Publications
Found 2 results
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“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
“Molecular cloning, expression and variation analyses of the dopamine D2 receptor gene in pig breeds in China”, vol. 10, pp. 3371-3384, 2011.
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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. A. 99: 14554- 14559.
http://dx.doi.org/10.1073/pnas.202498299
PMid:12391323 PMCid:137921
Jungerius BJ, Gu J, Crooijmans RP, van der Poel JJ, et al. (2005). Estimation of the extent of linkage disequilibrium in seven regions of the porcine genome. Anim. Biotechnol. 16: 41-54.
http://dx.doi.org/10.1081/ABIO-200053402
PMid:15926262
Kalani MY, Vaidehi N, Hall SE, Trabanino RJ, et al. (2004). The predicted 3D structure of the human D2 dopamine receptor and the binding site and binding affinities for agonists and antagonists. Proc. Natl. Acad. Sci. U. S. A. 101: 3815-3820.
http://dx.doi.org/10.1073/pnas.0400100101
PMid:14999101 PMCid:374327
Korchounov A, Meyer MF and Krasnianski M (2010). Postsynaptic nigrostriatal dopamine receptors and their role in movement regulation. J. Neural. Transm. 117: 1359-1369.
http://dx.doi.org/10.1007/s00702-010-0454-z
PMid:21076988 PMCid:3000910
Kruger J and Rehmsmeier M (2006). RNAhybrid: microRNA target prediction easy, fast and flexible. 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. Gene 257: 99-107.
http://dx.doi.org/10.1016/S0378-1119(00)00384-X
Nakano M, Hasunuma I, Okada R, Yamamoto K, et al. (2010). Molecular cloning of bullfrog D2 dopamine receptor cDNA: Tissue distribution of three isoforms of D2 dopamine receptor mRNA. Gen. Comp. Endocrinol. 168: 143- 148.
http://dx.doi.org/10.1016/j.ygcen.2010.04.016
PMid:20417207
Neve KA, Neve RL, Fidel S, Janowsky A, et al. (1991). Increased abundance of alternatively spliced forms of D2 dopamine receptor mRNA after denervation. Proc. Natl. Acad. Sci. U. S. A. 88: 2802-2806.
http://dx.doi.org/10.1073/pnas.88.7.2802
PMid:1826366 PMCid:51327
O'Malley KL, Mack KJ, Gandelman KY and Todd RD (1990). Organization and expression of the rat D2A receptor gene: identification of alternative transcripts and a variant donor splice site. Biochemistry 29: 1367-1371.
http://dx.doi.org/10.1021/bi00458a003
PMid:2139794
Obadiah J, Avidor-Reiss T, Fishburn CS, Carmon S, et al. (1999). 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. Reprod. 80: 753-761.
http://dx.doi.org/10.1095/biolreprod.108.070961
PMid:19074002
Sasabe T and Ishiura S (2010). Alcoholism and alternative splicing of candidate genes. Int. J. Environ. Res. Public Health 7: 1448-1466.
http://dx.doi.org/10.3390/ijerph7041448
PMid:20617039 PMCid:2872348
Schnell SA, You S, Foster DN and El Halawani ME (1999). Molecular cloning and tissue distribution of an avian D2 dopamine receptor mRNA from the domestic turkey (Maleagris gallopavo). J. Comp. Neurol. 407: 543-554.
http://dx.doi.org/10.1002/(SICI)1096-9861(19990517)407:4<543::AID-CNE6>3.0.CO;2-O
Seeman P, Nam D, Ulpian C, Liu IS, et al. (2000). New dopamine receptor, D2(Longer), with unique TG splice site, in human brain. Brain Res. Mol. Brain Res. 76: 132-141.
http://dx.doi.org/10.1016/S0169-328X(99)00343-5
Senogles SE, Heimert TL, Odife ER and Quasney MW (2004). A region of the third intracellular loop of the short form of the D2 dopamine receptor dictates Gi coupling specificity. J. Biol. Chem. 279: 1601-1606.
http://dx.doi.org/10.1074/jbc.M309792200
PMid:14581469
Shi L and Javitch JA (2002). The binding site of aminergic G protein-coupled receptors: the transmembrane segments and second extracellular loop. Annu. Rev. Pharmacol. Toxicol. 42: 437-467.
http://dx.doi.org/10.1146/annurev.pharmtox.42.091101.144224
PMid:11807179
Taylor TD, Noguchi H, Totoki Y, Toyoda A, et al. (2006). Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature 440: 497-500.
http://dx.doi.org/10.1038/nature04632
PMid:16554811
Usiello A, Baik JH, Rougé-Pont F, Picetti R, et al. (2000). Distinct functions of the two isoforms of dopamine D2 receptors. Nature 408: 199-203.
http://dx.doi.org/10.1038/35041572
PMid:11089973
Wiedmann RT, Smith TP and Nonneman DJ (2008). SNP discovery in swine by reduced representation and high throughput pyrosequencing. BMC Genet. 9: 81.
http://dx.doi.org/10.1186/1471-2156-9-81
PMid:19055830 PMCid:2612698
Zhang Y, Bertolino A, Fazio L, Blasi G, et al. (2007). Polymorphisms in human dopamine D2 receptor gene affect gene expression, splicing, and neuronal activity during working memory. Proc. Natl. Acad. Sci. U. S. A. 104: 20552- 20557.
http://dx.doi.org/10.1073/pnas.0707106104
PMid:18077373 PMCid:2154469
Zimin AV, Delcher AL, Florea L, Kelley DR, et al. (2009). A whole-genome assembly of the domestic cow, Bos taurus. Genome Biol. 10: R42.
http://dx.doi.org/10.1186/gb-2009-10-4-r42
PMid:19393038 PMCid:2688933