Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
NKTR
Introduction
NK-tumor recognition protein is a protein that in humans is encoded by the NKTR gene.[1][2][3]
This gene encodes a membrane-anchored protein with a hydrophobic amino terminal domain and a cyclophilin-like PPIase domain. It is present on the surface of natural killer cells and facilitates their binding to targets. Its expression is regulated by IL2 activation of the cells.[3]
References
References
- ↑ Young HA, Jenkins NA, Copeland NG, Simek S, Lerman MI, Zbar B, Glenn G, Ortaldo JR, Anderson SK (Jul 1993). “Localization of a novel natural killer triggering receptor locus to human chromosome 3p23-p21 and mouse chromosome 9”. Genomics. 16 (2): 548–549. doi:10.1006/geno.1993.1229. PMID 8314596.
- ↑ Chambers CA, Gallinger S, Anderson SK, Giardina S, Ortaldo JR, Hozumi N, Roder J (May 1994). “Expression of the NK-TR gene is required for NK-like activity in human T cells”. J Immunol. 152 (6): 2669–74. PMID 8144875.
- ↑ 3.0 3.1 “Entrez Gene: NKTR natural killer-tumor recognition sequence”.
Further reading
Further reading
- Frey JL, Bino T, Kantor RR, et al. (1992). “Mechanism of target cell recognition by natural killer cells: characterization of a novel triggering molecule restricted to CD3- large granular lymphocytes”. J. Exp. Med. 174 (6): 1527–1536. doi:10.1084/jem.174.6.1527. PMC 2119033. PMID 1720812.
- Rinfret A, Anderson SK (1993). “IL-2 regulates the expression of the NK-TR gene via an alternate RNA splicing mechanism”. Mol. Immunol. 30 (14): 1307–1313. doi:10.1016/0161-5890(93)90047-F. PMID 8413330.
- Anderson SK, Gallinger S, Roder J, et al. (1993). “A cyclophilin-related protein involved in the function of natural killer cells”. Proc. Natl. Acad. Sci. U.S.A. 90 (2): 542–546. doi:10.1073/pnas.90.2.542. PMC 45699. PMID 8421688.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.
- Sakashita E, Tatsumi S, Werner D, et al. (2004). “Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo”. Mol. Cell. Biol. 24 (3): 1174–1187. doi:10.1128/MCB.24.3.1174-1187.2004. PMC 321435. PMID 14729963.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Davis TL, Walker JR, Campagna-Slater V, et al. (2010). “Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases”. PLoS Biol. 8 (7): e1000439. doi:10.1371/journal.pbio.1000439. PMCÂ 2911226. PMIDÂ 20676357.