Neutral amino acid transporter B(0) is a protein that in humans is encoded by the SLC1A5 gene.[5][6][7]
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- Tailor CS, Nouri A, Zhao Y, Takeuchi Y, Kabat D (May 1999). "A sodium-dependent neutral-amino-acid transporter mediates infections of feline and baboon endogenous retroviruses and simian type D retroviruses". Journal of Virology. 73 (5): 4470–4. doi:10.1128/JVI.73.5.4470-4474.1999. PMC 104338. PMID 10196349.
- Tailor CS, Marin M, Nouri A, Kavanaugh MP, Kabat D (July 2001). "Truncated forms of the dual function human ASCT2 neutral amino acid transporter/retroviral receptor are translationally initiated at multiple alternative CUG and GUG codons". The Journal of Biological Chemistry. 276 (29): 27221–30. doi:10.1074/jbc.M100737200. PMID 11350958.
- Lavillette D, Marin M, Ruggieri A, Mallet F, Cosset FL, Kabat D (July 2002). "The envelope glycoprotein of human endogenous retrovirus type W uses a divergent family of amino acid transporters/cell surface receptors". Journal of Virology. 76 (13): 6442–52. doi:10.1128/JVI.76.13.6442-6452.2002. PMC 136247. PMID 12050356.
- Kudo Y, Boyd CA (August 2002). "Changes in expression and function of syncytin and its receptor, amino acid transport system B(0) (ASCT2), in human placental choriocarcinoma BeWo cells during syncytialization". Placenta. 23 (7): 536–41. doi:10.1053/plac.2002.0839. PMID 12175968.
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Potter SJ, Lu A, Wilcken B, Green K, Rasko JE (October 2002). "Hartnup disorder: polymorphisms identified in the neutral amino acid transporter SLC1A5". Journal of Inherited Metabolic Disease. 25 (6): 437–48. doi:10.1023/A:1021286714582. PMID 12555937. S2CID 21082701.
- Marin M, Lavillette D, Kelly SM, Kabat D (March 2003). "N-linked glycosylation and sequence changes in a critical negative control region of the ASCT1 and ASCT2 neutral amino acid transporters determine their retroviral receptor functions". Journal of Virology. 77 (5): 2936–45. doi:10.1128/JVI.77.5.2936-2945.2003. PMC 149750. PMID 12584318.
- Kudo Y, Boyd CA, Sargent IL, Redman CW (May 2003). "Hypoxia alters expression and function of syncytin and its receptor during trophoblast cell fusion of human placental BeWo cells: implications for impaired trophoblast syncytialisation in pre-eclampsia". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1638 (1): 63–71. doi:10.1016/s0925-4439(03)00043-7. PMID 12757936.
- Knerr I, Weigel C, Linnemann K, Dötsch J, Meissner U, Fusch C, Rascher W (August 2003). "Transcriptional effects of hypoxia on fusiogenic syncytin and its receptor ASCT2 in human cytotrophoblast BeWo cells and in ex vivo perfused placental cotyledons". American Journal of Obstetrics and Gynecology. 189 (2): 583–8. doi:10.1067/S0002-9378(03)00538-6. PMID 14520239.
- Palmada M, Speil A, Jeyaraj S, Böhmer C, Lang F (May 2005). "The serine/threonine kinases SGK1, 3 and PKB stimulate the amino acid transporter ASCT2". Biochemical and Biophysical Research Communications. 331 (1): 272–7. doi:10.1016/j.bbrc.2005.03.159. PMID 15845389.
- Uchiyama T, Matsuda Y, Wada M, Takahashi S, Fujita T (April 2005). "Functional regulation of Na+-dependent neutral amino acid transporter ASCT2 by S-nitrosothiols and nitric oxide in Caco-2 cells". FEBS Letters. 579 (11): 2499–506. doi:10.1016/j.febslet.2005.03.065. PMID 15848195. S2CID 23438613.
- Bungard CI, McGivan JD (November 2005). "Identification of the promoter elements involved in the stimulation of ASCT2 expression by glutamine availability in HepG2 cells and the probable involvement of FXR/RXR dimers". Archives of Biochemistry and Biophysics. 443 (1–2): 53–9. doi:10.1016/j.abb.2005.08.016. PMID 16197915.
- Brauers E, Vester U, Zerres K, Eggermann T (2006). "Search for mutations in SLC1A5 (19q13) in cystinuria patients". Journal of Inherited Metabolic Disease. 28 (6): 1169–71. doi:10.1007/s10545-005-0094-x. PMID 16435221. S2CID 29372429.
- Gegelashvili M, Rodriguez-Kern A, Pirozhkova I, Zhang J, Sung L, Gegelashvili G (2006). "High-affinity glutamate transporter GLAST/EAAT1 regulates cell surface expression of glutamine/neutral amino acid transporter ASCT2 in human fetal astrocytes". Neurochemistry International. 48 (6–7): 611–5. doi:10.1016/j.neuint.2005.12.033. PMID 16516348. S2CID 20686585.
- Cheynet V, Oriol G, Mallet F (July 2006). "Identification of the hASCT2-binding domain of the Env ERVWE1/syncytin-1 fusogenic glycoprotein". Retrovirology. 3: 41. doi:10.1186/1742-4690-3-41. PMC 1524976. PMID 16820059.
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF (November 2006). "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes". Journal of Proteome Research. 5 (11): 3135–44. doi:10.1021/pr060363j. PMID 17081065.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.