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Wei, S. C. et al. Distinct mobile mechanisms underlie anti-CTLA-4 and anti-PD-1 checkpoint blockade. Cell 170, 1120–1133.e17 (2017).
Sharma, P. & Allison, J. P. Dissecting the mechanisms of immune checkpoint remedy. Nat. Rev. Immunol. 20, 75–76 (2020).
Wolchok, J. Placing the immunologic brakes on most cancers. Cell 175, 1452–1454 (2018).
Kulkarni, A. et al. A designer self-assembled supramolecule amplifies macrophage immune responses in opposition to aggressive most cancers. Nat. Biomed. Eng. 2, 589–599 (2018).
Wei, S. C., Duffy, C. R. & Allison, J. P. Elementary mechanisms of immune checkpoint blockade remedy. Most cancers Discov. 8, 1069–1086 (2018).
Tseng, D. et al. Anti-CD47 antibody–mediated phagocytosis of most cancers by macrophages primes an efficient antitumor T-cell response. Proc. Natl Acad. Sci. USA 110, 11103–11108 (2013).
Sharma, P. & Allison, J. P. The way forward for immune checkpoint remedy. Science 348, 56–61 (2015).
Önfelt, B., Nedvetzki, S., Yanagi, Ok. & Davis, D. M. Innovative: membrane nanotubes join immune cells. J. Immunol. 173, 1511–1513 (2004).
Sowinski, S. et al. Membrane nanotubes bodily join T cells over lengthy distances presenting a novel route for HIV-1 transmission. Nat. Cell Biol. 10, 211–219 (2008).
Gousset, Ok. et al. Prions hijack tunnelling nanotubes for intercellular unfold. Nat. Cell Biol. 11, 328–336 (2009).
Osswald, M. et al. Mind tumour cells interconnect to a practical and resistant community. Nature 528, 93–98 (2015).
Connor, Y. et al. Bodily nanoscale conduit-mediated communication between tumour cells and the endothelium modulates endothelial phenotype. Nat. Commun. 6, 8671 (2015).
Rustom, A., Saffrich, R., Markovic, I., Walther, P. & Gerdes, H.-H. Nanotubular highways for intercellular organelle transport. Science 303, 1007–1010 (2004).
Ahmad, T. et al. Miro1 regulates intercellular mitochondrial transport & enhances mesenchymal stem cell rescue efficacy. EMBO J. 33, 994–1010 (2014).
Wang, X. & Gerdes, H. H. Switch of mitochondria through tunneling nanotubes rescues apoptotic PC12 cells. Cell Demise Differ. 22, 1181–1191 (2015).
Lu, J. et al. Tunneling nanotubes promote intercellular mitochondria switch adopted by elevated invasiveness in bladder most cancers cells. Oncotarget 8, 15539–15552 (2017).
Sena, L. A. et al. Mitochondria are required for antigen-specific T cell activation by means of reactive oxygen species signaling. Immunity 38, 225–236 (2013).
Kumar, A. et al. Enhanced oxidative phosphorylation in NKT cells is crucial for his or her survival and performance. Proc. Natl Acad. Sci. USA 116, 7439–7448 (2019).
Vyas, S., Zaganjor, E. & Haigis, M. C. Mitochondria and most cancers. Cell 166, 555–566 (2016).
Goldman, A. et al. Concentrating on tumor phenotypic plasticity and metabolic reworking in adaptive cross-drug tolerance. Sci. Sign. 12, eaas8779 (2019).
Clutton, G., Mollan, Ok., Hudgens, M. & Goonetilleke, N. A reproducible, goal technique utilizing MitoTracker® fluorescent dyes to evaluate mitochondrial mass in T cells by stream cytometry. Cytometry 95, 450–456 (2019).
Pham, A. H., McCaffery, J. M. & Chan, D. C. Mouse traces with photo-activatable mitochondria to check mitochondrial dynamics. Genesis 50, 833–843 (2012).
Pelletier, M., Billingham, L. Ok., Ramaswamy, M. & Siegel, R. M. in Strategies Enzymol, Vol. 542 (eds Galluzzi, L. & Kroemer, G.) 125–149 (Educational Press, 2014).
Kaplon, J. et al. A key position for mitochondrial gatekeeper pyruvate dehydrogenase in oncogene-induced senescence. Nature 498, 109–112 (2013).
Hase, Ok. et al. M-Sec promotes membrane nanotube formation by interacting with Ral and the exocyst complicated. Nat. Cell Biol. 11, 1427–1432 (2009).
Hashimoto, M. et al. Potential position of the formation of tunneling nanotubes in HIV-1 unfold in macrophages. J. Immunol. 196, 1832–1841 (2016).
Moskalenko, S. et al. The exocyst is a Ral effector complicated. Nat. Cell Biol. 4, 66–72 (2002).
Hanna, S. J. et al. The position of Rho-GTPases and actin polymerization throughout macrophage tunneling nanotube biogenesis. Sci. Rep. 7, 8547 (2017).
Guo, W., Tamanoi, F. & Novick, P. Spatial regulation of the exocyst complicated by Rho1 GTPase. Nat. Cell Biol. 3, 353–360 (2001).
Fransson, Å., Ruusala, A. & Aspenström, P. The atypical Rho GTPases Miro-1 and Miro-2 have important roles in mitochondrial trafficking. Biochem. Biophys. Res. Commun. 344, 500–510 (2006).
Glater, E. E., Megeath, L. J., Stowers, R. S. & Schwarz, T. L. Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is gentle chain impartial. J. Cell Biol. 173, 545–557 (2006).
Arkwright, P. D. et al. Fas stimulation of T lymphocytes promotes speedy intercellular trade of demise alerts through membrane nanotubes. Cell Res. 20, 72–88.
Bustelo, X. R., Sauzeau, V. & Berenjeno, I. M. GTP-binding proteins of the Rho/Rac household: regulation, effectors and capabilities in vivo. Bioessays 29, 356–370 (2007).
Majumder, B. et al. Predicting scientific response to anticancer medicine utilizing an ex vivo platform that captures tumour heterogeneity. Nat. Commun. 6, 6169 (2015).
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