The DOI matches its Crossref record; 74 of the 78 references it cites were found in a registry or an index.
NKG2D Receptor and Its Ligands in Host Defense
Open accessAbstract
NKG2D is an activating receptor expressed on the surface of natural killer (NK) cells, CD8+ T cells, and subsets of CD4+ T cells, invariant NKT cells (iNKT), and γδ T cells. In humans, NKG2D transmits signals by its association with the DAP10 adapter subunit, and in mice alternatively spliced isoforms transmit signals either using DAP10 or DAP12 adapter subunits. Although NKG2D is encoded by a highly conserved gene (KLRK1) with limited polymorphism, the receptor recognizes an extensive repertoire of ligands, encoded by at least eight genes in humans (MICA, MICB, RAET1E, RAET1G, RAET1H, RAET1I, RAET1L, and RAET1N), some with extensive allelic polymorphism. Expression of the NKG2D ligands is tightly regulated at the level of transcription, translation, and posttranslation. In general, healthy adult tissues do not express NKG2D glycoproteins on the cell surface, but these ligands can be induced by hyperproliferation and transformation, as well as when cells are infected by pathogens. Thus, the NKG2D pathway serves as a mechanism for the immune system to detect and eliminate cells that have undergone “stress.” Viruses and tumor cells have devised numerous strategies to evade detection by the NKG2D surveillance system, and diversification of the NKG2D ligand genes likely has been driven by selective pressures imposed by pathogens. NKG2D provides an attractive target for therapeutics in the treatment of infectious diseases, cancer, and autoimmune diseases. Cancer Immunol Res; 3(6); 575–82. ©2015 AACR.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Remarkably, the candidate signature gene RAET1G is one of the few genes that could encode a ligand recognized by NKG2D proteins in response to stress and infections (Eagle and Trowsdale, 2007; Tomasec et al., 2007; Lanier, 2015).”
From Identification of Candidate Signature Genes and Key Regulators Associated With Trypanotolerance in the Sheko Breed (2019) · cites this paper as Lanier, 2015
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Activation of NK cells and T cells by NKG2D, a receptor for stress-inducible MICA.
Bauer, S., Groh, V., Wu, J., Steinle, A., Phillips, J., Lanier, L., & Spies, T. (1999) · Science · doi:10.1126/science.285.5428.727 · Cited by 3,272 · cited 2×
“Although NKG2D is expressed constitutively on essentially all resting human NK cells and CD8þ T cells (14), engagement of NKG2D alone is insufficient to trigger cell-mediated cytotoxicity or cytokine production (12, 40), although the simultaneous engagement of NKG2D and other "costimulatory" receptors, such as CD335 (…”
BackgroundSelf-citationTumour-derived soluble MIC ligands impair expression of NKG2D and T-cell activation
Groh, V., Wu, J. D., Yee, C., & Spies, T. (2002) · Nature · doi:10.1038/nature01112 · Cited by 1,674 · cited 1×
“These include systemic release of NKG2D ligands by tumors in cancer patients (65, 66).”
BackgroundCosman, D., Müllberg, J., Sutherland, C. L., Chin, W. A., Armitage, R., Fanslow, W., Kubin, M., & Chalupny, N. (2001) · Immunity · doi:10.1016/s1074-7613(01)00095-4 · Cited by 1,394 · cited 11×
“MICA, MICB, RAET1E (ULBP4), and RAET1G (ULBP5) are transmembrane-anchored glycoproteins, whereas RAET1I (ULBP1), RAET1H (ULBP2), RAET1N (ULBP3), and RAET1L (ULBP6) are glycophosphatidylinositol (GPI)-anchored, although RAET1H (ULBP2) may be expressed in both transmembraneanchored and GPI-anchored forms (28), and RAET1…”
BackgroundInfluentialThe DNA damage pathway regulates innate immune system ligands of the NKG2D receptor
Gasser, S., Orsulic, S., Brown, E. J., & Raulet, D. H. (2005) · Nature · doi:10.1038/nature03884 · Cited by 1,308 · cited 1×
“In some cases, ligands may be induced due to the genomic instability of the transformed cells, resulting in activation of the ATM and ATR DNA repair pathways (61).”
BackgroundAn activating immunoreceptor complex formed by NKG2D and DAP10.
Wu, J., Song, Y., Bakker, A. B., Bauer, S., Spies, T., Lanier, L., & Phillips, J. (1999) · Science · doi:10.1126/science.285.5428.730 · Cited by 1,168 · cited 6×
“org Cancer Immunol Res; 3(6) June 2015 579”
BackgroundInfluentialSelf-citationRae1 and H60 ligands of the NKG2D receptor stimulate tumour immunity
Diefenbach, A., Jensen, E. R., Jamieson, A. M., & Raulet, D. H. (2001) · Nature · doi:10.1038/35093109 · Cited by 1,083 · cited 1×
“Studies using transplantable mouse tumors have demonstrated that expression of an NKG2D ligand is sufficient to cause rejection of the tumor (62, 63).”
BackgroundImmunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells
Lanier, L. L., Corliss, B. C., Wu, J., Leong, C. C., & Phillips, J. H. (1998) · Nature · doi:10.1038/35642 · Cited by 907 · cited 1×
“Association of NKG2D with DAP12 versus DAP10 has significant consequences for signal transduction in that DAP12 possesses a canonical immunotyrosine-based activation motif (ITAM), which recruits Syk and ZAP70 tyrosine kinases (7), whereas DAP10 has a YINM motif, which recruits a p85 PI3 kinase and Vav-1 signaling comp…”
BackgroundSelf-citationMeresse, B., Chen, Z., Ciszewski, C., Tretiakova, M., Bhagat, G., Krausz, T., Raulet, D., Lanier, L., Groh, V., Spies, T., et al. (2004) · Immunity · doi:10.1016/j.immuni.2004.06.020 · Cited by 901 · cited 1×
“NKG2D-dependent, TCR-independent cytolytic activity has also been observed in intraepithelial intestinal CD8þ T cells isolated from patients with celiac disease, possibly due to exposure to excess IL15 in the inflamed tissue (43).”
BackgroundSelf-citationBryceson, Y., March, M., Ljunggren, H., & Long, E. O. (2006) · Blood · doi:10.1182/blood-2005-04-1351 · Cited by 885 · cited 1×
“Although NKG2D is expressed constitutively on essentially all resting human NK cells and CD8þ T cells (14), engagement of NKG2D alone is insufficient to trigger cell-mediated cytotoxicity or cytokine production (12, 40), although the simultaneous engagement of NKG2D and other "costimulatory" receptors, such as CD335 (…”
BackgroundDiefenbach, A., Jamieson, A. M., Liu, S. D., Shastri, N., & Raulet, D. H. (2000) · Nature Immunology · doi:10.1038/77793 · Cited by 878
Regulation of Ligands for the NKG2D Activating Receptor
Raulet, D. H., Gasser, S., Gowen, B. G., Deng, W., & Jung, H. (2013) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-095951 · Cited by 877
NKG2D-deficient mice are defective in tumor surveillance in models of spontaneous malignancy
Guerra, N., Tan, Y. X., Joncker, N. T., Choy, A., Gallardo, F., Xiong, N., Knoblaugh, S., Cado, D., Greenberg, N. R., & Raulet, D. H. (2008) · Immunity · doi:10.1016/j.immuni.2008.02.016 · Cited by 850 · cited 2×
“Moreover, in these tumor models, higher amounts of NKG2D ligands were present on tumors arising in NKG2D-deficient mice, suggesting NKG2D-mediated immune editing of the tumors (64).”
BackgroundCerwenka, A., Bakker, A. B., McClanahan, T., Wagner, J., Wu, J., Phillips, J. H., & Lanier, L. (2000) · Immunity · doi:10.1016/s1074-7613(00)80222-8 · Cited by 789
Self-citationCostimulation of CD8αβ T cells by NKG2D via engagement by MIC induced on virus-infected cells
Groh, V., Rhinehart, R., Randolph-Habecker, J., Topp, M., Riddell, S., & Spies, T. (2001) · Nature Immunology · doi:10.1038/85321 · Cited by 725
Host Immune System Gene Targeting by a Viral miRNA
Stern-Ginossar, N., Elefant, N., Zimmermann, A., Wolf, D., Saleh, N., Biton, M., Horwitz, E., Prokocimer, Z., Prichard, M., Hahn, G., et al. (2007) · Science · doi:10.1126/science.1140956 · Cited by 713 · cited 1×
“47, 48), and HCMV microRNA-UL112 targeting MICB transcripts (49).”
BackgroundThe role of the NKG2D immunoreceptor in immune cell activation and natural killing.
Jamieson, A., Diefenbach, A., Mcmahon, C. W., Xiong, N., Carlyle, J., & Raulet, D. (2002) · Immunity · doi:10.1016/s1074-7613(02)00333-3 · Cited by 713 · cited 3×
“Resting mouse NK cells can be activated directly by crosslinking NKG2D ex vivo (11), and mice can reject normal hematopoietic cells that express a Raet1 transgene without prior priming (37), perhaps because mouse, but not human, NKG2D associates with DAP12 in addition to DAP10.”
BackgroundCutting Edge: Down-Regulation of MICA on Human Tumors by Proteolytic Shedding
Salih, H., Rammensee, H., & Steinle, A. (2002) · Journal of Immunology · doi:10.4049/jimmunol.169.8.4098 · Cited by 689
Cerwenka, A., Baron, J. L., & Lanier, L. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.201238598 · Cited by 606
Self-citationDiefenbach, A., Tomasello, E., Lucas, M., Jamieson, A., Hsia, J. K., Vivier, É., & Raulet, D. (2002) · Nature Immunology · doi:10.1038/ni858 · Cited by 507
NKG2D recruits two distinct adapters to trigger NK cell activation and costimulation
Gilfillan, S., Ho, E., Cella, M., Yokoyama, W., & Colonna, M. (2002) · Nature Immunology · doi:10.1038/ni857 · Cited by 500
Lee, J.-C., Lee, K.-M., Kim, D.-W., & Heo, D. (2004) · Journal of Immunology · doi:10.4049/jimmunol.172.12.7335 · Cited by 488
Houchins, J. P., Yabe, T., McSherry, C., & Bach, F. (1991) · Journal of Experimental Medicine · doi:10.1084/jem.173.4.1017 · Cited by 487
Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands
Kaiser, B., Yim, D., Chow, I.-T., González, S., Dai, Z., Mann, H. H., Strong, R., Groh, V., & Spies, T. (2007) · Nature · doi:10.1038/nature05768 · Cited by 403 · cited 1×
“These include systemic release of NKG2D ligands by tumors in cancer patients (65, 66).”
BackgroundRole of NKG2D signaling in the cytotoxicity of activated and expanded CD8+ T cells.
Verneris, M. R., Karami, M., Baker, J., Jayaswal, A., & Negrin, R. (2004) · Blood · doi:10.1182/blood-2003-06-2125 · Cited by 399 · cited 1×
“Similarly, although expressed on all na€ ve human CD8þ T cells, NKG2D fails to costimulate TCR-induced activation of resting CD8þ T cells (12, 19, 41), and only augments TCRdependent activation after the T cells have been activated and cultured for a period of time in vitro (18, 41, 42).”
BackgroundWu, J. D., Higgins, L. M., Steinle, A., Cosman, D., Haugk, K., & Plymate, S. (2004) · Journal of Clinical Investigation · doi:10.1172/jci22206 · Cited by 365
Crane, C. A., Han, S.-G. J., Barry, J., Ahn, B. J., Lanier, L., & Parsa, A. (2010) · Neuro-Oncology · doi:10.1093/neuonc/nop009 · Cited by 342
Self-citationRoberts, A. I., Lee, L., Schwarz, E. M., Groh, V., Spies, T. A., Ebert, E. C., & Jabrì, B. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.10.5527 · Cited by 341 · cited 1×
“Similarly, although expressed on all na€ ve human CD8þ T cells, NKG2D fails to costimulate TCR-induced activation of resting CD8þ T cells (12, 19, 41), and only augments TCRdependent activation after the T cells have been activated and cultured for a period of time in vitro (18, 41, 42).”
BackgroundMg2+ regulates cytotoxic functions of NK and CD8 T cells in chronic EBV infection through NKG2D
Chaigne-Delalande, B., Li, F.-Y., O'Connor, G., Lukacs, M., Jiang, P., Zheng, L.-X., Shatzer, A. N., Biancalana, M., Pittaluga, S., Matthews, H. F., et al. (2013) · Science · doi:10.1126/science.1240094 · Cited by 330 · cited 1×
“Intracellular concentrations of magnesium are critical for the assembly of the NKG2D–DAP10 receptor complex in that patients with a homozygous loss of the magnesium transporter 1 (MAGT1) gene have impaired expression of NKG2D on the surface of their T cells and NK cells, which can be restored by dietary Mgþþ supplemen…”
BackgroundLodoen, M. B., Ogasawara, K., Hamerman, J., Arase, H., Houchins, J. P., Mocarski, E., & Lanier, L. (2003) · Journal of Experimental Medicine · doi:10.1084/jem.20021973 · Cited by 326 · cited 1×
“Mouse CMV m152 protein blocks surface expression of Raet1 proteins (50, 51); m155 blocks H60 (52), m145 blocks MULT1 (53), and m138 blocks expression of MULT1 and H60 (54).”
BackgroundSelf-citationCarayannopoulos, L., Naidenko, O., Fremont, D., & Yokoyama, W. (2002) · Journal of Immunology · doi:10.4049/jimmunol.169.8.4079 · Cited by 322
Upshaw, J. L., Arneson, L. N., Schoon, R., Dick, C., Billadeau, D., & Leibson, P. (2006) · Nature Immunology · doi:10.1038/ni1325 · Cited by 312 · cited 1×
“Association of NKG2D with DAP12 versus DAP10 has significant consequences for signal transduction in that DAP12 possesses a canonical immunotyrosine-based activation motif (ITAM), which recruits Syk and ZAP70 tyrosine kinases (7), whereas DAP10 has a YINM motif, which recruits a p85 PI3 kinase and Vav-1 signaling comp…”
BackgroundA shed NKG2D ligand that promotes natural killer cell activation and tumor rejection
Deng, W., Gowen, B. G., Zhang, L., Wang, L., Lau, S., Iannello, A., Xu, J., Rovis, T., Xiong, N., & Raulet, D. (2015) · Science · doi:10.1126/science.1258867 · Cited by 264 · cited 1×
“cells and T cells, Deng and colleagues have reported that the high-affinity MULT1 mouse NKG2D ligand can stimulate NK cells and enhance their antitumor activity (73).”
BackgroundWu, J., Cherwinski, H., Spies, T., Phillips, J., & Lanier, L. (2000) · Journal of Experimental Medicine · doi:10.1084/jem.192.7.1059 · Cited by 261
Self-citationGarrity, D., Call, M., Feng, J., & Wucherpfennig, K. (2005) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0502439102 · Cited by 212 · cited 1×
“Each disulfide-bonded NKG2D homodimer associates with two DAP10 disulfide-bonded homodimers to form a hexameric receptor complex (9).”
BackgroundThomas, M., Boname, J., Field, S., Nejentsev, S., Salio, M., Cerundolo, V., Wills, M., & Lehner, P. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0707883105 · Cited by 203 · cited 1×
“Similarly, adenovirus E3/19k (56), U21 of human herpesvirus 7 (57), and the K5 ubiquitin ligase encoded by human herpesvirus 8 (58) cause the degradation of MICA and MICB.”
BackgroundCerboni, C., Neri, F., Casartelli, N., Zingoni, A., Cosman, D., Rossi, P., Santoni, A., & Doria, M. (2007) · Journal of General Virology · doi:10.1099/vir.0.82125-0 · Cited by 190
Function of NKG2D in natural killer cell–mediated rejection of mouse bone marrow grafts
Ogasawara, K., Benjamin, J., Takaki, R., Phillips, J., & Lanier, L. (2005) · Nature Immunology · doi:10.1038/ni1236 · Cited by 188 · cited 1×
“Resting mouse NK cells can be activated directly by crosslinking NKG2D ex vivo (11), and mice can reject normal hematopoietic cells that express a Raet1 transgene without prior priming (37), perhaps because mouse, but not human, NKG2D associates with DAP12 in addition to DAP10.”
BackgroundSelf-citationKrmpotić, A., Hasan, M., Loewendorf, A. I., Saulig, T., Halenius, A., Lenac, T., Polić, B., Bubić, I., Kriegeskorte, A. K., Pernjak-Pugel, E., et al. (2004) · Journal of Experimental Medicine · doi:10.1084/jem.20041617 · Cited by 182 · cited 3×
“The mouse ligands include Rae1a, Rae1b, Rae1g , Rae1d, and Rae1e, MULT1, and H60a, H60b, and H60c, with MULT1, H60a, and H60b being transmembraneanchored and the others GPI-anchored (30–33).”
BackgroundCrane, C. A., Austgen, K., Haberthur, K., Hofmann, C. C., Moyes, K., Avanesyan, L., Fong, L., Campbell, M., Cooper, S. L., Oakes, S. A., et al. (2014) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1413933111 · Cited by 179 · cited 1×
“Lactose dehydrogenase 5 released from tumor cells can induce expression of NKG2D ligands on healthy monocytes, allowing them to downregulate NKG2D on NK cells and T cells and serve as decoys (72).”
BackgroundSelf-citationCutting Edge: NKG2D Is a Costimulatory Receptor for Human Naive CD8+ T Cells
Maasho, K., Opoku-Anane, J., Marusina, A., Coligan, J., & Borrego, F. (2005) · Journal of Immunology · doi:10.4049/jimmunol.174.8.4480 · Cited by 176 · cited 1×
“Similarly, although expressed on all na€ ve human CD8þ T cells, NKG2D fails to costimulate TCR-induced activation of resting CD8þ T cells (12, 19, 41), and only augments TCRdependent activation after the T cells have been activated and cultured for a period of time in vitro (18, 41, 42).”
BackgroundA Cluster of Ten Novel MHC Class I Related Genes on Human Chromosome 6q24.2–q25.3
Radosavljevic, M., Cuillerier, B., Wilson, M. J., Clément, O., Wicker, S., Gilfillan, S., Beck, S., Trowsdale, J., & Bahram, S. (2002) · Genomics · doi:10.1006/geno.2001.6673 · Cited by 168
Lodoen, M. B., Abenes, G., Umamoto, S., Houchins, J. P., Liu, F.-Y., & Lanier, L. (2004) · Journal of Experimental Medicine · doi:10.1084/jem.20040583 · Cited by 168
Self-citationA Structural Basis for the Association of DAP12 with Mouse, but Not Human, NKG2D1
Rosen, D., Araki, M., Hamerman, J., Chen, T., Yamamura, T., & Lanier, L. (2004) · Journal of Immunology · doi:10.4049/jimmunol.173.4.2470 · Cited by 167
Self-citationDifferential Mechanisms of Shedding of the Glycosylphosphatidylinositol (GPI)-anchored NKG2D Ligands
Fernández‐Messina, L., Ashiru, O., Boutet, P., Agüera‐González, S., Skepper, J. N., Reyburn, H. T., & Valés‐Gómez, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045906 · Cited by 164
Mononuclear myeloid-derived "suppressor" cells express RAE-1 and activate natural killer cells.
Nausch, N., Galani, I., Schlecker, E., & Cerwenka, A. (2008) · Blood · doi:10.1182/blood-2008-03-143776 · Cited by 163
Ho, E., Heusel, J. W., Brown, M. G., Matsumoto, K., Scalzo, A., & Yokoyama, W. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.11.6320 · Cited by 158 · cited 1×
“The mouse ortholog, Klrk1, is present on the syntenic region of mouse chromosome 6 and similarly has limited polymorphism (3).”
BackgroundIL-21 Down-Regulates NKG2D/DAP10 Expression on Human NK and CD8+ T Cells1
Burgess, S., Marusina, A., Pathmanathan, I., Borrego, F., & Coligan, J. (2006) · Journal of Immunology · doi:10.4049/jimmunol.176.3.1490 · Cited by 140 · cited 1×
“In humans, IL2, IL7, IL12, and IL15 upregulate NKG2D expression (18–21), whereas TGFb (22–24), IFNb1 (25), and IL21 (26) downmodulate NKG2D.”
Two Novel Human Cytomegalovirus NK Cell Evasion Functions Target MICA for Lysosomal Degradation
Fielding, C. A., Aicheler, R., Stanton, R. J., Wang, E. C. Y., Han, S., Seirafian, S., Davies, J. A., McSharry, B. P., Weekes, M. P., Antrobus, R., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004058 · Cited by 133 · cited 10×
“MICA, MICB, RAET1E (ULBP4), and RAET1G (ULBP5) are transmembrane-anchored glycoproteins, whereas RAET1I (ULBP1), RAET1H (ULBP2), RAET1N (ULBP3), and RAET1L (ULBP6) are glycophosphatidylinositol (GPI)-anchored, although RAET1H (ULBP2) may be expressed in both transmembraneanchored and GPI-anchored forms (28), and RAET1…”
BackgroundInfluentialNKG2D Ligand MICA Is Retained in the cis-Golgi Apparatus by Human Cytomegalovirus Protein UL142
Ashiru, O., Bennett, N., Boyle, L. H., Thomas, M., Trowsdale, J., & Wills, M. (2009) · Journal of Virology · doi:10.1128/jvi.01175-09 · Cited by 130
Glienke, J., Sobanov, Y., Brostjan, C., Steffens, C., Nguyen, C., Lehrach, H., Hofer, E., & Francis, F. (1998) · Immunogenetics · doi:10.1007/s002510050420 · Cited by 128 · cited 1×
“2 flanked on the centromeric side by KLRD1 (CD94) and on the telomeric side by the cluster of KLRC4 (NKG2F), KLRC3 (NKG2E), KLRC2 (NKG2C), and KLRC1 (NKG2A) genes (2).”
BackgroundJung, H., Hsiung, B., Pestal, K., Procyk, E., & Raulet, D. H. (2012) · Journal of Experimental Medicine · doi:10.1084/jem.20120565 · Cited by 123 · cited 1×
“Induction of ligands might also be caused by hyperproliferation of the transformed cell that results in activation of E2F transcription factors (38).”
BackgroundPark, Y. P., Choi, S., Kiesler, P., Gil-Krzewska, A. J., Borrego, F., Weck, J., Krzewski, K., & Coligan, J. E. (2011) · Blood · doi:10.1182/blood-2011-04-346825 · Cited by 121
Mcsharry, B. P., Burgert, H., Owen, D., Stanton, R., Prod'homme, V., Sester, M., Koebernick, K., Groh, V., Spies, T., Cox, S., et al. (2008) · Journal of Virology · doi:10.1128/jvi.02251-07 · Cited by 121 · cited 1×
“Similarly, adenovirus E3/19k (56), U21 of human herpesvirus 7 (57), and the K5 ubiquitin ligase encoded by human herpesvirus 8 (58) cause the degradation of MICA and MICB.”
BackgroundNew prospects on the NKG2D/NKG2DL system for oncology
Ullrich, E., Koch, J., Cerwenka, A., & Steinle, A. (2013) · OncoImmunology · doi:10.4161/onci.26097 · Cited by 119
Ehrlich, L. I. R., Ogasawara, K., Hamerman, J., Takaki, R., Zingoni, A., Allison, J., & Lanier, L. (2005) · Journal of Immunology · doi:10.4049/jimmunol.174.4.1922 · Cited by 113 · cited 2×
“Although NKG2D is expressed constitutively on essentially all resting human NK cells and CD8þ T cells (14), engagement of NKG2D alone is insufficient to trigger cell-mediated cytotoxicity or cytokine production (12, 40), although the simultaneous engagement of NKG2D and other "costimulatory" receptors, such as CD335 (…”
BackgroundSelf-citationInterleukin-12 improves cytotoxicity of natural killer cells via upregulated expression of NKG2D.
Zhang, C., Zhang, J.-H., Niu, J.-F., Zhou, Z.-X., Zhang, J., & Tian, Z. (2008) · Human Immunology · doi:10.1016/j.humimm.2008.06.004 · Cited by 111
Zoonotic orthopoxviruses encode a high-affinity antagonist of NKG2D
Campbell, J. A., Trossman, D., Yokoyama, W., & Carayannopoulos, L. (2007) · Journal of Experimental Medicine · doi:10.1084/jem.20062026 · Cited by 110 · cited 1×
“The cowpox and monkeypox viruses secrete a soluble protein that functions as an NKG2D receptor antagonist, binding to NKG2D ligands on the surface of infected cells with high affinity to prevent detection by T cells andNK cells (59).”
BackgroundNKG2D CARs as Cell Therapy for Cancer
Sentman, C. L., & Meehan, K. R. (2014) · The Cancer Journal · doi:10.1097/ppo.0000000000000029 · Cited by 110
The herpesviral Fc receptor fcr-1 down-regulates the NKG2D ligands MULT-1 and H60
Roviš, T. L., Budt, M., Arapović, J., Hasan, M., Zimmermann, A., Šimić, H., Krmpotić, A., Messerle, M., Ruzsics, Z., Koszinowski, U. H., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20060514 · Cited by 99 · cited 2×
“The mouse ligands include Rae1a, Rae1b, Rae1g , Rae1d, and Rae1e, MULT1, and H60a, H60b, and H60c, with MULT1, H60a, and H60b being transmembraneanchored and the others GPI-anchored (30–33).”
BackgroundTakada, A., Yoshida, S., Kajikawa, M., Miyatake, Y., Tomaru, U., Sakai, M., Chiba, H., Maenaka, K., Kohda, D., Fugo, K., et al. (2008) · Journal of Immunology · doi:10.4049/jimmunol.180.3.1678 · Cited by 99
Zou, Z., Nomura, M., Takihara, Y., Yasunaga, T., & 島田, 和. (1996) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021242 · Cited by 91 · cited 1×
“Although the mouse Raet1 genes were originally identified as being constitutively expressed in the developing embryo (36), in general, the NKG2D ligands are not expressed on the surface of healthy cells and tissues in adults.”
BackgroundCytosolic PLA2 is required for CTL-mediated immunopathology of celiac disease via NKG2D and IL-15
Tang, F., Chen, Z., Ciszewski, C., Setty, M., Solus, J., Tretiakova, M., Ebert, E., Han, J., Lin, A., Guandalini, S., et al. (2009) · Journal of Experimental Medicine · doi:10.1084/jem.20071887 · Cited by 89 · cited 1×
“How NK cells and T cells are "primed" to make NKG2D become permissive to trigger effector functions has not been defined, although cytosolic phospholipase A2 has been implicated in the process (44).”
BackgroundSecretory pathways generating immunosuppressive NKG2D ligands
Raneros, A. B., Suárez-Álvarez, B., & López-Larrea, C. (2014) · Oncoimmunology · doi:10.4161/onci.28497 · Cited by 82
Intracellular Sequestration of the NKG2D Ligand ULBP3 by Human Cytomegalovirus
Bennett, N. J., Ashiru, O., Morgan, F. J. E., Pang, Y., Okecha, G., Eagle, R. A., Trowsdale, J., Sissons, J. G. P., & Wills, M. R. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000789 · Cited by 82
Structural Basis for Recognition of Cellular and Viral Ligands by NK Cell Receptors
Li, Y., & Mariuzza, R. A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00123 · Cited by 68
Muntasell, A., Magri, G., Pende, D., Angulo, A., & López‐Botet, M. (2010) · Blood · doi:10.1182/blood-2009-11-256479 · Cited by 64 · cited 1×
“In humans, IL2, IL7, IL12, and IL15 upregulate NKG2D expression (18–21), whereas TGFb (22–24), IFNb1 (25), and IL21 (26) downmodulate NKG2D.”
Schneider, C. L., & Hudson, A. W. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002362 · Cited by 51 · cited 1×
“Similarly, adenovirus E3/19k (56), U21 of human herpesvirus 7 (57), and the K5 ubiquitin ligase encoded by human herpesvirus 8 (58) cause the degradation of MICA and MICB.”
BackgroundA selective role of NKG2D in inflammatory and autoimmune diseases
Guerra, N., Pestal, K., Juarez, T., Beck, J., Tkach, K. E., Wang, L., & Raulet, D. H. (2013) · Clinical Immunology · doi:10.1016/j.clim.2013.09.003 · Cited by 49
Differential Susceptibility of RAE-1 Isoforms to Mouse Cytomegalovirus
Arapović, J., Lenac, T., Antulov, R., Polić, B., Ruzsics, Z., Carayannopoulos, L., Koszinowski, U., Krmpotić, A., & Jonjić, S. (2009) · Journal of Virology · doi:10.1128/jvi.02549-08 · Cited by 49 · cited 1×
“Mouse CMV m152 protein blocks surface expression of Raet1 proteins (50, 51); m155 blocks H60 (52), m145 blocks MULT1 (53), and m138 blocks expression of MULT1 and H60 (54).”
BackgroundFernández-Messina, L., Ashiru, O., Agüera-González, S., Reyburn, H., & Valés-Gómez, M. (2011) · Journal of Cell Science · doi:10.1242/jcs.076042 · Cited by 42 · cited 1×
“MICA, MICB, RAET1E (ULBP4), and RAET1G (ULBP5) are transmembrane-anchored glycoproteins, whereas RAET1I (ULBP1), RAET1H (ULBP2), RAET1N (ULBP3), and RAET1L (ULBP6) are glycophosphatidylinositol (GPI)-anchored, although RAET1H (ULBP2) may be expressed in both transmembraneanchored and GPI-anchored forms (28), and RAET1…”
BackgroundTrsan, T., Busche, A., Abram, M., Wensveen, F. M., Lemmermann, N., Arapović, M., Babić, M., Tomic, A., Golemac, M., Brinkmann, M., et al. (2013) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1310215110 · Cited by 28
Ohashi, M., Eagle, R. A., & Trowsdale, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077636 · Cited by 18 · cited 2×
“The mouse ligands include Rae1a, Rae1b, Rae1g , Rae1d, and Rae1e, MULT1, and H60a, H60b, and H60c, with MULT1, H60a, and H60b being transmembraneanchored and the others GPI-anchored (30–33).”
BackgroundA truncated human NKG2D splice isoform negatively regulates NKG2D-mediated function
Karimi, M., Aguilar, O., Zou, B., Bachmann, M. H., Carlyle, J., Baldwin, C., & Kambayashi, T. (2014) · Journal of Immunology · doi:10.4049/jimmunol.1400920 · Cited by 17
Buhtoiarov, I., Rakhmilevich, A., Lanier, L., Ranheim, E., & Sondel, P. (2009) · Journal of Immunology · doi:10.4049/jimmunol.0800443 · Cited by 13 · cited 1×
“org) and express NKG2D on the cell surface (11, 13).”
BackgroundSelf-citation
Research works printed but not linked: 2
- Castriconi, 2003, Transforming growth factor beta 1 inhibits expression of NKp30 and NKG2D receptors: consequences for the NK-mediated killing of dendritic cells, Proc Natl Acad Sci U S A, 100, 4120, 10.1073/pnas.0730640100 · DOI
- Spear, 2013, NKG2D ligands as therapeutic targets, Cancer Immun, 13, 8
Cited by
Sorted by citations
NK cells and cancer: you can teach innate cells new tricks
Morvan, M. G., & Lanier, L. L. (2015) · Nature reviews. Cancer · doi:10.1038/nrc.2015.5 · Cited by 1,190
Self-citationTargeting natural killer cells in cancer immunotherapy
Guillerey, C., Huntington, N. D., & Smyth, M. J. (2016) · Nature Immunology · doi:10.1038/ni.3518 · Cited by 1,081
Metastatic Latency and Immune Evasion through Autocrine Inhibition of WNT
Malladi, S., Macalinao, D. G., Jin, X., He, L., Basnet, H., Zou, Y., de Stanchina, E., & Massagué, J. (2016) · Cell · doi:10.1016/j.cell.2016.02.025 · Cited by 791
C-type lectins in immunity and homeostasis
Brown, G. D., Willment, J. A., & Whitehead, L. (2018) · Nature reviews. Immunology · doi:10.1038/s41577-018-0004-8 · Cited by 609
Human NK cells: surface receptors, inhibitory checkpoints, and translational applications
Sivori, S., Vacca, P., Zotto, G. D., Munari, E., Mingari, M., & Moretta, L. (2019) · Cellular & Molecular Immunology · doi:10.1038/s41423-019-0206-4 · Cited by 493
Metadata
- Authors
- Lanier, L. L.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Lanier, Lewis L.
- ORCID
- Lanier, Lewis L.
- Venue
- Cancer Immunology Research
- Published
- 2015-06-01
- Volume
- 3
- Issue
- 6
- Pages
- 575-582
- ISSN
- 2326-6066 (ISSN-L)
- 2326-6074
- PMC
- PMC4457299
- OpenAlex
- W2142548447
- Cited by
- 599
- References
- 78
- Citations by year
- 2026: 27 · 2025: 53 · 2024: 56 · 2023: 73 · 2022: 56 · 2021: 66 · 2020: 63 · 2019: 51 · 2018: 65 · 2017: 47 · 2016: 37 · 2015: 4
- FWCI
- 4.80
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cancer Immunology Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute (R01CA089189)
- National Institute of Allergy and Infectious Diseases (AI-068129, R01AI068129, R37AI066897, AI066897)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Cell Function and Interaction
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › Reproductive System and Pregnancy
- Keywords
- NKG2D, NKG2D ligands, mica, MICB, natural killer cells, DAP10, DAP12, immune evasion, viral evasion, tumor immune evasion, host defense, NK cell activation
- MeSH terms
- Animals, Communicable Diseases, Humans, Killer Cells, Natural, Ligands, Lymphocyte Activation, Neoplasms, Lymphocyte Subsets, NK Cell Lectin-Like Receptor Subfamily K, Disease Resistance
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
