Proteome Res 2009, 8(3):1464–1473.
36. Koop H: Serum levels of pancreatic enzymes and their clinical significance. Clin Gastroenterol 1984, 13(3):739–761.
37. Sherwood RF, Melton RG, Alwan SM, Hughes P: Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Use of a novel triazine dye affinity method. Eur J Biochem 1985, 148(3):447–453.
38. Boldbaatar D, Sikalizyo Sikasunge C, Battsetseg B, Xuan X, Fujisaki K: Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis. Insect Biochem Molec 2006, 36(1):25–36.
39. Kikkawa F, Kajiyama H, Shibata K, Ino K, Nomura S, Mizutani S: Dipeptidyl peptidase IV in tumor progression. BBA-Proteins Proteom 2005, 1751:45–51.
40. Wesley UVMM, Homoyouni A: Dipeptidyl peptidase inhibits malignant phenotype of prostate cancer cells by blocking basic fibroblast growth factor signaling pathway. Cancer Res 2005, 65:1325–1334.