Karasneh, G. A. & Shukla, D. Herpes simplex virus infects most cell types in vitro: clues to its success. Virol. J. 8, 481 (2011).
Tang, R. et al. Direct delivery of functional proteins and enzymes to the cytosol using nanoparticle-stabilized nanocapsules. ACS Nano 7, 6667 – 6673 (2013).
Mout, R. et al. General strategy for direct cytosolic protein delivery via protein–nanoparticle co-engineering. ACS Nano 11, 6416 – 6421 (2017).
Wilhelm, S. vd. Tümörlere nanopartikül dağıtımının analizi. Nat. Rahip Mater. 1, 16014 (2016).
Tsoi, KM vd. Karaciğer tarafından sert nanomateryal temizleme mekanizması. Nat. Anne. 15, 1212 – 1221 (2016).
Chew, H. Y. et al. Endocytosis inhibition in humans to improve responses to ADCC-mediating antibodies. Hücre 180, 895-914.e27 (2020).
Yamashita, T., Takahashi, Y. & Takakura, Y. Ekzozom bazlı terapötiklerin olasılığı ve terapötik uygulama için uygun eksozomların üretiminde zorluklar. Biol. Ecz. Boğa. 41, 835 – 842 (2018).
Gilleron, J. et al. Image-based analysis of lipid nanoparticle-mediated siRNA delivery, intracellular trafficking and endosomal escape. Nat. Biyoteknoloji. 31, 638 – 646 (2013). Detailed ultrastructural analysis of lipid nanoparticle uptake, and siRNA delivery, in cultured cells and in mouse liver.
Sahay, G., Alakhova, D. Y. & Kabanov, A. V. Endocytosis of nanomedicines. J. Kontrol. Serbest bırakmak 145, 182 – 195 (2010).
Johannes, L., Parton, R. G., Bassereau, P. & Mayor, S. Building endocytic pits without clathrin. Nat. Rev. Mol. Hücre Biol. 16, 311 – 321 (2015).
Thottacherry, J. J., Sathe, M., Prabhakara, C. & Mayor, S. Spoiled for choice: diverse endocytic pathways function at the cell surface. Annu. Rev. Celi Dev. Biol. 35, 55 – 84 (2019). A comprehensive topical review of clathrin-dependent and clathrin-independent endocytic pathways.
Parton, R. G. Caveolae: structure, function, and relationship to disease. Annu. Rev. Celi Dev. Biol. 34, 111 – 136 (2018).
Kumari, S., MG, S. & Mayor, S. Endocytosis unplugged: multiple ways to enter the cell. Hücre Araş. 20, 256 – 275 (2010).
Chaudhary, N. et al. Endocytic crosstalk: cavins, caveolins, and caveolae regulate clathrin-independent endocytosis. PLoS Biol. 12, e1001832 (2014).
Damke, H., Baba, T., van der Bliek, A. M. & Schmid, S. L. Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin. J. Hücre Biol. 131, 69 – 80 (1995).
Boucrot, E. et al. Endophilin marks and controls a clathrin-independent endocytic pathway. Tabiat 517, 460 – 465 (2015). Characterization of a novel endophilin-dependent pathway, termed FEME.
Brown, C. M. & Petersen, N. O. Free clathrin triskelions are required for the stability of clathrin-associated adaptor protein (AP-2) coated pit nucleation sites. Biyokimya. Hücre Biol. 77, 439 – 448 (1999).
Ehrlich, M. vd. Klatrin kaplı çukurların rastgele başlatılması ve stabilizasyonu ile endositoz. Hücre 118, 591 – 605 (2004).
Veiga, E. et al. Invasive and adherent bacterial pathogens co-opt host clathrin for infection. Hücre Konakçı Mikrop 2, 340 – 351 (2007).
Li, Z. et al. Shape effect of glyco-nanoparticles on macrophage cellular uptake and immune response. ACS Makro Let. 5, 1059 – 1064 (2016).
Howes, M. T. et al. Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells. J. Hücre Biol. 190, 675 – 691 (2010).
Hemalatha, A., Prabhakara, C. & Mayor, S. Endocytosis of Wingless via a dynamin-independent pathway is necessary for signaling in Drosophila wing discs. Proc. Natl Acad. Sci. Amerika Birleşik Devletleri 113E6993 --- E7002 (2016).
Sathe, M. et al. Small GTPases and BAR domain proteins regulate branched actin polymerisation for clathrin and dynamin-independent endocytosis. Nat. Commun. 9, 1835 (2018).
Lakshminarayan, R. et al. Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers. Nat. Celi Biol. 16, 592 – 603 (2014).
Sandvig, K. & van Deurs, B. Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin. Physiol. Rev. 76, 949 – 966 (1996).
Thottacherry, J. J. et al. Mechanochemical feedback control of dynamin independent endocytosis modulates membrane tension in adherent cells. Nat. Commun. 9, 4217 (2018).
Condon, N. D. et al. Macropinosome formation by tent pole ruffling in macrophages. J. Hücre Biol. 217, 3873 – 3885 (2018).
Lin, X. P., Mintern, J. D. & Gleeson, P. A. Macropinocytosis in different cell types: similarities and differences. Zarlar 10, 177 (2020).
Kerr, M. C. & Teasdale, R. D. Defining macropinocytosis. Trafik 10, 364 – 371 (2009).
Lim, J. P. & Gleeson, P. A. Macropinocytosis: an endocytic pathway for internalising large gulps. immünol. Hücre Biol. 89, 836 – 843 (2011).
Commisso, C. vd. Proteinin makropinositozu, Ras ile dönüştürülmüş hücrelerde bir amino asit tedarik yoludur. Tabiat 497, 633 – 637 (2013). Macropinocytosis is shown to have a crucial role in providing nutrients for cancer cells through the internalization and catabolism of extracellular proteins.
Ha, K. D., Bidlingmaier, S. M. & Liu, B. Macropinocytosis exploitation by cancers and cancer therapeutics. Ön. Physiol. 7, 381 (2016).
Palm, W. Metabolic functions of macropinocytosis. Philos. Trans. R. Soc. B 374, 20180285 (2019).
Niedergang, F. & Grinstein, S. How to build a phagosome: new concepts for an old process. Kör. Görüş. Hücre Biol. 50, 57 – 63 (2018).
Lim, J. J., Grinstein, S. & Roth, Z. Diversity and versatility of phagocytosis: roles in innate immunity, tissue remodeling, and homeostasis. Ön. Hücre. Infect. Microbiol. 7, 191 (2017).
Desjardins, M. & Griffiths, G. Phagocytosis: latex leads the way. Kör. Görüş. Hücre Biol. 15, 498 – 503 (2003).
Doherty, G. J. & McMahon, H. T. Mechanisms of endocytosis. Annu. Rev. Biochem. 78, 857 – 902 (2009).
Harrison, R. E., Bucci, C., Vieira, O. V., Schroer, T. A. & Grinstein, S. Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP. Mol. Hücre. Biol. 23, 6494 – 6506 (2003).
Parton, R. G. et al. Caveolae: the FAQs. Trafik 21, 181 – 185 (2020).
Schubert, W. et al. Microvascular hyperpermeability in caveolin-1 (−/−) knock-out mice. J. Biol. Chem. 277, 40091 – 40098 (2002).
Kirkham, M. et al. Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles. J. Hücre Biol. 168, 465 – 476 (2005).
Rewatkar, P. V., Parton, R. G., Parekh, H. S. & Parat, M.-O. Are caveolae a cellular entry route for non-viral therapeutic delivery systems? Gelişmiş. İlaç Deliv. Rev. 91, 92 – 108 (2015). A critical review of studies implicating caveolae in nanoparticle uptake.
Richter, T. et al. High-resolution 3D quantitative analysis of caveolar ultrastructure and caveola–cytoskeleton interactions. Trafik 9, 893 – 909 (2008).
Chadda, R. et al. Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway. Trafik 8, 702 – 717 (2007).
Pelkmans, L., Kartenbeck, J. & Helenius, A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Celi Biol. 3, 473 – 483 (2001).
Parton, R. G. & Howes, M. T. Revisiting caveolin trafficking: the end of the caveosome. J. Hücre Biol. 191, 439 – 441 (2010).
Shin, J. S., Gao, Z. & Abraham, S. N. Involvement of cellular caveolae in bacterial entry into mast cells. Bilim 289, 785 – 788 (2000).
Rejman, J., Oberle, V., Zuhorn, I. S. & Hoekstra, D. Size-dependent internalization of particles via the pathways of clathrin- and caveolae-mediated endocytosis. Biyokimya. J. 377, 159 – 169 (2004).
Iversen, T.-G., Skotland, T. & Sandvig, K. Endositoz ve nanopartiküllerin hücre içi taşınması: mevcut bilgi ve gelecekteki çalışmalara ihtiyaç. Nano Bugün 6, 176 – 185 (2011).
Liebl, D., Qi, X., Zhe, Y., Barnett, T. C. & Teasdale, R. D. SopB-mediated recruitment of SNX18 facilitates Salmonella typhimurium internalization by the host cell. Ön. Hücre. Infect. Microbiol. 7, 257 (2017).
Aggeler, J. & Werb, Z. Initial events during phagocytosis by macrophages viewed from outside and inside the cell: membrane–particle interactions and clathrin. J. Hücre Biol. 94, 613 – 623 (1982).
Caracciolo, G. et al. Selective targeting capability acquired with a protein corona adsorbed on the surface of 1,2-dioleoyl-3-trimethylammonium propane/DNA nanoparticles. ACS Uyg. Mater. Arayüzler 5, 13171 – 13179 (2013).
Faria, M. vd. Biyo-nano deneysel literatürde minimum bilgi raporlama. Nat. Nanoteknoloji. 13, 777 – 785 (2018). Practical guidelines for studying nanoparticle uptake.
Francia, V., Reker-Smit, C., Boel, G. & Salvati, A. Limits and challenges in using transport inhibitors to characterize how nano-sized drug carriers enter cells. Nanotıp 14, 1533 – 1549 (2019).
Johnston, A. P. R. Life under the microscope: quantifying live cell interactions to improve nanoscale drug delivery. ACS Sensörleri 2, 4 – 9 (2017).
Liu, H. & Johnston, A. P. R. A programmable sensor to probe the internalization of proteins and nanoparticles in live cells. Ange. Kimya Int. Ed. 52, 5744 – 5748 (2013).
Selby, L. I., Aurelio, L., Yuen, D., Graham, B. & Johnston, A. P. R. Quantifying cellular internalization with a fluorescent click sensor. ACS Sensörleri 3, 1182 – 1189 (2018).
FitzGerald, L. I. & Johnston, A. P. R. It’s what’s on the inside that counts: techniques for investigating the uptake and recycling of nanoparticles and proteins in cells. J. Kolloid Arayüz Bilimi. 587, 64 – 78 (2021).
Pelkmans, L. et al. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Tabiat 436, 78 – 86 (2005).
Sundaramurthy, V. et al. Integration of chemical and RNAi multiparametric profiles identifies triggers of intracellular mycobacterial killing. Hücre Konakçı Mikrop 13, 129 – 142 (2013).
Jovic, M., Sharma, M., Rahajeng, J. & Caplan, S. The early endosome: a busy sorting station for proteins at the crossroads. Histol. Histopatol. 25, 99 – 112 (2010).
Kalaidzidis, I. et al. APPL endosomes are not obligatory endocytic intermediates but act as stable cargo-sorting compartments. J. Hücre Biol. 211, 123 – 144 (2015).
Zoncu, R. et al. A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes. Hücre 136, 1110 – 1121 (2009).
Eyster, C. A. et al. Discovery of new cargo proteins that enter cells through clathrin-independent endocytosis. Trafik 10, 590 – 599 (2009).
Maldonado-Báez, L., Cole, N. B., Krämer, H. & Donaldson, J. G. Microtubule-dependent endosomal sorting of clathrin-independent cargo by Hook1. J. Hücre Biol. 201, 233 – 247 (2013).
Khalil, I. A., Kogure, K., Futaki, S. & Harashima, H. High density of octaarginine stimulates macropinocytosis leading to efficient intracellular trafficking for gene expression. J. Biol. Chem. 281, 3544 – 3551 (2006).
Selby, L. I., Cortez-Jugo, C. M., Such, G. K. & Johnston, A. P. R. Nanoescapology: progress toward understanding the endosomal escape of polymeric nanoparticles. TELLER Nanomed. Nanobiotechnol. 9, e1452 (2017). A review of our current understanding of endosomal escape in relation to nanoparticle delivery.
Erazo-Oliveras, A. et al. The late endosome and its lipid BMP act as gateways for efficient cytosolic access of the delivery agent dfTAT and its macromolecular cargos. Hücre Kimyası. Biol. 23, 598 – 607 (2016).
Cupic, K. I., Rennick, J. J., Johnston, A. P. & Such, G. K. Controlling endosomal escape using nanoparticle composition: current progress and future perspectives. Nanotıp 14, 215 – 223 (2019).
Smith, S. A., Selby, L. I., Johnston, A. P. R. & Such, G. K. The endosomal escape of nanoparticles: toward more efficient cellular delivery. Bıoconjug. Chem. 30, 263 – 272 (2019).
Weigert, R. Imaging the dynamics of endocytosis in live mammalian tissues. Soğuk Bahar Harb. Perspet. Biol. 6, a017012 (2014).
Hinze, C. & Boucrot, E. Endocytosis in proliferating, quiescent and terminally differentiated cells. J. Celi Sci. 131, jcs216804 (2018).
Masedunskas, A., Porat-Shliom, N., Rechache, K., Aye, M.-P. & Weigert, R. Intravital microscopy reveals differences in the kinetics of endocytic pathways between cell cultures and live animals. Hücreler 1, 1121 – 1132 (2012).
Bhirde, A. A. et al. Targeted therapeutic nanotubes influence the viscoelasticity of cancer cells to overcome drug resistance. ACS Nano 8, 4177 – 4189 (2014).
Pinilla-Macua, I., Grassart, A., Duvvuri, U., Watkins, S. C. & Sorkin, A. EGF receptor signaling, phosphorylation, ubiquitylation and endocytosis in tumors in vivo. elife 6, e31993 (2017).
Ebrahim, S. & Weigert, R. Intravital microscopy in mammalian multicellular organisms. Curr. Opin. Celi Biol. 59, 97 – 103 (2019). A summary of state-of-the-art methods in intravital microscopy being used to study cell biology in vivo.
Fung, K. Y. Y., Fairn, G. D. & Lee, W. L. Transcellular vesicular transport in epithelial and endothelial cells: challenges and opportunities. Trafik 19, 5 – 18 (2018).
Joseph, S. R. et al. An ex vivo human tumor assay shows distinct patterns of EGFR trafficking in squamous cell carcinoma correlating to therapeutic outcomes. J. Yatırım. Dermatol. 139, 213 – 223 (2019). An imaging method to study ligand-induced epidermal growth factor receptor internalization in ex vivo human tumour samples.
Hansen, S. H., Sandvig, K. & van Deurs, B. Molecules internalized by clathrin-independent endocytosis are delivered to endosomes containing transferrin receptors. J. Hücre Biol. 123, 89 – 97 (1993).
Carpentier, J.-L. et al. Potassium depletion and hypertonic medium reduce non-coated and clathrin-coated pit formation, as well as endocytosis through these two gates. J. Celi. Physiol. 138, 519 – 526 (1989).
Larkin, J. M., Brown, M. S., Goldstein, J. L. & Anderson, R. G. W. Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts. Hücre 33, 273 – 285 (1983).
Daniel, J. A. et al. Phenothiazine-derived antipsychotic drugs inhibit dynamin and clathrin-mediated endocytosis. Trafik 16, 635 – 654 (2015).
Wang, L. H., Rothberg, K. G. & Anderson, R. G. W. Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J. Hücre Biol. 123, 1107 – 1117 (1993).
Sasso, L., Purdie, L., Grabowska, A., Jones, A. T. & Alexander, C. Time and cell-dependent effects of endocytosis inhibitors on the internalization of biomolecule markers and nanomaterials. J. Interdiscip. Nanomedicine 3, 67 – 81 (2018).
Chen, C.-L. et al. Inhibitors of clathrin-dependent endocytosis enhance TGF signaling and responses. J. Celi Sci. 122, 1863 – 1871 (2009).
von Kleist, L. et al. Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. Hücre 146, 471 – 484 (2011).
Dutta, D., Williamson, C. D., Cole, N. B. & Donaldson, J. G. Pitstop 2 is a potent inhibitor of clathrin-independent endocytosis. PLoS ONE 7, e45799 (2012).
Willox, A. K., Sahraoui, Y. M. E. & Royle, S. J. Non-specificity of Pitstop 2 in clathrin-mediated endocytosis. Biol. Açık 3, 326 – 331 (2014).
Macia, E. vd. Dynasore, hücre geçirgen bir dinamin inhibitörü. Dev. Hücre 10, 839 – 850 (2006).
McCluskey, A. et al. Building a better dynasore: the Dyngo compounds potently inhibit dynamin and endocytosis. Trafik 14, 1272 – 1289 (2013).
Park, R. J. et al. Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors. J. Celi Sci. 126, 5305 – 5312 (2013).
Kilsdonk, E. P. C. et al. Cellular cholesterol efflux mediated by cyclodextrins. J. Biol. Chem. 270, 17250 – 17256 (1995).
Hao, M., Mukherjee, S., Sun, Y. & Maxfield, F. R. Effects of cholesterol depletion and increased lipid unsaturation on the properties of endocytic membranes. J. Biol. Chem. 279, 14171 – 14178 (2004).
Bolard, J. How do the polyene macrolide antibiotics affect the cellular membrane properties? Biochim. Biophys. Acta Rev. Biomembr. 864, 257 – 304 (1986).
Rentero, C. et al. Functional implications of plasma membrane condensation for T cell activation. PLoS ONE 3, e2262 (2008).
Akiyama, T. et al. Genistein, a specific inhibitor of tyrosine-specific protein kinases. J. Biol. Chem. 262, 5592 – 5595 (1987).
Parton, R. G., Joggerst, B. & Simons, K. Regulated internalization of caveolae. J. Hücre Biol. 127, 1199 – 1215 (1994).
Brenner, S. L. & Korn, E. D. Substoichiometric concentrations of cytochalasin D inhibit actin polymerization. Additional evidence for an F-actin treadmill. J. Biol. Chem. 254, 9982 – 9985 (1979).
Fujimoto, L. M., Roth, R., Heuser, J. E. & Schmid, S. L. Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis. Trafik 1, 161 – 171 (2000).
Gladhaug, I. P. & Christoffersen, T. Amiloride inhibits constitutive internalization and increases the surface number of epidermal growth factor receptors in intact rat hepatocytes. J. Celi. Physiol. 143, 188 – 195 (1990).
Kleyman, T. R. & Cragoe, E. J. Amiloride and its analogs as tools in the study of ion transport. J. Membr. Biol. 105, 1 – 21 (1988).
Henriksen, L., Grandal, M. V., Knudsen, S. L. J., van Deurs, B. & Grøvdal, L. M. Internalization mechanisms of the epidermal growth factor receptor after activation with different ligands. PLoS ONE 8, e58148 (2013).
Ceresa, B. P., Kao, A. W., Santeler, S. R. & Pessin, J. E. Inhibition of clathrin-mediated endocytosis selectively attenuates specific insulin receptor signal transduction pathways. Mol. Hücre. Biol. 18, 3862 – 3870 (1998).
Liu, S.-H., Marks, M. S. & Brodsky, F. M. A dominant-negative clathrin mutant differentially affects trafficking of molecules with distinct sorting motifs in the class II major histocompatibility complex (MHC) pathway. J. Hücre Biol. 140, 1023 – 1037 (1998).
Hill, M. M. et al. PTRF-cavin, a conserved cytoplasmic protein required for caveola formation and function. Hücre 132, 113 – 124 (2008).
Liberali, P. et al. The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS. EMBO J. 27, 970 – 981 (2008).
Kalin, S. et al. Macropinocytotic uptake and infection of human epithelial cells with species B2 adenovirus type 35. J.Virol. 84, 5336 – 5350 (2010).
Licona-Limón, I., Garay-Canales, C. A., Muñoz-Paleta, O. & Ortega, E. CD13 mediates phagocytosis in human monocytic cells. J. Leukoc. Biyol. 98, 85 – 98 (2015).
Gambin, Y. et al. Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae. elife 3, e01434 (2014).
Bitsikas, V., Corrêa, I. R. & Nichols, B. J. Clathrin-independent pathways do not contribute significantly to endocytic flux. elife 3, e03970 (2014).
Arredouani, M. S. et al. MARCO Is the major binding receptor for unopsonized particles and bacteria on human alveolar macrophages. J. İmmünol. 175, 6058 – 6064 (2005).
Conner, S. D. & Schmid, S. L. Regulated portals of entry into the cell. Tabiat 422, 37 – 44 (2003).
King, J. S. & Kay, R. R. The origins and evolution of macropinocytosis. Philos. Trans. R. Soc. B 374, 20180158 (2019).
Yuan, M. et al. Enhanced human enterovirus 71 infection by endocytosis inhibitors reveals multiple entry pathways by enterovirus causing hand-foot-and-mouth diseases. Virol. J. 15, 1 (2018).
Volonte, D. et al. Caveolin-1 promotes the tumor suppressor properties of oncogene-induced cellular senescence. J. Biol. Chem. 293, 1794 – 1809 (2018).
Yang, C.-P. H., Galbiati, F., Volonté, D., Horwitz, S. B. & Lisanti, M. P. Upregulation of caveolin-1 and caveolae organelles in Taxol-resistant A549 cells. FEBS Lett. 439, 368 – 372 (1998).
Qhattal, H. S. S. & Liu, X. Characterization of CD44-mediated cancer cell uptake and intracellular distribution of hyaluronan-grafted liposomes. Mol. Ecz. 8, 1233 – 1246 (2011).
Yoon, Y.-K. et al. KRAS mutant lung cancer cells are differentially responsive to MEK inhibitor due to AKT or STAT3 activation: implication for combinatorial approach. Mol. kanserojen. 49, 353 – 362 (2010).
Yang, Y. et al. Endophilin A1 regulates dendritic spine morphogenesis and stability through interaction with p140Cap. Hücre Araş. 25, 496 – 516 (2015).
Torrino, S. et al. EHD2 is a mechanotransducer connecting caveolae dynamics with gene transcription. J. Hücre Biol. 217, 4092 – 4105 (2018).
Aït-Slimane, T., Galmes, R., Trugnan, G. & Maurice, M. Basolateral internalization of GPI-anchored proteins occurs via a clathrin-independent flotillin-dependent pathway in polarized hepatic cells. Mol. Biol. Hücre 20, 3792 – 3800 (2009).
Zhang, J. et al. Distinct functions of endophilin isoforms in synaptic vesicle endocytosis. Nöral Plast. 2015, 371496 (2015).
Moore, R. H. et al. Ligand-stimulated β2-adrenergic receptor internalization via the constitutive endocytic pathway into rab5-containing endosomes. J. Celi Sci. 108, 2983 – 2991 (1995).
Nonnenmacher, M. & Weber, T. Adeno-associated virus 2 infection requires endocytosis through the CLIC/GEEC pathway. Hücre Konakçı Mikrop 10, 563 – 576 (2011).
Chen, S.-L. et al. Endophilin-A2-mediated endocytic pathway is critical for enterovirus 71 entry into caco-2 cells. Ortaya çıktı. Mikroplar Bulaşır. 8, 773 – 786 (2019).
Mirre, C., Monlauzeur, L., Garcia, M., Delgrossi, M. H. & Le Bivic, A. Detergent-resistant membrane microdomains from Caco-2 cells do not contain caveolin. Am. J. Physiol. Celi Physiol. 271, C887-C894 (1996).
Zachos, N. C., Alamelumangpuram, B., Lee, L. J., Wang, P. & Kovbasnjuk, O. Carbachol-mediated endocytosis of NHE3 involves a clathrin-independent mechanism requiring lipid rafts and Cdc42. Hücre. Physiol. Biochem. 33, 869 – 881 (2014).
Ödeme PrimeXBT
AC Milan'ın Resmi CFD Ortaklarıyla Ticaret Yapın
Kaynak: https://www.nature.com/articles/s41565-021-00858-8