CD47 functions as a molecular switch for erythrocyte phagocytosis

Structure and function of the spleen

Mebius, R. E., & Kraal, G. (2005) · Nature reviews. Immunology · doi:10.1038/nri1669 · Cited by 2,245 · see citing works

Role of CD47 as a Marker of Self on Red Blood Cells

Oldenborg, P., Zheleznyak, A., Fang, Y., Lagenaur, C. F., Gresham, H. D., & Lindberg, F. P. (2000) · Science · doi:10.1126/science.288.5473.2051 · Cited by 1,975 · see citing works

Transfusion of red blood cells after prolonged storage produces harmful effects that are mediated by iron and inflammation

Hod, E. A., Zhang, N., Sokol, S. A., Wojczyk, B. S., Francis, R. O., Ansaldi, D., Francis, K. P., Della-Latta, P., Whittier, S., Sheth, S., et al. (2010) · Blood · doi:10.1182/blood-2009-10-245001 · Cited by 485 · see citing works

Functions and molecular mechanisms of the CD47–SIRPα signalling pathway

Matozaki, T., Murata, Y., Okazawa, H., & Ohnishi, H. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.12.001 · Cited by 477 · see citing works

Thrombospondins as matricellular modulators of cell function

BORNSTEIN, P. K. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12749 · Cited by 470 · see citing works

Cd47-Signal Regulatory Protein α (Sirpα) Regulates Fcγ and Complement Receptor–Mediated Phagocytosis

Oldenborg, P., Gresham, H. D., & Lindberg, F. P. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.7.855 · Cited by 453 · see citing works

Phosphatidylserine exposure and red cell viability in red cell aging and in hemolytic anemia

Boas, F. E., Forman, L., & Beutler, E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3077 · Cited by 405 · see citing works

Integrin-associated Protein Is a Receptor for the C-terminal Domain of Thrombospondin

Gao, A.-G., Lindberg, F. P., Finn, M. B., Blystone, S. D., Brown, E. J., & Frazier, W. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.21 · Cited by 402 · see citing works

Fatalities caused by TRALI

Holness, L. G., Knippen, M. A., Simmons, L., & Lachenbruch, P. A. (2004) · Transfusion Medicine Reviews · doi:10.1016/j.tmrv.2004.03.004 · Cited by 318 · see citing works

Signal-Regulatory Protein Is Selectively Expressed by Myeloid and Neuronal Cells

Adams, S., van der Laan, L. J. W., Vernon-Wilson, E. F., de Lavalette, C. R., Döpp, E. A., Dijkstra, C. D., Simmons, D. L., & van den Berg, T. K. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.4.1853 · Cited by 260 · see citing works

Bidirectional Negative Regulation of Human T and Dendritic Cells by CD47 and Its Cognate Receptor Signal-Regulator Protein-α: Down-Regulation of IL-12 Responsiveness and Inhibition of Dendritic Cell Activation

Latour, S., Tanaka, H., Demeure, C. E., Mateo, V., Rubio, M., Brown, E. J., Maliszewski, C. R., Lindberg, F. P., Oldenborg, A., Ullrich, A., et al. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.5.2547 · Cited by 238 · see citing works

Survival of red blood cells after transfusion: a comparison between red cells concentrates of different storage periods

Luten, M., Roerdinkholder‐Stoelwinder, B., Schaap, N. P., DeGrip, W. J., Bos, H. J., & Bosman, G. J. C. G. M. (2008) · Transfusion · doi:10.1111/j.1537-2995.2008.01734.x · Cited by 226 · see citing works

Storage of red blood cells: New approaches

Hess, J. R., & Greenwalt, T. G. (2002) · Transfusion Medicine Reviews · doi:10.1053/tmrv.2002.35212 · Cited by 203 · see citing works

Thrombospondins: from structure to therapeutics

Carlson, C. B., Lawler, J., & Mosher, D. F. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7484-1 · Cited by 194 · see citing works

Senescent cell antigen is immunologically related to band 3.

Kay, M. M. B., Goodman, S. R., Sørensen, K., Whitfield, C. F., Wong, P., Zaki, L., & RUDLOFF, V. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.6.1631 · Cited by 186 · see citing works

Localization of senescent cell antigen on band 3.

Kay, M. M. B. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.18.5753 · Cited by 176 · see citing works

Self inhibition of phagocytosis: The affinity of ‘marker of self’ CD47 for SIRPα dictates potency of inhibition but only at low expression levels

Tsai, R. K., Rodriguez, P. L., & Discher, D. E. (2010) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2010.02.016 · Cited by 143 · see citing works

sst2 Somatostatin Receptor Inhibits Cell Proliferation through Ras-, Rap1-, and B-Raf-dependent ERK2 Activation

Lahlou, H., Saint‐Laurent, N., Estève, J., Eychène, A., Pradayrol, L., Pyronnet, S., & Susini, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304524200 · Cited by 126 · see citing works

SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages

Ishikawa-Sekigami, T., Kaneko, Y., Okazawa, H., Tomizawa, T., Okajo, J., Saito, Y., Okuzawa, C., Sugawara-Yokoo, M., Nishiyama, U., Ohnishi, H., et al. (2005) · Blood · doi:10.1182/blood-2005-05-1896 · Cited by 119 · see citing works

Characteristics of red blood cell populations fractionated with a combination of counterflow centrifugation and Percoll separation

Bosch, F. H., Werre, J. M., Roerdinkholder‐Stoelwinder, B., Huls, T., Willekens, F. L. A., & Halie, M. (1992) · Blood · doi:10.1182/blood.v79.1.254.bloodjournal791254 · Cited by 111 · see citing works

Innate immune and non-immune mediators of erythrocyte clearance.

Lutz, H. U. (2004) · PubMed · Cited by 108 · see citing works

Nonphlogistic Clearance of Late Apoptotic Neutrophils by Macrophages: Efficient Phagocytosis Independent of β2 Integrins

Ren, Y., Stuart, L. M., Lindberg, F. P., Rosenkranz, A. R., Chen, Y., Mayadas, T. N., & Savill, J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.7.4743 · Cited by 106 · see citing works

The application of a new quantitative assay for the monitoring of integrin‐associated protein CD47 on red blood cells during storage and comparison with the expression of CD47 and phosphatidylserine with flow cytometry

Stewart, A., Urbaniak, S. J., Turner, M., & Bessos, H. (2005) · Transfusion · doi:10.1111/j.1537-2995.2005.00564.x · Cited by 92 · see citing works

Expression of CD47 (integrin-associated protein) decreases on red blood cells during storage

Anniss, A. M., & Sparrow, R. L. (2002) · Transfusion and Apheresis Science · doi:10.1016/s1473-0502(02)00070-8 · Cited by 92 · see citing works

CD47 on experimentally senescent murine RBCs inhibits phagocytosis following Fcγ receptor–mediated but not scavenger receptor–mediated recognition by macrophages

Olsson, M., & Oldenborg, P. (2008) · Blood · doi:10.1182/blood-2008-03-143008 · Cited by 85 · see citing works

The Structure of the Macrophage Signal Regulatory Protein α (SIRPα) Inhibitory Receptor Reveals a Binding Face Reminiscent of That Used by T Cell Receptors

Hatherley, D., Harlos, K., Dunlop, D. C., Stuart, D. I., & Barclay, A. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611511200 · Cited by 78 · see citing works

Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin

Brittain, J. E., Mlinar, K. J., Anderson, C., Orringer, E. P., & Parise, L. V. (2001) · Blood · doi:10.1182/blood.v97.7.2159 · Cited by 71 · see citing works

Tethering of Apoptotic Cells to Phagocytes through Binding of CD47 to Src Homology 2 Domain-Bearing Protein Tyrosine Phosphatase Substrate-1

Tada, K., Tanaka, M., Hanayama, R., Miwa, K., Shinohara, A., Iwamatsu, A., & Nagata, S. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.11.5718 · Cited by 70 · see citing works

A hallmark of immunoreceptor, the tyrosine‐based inhibitory motif ITIM, is present in the G protein‐coupled receptor OX1R for orexins and drives apoptosis: a novel mechanism

Voisin, T., Firar, A. E., Rouyer‐Fessard, C., Gratio, V., & Laburthe, M. (2008) · The FASEB Journal · doi:10.1096/fj.07-098723 · Cited by 65 · see citing works

SHPS-1 Induces Aggregation of Ba/F3 Pro-B Cells Via an Interaction with CD47

Babić, I., Schallhorn, A., Lindberg, F. P., & Jirik, F. R. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.7.3652 · Cited by 52 · see citing works

Dose-dependent inhibitory effect of CD47 in macrophage uptake of IgG-opsonized murine erythrocytes

Olsson, M., Nilsson, A. K., & Oldenborg, P. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.11.002 · Cited by 52 · see citing works

Ligation of CD47 mediates phosphatidylserine expression on erythrocytes and a concomitant loss of viability in vitro

Head, D. J., Lee, Z. E., Swallah, M. M., & Avent, N. D. (2005) · British Journal of Haematology · doi:10.1111/j.1365-2141.2005.05668.x · Cited by 51 · see citing works

An improved red blood cell additive solution maintains 2,3‐diphosphoglycerate and adenosine triphosphate levels by an enhancing effect on phosphofructokinase activity during cold storage

Burger, P., Korsten, H., de Korte, D., Rombout‐Sestrienkova, E., van Bruggen, R., & Verhoeven, A. J. (2010) · Transfusion · doi:10.1111/j.1537-2995.2010.02700.x · Cited by 46 · see citing works

Phosphatidylserine-positive erythrocytes bind to immobilized and soluble thrombospondin-1 via its heparin-binding domain

Betal, S. G., & Setty, Y. (2008) · Translational research · doi:10.1016/j.trsl.2008.07.007 · Cited by 44 · see citing works

The Red Pulp of the Spleen: Structural Basis of Blood Flow

WEISS, L. P. (1983) · Clinics in Haematology · doi:10.1016/s0308-2261(21)00392-1 · Cited by 41 · see citing works

Functional Elements on SIRPα IgV Domain Mediate Cell Surface Binding to CD47

Liu, Y., Tong, Q. Z., Zhou, Y., Lee, H., Yang, J. J., Bühring, H., Chen, Y.-T., Ha, B., Chen, C. X.-J., Yang, Y., et al. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.09.079 · Cited by 40 · see citing works

Membrane mobility and clustering of Integrin Associated Protein (IAP, CD47)—Major differences between mouse and man and implications for signaling

Subramanian, S., Tsai, R., Sen, S., Dahl, K. N., & Discher, D. E. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2006.01.012 · Cited by 39 · see citing works

Residue Gln-30 of human erythrocyte anion transporter is a prime site for reaction with intrinsic transglutaminase.

Murthy, S. N. P., Wilson, J., Zhang, Y., & Lorand, L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31731-3 · Cited by 35 · see citing works

Hereditary sideroblastic anemia and glucose-6-phosphate dehydrogenase deficiency in a negro family

Prasad, A. S., Tranchida, L., Konno, E. T., Berman, L., Albert, S., Sing, C. F., & Brewer, G. J. (1968) · Journal of Clinical Investigation · doi:10.1172/jci105833 · Cited by 34 · see citing works

Trans-endocytosis of CD47 and SHPS-1 and its role in regulation of the CD47–SHPS-1 system

Kusakari, S., Ohnishi, H., Jin, F.-J., Kaneko, Y., Murata, T., Murata, Y., Okazawa, H., & Matozaki, T. (2008) · Journal of Cell Science · doi:10.1242/jcs.025015 · Cited by 33 · see citing works

The Carboxy-Terminal Cell-Binding Domain of Thrombospondin Is Essential for Sickle Red Blood Cell Adhesion

Hillery, C. A., Scott, J. P., & Du, M. C. (1999) · Blood · doi:10.1182/blood.v94.1.302.413k38_302_309 · Cited by 27 · see citing works

The thalassemic red cell membrane.

Wilairat, P., Kittikalayawong, A., & Chaicharoen, S. (1992) · PubMed · Cited by 23 · see citing works

Structural physiology of the human spleen.

Barnhart, M. I., & Jm, L. (1979) · PubMed · Cited by 22 · see citing works

Regulation of multiple functions of SHPS-1, a transmembrane glycoprotein, by its cytoplasmic region

Sato, R., Ohnishi, H., Kobayashi, H., Kiuchi, D., Hayashi, A., Kaneko, Y., Honma, N., Okazawa, H., Hirata, Y., & Matozaki, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.08.031 · Cited by 20 · see citing works

Regulation of membrane band 3 Tyr-phosphorylation by proteolysis of p72Syk and possible involvement in senescence process

Bordin, L., Fiore, C., Bragadin, M., Brunati, A. M., & Clari, G. (2009) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmp071 · Cited by 20 · see citing works

Mechanisms of red cell clearance in favism.

Fischer, T., Pescarmona, G., Bosìa, A., Naitana, A. F., Turrini, F., & Arese, P. (1983) · PubMed · Cited by 5 · see citing works

Nanoparticle uptake: The phagocyte problem

Gustafson, H. H., Holt‐Casper, D., Grainger, D. W., & Ghandehari, H. (2015) · Nano Today · doi:10.1016/j.nantod.2015.06.006 · Cited by 1,424 · see citing works

Alveolar macrophages: plasticity in a tissue-specific context

Hussell, T., & Bell, T. J. (2014) · Nature Reviews Immunology · doi:10.1038/nri3600 · Cited by 1,377 · see citing works

The Interaction Between Signal Regulatory Protein Alpha (SIRPα) and CD47: Structure, Function, and Therapeutic Target

Barclay, A. N., & van den Berg, T. K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120142 · Cited by 841 · see citing works

Pre-Clinical Development of a Humanized Anti-CD47 Antibody with Anti-Cancer Therapeutic Potential

Liu, J., Wang, L., Zhao, F., Tseng, S., Narayanan, C., Shura, L., Willingham, S. B., Howard, M., Prohaska, S. S., Volkmer, J. P., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137345 · Cited by 479 · see citing works

Primitive and definitive erythropoiesis in mammals

Palis, J. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00003 · Cited by 442 · see citing works

Advances in Anti-Tumor Treatments Targeting the CD47/SIRPα Axis

Zhang, W., Huang, Q., Xiao, W., Zhao, Y., Pi, J., Xu, H., Zhao, H., Xu, J., Evans, C. E., & Jin, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00018 · Cited by 352 · see citing works

Anti-CD47 Treatment Stimulates Phagocytosis of Glioblastoma by M1 and M2 Polarized Macrophages and Promotes M1 Polarized Macrophages In Vivo

Zhang, M., Hütter, G., Kahn, S. A., Azad, T. D., Gholamin, S., Xu, C. Y., Liu, J., Achrol, A. S., Richard, C., Sommerkamp, P., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153550 · Cited by 327 · see citing works

Of macrophages and red blood cells; a complex love story

de Back, D. Z., Kostova, E., van Kraaij, M., van den Berg, T. K., & van Bruggen, R. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00009 · Cited by 325 · see citing works

An update on red blood cell storage lesions, as gleaned through biochemistry and omics technologies

D’Alessandro, A., Kriebardis, A. G., Rinalducci, S., Antonelou, M. H., Hansen, K. C., Papassideri, I. S., & Zolla, L. (2014) · Transfusion · doi:10.1111/trf.12804 · Cited by 324 · see citing works

Squeezing for Life – Properties of Red Blood Cell Deformability

Huisjes, R., Bogdanova, A. Y., van Solinge, W. W., Schiffelers, R. M., Kaestner, L., & van Wijk, R. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00656 · Cited by 325 · see citing works

Red blood cell storage lesion: causes and potential clinical consequences.

Yoshida, T., Prudent, M., & D’Alessandro, A. (1969) · Blood transfusion · doi:10.2450/2019.0217-18 · Cited by 329 · see citing works

Mechanisms and Consequences of Defective Efferocytosis in Atherosclerosis

Yurdagul, A., Doran, A. C., Cai, B., Fredman, G., & Tabas, I. A. (2018) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2017.00086 · Cited by 300 · see citing works

The Role of Iron Regulation in Immunometabolism and Immune-Related Disease

Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works

Emerging phagocytosis checkpoints in cancer immunotherapy

Liu, Y., Wang, Y., Yang, Y., Weng, L., Wu, Q., Zhang, J., Zhao, P., Fang, L., Shi, Y., & Wang, P. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01365-z · Cited by 287 · see citing works

TTI-621 (SIRPαFc): A CD47-Blocking Innate Immune Checkpoint Inhibitor with Broad Antitumor Activity and Minimal Erythrocyte Binding

Petrova, P. S., Viller, N. N., Wong, M., Pang, X., Lin, G. H. Y., Dodge, K., Chai, V., Chen, H., Lee, V., House, V., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-1700 · Cited by 277 · see citing works

Surface modification of nanoparticles enables selective evasion of phagocytic clearance by distinct macrophage phenotypes

Qie, Y., Yuan, H., Roemeling, C. A. V., Chen, Y., Liu, X., Shih, K. D., Knight, J. A., Tun, H. W., Wharen, R. E., Jiang, W., et al. (2016) · Scientific Reports · doi:10.1038/srep26269 · Cited by 259 · see citing works

From the Cradle to the Grave: The Role of Macrophages in Erythropoiesis and Erythrophagocytosis

Klei, T. R. L., Meinderts, S. M., van den Berg, T. K., & van Bruggen, R. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00073 · Cited by 262 · see citing works

CD47: A Cell Surface Glycoprotein Which Regulates Multiple Functions of Hematopoietic Cells in Health and Disease

Oldenborg, P. (2013) · ISRN Hematology · doi:10.1155/2013/614619 · Cited by 235 · see citing works

Mechanisms tagging senescent red blood cells for clearance in healthy humans

Lutz, H. U., & Bogdanova, A. Y. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00387 · Cited by 219 · see citing works

DNA binding to TLR9 expressed by red blood cells promotes innate immune activation and anemia

Lam, L., Murphy, S., Kokkinaki, D., Venosa, A., Sherrill-Mix, S. A., Casu, C., Rivella, S., Weiner, A. I., Park, J., Shin, S., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abj1008 · Cited by 209 · see citing works

Macrophages: sentinels and regulators of the immune system

Franken, L., Schiwon, M., & Kurts, C. (2016) · Cellular Microbiology · doi:10.1111/cmi.12580 · Cited by 211 · see citing works

Splenic Macrophage Subsets and Their Function during Blood-Borne Infections

da Silva, H. B., Fonseca, R., Pereira, R. M., Cassado, A. D. A., Álvarez, J. M., & Lima, M. R. D. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00480 · Cited by 201 · see citing works

Recent advances in long-acting drug delivery systems for anticancer drug

Pacheco, C., Baião, A., Ding, T., Cui, W., & Sarmento, B. F. C. C. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.114724 · Cited by 195 · see citing works

Inborn defects in the antioxidant systems of human red blood cells

van Zwieten, R., Verhoeven, A. J., & Roos, D. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.11.022 · Cited by 179 · see citing works

Functions of Thrombospondin-1 in the Tumor Microenvironment

Kaur, S., Bronson, S. M., Pal-Nath, D., Miller, T. W., Soto‐Pantoja, D. R., & Roberts, D. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094570 · Cited by 177 · see citing works

The CD47-SIRP signalling system: its physiological roles and therapeutic application

Murata, Y., Kotani, T., Ohnishi, H., & Matozaki, T. (2014) · The Journal of Biochemistry · doi:10.1093/jb/mvu017 · Cited by 171 · see citing works

Measures of stored red blood cell quality

Hess, J. R. (2014) · Vox Sanguinis · doi:10.1111/vox.12130 · Cited by 163 · see citing works

Cell rigidity and shape override CD47’s “self”-signaling in phagocytosis by hyperactivating myosin-II

Sosale, N. G., Rouhiparkouhi, T., Bradshaw, A. M., Dimova, R., Lipowsky, R., & Discher, D. E. (2014) · Blood · doi:10.1182/blood-2014-06-585299 · Cited by 154 · see citing works

Cell death by phagocytosis

Brown, G. C. (2024) · Nature Reviews Immunology · doi:10.1038/s41577-023-00921-6 · Cited by 129 · see citing works

Eryptosis in health and disease: A paradigm shift towards understanding the (patho)physiological implications of programmed cell death of erythrocytes

Qadri, S. M., Bissinger, R., Solh, Z., & Oldenborg, P. (2017) · Blood Reviews · doi:10.1016/j.blre.2017.06.001 · Cited by 125 · see citing works

Hematoma Changes During Clot Resolution After Experimental Intracerebral Hemorrhage

Cao, S., Zheng, M., Hua, Y., Chen, G., Keep, R. F., & Xi, G. (2016) · Stroke · doi:10.1161/strokeaha.116.013146 · Cited by 123 · see citing works

Comparison of exosomes and ferritin protein nanocages for the delivery of membrane protein therapeutics

Cho, E., Nam, G., Hong, Y., Kim, Y. K., Kim, D., Yang, Y., & Kim, I. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.04.037 · Cited by 114 · see citing works

Delivery of Drugs Bound to erythrocytes: New Avenues for an Old Intravascular Carrier

Villa, C. H., Pan, D. C., Zaitsev, S. V., Cines, D. B., Siegel, D. L., & Muzykantov, V. R. (2015) · Therapeutic Delivery · doi:10.4155/tde.15.34 · Cited by 114 · see citing works

Loss of Cell Surface CD47 Clustering Formation and Binding Avidity to SIRPα Facilitate Apoptotic Cell Clearance by Macrophages

Lv, Z., Bian, Z., Shi, L., Niu, S., Ha, B., Tremblay, A., Li, L., Zhang, X., Paluszynski, J. P., Liu, M., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401719 · Cited by 114 · see citing works

The Phagocytic Code Regulating Phagocytosis of Mammalian Cells

Cockram, T. O. J., Dundee, J. M., Popescu, A. S., & Brown, G. C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.629979 · Cited by 111 · see citing works

Functions and development of red pulp macrophages

Kurotaki, D., Uede, T., & Tamura, T. (2015) · Microbiology and Immunology · doi:10.1111/1348-0421.12228 · Cited by 111 · see citing works

Advances in refunctionalization of erythrocyte-based nanomedicine for enhancing cancer-targeted drug delivery

Sun, D., Chen, J., Wang, Y., Ji, H., Peng, R., Jin, L., & Wu, W. (2019) · Theranostics · doi:10.7150/thno.36510 · Cited by 113 · see citing works

Putting the brakes on phagocytosis: “don't-eat-me” signaling in physiology and disease

Kelley, S. M., & Ravichandran, K. S. (2021) · EMBO Reports · doi:10.15252/embr.202152564 · Cited by 110 · see citing works

Crosstalk between Red Blood Cells and the Immune System and Its Impact on Atherosclerosis

Buttari, B., Profumo, E., & Riganò, R. (2015) · BioMed Research International · doi:10.1155/2015/616834 · Cited by 107 · see citing works

Application of advances in endocytosis and membrane trafficking to drug delivery

Ju, Y., Guo, H., Edman, M. C., & Hamm‐Alvarez, S. F. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.07.026 · Cited by 107 · see citing works

PLGA's Plight and the Role of Stealth Surface Modification Strategies in Its Use for Intravenous Particulate Drug Delivery

Sheffey, V. V., Siew, E. B., Tanner, E. E. L., & Eniola‐Adefeso, O. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202101536 · Cited by 103 · see citing works

Immune cells as tumor drug delivery vehicles

Combes, F., Meyer, E., & Sanders, N. N. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.07.043 · Cited by 98 · see citing works

Red Blood Cell Clearance in Inflammation

Straat, M., van Bruggen, R., de Korte, D., & Juffermans, N. P. (2012) · Transfusion Medicine and Hemotherapy · doi:10.1159/000342229 · Cited by 99 · see citing works

Abnormal erythropoiesis and the pathophysiology of chronic anemia

Koury, M. J. (2014) · Blood Reviews · doi:10.1016/j.blre.2014.01.002 · Cited by 96 · see citing works

Donor variation effect on red blood cell storage lesion: a multivariable, yet consistent, story

Tzounakas, V. L., Georgatzakou, H. Τ., Kriebardis, A. G., Voulgaridou, A. I., Stamoulis, K. E., Foudoulaki‐Paparizos, L. E., Antonelou, M. H., & Papassideri, I. S. (2016) · Transfusion · doi:10.1111/trf.13582 · Cited by 94 · see citing works

Physical Properties of Blood and their Relationship to Clinical Conditions

Alexy, T., Detterich, J. A., Connes, P., Tóth, K., Nader, É., Kenyeres, P., Arriola‐Montenegro, J., Ülker, P., & Simmonds, M. J. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.906768 · Cited by 94 · see citing works

Emerging functions of thrombospondin-1 in immunity

Kaur, S., & Roberts, D. D. (2024) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2023.05.008 · Cited by 96 · see citing works

Erythrocytes and their role as health indicator: Using structure in a patient-orientated precision medicine approach

Pretorius, E., Olumuyiwa-Akeredolu, O.-O. O., Mbotwe, S., & Bester, J. (2016) · Blood Reviews · doi:10.1016/j.blre.2016.01.001 · Cited by 91 · see citing works

Survival of red blood cells after transfusion: processes and consequences

Bosman, G. J. C. G. M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00376 · Cited by 90 · see citing works

Reversible binding of hemoglobin to band 3 constitutes the molecular switch that mediates O2 regulation of erythrocyte properties

Chu, H., McKenna, M. M., Krump, N. A., Zheng, S., Mendelsohn, L. G., Thein, S. L., Garrett, L. J., Bodine, D. M., & Low, P. S. (2016) · Blood · doi:10.1182/blood-2016-01-692079 · Cited by 89 · see citing works

Red Blood Cell Extracellular Vesicle-Based Drug Delivery: Challenges and Opportunities

Chiangjong, W., Netsirisawan, P., Hongeng, S., & Chutipongtanate, S. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.761362 · Cited by 85 · see citing works

Transgenic Expression of Human CD47 Markedly Increases Engraftment in a Murine Model of Pig-to-Human Hematopoietic Cell Transplantation

Tena, A., Kurtz, J., Leonard, D. A., Dobrinsky, J. R., Terlouw, S. L., Mtango, N. R., Verstegen, J., Germana, S. K., Mallard, C. A., Arn, J. S., et al. (2014) · American Journal of Transplantation · doi:10.1111/ajt.12918 · Cited by 88 · see citing works

Spherocytic shift of red blood cells during storage provides a quantitative whole cell–based marker of the storage lesion

Roussel, C., Dussiot, M., Marin, M., Morel, A., Ndour, P. A., Duez, J., Kim, C. L. V., Hermine, O., Colin, Y., Buffet, P. A., et al. (2017) · Transfusion · doi:10.1111/trf.14015 · Cited by 84 · see citing works

Y‐RNA subtype ratios in plasma extracellular vesicles are cell type‐ specific and are candidate biomarkers for inflammatory diseases

Driedonks, T. A. P., Mol, S., de Bruin, S., Peters, A.-L., Zhang, X., Lindenbergh, M. F. S., Beuger, B. M., van Stalborch, A.-M. D., Spaan, T., de Jong, E. C., et al. (2020) · Journal of Extracellular Vesicles · doi:10.1080/20013078.2020.1764213 · Cited by 84 · see citing works

How do red blood cells know when to die?

Arias, C. F., & Arias, C. (2017) · Royal Society Open Science · doi:10.1098/rsos.160850 · Cited by 81 · see citing works

Red Blood Cells-Derived Vesicles for Delivery of Lipophilic Drug Camptothecin

Malhotra, S., Dumoga, S., Sirohi, P., & Singh, N. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b04827 · Cited by 79 · see citing works

CD47 Agonist Peptides Induce Programmed Cell Death in Refractory Chronic Lymphocytic Leukemia B Cells via PLCγ1 Activation: Evidence from Mice and Humans

Martínez‐Torres, A. C., Quiney, C., Attout, T., Boullet, H., Herbi, L., Vela, L., Barbier, S., Château, D., Chapiro, É., Nguyen‐Khac, F., et al. (2015) · PLoS Medicine · doi:10.1371/journal.pmed.1001796 · Cited by 76 · see citing works

Hemolysis in the spleen drives erythrocyte turnover

Klei, T. R. L., Dalimot, J. J., Nota, B., Veldthuis, M., Mul, E. P. J., Rademakers, T., Hoogenboezem, M., Nagelkerke, S. Q., van IJcken, W. F. J., Oole, E., et al. (2020) · Blood · doi:10.1182/blood.2020005351 · Cited by 74 · see citing works

Development of a prosaposin-derived therapeutic cyclic peptide that targets ovarian cancer via the tumor microenvironment

Wang, S., Blois, A. L., Rayes, T. E., Liu, J. F., Hirsch, M. S., Gravdal, K., Palakurthi, S. S., Bielenberg, D. R., Akslen, L. A., Drapkin, R., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad5653 · Cited by 71 · see citing works

Detection of Immune Checkpoint Receptors – A Current Challenge in Clinical Flow Cytometry

Shibru, B., Fey, K., Fricke, S., Blaudszun, A., Fürst, F., Weise, M., Seiffert, S., Weyh, M. K., Koehl, U., Sack, U., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.694055 · Cited by 68 · see citing works

Neutrophils acquire antigen-presenting cell features after phagocytosis of IgG-opsonized erythrocytes

Meinderts, S. M., Baker, G., van Wijk, S. W., Beuger, B. M., Geissler, J., Jansen, M. H., Saris, A., ten Brinke, A., Kuijpers, T. W., van den Berg, T. K., et al. (2019) · Blood Advances · doi:10.1182/bloodadvances.2018028753 · Cited by 68 · see citing works

Immunological barriers to haematopoietic stem cell gene therapy

Charlesworth, C. T., Hsu, I., Wilkinson, A. C., & Nakauchi, H. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00698-0 · Cited by 67 · see citing works

Manipulating Eryptosis of Human Red Blood Cells: A Novel Antimalarial Strategy?

Boulet, C., Doerig, C., & Carvalho, T. G. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00419 · Cited by 68 · see citing works

Engineering polymer nanoparticles using cell membrane coating technology and their application in cancer treatments: Opportunities and challenges

Guo, K., Xiao, N.-Y., Liu, Y., Wang, Z.-M., Tóth, J., Gyenis, J., Thakur, V., Oyane, A., & Shubhra, Q. T. (2021) · Nano Materials Science · doi:10.1016/j.nanoms.2021.12.001 · Cited by 61 · see citing works

Platelet-Like Gold Nanostars for Cancer Therapy: The Ability to Treat Cancer and Evade Immune Reactions

Kim, M. W., Lee, G., Niidome, T., Komohara, Y., Lee, A., & Park, Y. I. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00133 · Cited by 66 · see citing works

Therapeutic opportunities for targeting the ubiquitous cell surface receptor CD47

Soto‐Pantoja, D. R., Stein, E. V., Rogers, N. M., Sharifi‐Sanjani, M., Isenberg, J. S., & Roberts, D. D. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.733699 · Cited by 65 · see citing works

Acute CD47 Blockade During Ischemic Myocardial Reperfusion Enhances Phagocytosis-Associated Cardiac Repair

Zhang, S., Yeap, X., DeBerge, M., Naresh, N. K., Wang, K., Jiang, Z., Wilcox, J. E., White, S. M., Morrow, J., Burridge, P. W., et al. (2017) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2017.03.013 · Cited by 63 · see citing works

Targeting CD47/TNFAIP8 by miR-155 overcomes drug resistance and inhibits tumor growth through induction of phagocytosis and apoptosis in multiple myeloma

Rastgoo, N., Wu, J., Liu, M., Pourabdollah, M., Atenafu, E. G., Reece, D. E., Chen, W., & Chang, H. (2019) · Haematologica · doi:10.3324/haematol.2019.227579 · Cited by 62 · see citing works

Preclinical and clinical development of therapeutic antibodies targeting functions of CD47 in the tumor microenvironment

Kaur, S., Cicalese, K. V., Banerjee, R., & Roberts, D. D. (2020) · Antibody Therapeutics · doi:10.1093/abt/tbaa017 · Cited by 63 · see citing works

The Multiple Facets of Iron Recycling

Slusarczyk, P., & Mleczko‐Sanecka, K. (2021) · Genes · doi:10.3390/genes12091364 · Cited by 60 · see citing works

Genetically Engineered‐Cell‐Membrane Nanovesicles for Cancer Immunotherapy

Cheng, Q., Kang, Y., Yao, B. W., Dong, J., Zhu, Y., He, Y., & Ji, X. (2023) · Advanced Science · doi:10.1002/advs.202302131 · Cited by 60 · see citing works

Measurement of Posttransfusion Red Cell Survival With the Biotin Label

Mock, D. M., Widness, J. A., Veng‐Pedersen, P., Strauss, R. G., Cancelas, J. A., Cohen, R. M., Lindsell, C. J., & Franco, R. S. (2014) · Transfusion Medicine Reviews · doi:10.1016/j.tmrv.2014.03.003 · Cited by 63 · see citing works

Microfluidic study of retention and elimination of abnormal red blood cells by human spleen with implications for sickle cell disease

Qiang, Y., Sissoko, A., Liu, Z. L., Dong, T., Zheng, F., Kong, F., Higgins, J. M., Karniadakis, G. E., Buffet, P. A., Suresh, S., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217607120 · Cited by 59 · see citing works

Utilization and quality of cryopreserved red blood cells in transfusion medicine

Henkelman, S., Noorman, F., Badloe, J. F., & Lagerberg, J. W. M. (2014) · Vox Sanguinis · doi:10.1111/vox.12218 · Cited by 58 · see citing works

Plasmodium falciparum malaria and invasive bacterial co-infection in young African children: the dysfunctional spleen hypothesis

Gómez-Pérez, G. P., van Bruggen, R., Grobusch, M. P., & Dobaño, C. (2014) · Malaria Journal · doi:10.1186/1475-2875-13-335 · Cited by 59 · see citing works

Aging and glycation promote erythrocyte phagocytosis by human endothelial cells: Potential impact in atherothrombosis under diabetic conditions

Catan, A., Turpin, C., Diotel, N., Patché, J., Guérin-Dubourg, A., Debussche, X., Bourdon, E., Ah-You, N., Moullec, N. L., Besnard, M., et al. (2019) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2019.10.015 · Cited by 58 · see citing works

Phagoptosis - Cell Death By Phagocytosis - Plays Central Roles in Physiology, Host Defense and Pathology

Brown, G. C., Vilalta, A., & Fricker, M. (2015) · Current Molecular Medicine · doi:10.2174/156652401509151105130628 · Cited by 58 · see citing works

Insights into red blood cell storage lesion: Toward a new appreciation

Antonelou, M. H., & Seghatchian, J. (2016) · Transfusion and Apheresis Science · doi:10.1016/j.transci.2016.10.019 · Cited by 57 · see citing works

CD47 as a promising therapeutic target in oncology

Hai, Z., Song, S., Ma, J., Yan, Z., Xie, H., Feng, Y., & Che, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.757480 · Cited by 56 · see citing works

Cancer Therapy Targeting CD47/SIRPα

Dizman, N., & Buchbinder, E. I. (2021) · Cancers · doi:10.3390/cancers13246229 · Cited by 53 · see citing works

Stored red blood cell transfusions: iron, inflammation, immunity, and infection

Spitalnik, S. L. (2014) · Transfusion · doi:10.1111/trf.12848 · Cited by 53 · see citing works

Deformability based sorting of stored red blood cells reveals donor-dependent aging curves

Islamzada, E., Matthews, K., Guo, Q., Santoso, A. T., Duffy, S. P., Scott, M. D., & Ma, H. (2019) · Lab on a Chip · doi:10.1039/c9lc01058k · Cited by 52 · see citing works

Aging‐associated changes in CD47 arrangement and interaction with thrombospondin‐1 on red blood cells visualized by super‐resolution imaging

Wang, F., Liu, Y., Zhang, T., Gao, J., Xu, Y., Xie, G., Zhao, W., Wang, H., & Yang, Y. (2020) · Aging Cell · doi:10.1111/acel.13224 · Cited by 51 · see citing works

Crosstalk between Heme Oxygenase-1 and Iron Metabolism in Macrophages: Implications for the Modulation of Inflammation and Immunity

de Oliveira, J., Denadai, M. B., & Costa, D. L. (2022) · Antioxidants · doi:10.3390/antiox11050861 · Cited by 53 · see citing works

Artificial cells for in vivo biomedical applications through red blood cell biomimicry

Waeterschoot, J., Gosselé, W., Lemež, Š., & Solvas, X. C. I. (2024) · Nature Communications · doi:10.1038/s41467-024-46732-8 · Cited by 50 · see citing works

CD47 regulates the phagocytic clearance and replication of the Plasmodium yoelii malaria parasite

Banerjee, R., Khandelwal, S., Kozakai, Y., Sahu, B. R., & Kumar, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1418144112 · Cited by 50 · see citing works

Erythrocytes: Central Actors in Multiple Scenes of Atherosclerosis

Turpin, C., Catan, A., Meilhac, O., Bourdon, E., Canonne‐Hergaux, F., & Rondeau, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115843 · Cited by 51 · see citing works

CD47-SIRPα Interactions Regulate Macrophage Uptake of Plasmodium falciparum-Infected Erythrocytes and Clearance of Malaria In Vivo

Ayi, K., Lu, Z., Serghides, L., Ho, J., Finney, C. A. M., Wang, J. C. Y., Liles, W. C., & Kain, K. C. (2016) · Infection and Immunity · doi:10.1128/iai.01426-15 · Cited by 49 · see citing works

Update on extracellular vesicles inside red blood cell storage units: Adjust the sails closer to the new wind

Antonelou, M. H., & Seghatchian, J. (2016) · Transfusion and Apheresis Science · doi:10.1016/j.transci.2016.07.016 · Cited by 48 · see citing works

Mononuclear phagocytes as a target, not a barrier, for drug delivery

Yong, S., Song, Y., Kim, H. J., Ain, Q. U., & Kim, Y. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.01.024 · Cited by 47 · see citing works

Human and murine splenic neutrophils are potent phagocytes of IgG-opsonized red blood cells

Meinderts, S. M., Oldenborg, P., Beuger, B. M., Klei, T. R. L., Johansson, J., Kuijpers, T. W., Matozaki, T., Huisman, E. J., de Haas, M., van den Berg, T. K., et al. (2017) · Blood Advances · doi:10.1182/bloodadvances.2017004671 · Cited by 48 · see citing works

Multinucleated Giant Cells in Experimental Intracerebral Hemorrhage

Wei, J., Wang, M., Jing, C., Keep, R. F., Hua, Y., & Xi, G. (2020) · Translational Stroke Research · doi:10.1007/s12975-020-00790-4 · Cited by 47 · see citing works

How the spleen reshapes and retains young and old red blood cells: A computational investigation

Li, H., Liu, Z. L., Lu, L., Buffet, P. A., & Karniadakis, G. E. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009516 · Cited by 45 · see citing works

Processing methods and storage duration impact extracellular vesicle counts in red blood cell units

Gamonet, C., Desmarets, M., Mourey, G., Biichlé, S., Aupet, S., Laheurte, C., François, A. I., Resch, É., Bigey, F., Binda, D., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2020001658 · Cited by 44 · see citing works

Gateway to Understanding Microparticles: Standardized Isolation and Identification of Plasma Membrane-Derived Vesicles

Dinkla, S., Brock, R. E., Joosten, I., & Bosman, G. J. C. G. M. (2013) · Nanomedicine · doi:10.2217/nnm.13.149 · Cited by 43 · see citing works

Fluorogenic 2D Peptidosheet Unravels CD47 as a Potential Biomarker for Profiling Hepatocellular Carcinoma and Cholangiocarcinoma Tissues

Ma, Y., Dou, W., Pan, Y., Dong, L., Tan, Y., He, X., Tian, H., & Wang, H. (2016) · Advanced Materials · doi:10.1002/adma.201604253 · Cited by 42 · see citing works

Biomimetic erythrocytes engineered drug delivery for cancer therapy

Zhang, W., Zhao, M., Gao, Y., Xu, C., Liu, X., Tang, S., Peng, Y., Wang, N., Hu, D., Peng, H., et al. (2021) · Chemical Engineering Journal · doi:10.1016/j.cej.2021.133498 · Cited by 41 · see citing works

Mechanical clearance of red blood cells by the human spleen: Potential therapeutic applications of a biomimetic RBC filtration method

Duez, J., Holleran, J. P., Ndour, P. A., Pionneau, C., Diakité, S. A. S., Roussel, C., Dussiot, M., Amireault, P., Avery, V. M., & Buffet, P. A. (2015) · Transfusion Clinique et Biologique · doi:10.1016/j.tracli.2015.05.004 · Cited by 42 · see citing works

Inhibition of Suicidal Erythrocyte Death by Chronic Hypoxia

Tang, F. S., Feng, L., Li, R., Wang, W., Liu, H., Yang, Q., & Ge, R. (2018) · High Altitude Medicine & Biology · doi:10.1089/ham.2017.0159 · Cited by 41 · see citing works

Extracellular Vesicles as New Players in Drug Delivery: A Focus on Red Blood Cells-Derived EVs

Biagiotti, S., Abbas, F., Montanari, M., Barattini, C., Rossi, L., Magnani, M., Papa, S., & Canonico, B. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15020365 · Cited by 42 · see citing works

CD47 functions as a removal marker on aged erythrocytes

van Bruggen, R. (2013) · ISBT Science Series · doi:10.1111/voxs.12038 · Cited by 10 · see citing works

RED CELLS, IRON, AND ERYTHROPOIESIS

(2016)

CD47 in Erythrocyte Ageing and Clearance the Dutch Point of View

Burger, P., de Korte, D., van den Berg, T. K., & van Bruggen, R. (2012) · Transfusion Medicine and Hemotherapy · doi:10.1159/000342231 · Cited by 40 · see citing works

Comment Concerning the Role of CD47 and Signal Regulatory Protein Alpha in Regulating the Clearance of Aged Red Blood Cells

Lutz, H. U. (2013) · Transfusion Medicine and Hemotherapy · doi:10.1159/000350507 · Cited by 3 · see citing works

Role of CD47 and Signal Regulatory Protein Alpha (SIRPa) in Regulating the Clearance of Viable or Aged Blood Cells

Oldenborg, P. (2012) · Transfusion Medicine and Hemotherapy · doi:10.1159/000342537 · Cited by 24 · see citing works