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Red cell membrane: past, present, and future
Open accessAbstract
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.
Cited by
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Pepona, M., Gounley, J. P., & Randles, A. P. (2023) · Computers & Mathematics with Applications · doi:10.1016/j.camwa.2022.12.009 · Cited by 8
Shih, Y.-H., Huang, Y., Lin, C., Lin, H., Kuo, S.-F., Lin, J., & Shen, M. (2023) · Medicine · doi:10.1097/md.0000000000032708 · Cited by 8
Blood Rheology and Microcirculation
Tikhomirova, I. A. (2023) · Успехи физиологических наук · doi:10.31857/s0301179823010071 · Cited by 8
Defects in Erythrocyte Membrane Skeletal Architecture
Basu, A., & Chakrabarti, A. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-11280-0_4 · Cited by 7
Chen-Chi, W., Sato, K., Otsuka, Y., Otsu, W., & Inaba, M. (2011) · Journal of Veterinary Medical Science · doi:10.1292/jvms.11-0345 · Cited by 8
Proper cytoskeletal architecture beneath the plasma membrane of red blood cells requiresTtll4
Ijaz, F., Hatanaka, Y., Hatanaka, T., Tsutsumi, K., Iwaki, T., Umemura, K., Ikegami, K., & Setou, M. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-02-0089 · Cited by 8
Tripodi, S. I., Shamberger, R. C., Heeney, M. M., & Tubman, V. N. (2019) · Pediatric Hematology and Oncology · doi:10.1080/08880018.2019.1637983 · Cited by 8
Balogh, G. E., Chakraborty, P., Dugmonits, K. N., Péter, M., Végh, A. G., Vígh, L., & Hermesz, E. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158615 · Cited by 8
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Tibaldi, E. V., Federti, E., Mattè, A., Iatcenko, I., Wilson, A. B., Riccardi, V., Pagano, M. A., & Franceschi, L. D. (2020) · Antioxidants · doi:10.3390/antiox9040353 · Cited by 9
Self-Assembly of F0F1-ATPase Motors and Ghost
Tao, N., Cheng, J., Wei, L., & Yue, J. (2009) · Langmuir · doi:10.1021/la804083f · Cited by 8
Non‐uniform force allocation for area preservation in spring network models
Jančigová, I., & Cimrák, I. (2015) · International Journal for Numerical Methods in Biomedical Engineering · doi:10.1002/cnm.2757 · Cited by 8
Li, C., Li, Z., Xun, S., Jiang, P., Yan, R., Chen, M., Hu, F. Z., Rupp, R. A., Zhang, X., Pan, L., et al. (2017) · Cell Death Discovery · doi:10.1038/cddiscovery.2017.40 · Cited by 8
The erythrocyte membrane stability is associated with sleep time and social jetlag in shift workers
Teixeira, K. R., de Medeiros, L. A., Mendes, J. A., Vaz, E. R., Cunha, T. M., de Oliveira, E. P., Penha‐Silva, N., & Crispim, C. A. (2019) · PLoS ONE · doi:10.1371/journal.pone.0222698 · Cited by 8
Kindlin-3 deficiency leads to impaired erythropoiesis and erythrocyte cytoskeleton
Szpak, D., Turpin, C., Goreke, U., Białkowska, K., Bledzka, K. M., Verbovetskiy, D., Mohandas, N., Gurkan, U. A., Qin, J., Plow, E. F., et al. (2023) · Blood Advances · doi:10.1182/bloodadvances.2022008498 · Cited by 7
Self-citationSongdej, D., Surapolchai, P., Komwilaisak, P., Sripornsawan, P., Lauhasurayotin, S., Teawtrakul, N., Rungjirajittranon, T., Tantiworawit, A., Sinlapamongkolkul, P., Torcharus, K., et al. (2023) · Annals of Hematology · doi:10.1007/s00277-023-05555-1 · Cited by 7
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Иноятович, А. Ф., Martinov, M. V., Shi, Q., & Vitvitsky, V. (2022) · PLoS ONE · doi:10.1371/journal.pone.0272675 · Cited by 7
Shabanpour, Y., Verdom, B. H., Abdolmaleki, P., & Alipour, M. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1494257 · Cited by 7
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Chasis, J. A. (2011) · Blood · doi:10.1182/blood-2011-05-352567 · Cited by 7
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Lesesve, J. (2010) · American Journal of Hematology · doi:10.1002/ajh.21962 · Cited by 7
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Kaczmarska, M. J., Żydek, D., Wilkłacz‐Potoczny, J., Fornal, M., Grodzicki, T. K., Kochowska, E., Kozak, K., Gocal, Ł., Pohorecki, W., Matlak, K., et al. (2016) · Microscopy Research and Technique · doi:10.1002/jemt.22803 · Cited by 7
Kilili, G. K., Shakya, B., Dolan, P., Wang, L., Husby, M. L., Stahelin, R. V., Nakayasu, E. S., & LaCount, D. J. (2019) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2019.111189 · Cited by 7
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Ivanov, I. T., & Paarvanova, B. (2023) · General Physiology and Biophysics · doi:10.4149/gpb_2022004 · Cited by 7
Vizzoca, A., Lucarini, G., Tognoni, E., Tognarelli, S., Ricotti, L., Gherardini, L. M., Pelosi, G., Pellegrino, M., Menciassi, A., Grimaldi, S., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179893 · Cited by 7
Härtel, J. A., Müller, N., Breuer, J., Jordan, J., Tank, J., Bros, J., Seeger, B., Zollmann, E., Bloch, W., & Grau, M. (2022) · Metabolites · doi:10.3390/metabo12111025 · Cited by 7
SİNAN, M., Yalçın, Ö., Karakaş, Z., Goksel, E., & Ertan, N. Z. (2023) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-221452 · Cited by 7
Proteomic mining of the red blood cell: focus on the membrane proteome
Alexandre, B. M. (2010) · Expert Review of Proteomics · doi:10.1586/epr.09.96 · Cited by 7
Tang, F., Lei, X., Xiong, Y., Wang, R., Mao, J., & Wang, X. (2014) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2014.07.022 · Cited by 7
Blood groups on red cells, platelets and neutrophils
Daniels, G. L. (2011) · Elsevier eBooks · doi:10.1016/b978-0-7020-3147-2.00037-7 · Cited by 7
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Qiang, Y., Liu, J., Mian, M., & Du, E. (2016) · Conference proceedings of the Society for Experimental Mechanics · doi:10.1007/978-3-319-41351-8_18 · Cited by 7
Al-Hatamleh, M. A. I., Baig, A. A., Simbak, N., Nadeem, M. I., Khan, S. U., & Ariff, T. M. (2017) · Pakistan Journal of Biological Sciences · doi:10.3923/pjbs.2017.478.488 · Cited by 7
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Ensinck, A., Brajovich, M. E. L., Borrás, S. G., Cotorruelo, C., & Biondi, C. S. (2019) · Open Journal of Blood Diseases · doi:10.4236/ojbd.2019.93006 · Cited by 7
Bakker, N., Schoorl, M., Stoutjesdijk, E., & Houdijk, A. P. J. (2019) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-190687 · Cited by 7
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Mignon, T., & Mendez, S. (2021) · Mathematical Modelling of Natural Phenomena · doi:10.1051/mmnp/2021014 · Cited by 7
Sun, P., Zhou, W., Fu, Y., Cheung, C. Y. Y., Dong, Y., Yang, M., Zhang, H., Jia, J., Huo, Y., Willer, C. J., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab062 · Cited by 7
van Dooijeweert, B., Broeks, M. H., Verhoeven‐Duif, N. M., van Solinge, W. W., van Beers, E. J., Rab, M. A. E., Nieuwenhuis, E. E. S., Jans, J. J. M., Bartels, M., & van Wijk, R. (2021) · HemaSphere · doi:10.1097/hs9.0000000000000591 · Cited by 7
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Ndour, P. A., Safeukui, I., Diakité, S. A. S., Duez, J., Jauréguiberry, S., & Buffet, P. A. (2015) · Springer eBooks · doi:10.1007/978-1-4614-8326-7_89 · Cited by 7
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Kumar, S., Yokoyama, N., Kim, J., Bork, S., Inoue, N., Xuan, X., Igarashi, I., & Sugimoto, C. (2012) · Experimental Parasitology · doi:10.1016/j.exppara.2012.09.013 · Cited by 6
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Chang, C., Chang, C.-H., Yang, Y.-W., Chen, H., Yang, S., Yao, W.-C., & Chao, C. (2022) · Polymers · doi:10.3390/polym14020250 · Cited by 6
Ghosh, A., Coffin, M., West, R., & Fowler, V. M. (2022) · The FASEB Journal · doi:10.1096/fj.202101011r · Cited by 6
Cryoprotectants for red blood cells: Evaluate safety and effectiveness by in vitro measures
Hu, Y., Liu, X., Ahmad, A., Chen, J., Chen, X., Zhang, W., & Tan, S. (2023) · MedComm – Future Medicine · doi:10.1002/mef2.67 · Cited by 6
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Lomako, V., Shylo, O. V., Kovalenko, I., & Бабийчук, Г. А. (2015) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093015010081 · Cited by 6
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Kaestner, L. (2012) · Springer eBooks · doi:10.1007/978-3-642-34617-0_28 · Cited by 6
The knockout of urea transporter-B improves the hemorheological properties of erythrocyte
Geng, X., Lei, T., Zhou, H., Yao, W., Xin, W., & Yang, B. (2016) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-16174 · Cited by 6
Семенов, А. Н., Александрович, Г. Д., Moysenovich, A. M., Zlenko, D. V., Parshina, E. Y., Байжуманов, А. А., Budylin, G. S., & Maksimov, E. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415767 · Cited by 6
Stilgoe, A. B., Kashchuk, A. V., Balanant, M. A., Santangelo, D., Nieminen, T. A., Sauret, E., Flower, R. L., & Rubinsztein-Dunlop, H. H. (2023) · Biomedical Optics Express · doi:10.1364/boe.504779 · Cited by 6
Weikard, R., Demasius, W., Hadlich, F., & Kühn, C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136927 · Cited by 6
Wu, J., Bakerink, K. J., Evangelista, M. E., & Thomas, G. H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093680 · Cited by 6
Yu, D., Yin, Z., Fu, C., & Yu, R. (2014) · Central European Journal of Immunology · doi:10.5114/ceji.2014.45951 · Cited by 6
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Tikhomirova, I. A., Muravyov, A. V., Петровна, П. Е., Kislov, N. V., Валентинович, Ч. С., & Peganova, E. V. (2016) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747815050153 · Cited by 6
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Russo, R., & Andolfo, I. (2019) · HemaSphere · doi:10.1097/hs9.0000000000000198 · Cited by 6
Uğurel, E., Connes, P., Yavas, G., Eglenen, B., Türkay, M., Aksu, A. C., Renoux, C., Joly, P., Gauthier, A., Hot, A., et al. (2019) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-190563 · Cited by 6
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Hale, J., An, X., Guo, X., Gao, E., Papoin, J., Blanc, L., Hillyer, C. D., Gratzer, W. B., Baines, A. J., & Mohandas, N. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.07.027 · Cited by 6
Self-citationJonsdottir, T. K., Gabriela, M., & Gilson, P. R. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-78397-6_6 · Cited by 6
Intravascular hemolysis: the sacrifice of few…
Thomas, S. L. Y. (2014) · Blood · doi:10.1182/blood-2014-08-595447 · Cited by 6
Wang, Y., Zhang, H., Kang, Q., Liu, J., Weng, H., Li, W., Mohandas, N., An, X., & Chen, L. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.02.009 · Cited by 6
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Daniels, G. L. (2013) · doi:10.1002/9781118493595.ch18 · Cited by 6
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Longo, G., Dinarelli, S., Collacchi, F., & Girasole, M. (2025) · Methods and Protocols · doi:10.3390/mps8040086 · Cited by 5
Wang, B., Li, W., Lu, G., Wen, J., Wang, M., Bai, L., Wang, Y., Huang, X., Mei, W., Huan, S., et al. (2025) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2025.118003 · Cited by 5
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Man, Y., Wu, D. H., An, R., Wei, P., Monchamp, K., Goreke, U., Sekyonda, Z., Wulftange, W. J., Federici, C., Bode, A., et al. (2023) · Sensors & Diagnostics · doi:10.1039/d2sd00095d · Cited by 5
Beri, D., Rodriguez, M., Singh, M., McLaughlin, D. J., Liu, Y., Zhong, H., Mendelson, A., An, X., Manwani, D. G., Yazdanbakhsh, K., et al. (2025) · Blood · doi:10.1182/blood.2024027602 · Cited by 5
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Blanch, A. J., Nunez-Iglesias, J., Namvar, A., Menant, S., Looker, O., Rajagopal, V., Tham, W., Tilley, L. M., & Dixon, M. W. A. (2021) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2021.100056 · Cited by 5
Laszuk, P., Urbaniak, W., & Petelska, A. D. (2023) · Molecules · doi:10.3390/molecules28031013 · Cited by 5
Ivanov, I. T., & Paarvanova, B. (2023) · Membranes · doi:10.3390/membranes13070658 · Cited by 5
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Sharma, R., & Jain, A. (2024) · Pediatric Hematology Oncology Journal · doi:10.1016/j.phoj.2024.02.003 · Cited by 5
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Sharma, S., Punjabi, V., Zingde, S. M., & Gokhale, S. M. (2014) · The Journal of Membrane Biology · doi:10.1007/s00232-014-9718-0 · Cited by 5
Joshi, K. B., Venkatesh, V., & Verma, S. K. (2010) · Chemical Communications · doi:10.1039/c001924k · Cited by 5
Sigüenza, J., Mendez, S., & Nicoud, F. (2014) · Computer Methods in Biomechanics & Biomedical Engineering · doi:10.1080/10255842.2014.931083 · Cited by 5
Tanaka, S., & Takakuwa, Y. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.01.058 · Cited by 5
Evaluation of Anemia, Leukopenia, and Thrombocytopenia
Wilson, C. S., & Brynes, R. K. (2011) · Elsevier eBooks · doi:10.1016/b978-0-7216-0040-6.00011-3 · Cited by 5
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Perez, J. E., Alsharif, N. A., Martínez-Banderas, A. I., Othman, B. A., Merzaban, J. S., Ravasi, T., & Kosel, J. (2018) · InTech eBooks · doi:10.5772/intechopen.76365 · Cited by 5
Wang, Z., Guan, J. H., Chen, L., & Tao, W. (2019) · International Journal of Heat and Fluid Flow · doi:10.1016/j.ijheatfluidflow.2019.108520 · Cited by 5
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Flegel, W. A., Srivastava, K., Sissung, T. M., Goldspiel, B. R., & Figg, W. D. (2020) · Vox Sanguinis · doi:10.1111/vox.12999 · Cited by 5
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Kępińska, M., Szyguła, Z., Dąbrowski, Z., & Szarek, M. (2017) · Diagnostyka Laboratoryjna · doi:10.5604/01.3001.0013.7992 · Cited by 5
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Cortese-Krott, M. M., Kramer, C. M., & Kelm, M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804273-1.00014-4 · Cited by 5
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de Santis, L. P., Garcia, P. C., Secco, V. N. D. P., Ferreira, R. R., & Deffune, E. (2019) · Einstein (São Paulo) · doi:10.31744/einstein_journal/2019ao4328 · Cited by 5
Kang, Y. J. (2020) · Applied Sciences · doi:10.3390/app10155273 · Cited by 5
Kalfa, T. A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-386456-7.07907-7 · Cited by 5
Liao, X., Du, K., Zhang, J., Meng, W., Zuo, S., Huang, Q., Wang, H., & Gou, D.-M. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.036 · Cited by 5
An antioxidant metabolon at the red blood cell membrane
Li, B. (2009) · Spectrum Research Repository (Concordia University) · Cited by 5
Huang, S., Bow, H. C., Diez-Silva, M., & Han, J. (2010) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 5
Hereditary Disorders of the Red Cell Membrane and Disorders of Red Cell Metabolism
Bianchi, P. I., & Mohandas, N. (2015) · doi:10.1002/9781118853771.ch8 · Cited by 5
Self-citationExperimental Studies of Red Blood Cells During Storage
Balanant, M. A. (2018) · Queensland University of Technology · doi:10.5204/thesis.eprints.119221 · Cited by 5
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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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