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Red cell membrane: past, present, and future
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As a result of natural selection driven by severe forms of malaria, 1 in 6 humans in the world, more than 1 billion people, are affected by red cell abnormalities, making them the most common of the inherited disorders. The non-nucleated red cell is unique among human cell type in that the plasma membrane, its only structural component, accounts for all of its diverse antigenic, transport, and mechanical characteristics. Our current concept of the red cell membrane envisions it as a composite structure in which a membrane envelope composed of cholesterol and phospholipids is secured to an elastic network of skeletal proteins via transmembrane proteins. Structural and functional characterization of the many constituents of the red cell membrane, in conjunction with biophysical and physiologic studies, has led to detailed description of the way in which the remarkable mechanical properties and other important characteristics of the red cells arise, and of the manner in which they fail in disease states. Current studies in this very active and exciting field are continuing to produce new and unexpected revelations on the function of the red cell membrane and thus of the cell in health and disease, and shed new light on membrane function in other diverse cell types.
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“The discoid shape is defined by cytoskeletal structural proteins and ion channels (127).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [127]
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Cites
The Fluid Mosaic Model of the Structure of Cell Membranes
Singer, S. J., & Nicolson, G. L. (1972) · Science · doi:10.1126/science.175.4023.720 · Cited by 9,158
Pathophysiologic Implications of Membrane Phospholipid Asymmetry in Blood Cells
Zwaal, R. F. A., & Schroit, A. J. (1997) · Blood · doi:10.1182/blood.v89.4.1121 · Cited by 1,340
Verkleij, A. J., Zwaal, R. F. A., Roelofsen, B., Comfurius, P., Kastelijn, D., & Deenen, L. L. M. V. (1973) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(73)90143-0 · Cited by 1,128
Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues.
Bennett, V., & Baines, A. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.3.1353 · Cited by 993
ON BIMOLECULAR LAYERS OF LIPOIDS ON THE CHROMOCYTES OF THE BLOOD
Gorter, E., & Grendel, F. (1925) · Journal of Experimental Medicine · doi:10.1084/jem.41.4.439 · Cited by 791
Mohandas, N., & Evans, E. (1994) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.23.060194.004035 · Cited by 563
Self-citationWood, B., Gibson, D., & Tait, J. (1996) · Blood · doi:10.1182/blood.v88.5.1873.1873 · Cited by 445
Selective Solubilization of a Protein Component of the Red Cell Membrane
Marchesi, V. T., & Steers, E. (1968) · Science · doi:10.1126/science.159.3811.203 · Cited by 429
In-depth analysis of the membrane and cytosolic proteome of red blood cells
Pasini, E. M., Kirkegaard, M., Mortensen, P., Lutz, H. U., Thomas, A. W., & Mann, M. (2006) · Blood · doi:10.1182/blood-2005-11-007799 · Cited by 426
Erythrocyte spectrin is comprised of many homologous triple helical segments
Speicher, D. W., & Marchesi, V. T. (1984) · Nature · doi:10.1038/311177a0 · Cited by 421
Research works printed but not linked: 1
- Gulliver, 1862, Blood of Vertebrata.
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Nowak, R. B., & Fowler, V. M. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412440881 · Cited by 21
Tissue Oxygen Demand in Regulation of the Behavior of the Cells in the Vasculature
Barvitenko, N. N., Aslam, M., Filosa, J. A., Matteucci, E., Nikinmaa, M., Pantaleo, A., Saldanha, C., & Baskurt, O. K. (2013) · Microcirculation · doi:10.1111/micc.12052 · Cited by 21
Stable equilibrium configurations of an oblate capsule in simple shear flow
Dupont, C., Delahaye, F., Barthès‐Biesel, D., & Salsac, A. (2016) · Journal of Fluid Mechanics · doi:10.1017/jfm.2015.759 · Cited by 21
Cell Membrane-Based Nanoreactor To Mimic the Bio-Compartmentalization Strategy of a Cell
Balasubramanian, V., Poillucci, A., Correia, A., Zhang, H., Celia, C., & Santos, H. A. (2018) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.7b00944 · Cited by 21
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Kiser, Z. M., Lizcano, A., Nguyen, J., Becker, G. L., Belcher, J. D., Varki, A. P., & Vercellotti, G. M. (2019) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2019.102399 · Cited by 21
Chan, M. M., Wooden, J. M., Tsang, M., Gilligan, D. M., Hirenallur-S, D. K., Finney, G. L., Rynes, E., MacCoss, M., Ramirez, J. A., Park, H., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054902 · Cited by 20
Piagnerelli, M., COTTON, F. J., Nuffelen, M. V., Vincent, J., & Gulbis, B. (2011) · Shock · doi:10.1097/shk.0b013e318237d55a · Cited by 21
Biology of Erythropoiesis, Erythroid Differentiation, and Maturation
Papayannopoulou, T., & Migliaccio, A. R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-323-35762-3.00026-3 · Cited by 21
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Liu, Y., & Sun, D. B. (2012) · CRC Press eBooks · doi:10.1201/b11365 · Cited by 21
Deformability of Heterogeneous Red Blood Cells in Aging and Related Pathologies
Prudinnik, D. S., Kussanova, A., Vorobjev, I. A., Tikhonov, A., Ataullakhanov, F. I., & Barteneva, N. S. (2024) · Aging and Disease · doi:10.14336/ad.2024.0526 · Cited by 21
Han, J., Cho, J.-S., Cheng, Y., Muh, F., Yoo, W. G., Russell, B., Nosten, F. H., Na, S., Ha, K., Park, W. S., et al. (2018) · Infection and Immunity · doi:10.1128/iai.00239-18 · Cited by 20
Targeting spectrin redox switches to regulate the mechanoproperties of red blood cells
Barbarino, F., Wäschenbach, L., Cavalho-Lemos, V., Dillenberger, M., Becker, K., Gohlke, H., & Cortese-Krott, M. M. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0293 · Cited by 20
Ye, Z., Yang, W., Zheng, Y., Wang, S., Zhang, X., Yu, H., Li, S., Luo, C., Peng, X., & Xiao, Y. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202211540 · Cited by 20
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Owen, B., Kechagidis, K., Bazaz, S. R., Enjalbert, R., Essmann, E., Mallorie, C., Mirghaderi, F., Schaaf, C. P., Thota, K., Vernekar, R. R., et al. (2023) · Advances in Physics X · doi:10.1080/23746149.2023.2246704 · Cited by 21
Multi-omics Evidence for Inheritance of Energy Pathways in Red Blood Cells
Weisenhorn, E., Erve, T. J. V. ‘., Riley, N. M., Hess, J. R., Raife, T. J., & Coon, J. J. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.062349 · Cited by 20
Sui, Z., Gokhin, D. S., Nowak, R. B., Guo, X., An, X., & Fowler, V. M. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-10-0699 · Cited by 20
Analysis of subcellular structural tension in axonal growth of neurons
Guo, Y. C., Wang, Y. X., Ge, Y. P., Yu, L., & Guo, J. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0047 · Cited by 21
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Bigdelou, P., & Farnoud, A. M. (2020) · Journal of Visualized Experiments · doi:10.3791/60659 · Cited by 20
Structure and function of red and white blood cells
Gordon-Smith, T. (2009) · Medicine · doi:10.1016/j.mpmed.2009.01.013 · Cited by 20
Selectively Permeable Double Emulsions
Ong, I. L. H., & Amstad, E. (2019) · Small · doi:10.1002/smll.201903054 · Cited by 21
Семенов, А. Н., Lugovtsov, A. E., Ermolinskiy, P. B., Lee, K., & Priezzhev, A. V. (2022) · Photonics · doi:10.3390/photonics9040238 · Cited by 19
Scanes, C. G., Witt, J., Ebeling, M., Schaller, S., Baier, V., Bone, A. J., Preuß, T. G., & Heckmann, D. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.858386 · Cited by 20
Barshtein, G., Livshits, L., Gural, A., Arbell, D., Barkan, R. B., Pajić‐Lijaković, I., & Yedgar, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115814 · Cited by 19
Arashiki, N., Otsuka, Y., Ito, D., Yang, M.-R., Komatsu, T., Sato, K., & Inaba, M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.121 · Cited by 19
Ревин, В. В., Gromova, N. V., Revina, E. S., Martynova, M. I., Seikina, A. I., Revina, N. V., Imarova, O. G., Solomadin, I., Tychkov, A. Y., & Zhelev, N. (2016) · BioMed Research International · doi:10.1155/2016/3429604 · Cited by 19
Red blood cell membrane water permeability increases with length of ex vivo storage
Alshalani, A., & Acker, J. P. (2017) · Cryobiology · doi:10.1016/j.cryobiol.2017.04.009 · Cited by 19
Mineo, H., Amita, N., Kawawake, M., & Higuchi, A. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.06.002 · Cited by 19
Yang, Q., Chen, D., Li, C., Liu, R., & Wang, X. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1399154 · Cited by 18
Overview on Hereditary Spherocytosis Diagnosis
Polizzi, A., DICEMBRE, L. P., Failla, C., Matola, T. D., Moretti, M., Ranieri, S. C., Papa, F., Cenci, A. M., & Buttarello, M. (2024) · International Journal of Laboratory Hematology · doi:10.1111/ijlh.14376 · Cited by 18
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Lu, T., Lee, C.-H., & Anvari, B. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c03472 · Cited by 18
Hou, M., Xing, F., Yang, J., Hu, F. Z., Pan, L., & Xu, J. (2022) · Small Methods · doi:10.1002/smtd.202201243 · Cited by 18
Birefringence of a normal human red blood cell and related optomechanics in an optical trap
Nagesh, B. V., Yogesha, Ramarao, P., Parthasarathi, P., Iyengar, S. S., Bhattacharya, S., & Ananthamurthy, S. (2014) · Journal of Biomedical Optics · doi:10.1117/1.jbo.19.11.115004 · Cited by 18
Yau, T. W., Kuchel, R. P., Koh, J. M. S., Szekely, D., Mirtschin, P. J., & Kuchel, P. W. (2011) · Cell Biology International · doi:10.1042/cbi20110012 · Cited by 18
Walpurgis, K., Kohler, M., Thomas, A., Wenzel, F., Geyer, H., Schänzer, W., & Thevis, M. (2012) · PROTEOMICS · doi:10.1002/pmic.201200280 · Cited by 18
Li, H., Papageorgiou, D. P., Chang, H.-Y., Lu, L., Yang, J., & Deng, Y. (2018) · Biosensors · doi:10.3390/bios8030076 · Cited by 18
Uğurel, E., Pişkin, Ş., Aksu, A. C., Eser, A., & Yalçın, Ö. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2019.01559 · Cited by 18
Motta, I., Giannotta, J. A., Ferraresi, M., Barbullushi, K., Revelli, N., Graziadei, G., Barcellini, W., & Fattizzo, B. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10153439 · Cited by 18
Hu, Q., Wang, Z., Shen, L., & Zhao, G. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c01858 · Cited by 18
Man, Y., An, R., Monchamp, K., Sekyonda, Z., Kucukal, E., Federici, C., Wulftange, W. J., Goreke, U., Bode, A., Sheehan, V., et al. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.954106 · Cited by 17
Wang, J., Song, J., An, C., Dong, W.-J., Zhang, J., Yin, C., Hale, J., Baines, A. J., Mohandas, N., & An, X. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.516617 · Cited by 18
Self-citationSerum Pantetheinase/Vanin Levels Regulate Erythrocyte Homeostasis and Severity of Malaria
Rommelaere, S., Millet, V., Rihet, P., Atwell, S. X., Helfer, E., Chasson, L., Beaumont, C., Chimini, G., Sambo, M. D. R., Viallat, A., et al. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.07.011 · Cited by 19
Fang, Z., Jiang, C., Tang, J., He, M. L., Lin, X., Chen, X., Han, L., Zhang, Z., Feng, Y., Guo, Y., et al. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.10.015 · Cited by 18
Satyam, A., Andreo, K., Lapchak, P. H., Lucca, J. J. D., Davis, R. B., Tsokos, M., Shapiro, N. I., & Tsokos, G. C. (2019) · Shock · doi:10.1097/shk.0000000000001348 · Cited by 18
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Hao, L., Li, S., Ma, D., Chen, S., Zhang, B., Xiao, D., Zhang, J., Jiang, N., Jiang, S., & Ma, J. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14343 · Cited by 17
Ревин, В. В., Gromova, N. V., Revina, E. S., Prosnikova, K. V., Revina, N. V., Bochkareva, S. S., Stepushkina, O. G., Grunyushkin, I. P., Tairova, M. R., & Incina, V. I. (2019) · BioMed Research International · doi:10.1155/2019/6758017 · Cited by 17
Effective cell membrane tension protects red blood cells against malaria invasion
Alimohamadi, H., & Rangamani, P. (2023) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1011694 · Cited by 17
Ghisleni, A., Bonilla-Quintana, M., Crestani, M., Lavagnino, Z., Galli, C., Rangamani, P., & Gauthier, N. C. (2024) · Nature Communications · doi:10.1038/s41467-024-49906-6 · Cited by 17
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Minetti, G., Dorn, I., Köfeler, H. C., Perotti, C. G., & Kaestner, L. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02318-x · Cited by 17
Targeted quantitative phosphoproteomic analysis of erythrocyte membranes during blood bank storage
Rinalducci, S., Longo, V., Ceci, L. R., & Zolla, L. (2015) · Journal of Mass Spectrometry · doi:10.1002/jms.3531 · Cited by 17
Polin, H., Pelc‐Kłopotowska, M., Danzer, M., Suessner, S., Gabriel, C., Wilflingseder, J., Żmudzin, A., Orzińska, A., Guz, K., Michalewska, B., et al. (2016) · Transfusion · doi:10.1111/trf.13476 · Cited by 17
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Abkarian, M., & Viallat, A. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782628491-00347 · Cited by 17
Światły‐Błaszkiewicz, A., Mrówczyńska, L., Matuszewska, E., Lubawy, J., Urbański, A., Kokot, Z. J., Rosiński, G., & Matysiak, J. (2020) · Metabolites · doi:10.3390/metabo10050191 · Cited by 17
Alexandre, B. M., Charro, N., Blonder, J., Lopes, C. M., Azevedo, P., de Almeida, A. B., Chan, K. C., Prieto, D. A., Issaq, H. J., Veenstra, T. D., et al. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.04.008 · Cited by 17
Bosman, G. J. G. C. M. (2016) · Proteomes · doi:10.3390/proteomes4040035 · Cited by 16
Li, S., Liu, T., Li, K., Bai, X., Xi, K., Chai, X., Mi, L., & Li, J. (2021) · Translational research · doi:10.1016/j.trsl.2021.12.009 · Cited by 16
Mattè, A., Wilson, A. B., Gevi, F., Federti, E., Recchiuti, A., Ferri, G., Brunati, A. M., Pagano, M. A., Russo, R., Lebœuf, C., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.172656 · Cited by 16
Self-citationMicrocirculation and Hemorheology: points of interaction
Muravyov, A. V., Михайлов, П. В., & Tikhomirova, I. A. (2017) · Regional blood circulation and microcirculation · doi:10.24884/1682-6655-2017-16-2-90-100 · Cited by 16
Zingariello, M., Bardelli, C., Sancillo, L., Ciaffoni, F., Genova, M. L., Girelli, G., & Migliaccio, A. R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00281 · Cited by 16
Benjaporn, K., Sato, K., Otsuka, Y., Arashiki, N., Chen, Y., Tsumita, T., Otsu, W., Yamamoto, A., Kawata, R., Yamazaki, J., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011679 · Cited by 19
Self-citationModulation of Redox Signaling and Thiol Homeostasis in Red Blood Cells by Peroxiredoxin Mimetics
Chakrabarty, G., NaveenKumar, S. K., Kumar, S., & Mugesh, G. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00309 · Cited by 16
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PEGylation enhances the antibacterial and therapeutic potential of amphibian host defence peptides
Dennison, S. R., Reddy, S. M., Morton, L. H. G., Harris, F., Badiani, K., & Phoenix, D. A. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183806 · Cited by 16
Remodeling of human red cells infected with Plasmodium falciparum and the impact of PHIST proteins
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Urinary Red Blood Cells: Not Only Glomerular or Nonglomerular
Poloni, J. A. T., Bosan, I. B., Garigali, G., & Fogazzi, G. B. (2011) · Nephron Clinical Practice · doi:10.1159/000330286 · Cited by 16
Locating the Band III protein in quasi-native cell membranes
Shan, Y., Wang, Z., Hao, X. F., Shang, X. C., Cai, M., Jiang, J., Fang, X., Wang, H., & Tang, Z. (2010) · Analytical Methods · doi:10.1039/c0ay00278j · Cited by 16
Zebrafish etv7 regulates red blood cell development through the cholesterol synthesis pathway
Quintana, A. M., Picchione, F., Geltink, R. I. K., Taylor, M. R., & Grosveld, G. C. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.012526 · Cited by 16
Storti, F. (2008) · Cited by 16
More, T. A., & Kedar, P. S. (2022) · Gene · doi:10.1016/j.gene.2022.146796 · Cited by 15
Proteomes of Micro- and Nanosized Carriers Engineered from Red Blood Cells
Lee, C.-H., Tang, J. C., Hendricks, N. G., & Anvari, B. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00695 · Cited by 15
Kamysz, E., Sikorska, E., Bauer, M., Sikora, K., & Neubauer, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065505 · Cited by 15
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Banerjee, S., & Datta, R. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105064 · Cited by 15
Huang, Y., Delgadillo, L. F., Cyr, K. H., Kingsley, P. D., An, X., McGrath, K. E., Mohandas, N., Conboy, J. G., Waugh, R. E., Wan, J., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05498-4 · Cited by 15
Self-citationKabacaoğlu, G., & Biros, G. (2018) · Physical Review Fluids · doi:10.1103/physrevfluids.3.124201 · Cited by 15
Optimizing red blood cell protein extraction for biomarker quantitation with mass spectrometry
Klatt, S., Roberts, A. M., Lothian, A., Masters, C. L., Cappai, R., Fowler, C. J., & Roberts, B. R. (2020) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-020-02439-5 · Cited by 15
Vital erythrocyte phenomena: what can theory, modeling, and simulation offer?
Asaro, R. J., & Zhu, Q. (2020) · Biomechanics and Modeling in Mechanobiology · doi:10.1007/s10237-020-01302-x · Cited by 15
Jin, Y., Liang, Q. D., & Tieleman, D. P. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c01055 · Cited by 14
Wang, Y., Sang, J., Ao, R., Ma, Y., & Fu, B. (2020) · Computer Methods in Biomechanics & Biomedical Engineering · doi:10.1080/10255842.2020.1791836 · Cited by 15
Chen, W., Shao, S., Cai, H., Han, J., Guo, T., Fu, Y., Yu, C., Zhao, M., Bo, T., Yao, Z., et al. (2020) · International Journal of Endocrinology · doi:10.1155/2020/9501826 · Cited by 15
Inertial migration of red blood cells under a Newtonian fluid in a circular channel
Takeishi, N., Yamashita, H., Omori, T., Yokoyama, N., Wada, S., & Sugihara‐Seki, M. (2022) · Journal of Fluid Mechanics · doi:10.1017/jfm.2022.936 · Cited by 15
Perona, J. S., González‐Jiménez, E., Cordero, M. J. A., Sureda, A., & Barceló, F. (2013) · The Journal of Membrane Biology · doi:10.1007/s00232-013-9596-x · Cited by 15
Orientational dynamics of human red blood cells in an optical trap
Parthasarathi, P., Nagesh, B. V., Lakkegowda, Y., Lyengar, S. S., Ananthamurthy, S., & Bhattacharya, S. (2013) · Journal of Biomedical Optics · doi:10.1117/1.jbo.18.2.025001 · Cited by 15
Detergent-free isolation of native red blood cell membrane complexes
Desrames, A., Genetet, S., Delcourt, M. P., Goossens, D., & Mouro-Chanteloup, I. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.183126 · Cited by 15
Effects of ethanol on red blood cell rheological behavior
Rábai, M., Detterich, J. A., Wenby, R. B., Tóth, K., & Meiselman, H. J. (2014) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-2012-1632 · Cited by 15
Penetration of laser light through red blood cell ghosts
Šikurová, L., Bališ, P., & Zvarík, M. (2011) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2011.03.015 · Cited by 15
Rooney, S., Hoffmann, J. J. M. L., Cormack, O. M., & McMahon, C. (2014) · International Journal of Laboratory Hematology · doi:10.1111/ijlh.12245 · Cited by 15
Erythropoiesis in the Absence of Adult Hemoglobin
Liu, S., McConnell, S. C., & Ryan, T. M. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01734-12 · Cited by 15
Glenthøj, A. B., Brieghel, C., Nardo‐Marino, A., van Wijk, R., Birgens, H., & Petersen, J. (2021) · eJHaem · doi:10.1002/jha2.277 · Cited by 14
Biomechanics of phagocytosis of red blood cells by macrophages in the human spleen
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Shi, Q., Xu, X., Fan, Q., Hou, J., Wei, Y., & Yin, J. (2015) · Journal of Materials Chemistry B · doi:10.1039/c4tb01854k · Cited by 14
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Kar, S., Ghosh, U., Maiti, T. K., & Chakraborty, S. K. (2015) · Lab on a Chip · doi:10.1039/c5lc00968e · Cited by 14
Robledo, R. F., Lambert, A. J., Birkenmeier, C. S., Cirlan, M. V., Cirlan, A. F. M., Campagna, D. R., Lux, S. E., & Peters, L. L. (2010) · Blood · doi:10.1182/blood-2009-07-232199 · Cited by 14
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Krbec, M., Waldauf, P., Zadek, F., Brusatori, S., Zanella, A., Duška, F., & Länger, T. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1009378 · Cited by 13
Wei, Q., Xiong, Y., Ma, Y., Liu, D., Lu, Y., Zhang, S., Wang, X., Huang, H., Liu, Y., Dao, M., et al. (2023) · Lab on a Chip · doi:10.1039/d3lc00323j · Cited by 13
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Li, Y., Wang, Y., Luo, Y.-G., Yang, H., Ren, J., & Xiao, L. (2024) · Chinese Chemical Letters · doi:10.1016/j.cclet.2024.109576 · Cited by 14
Metadata
- Authors
- Mohandas, N., & Gallagher, P. G.
- Affiliations
- New York Blood Center (US)
- Yale University (US)
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2008-11-15
- Volume
- 112
- Issue
- 10
- Pages
- 3939-3948
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC2582001
- OpenAlex
- W2022066534
- Cited by
- 1,089
- References
- 104
- Citations by year
- 2026: 67 · 2025: 61 · 2024: 48 · 2023: 70 · 2022: 75 · 2021: 71 · 2020: 71 · 2019: 70 · 2018: 66 · 2017: 62 · 2016: 66 · 2015: 60 · 2014: 65 · 2013: 61 · 2012: 62
- FWCI
- 4.05
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Blood (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Washington
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL031579)
- National Institute of Diabetes and Digestive and Kidney Diseases (R37DK026263, P01DK032094, R01DK026263, R01DK062039)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Erythrocyte Function and Pathophysiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Keywords
- erythrocyte membrane, erythrocyte membrane structure, malaria resistance, membrane mechanics, membrane skeleton, transmembrane proteins, membrane transport, membrane biophysics
- MeSH terms
- Biological Transport, Erythrocyte Membrane, Erythrocytes, Abnormal, Humans, Isoantigens, Malaria, Membrane Proteins, Selection, Genetic, Structure-Activity Relationship
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