1. Wendel, M., et al., Natural killer cell accumulation in tumors is dependent on IFN-gamma and CXCR3 ligands. Cancer Res, 2008. 68(20): p. 8437-45.
2. Voshtani, R., et al., Progranulin promotes melanoma progression by inhibiting natural killer cell recruitment to the tumor microenvironment. Cancer Lett, 2019. 465: p. 24-35.
3. Bottcher, J.P., et al., NK Cells Stimulate Recruitment of cDC1 into the Tumor Microenvironment Promoting Cancer Immune Control. Cell, 2018. 172(5): p. 1022-1037 e14.
4. Bald, T., et al., The NK cell-cancer cycle: advances and new challenges in NK cell-based immunotherapies. Nat Immunol, 2020. 21(8): p. 835-847.
5. Franciszkiewicz, K., et al., Role of chemokines and chemokine receptors in shaping the effector phase of the antitumor immune response. Cancer Res, 2012. 72(24): p. 6325-32.
6. Barber, D.F., M. Faure, and E.O. Long, LFA-1 contributes an early signal for NK cell cytotoxicity. J Immunol, 2004. 173(6): p. 3653-9.
7. Huntington, N.D., J. Cursons, and J. Rautela, The cancer-natural killer cell immunity cycle. Nat Rev Cancer, 2020. 20(8): p. 437-454.
8. Koch, J., et al., Activating natural cytotoxicity receptors of natural killer cells in cancer and infection. Trends Immunol, 2013. 34(4): p. 182-91.
9. Wu, Y., Z. Tian, and H. Wei, Developmental and Functional Control of Natural Killer Cells by Cytokines. Front Immunol, 2017. 8: p. 930.
10. Trapani, J.A. and M.J. Smyth, Functional significance of the perforin/granzyme cell death pathway. Nat Rev Immunol, 2002. 2(10): p. 735-47.
11. Gras Navarro, A., A.T. Bjorklund, and M. Chekenya, Therapeutic potential and challenges of natural killer cells in treatment of solid tumors. Front Immunol, 2015. 6: p. 202.
12. Derakhshan, A., Z. Chen, and C. Van Waes, Therapeutic Small Molecules Target Inhibitor of Apoptosis Proteins in Cancers with Deregulation of Extrinsic and Intrinsic Cell Death Pathways. Clin Cancer Res, 2017. 23(6): p. 1379-1387.
13. Dejardin, E., et al., Regulation of major histocompatibility complex class I expression by NF-kappaB-related proteins in breast cancer cells. Oncogene, 1998. 16(25): p. 3299-307.
14. Roberts, E.W., et al., Critical Role for CD103(+)/CD141(+) Dendritic Cells Bearing CCR7 for Tumor Antigen Trafficking and Priming of T Cell Immunity in Melanoma. Cancer Cell, 2016. 30(2): p. 324-336.
15. Tay, R.E., E.K. Richardson, and H.C. Toh, Revisiting the role of CD4(+) T cells in cancer immunotherapy-new insights into old paradigms. Cancer Gene Ther, 2020.
16. Melero, I., et al., Clinical development of immunostimulatory monoclonal antibodies and opportunities for combination. Clin Cancer Res, 2013. 19(5): p. 997-1008.
17. Sackstein, R., T. Schatton, and S.R. Barthel, T-lymphocyte homing: an underappreciated yet critical hurdle for successful cancer immunotherapy. Lab Invest, 2017. 97(6): p. 669- 697.
18. Lieberman, J., The ABCs of granule-mediated cytotoxicity: new weapons in the arsenal. Nat Rev Immunol, 2003. 3(5): p. 361-70.
19. Bauer, S., et al., Activation of NK cells and T cells by NKG2D, a receptor for stress- inducible MICA. Science, 1999. 285(5428): p. 727-9.
20. Jamieson, A.M., et al., The role of the NKG2D immunoreceptor in immune cell activation and natural killing. Immunity, 2002. 17(1): p. 19-29.
21. Amsen, D., et al., Tissue-resident memory T cells at the center of immunity to solid tumors. Nat Immunol, 2018. 19(6): p. 538-546.
22. Kaech, S.M. and W. Cui, Transcriptional control of effector and memory CD8+ T cell differentiation. Nat Rev Immunol, 2012. 12(11): p. 749-61.
23. Dunn, G.P., L.J. Old, and R.D. Schreiber, The immunobiology of cancer immunosurveillance and immunoediting. Immunity, 2004. 21(2): p. 137-48.
24. O'Donnell, J.S., M.W.L. Teng, and M.J. Smyth, Cancer immunoediting and resistance to T cell-based immunotherapy. Nat Rev Clin Oncol, 2019. 16(3): p. 151-167.
25. Schreiber, R.D., L.J. Old, and M.J. Smyth, Cancer immunoediting: integrating immunity's roles in cancer suppression and promotion. Science, 2011. 331(6024): p. 1565-70.
26. Nirschl, C.J. and C.G. Drake, Molecular pathways: coexpression of immune checkpoint molecules: signaling pathways and implications for cancer immunotherapy. Clin Cancer Res, 2013. 19(18): p. 4917-24.
27. Li, X., et al., Emerging predictors of the response to the blockade of immune checkpoints in cancer therapy. Cell Mol Immunol, 2019. 16(1): p. 28-39.
28. Marin-Acevedo, J.A., et al., Next generation of immune checkpoint therapy in cancer: new developments and challenges. J Hematol Oncol, 2018. 11(1): p. 39.
29. Cassetta, L. and J.W. Pollard, Targeting macrophages: therapeutic approaches in cancer. Nat Rev Drug Discov, 2018.
30. Chabanon, R.M., et al., Mutational Landscape and Sensitivity to Immune Checkpoint Blockers. Clin Cancer Res, 2016. 22(17): p. 4309-21.
31. Bruno, A., et al., Myeloid Derived Suppressor Cells Interactions With Natural Killer Cells and Pro-angiogenic Activities: Roles in Tumor Progression. Front Immunol, 2019. 10: p. 771.
32. Kobayashi, H., et al., Cancer-associated fibroblasts in gastrointestinal cancer. Nat Rev Gastroenterol Hepatol, 2019. 16(5): p. 282-295.
33. Togashi, Y., K. Shitara, and H. Nishikawa, Regulatory T cells in cancer immunosuppression - implications for anticancer therapy. Nat Rev Clin Oncol, 2019. 16(6): p. 356-371.
34. Jenkins, R.W., D.A. Barbie, and K.T. Flaherty, Mechanisms of resistance to immune checkpoint inhibitors. Br J Cancer, 2018. 118(1): p. 9-16.
35. Masson, D., et al., Overexpression of the CD155 gene in human colorectal carcinoma. Gut, 2001. 49(2): p. 236-40.
36. Nakai, R., et al., Overexpression of Necl-5 correlates with unfavorable prognosis in patients with lung adenocarcinoma. Cancer Sci, 2010. 101(5): p. 1326-30.
37. Bevelacqua, V., et al., Nectin like-5 overexpression correlates with the malignant phenotype in cutaneous melanoma. Oncotarget, 2012. 3(8): p. 882-92.
38. Nishiwada, S., et al., Clinical significance of CD155 expression in human pancreatic cancer. Anticancer Res, 2015. 35(4): p. 2287-97.
39. Tahara-Hanaoka, S., et al., Tumor rejection by the poliovirus receptor family ligands of the DNAM-1 (CD226) receptor. Blood, 2006. 107(4): p. 1491-6.
40. Takai, Y., et al., Nectins and nectin-like molecules: roles in contact inhibition of cell movement and proliferation. Nat Rev Mol Cell Biol, 2008. 9(8): p. 603-15.
41. Tane, S., et al., The role of Necl-5 in the invasive activity of lung adenocarcinoma. Exp Mol Pathol, 2013. 94(2): p. 330-5.
42. Enloe, B.M. and D.G. Jay, Inhibition of Necl-5 (CD155/PVR) reduces glioblastoma dispersal and decreases MMP-2 expression and activity. J Neurooncol, 2011. 102(2): p. 225-35.
43. Shibuya, A., et al., DNAM-1, a novel adhesion molecule involved in the cytolytic function of T lymphocytes. Immunity, 1996. 4(6): p. 573-81.
44. Tahara-Hanaoka, S., et al., Functional characterization of DNAM-1 (CD226) interaction with its ligands PVR (CD155) and nectin-2 (PRR-2/CD112). Int. Immunol, 2004. 16: p. 533-8.
45. Bottino, C., et al., Identification of PVR (CD155) and Nectin-2 (CD112) as cell surface ligands for the human DNAM-1 (CD226) activating molecule. J Exp Med, 2003. 198(4): p. 557-67.
46. Shibuya, K., et al., Physical and functional association of LFA-1 with DNAM-1 adhesion molecule. Immunity, 1999. 11(5): p. 615-23.
47. Shibuya, K., et al., CD226 (DNAM-1) is involved in lymphocyte function-associated antigen 1 costimulatory signal for naive T cell differentiation and proliferation. J Exp Med, 2003. 198(12): p. 1829-39.
48. Iguchi-Manaka, A., et al., Accelerated tumor growth in mice deficient in DNAM-1 receptor. J Exp Med, 2008. 205(13): p. 2959-64.
49. Zhang, Z., et al., DNAM-1 controls NK cell activation via an ITT-like motif. J Exp Med, 2015. 212(12): p. 2165-82.
50. Wang, B., et al., Combination cancer immunotherapy targeting PD-1 and GITR can rescue CD8(+) T cell dysfunction and maintain memory phenotype. Sci Immunol, 2018. 3(29).
51. Yu, X., et al., The surface protein TIGIT suppresses T cell activation by promoting the generation of mature immunoregulatory dendritic cells. Nat Immunol, 2009. 10(1): p. 48- 57.
52. Johnston, R.J., et al., The immunoreceptor TIGIT regulates antitumor and antiviral CD8(+) T cell effector function. Cancer Cell, 2014. 26(6): p. 923-937.
53. Solomon, B.L. and I. Garrido-Laguna, TIGIT: a novel immunotherapy target moving from bench to bedside. Cancer Immunol Immunother, 2018. 67(11): p. 1659-1667.
54. Guillerey, C., et al., TIGIT immune checkpoint blockade restores CD8(+) T-cell immunity against multiple myeloma. Blood, 2018. 132(16): p. 1689-1694.
55. Joller, N., et al., Treg cells expressing the coinhibitory molecule TIGIT selectively inhibit proinflammatory Th1 and Th17 cell responses. Immunity, 2014. 40(4): p. 569-81.
56. Kurtulus, S., et al., TIGIT predominantly regulates the immune response via regulatory T cells. J Clin Invest, 2015. 125(11): p. 4053-62.
57. Dixon, K.O., et al., Functional Anti-TIGIT Antibodies Regulate Development of Autoimmunity and Antitumor Immunity. J Immunol, 2018. 200(8): p. 3000-3007.
58. Tiragolumab Impresses in Multiple Trials. Cancer Discov, 2020. 10(8): p. 1086-1087.
59. Gramatzki, M., et al., Antibodies TC-12 ("unique") and TH-111 (CD96) characterize T- cell acute lymphoblastic leukemia and a subgroup of acute myeloid leukemia. Exp Hematol, 1998. 26(13): p. 1209-14.
60. Hosen, N., et al., CD96 is a leukemic stem cell-specific marker in human acute myeloid leukemia. Proc Natl Acad Sci U S A, 2007. 104(26): p. 11008-13.
61. Fuchs, A., et al., Cutting edge: CD96 (tactile) promotes NK cell-target cell adhesion by interacting with the poliovirus receptor (CD155). J Immunol, 2004. 172(7): p. 3994-8.
62. Blake, S.J., et al., Suppression of Metastases Using a New Lymphocyte Checkpoint Target for Cancer Immunotherapy. Cancer Discov, 2016. 6(4): p. 446-59.
63. Chiang, E.Y., et al., CD96 functions as a co-stimulatory receptor to enhance CD8(+) T cell activation and effector responses. Eur J Immunol, 2020. 50(6): p. 891-902.
64. Georgiev, H., et al., Coming of Age: CD96 Emerges as Modulator of Immune Responses. Front Immunol, 2018. 9: p. 1072.
65. Martinet, L. and M.J. Smyth, Balancing natural killer cell activation through paired receptors. Nat Rev Immunol, 2015. 15(4): p. 243-54.
66. Baury, B., et al., Identification of secreted CD155 isoforms. Biochem Biophys Res Commun, 2003. 309(1): p. 175-82.
67. Iguchi-Manaka, A., et al., Increased Soluble CD155 in the Serum of Cancer Patients. PLoS One, 2016. 11(4): p. e0152982.
68. Cuff, S., et al., Antigen specificity determines the pro- or antitumoral nature of CD8+ T cells. J Immunol, 2010. 184(2): p. 607-14.
69. Martins, F., et al., Adverse effects of immune-checkpoint inhibitors: epidemiology, management and surveillance. Nat Rev Clin Oncol, 2019. 16(9): p. 563-580.
70. Gerhardt, T. and K. Ley, Monocyte trafficking across the vessel wall. Cardiovasc Res, 2015. 107(3): p. 321-30.
71. Justus, C.R., et al., In vitro cell migration and invasion assays. J Vis Exp, 2014(88).
72. Triki, H., et al., CD155 expression in human breast cancer: Clinical significance and relevance to natural killer cell infiltration. Life Sci, 2019: p. 116543.
73. Groh, V., et al., Tumour-derived soluble MIC ligands impair expression of NKG2D and T-cell activation. Nature, 2002. 419(6908): p. 734-8.
74. Schlecker, E., et al., Metalloprotease-Mediated Tumor Cell Shedding of B7-H6, the Ligand of the Natural Killer Cell-Activating Receptor NKp30. Cancer Research, 2014. 74(13): p. 3429-3440.
75. Pesce, S., et al., B7-H6-mediated downregulation of NKp30 in NK cells contributes to ovarian carcinoma immune escape. Oncoimmunology, 2015. 4(4).
76. Deng, W.W., et al., A shed NKG2D ligand that promotes natural killer cell activation and tumor rejection. Science, 2015. 348(6230): p. 136-139.
77. Jin, H.S., et al., CD226(hi)CD8(+) T Cells Are a Prerequisite for Anti-TIGIT Immunotherapy. Cancer Immunol Res, 2020. 8(7): p. 912-925.
78. Li, X.Y., et al., CD155 loss enhances tumor suppression via combined host and tumor- intrinsic mechanisms. J Clin Invest, 2018. 128(6): p. 2613-2625.