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2013
X. M. He, Fang, M. X., Zhang, Z. T., Hu, Y. S., Jia, X. Z., He, D. L., Liang, S. D., Nie, Q. H., and Zhang, X. Q., Characterization of chicken natural resistance-associated macrophage protein encoding genes (Nramp1 and Nramp2) and association with salmonellosis resistance, vol. 12, pp. 618-630, 2013.
Ates O, Dalyan L, Musellim B, Hatemi G, et al. (2009). NRAMP1 (SLC11A1) gene polymorphisms that correlate with autoimmune versus infectious disease susceptibility in tuberculosis and rheumatoid arthritis. Int. J. Immunogenet. 36: 15-19. http://dx.doi.org/10.1111/j.1744-313X.2008.00814.x PMid:19055603   Baker ST, Barton CH and Biggs TE (2000). A negative autoregulatory link between Nramp1 function and expression. J. Leukoc. Biol. 67: 501-507. PMid:10770282   Barshes NR, Lee TR, Goss JA, Goodpastor SE, et al. (2006). Slc11a1 (formerly Nramp1) polymorphisms and susceptibility to post-transplant lymphoproliferative disease following pediatric liver transplantation. Transpl. Infect. Dis. 8: 108-112. http://dx.doi.org/10.1111/j.1399-3062.2006.00139.x PMid:16734634   Blackwell JM and Searle S (1999). Genetic regulation of macrophage activation: understanding the function of Nramp1 (=Ity/Lsh/Bcg). Immunol. Lett. 65: 73-80. http://dx.doi.org/10.1016/S0165-2478(98)00127-8   Blackwell JM, Searle S, Goswami T and Miller EN (2000). Understanding the multiple functions of Nramp1. Microbes. Infect. 2: 317-321. http://dx.doi.org/10.1016/S1286-4579(00)00295-1   Blackwell JM, Searle S, Mohamed H and White JK (2003). Divalent cation transport and susceptibility to infectious and autoimmune disease: continuation of the Ity/Lsh/Bcg/Nramp1/Slc11a1 gene story. Immunol. Lett. 85: 197-203. http://dx.doi.org/10.1016/S0165-2478(02)00231-6   Blasco H, Vourc'h P, Nadjar Y, Ribourtout B, et al. (2011). Association between divalent metal transport 1 encoding gene (SLC11A2) and disease duration in amyotrophic lateral sclerosis. J. Neurol. Sci. 303: 124-127. http://dx.doi.org/10.1016/j.jns.2010.12.018 PMid:21276595   Boyer E, Bergevin I, Malo D, Gros P, et al. (2002). Acquisition of Mn(II) in addition to Fe(II) is required for full virulence of Salmonella enterica serovar Typhimurium. Infect. Immun. 70: 6032-6042. http://dx.doi.org/10.1128/IAI.70.11.6032-6042.2002 PMid:12379679 PMCid:130432   Canonne-Hergaux F, Gruenheid S, Ponka P and Gros P (1999). Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood 93: 4406-4417. PMid:10361139   Canonne-Hergaux F, Calafat J, Richer E, Cellier M, et al. (2002). Expression and subcellular localization of NRAMP1 in human neutrophil granules. Blood 100: 268-275. http://dx.doi.org/10.1182/blood.V100.1.268 PMid:12070036   Cellier MF, Courville P and Campion C (2007). Nramp1 phagocyte intracellular metal withdrawal defense. Microbes. Infect. 9: 1662-1670. http://dx.doi.org/10.1016/j.micinf.2007.09.006 PMid:18024118   Cohen A, Nevo Y and Nelson N (2003). The first external loop of the metal ion transporter DCT1 is involved in metal ion binding and specificity. Proc. Natl. Acad. Sci. U. S. A. 100: 10694-10699. http://dx.doi.org/10.1073/pnas.1934572100 PMid:12954986 PMCid:196866   Courville P, Chaloupka R and Cellier MF (2006). Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters. Biochem. Cell Biol. 84: 960-978. http://dx.doi.org/10.1139/o06-193 PMid:17215883   Ganguly I, Sharma A, Singh R, Deb SM, et al. (2008). Association of microsatellite (GT)n polymorphism at 3'UTR of NRAMP1 with the macrophage function following challenge with Brucella LPS in buffalo (Bubalus bubalis). Vet. Microbiol. 129: 188-196. http://dx.doi.org/10.1016/j.vetmic.2007.10.033 PMid:18078724   Gazouli M, Atsaves V, Mantzaris G, Economou M, et al. (2008). Role of functional polymorphisms of NRAMP1 gene for the development of Crohn's disease. Inflamm. Bowel. Dis. 14: 1323-1330. http://dx.doi.org/10.1002/ibd.20488 PMid:18454481   Gruenheid S, Cellier M, Vidal S and Gros P (1995). Identification and characterization of a second mouse Nramp gene. Genomics 25: 514-525. http://dx.doi.org/10.1016/0888-7543(95)80053-O   Gruenheid S, Canonne-Hergaux F, Gauthier S, Hackam DJ, et al. (1999). The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes. J. Exp. Med. 189: 831-841. http://dx.doi.org/10.1084/jem.189.5.831 PMid:10049947 PMCid:2192949   Gunshin H, Mackenzie B, Berger UV, Gunshin Y, et al. (1997). Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388: 482-488. http://dx.doi.org/10.1038/41343 PMid:9242408   Hu J, Bumstead N, Skamene E, Gros P, et al. (1996). Structural organization, sequence, and expression of the chicken NRAMP1 gene encoding the natural resistance-associated macrophage protein 1. DNA Cell Biol. 15: 113-123. http://dx.doi.org/10.1089/dna.1996.15.113 PMid:8634139   Hu J, Bumstead N, Barrow P, Sebastiani G, et al. (1997). Resistance to salmonellosis in the chicken is linked to NRAMP1 and TNC. Genome Res. 7: 693-704. PMid:9253598   Jabado N, Jankowski A, Dougaparsad S, Picard V, et al. (2000). Natural resistance to intracellular infections: natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane. J. Exp. Med. 192: 1237-1248. http://dx.doi.org/10.1084/jem.192.9.1237 PMid:11067873 PMCid:2193348   Jabado N, Cuellar-Mata P, Grinstein S and Gros P (2003). Iron chelators modulate the fusogenic properties of Salmonella-containing phagosomes. Proc. Natl. Acad. Sci. U. S. A. 100: 6127-6132. http://dx.doi.org/10.1073/pnas.0937287100 PMid:12711734 PMCid:156337   Kishi F, Yoshida T and Aiso S (1996). Location of NRAMP1 molecule on the plasma membrane and its association with microtubules. Mol. Immunol. 33: 1241-1246. http://dx.doi.org/10.1016/S0161-5890(96)00088-0   Lam-Yuk-Tseung S, Govoni G, Forbes J and Gros P (2003). Iron transport by Nramp2/DMT1: pH regulation of transport by 2 histidines in transmembrane domain 6. Blood 101: 3699-3707. http://dx.doi.org/10.1182/blood-2002-07-2108 PMid:12522007   Lam-Yuk-Tseung S, Camaschella C, Iolascon A and Gros P (2006). A novel R416C mutation in human DMT1 (SLC11A2) displays pleiotropic effects on function and causes microcytic anemia and hepatic iron overload. Blood Cells Mol. Dis. 36: 347-354. http://dx.doi.org/10.1016/j.bcmd.2006.01.011 PMid:16584902   Leung KH, Yip SP, Wong WS, Yiu LS, et al. (2007). Sex- and age-dependent association of SLC11A1 polymorphisms with tuberculosis in Chinese: a case control study. BMC Infect. Dis. 7: 19. http://dx.doi.org/10.1186/1471-2334-7-19 PMid:17371589 PMCid:1847518   Liu W, Kaiser MG and Lamont SJ (2003). Natural resistance-associated macrophage protein 1 gene polymorphisms and response to vaccine against or challenge with Salmonella enteritidis in young chicks. Poult. Sci. 82: 259-266. PMid:12619803   Mackenzie B and Hediger MA (2004). SLC11 family of H+-coupled metal-ion transporters NRAMP1 and DMT1. Pflugers Arch. 447: 571-579. http://dx.doi.org/10.1007/s00424-003-1141-9 PMid:14530973   Mackenzie B, Ujwal ML, Chang MH, Romero MF, et al. (2006). Divalent metal-ion transporter DMT1 mediates both H+ -coupled Fe2+ transport and uncoupled fluxes. Pflugers Arch. 451: 544-558. http://dx.doi.org/10.1007/s00424-005-1494-3 PMid:16091957   Peracino B, Wagner C, Balest A, Balbo A, et al. (2006). Function and mechanism of action of Dictyostelium Nramp1 (Slc11a1) in bacterial infection. Traffic 7: 22-38. http://dx.doi.org/10.1111/j.1600-0854.2005.00356.x PMid:16445684   Rose PP, Hanna SL, Spiridigliozzi A, Wannissorn N, et al. (2011). Natural resistance-associated macrophage protein is a cellular receptor for sindbis virus in both insect and mammalian hosts. Cell Host Microbe 10: 97-104. http://dx.doi.org/10.1016/j.chom.2011.06.009 PMid:21843867 PMCid:3164510   Stiles KM and Kielian M (2011). Alphavirus entry: NRAMP leads the way. Cell Host Microbe 10: 92-93. http://dx.doi.org/10.1016/j.chom.2011.07.008 PMid:21843864 PMCid:3163168   Tandy S, Williams M, Leggett A, Lopez-Jimenez M, et al. (2000). Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells. J. Biol. Chem. 275: 1023-1029. http://dx.doi.org/10.1074/jbc.275.2.1023 PMid:10625641   Touret N, Furuya W, Forbes J, Gros P, et al. (2003). Dynamic traffic through the recycling compartment couples the metal transporter Nramp2 (DMT1) with the transferrin receptor. J. Biol. Chem. 278: 25548-25557. http://dx.doi.org/10.1074/jbc.M212374200 PMid:12724326   Trinder D, Macey DJ and Olynyk JK (2000). The new iron age. Int. J. Mol. Med. 6: 607-612. PMid:11078817
2011
H. P. Xu, He, X. M., Fang, M. X., Hu, Y. S., Jia, X. Z., Nie, Q. H., and Zhang, X. Q., Molecular cloning, expression and variation analyses of the dopamine D2 receptor gene in pig breeds in China, vol. 10, pp. 3371-3384, 2011.
Baskerville TA and Douglas AJ (2010). Dopamine and oxytocin interactions underlying behaviors: potential contributions to behavioral disorders. CNS Neurosci. Ther. 16: e92-123. http://dx.doi.org/10.1111/j.1755-5949.2010.00154.x PMid:20557568   Blasi G, Lo Bianco L, Taurisano P, Gelao B, et al. (2009). Functional variation of the dopamine D2 receptor gene is associated with emotional control as well as brain activity and connectivity during emotion processing in humans. J. Neurosci. 29: 14812-14819. http://dx.doi.org/10.1523/JNEUROSCI.3609-09.2009 PMid:19940176 PMCid:2834475   Bunzow JR, Van Tol HH, Grandy DK, Albert P, et al. (1988). Cloning and expression of a rat D2 dopamine receptor cDNA. Nature 336: 783-787. http://dx.doi.org/10.1038/336783a0 PMid:2974511   Dal Toso R, Sommer B, Ewert M, Herb A, et al. (1989). The dopamine D2 receptor: two molecular forms generated by alternative splicing. EMBO J. 8: 4025-4034. PMid:2531656 PMCid:401577   Duan J, Wainwright MS, Comeron JM, Saitou N, et al. (2003). Synonymous mutations in the human dopamine receptor D2 (DRD2) affect mRNA stability and synthesis of the receptor. Hum. Mol. Genet. 12: 205-216. http://dx.doi.org/10.1093/hmg/ddg055 PMid:12554675   Grandy DK, Marchionni MA, Makam H, Stofko RE, et al. (1989). Cloning of the cDNA and gene for a human D2 dopamine receptor. Proc. Natl. Acad. Sci. U. S. A. 86: 9762-9766. http://dx.doi.org/10.1073/pnas.86.24.9762 PMid:2532362 PMCid:298581   Guiramand J, Montmayeur JP, Ceraline J, Bhatia M, et al. (1995). Alternative splicing of the dopamine D2 receptor directs specificity of coupling to G-proteins. J. Biol. Chem. 270: 7354-7358. http://dx.doi.org/10.1074/jbc.270.13.7354 PMid:7706278   Hearn MG, Ren Y, McBride EW, Reveillaud I, et al. (2002). A Drosophila dopamine 2-like receptor: Molecular characterization and identification of multiple alternatively spliced variants. Proc. Natl. Acad. Sci. U. S. 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Nucleic Acids Res. 34: W451-W454. http://dx.doi.org/10.1093/nar/gkl243 PMid:16845047 PMCid:1538877   Levavi-Sivan B, Aizen J and Avitan A (2005). Cloning, characterization and expression of the D2 dopamine receptor from the tilapia pituitary. Mol. Cell Endocrinol. 236: 17-30. http://dx.doi.org/10.1016/j.mce.2005.03.010 PMid:15876479   Lindgren N, Usiello A, Goiny M, Haycock J, et al. (2003). Distinct roles of dopamine D2L and D2S receptor isoforms in the regulation of protein phosphorylation at presynaptic and postsynaptic sites. Proc. Natl. Acad. Sci. U. S. A. 100: 4305-4309. http://dx.doi.org/10.1073/pnas.0730708100 PMid:12651945 PMCid:153088   Livak KJ and Schmittgen TD (2001). Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCt method. Methods 25: 402-408. http://dx.doi.org/10.1006/meth.2001.1262 PMid:11846609   Mack KJ, Todd RD and O'Malley KL (1991). The mouse dopamine D2A receptor gene: sequence homology with the rat and human genes and expression of alternative transcripts. J. Neurochem. 57: 795-801. http://dx.doi.org/10.1111/j.1471-4159.1991.tb08221.x PMid:1861151   Missale C, Nash SR, Robinson SW, Jaber M, et al. (1998). Dopamine receptors: from structure to function. Physiol. Rev. 78: 189-225. PMid:9457173   Montmayeur JP, Bausero P, Amlaiky N, Maroteaux L, et al. (1991). Differential expression of the mouse D2 dopamine receptor isoforms. FEBS Lett. 278: 239-243. http://dx.doi.org/10.1016/0014-5793(91)80125-M   Moyer RA, Wang D, Papp AC, Smith RM, et al. (2011). Intronic polymorphisms affecting alternative splicing of human dopamine D2 receptor are associated with cocaine abuse. Neuropsychopharmacology 36: 753-762. http://dx.doi.org/10.1038/npp.2010.208 PMid:21150907 PMCid:3055737   Myeong H, Jeoung D, Kim H, Ha JH, et al. (2000). Genomic analysis and functional expression of canine dopamine D2 receptor. 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Adenylyl cyclase interaction with the D2 dopamine receptor family; differential coupling to Gi, Gz, and Gs. Cell Mol. Neurobiol. 19: 653-664. http://dx.doi.org/10.1023/A:1006988603199 PMid:10384262   Pasqualini C, Weltzien FA, Vidal B, Baloche S, et al. (2009). Two distinct dopamine D2 receptor genes in the European eel: molecular characterization, tissue-specific transcription, and regulation by sex steroids. Endocrinology 150: 1377-1392. http://dx.doi.org/10.1210/en.2008-0578 PMid:18974275   Pivonello R, Ferone D, Lombardi G, Colao A, et al. (2007). Novel insights in dopamine receptor physiology. Eur. J. Endocrinol. 156 (Suppl 1): S13-S21. http://dx.doi.org/10.1530/eje.1.02353 PMid:17413183   Ramírez AR, Castro MA, Angulo C, Ramió L, et al. (2009). The presence and function of dopamine type 2 receptors in boar sperm: a possible role for dopamine in viability, capacitation, and modulation of sperm motility. Biol. 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