The DOI matches its Crossref record; 106 of the 106 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Mechanical Properties of the Red Cell Membrane
Rand, R. P., & Burton, A. C. (1964) · Biophysical Journal · doi:10.1016/s0006-3495(64)86773-4 · Cited by 407
The Role of Hemoglobin Denaturation and Band 3 Clustering in Red Blood Cell Aging
Low, P. S., Waugh, S. M., Zinke, K., & Drenckhahn, D. (1985) · Science · doi:10.1126/science.2578228 · Cited by 395
Mohandas, N., & Chasis, J. A. (1993) · PubMed · Cited by 393
Self-citationForced Unfolding of Proteins Within Cells
Johnson, C. P., Tang, H., Krieger, C. C., Speicher, D. W., & Discher, D. E. (2007) · Science · doi:10.1126/science.1139857 · Cited by 377
Blood. Principles and practice of hematology
(1997) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(97)81612-5 · Cited by 373
Mechanical Properties of the Red Cell Membrane
Rand, R. P. (1964) · Biophysical Journal · doi:10.1016/s0006-3495(64)86784-9 · Cited by 357
A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane
Bruce, L. J. (2003) · Blood · doi:10.1182/blood-2002-09-2824 · Cited by 355
Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts
Salzer, U., & Prohaska, R. (2001) · Blood · doi:10.1182/blood.v97.4.1141 · Cited by 348
Disposition of the major proteins in the isolated erythrocyte membrane. Proteolytic dissection
Steck, T. L., Fairbanks, G., & Wallach, D. F. H. (1971) · Biochemistry · doi:10.1021/bi00789a031 · Cited by 321
The spectrin-actin junction of erythrocyte membrane skeletons
Bennett, V. (1989) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(89)90006-3 · Cited by 299
Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis.
Jarolim, P., Palek, J., Amato, D., Hassan, K., Sapak, P., Nurse, G. T., Rubin, H. L., Zhai, S., Sahr, K. E., & Liu, S. C. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11022 · Cited by 291
The spectrin repeat: a structural platform for cytoskeletal protein assemblies
Djinović‐Carugo, K., Gautel, M., Ylänne, J., & Young, P. W. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03304-x · Cited by 286
The molecular basis of hereditary red cell membrane disorders
Delaunay, J. (2006) · Blood Reviews · doi:10.1016/j.blre.2006.03.005 · Cited by 285
Manno, S., Takakuwa, Y., & Mohandas, N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042688399 · Cited by 274
Self-citationHereditary spherocytosis—defects in proteins that connect the membrane skeleton to the lipid bilayer
Eber, S., & Lux, S. E. (2004) · Seminars in Hematology · doi:10.1053/j.seminhematol.2004.01.002 · Cited by 259
Chasis, J. A., & Mohandas, N. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.2.343 · Cited by 254
Self-citationSalomao, M. A., Zhang, X., Yang, Y., Lee, S., Hartwig, J. H., Chasis, J. A., Mohandas, N., & An, X. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803225105 · Cited by 253
Self-citationIn vitro formation of a complex between cytoskeletal proteins of the human erythrocyte
Ungewickell, E. J., Bennett, P. M., Calvert, R. A., Ohanian, V., & Gratzer, W. B. (1979) · Nature · doi:10.1038/280811a0 · Cited by 253
Bennett, V. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(83)96029-9 · Cited by 238
Blood: Principles and Practice of Hematology
Nand, S. (2003) · JAMA · doi:10.1001/jama.290.17.2334 · Cited by 230
Evans, E., Mohandas, N., & Leung, A. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111234 · Cited by 228
Self-citationMohandas, N., Chasis, J. A., & Shohet, S. (1983) · PubMed · Cited by 216
Self-citationFayrer, J. (2024) · Routledge eBooks · doi:10.4324/9781003102076-30 · Cited by 213
Unraveling the Mysteries of Phospholipid Scrambling
Wiedmer, T., & Sims, P. (2001) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1616224 · Cited by 212
Tchernia, G., Mohandas, N., & Shohet, S. (1981) · Journal of Clinical Investigation · doi:10.1172/jci110275 · Cited by 212
Self-citationAnkyrin–1 mutations are a major cause of dominant and recessive hereditary spherocytosis
Eber, S., Gonzalez, J. M., Lux, M. L., Scarpa, A. L., Tse, W. T., Dornwell, M., Herbers, J., Kugler, W., Özcan, R., Pekrun, A., et al. (1996) · Nature Genetics · doi:10.1038/ng0696-214 · Cited by 211
Self-citationRole of erythrocyte phosphatidylserine in sickle red cell–endothelial adhesion
Setty, Y. B. N., Kulkarni, S., & Stuart, M. J. (2002) · Blood · doi:10.1182/blood.v99.5.1564 · Cited by 211
Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8
Lux, S. E., Tse, W. T., Menninger, J. C., John, K. M., Harris, P. C., Shalev, O., Chilcote, R. R., Marchesi, S. L., Watkins, P. C., Bennett, V., et al. (1990) · Nature · doi:10.1038/345736a0 · Cited by 203
Membrane Phospholipid Asymmetry in Human Thalassemia
Kuypers, F. A., Yuan, J., Lewis, R. A., Snyder, L. M., Kiefer, C. R., Bunyaratvej, A., Fucharoen, S., Ma, L., Styles, L. A., de Jong, K., et al. (1998) · Blood · doi:10.1182/blood.v91.8.3044.3044_3044_3051 · Cited by 202
Hereditary elliptocytosis: spectrin and protein 4.1R
Gallagher, P. G. (2004) · Seminars in Hematology · doi:10.1053/j.seminhematol.2004.01.003 · Cited by 201
Self-citationKuhlman, P. A., Hughes, C. A., Bennett, V., & Fowler, V. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.14.7986 · Cited by 199
Red blood cell blood group antigens: structure and function
Reid, M. E., & Mohandas, N. (2004) · Seminars in Hematology · doi:10.1053/j.seminhematol.2004.01.001 · Cited by 193
Self-citationPartial deficiency of erythrocyte spectrin in hereditary spherocytosis
Agre, P. C., Casella, J. F., Zinkham, W. H., McMillan, C. W., & Bennett, V. (1985) · Nature · doi:10.1038/314380a0 · Cited by 190
Rheological Comparison of Hemoglobin Solutions and Erythrocyte Suspensions
Cokelet, G. R., & Meiselman, H. J. (1968) · Science · doi:10.1126/science.162.3850.275 · Cited by 172
Ion Transport Pathology in the Mechanism of Sickle Cell Dehydration
Lew, V. L., & Bookchin, R. M. (2004) · Physiological Reviews · doi:10.1152/physrev.00052.2003 · Cited by 171
Red cell membrane skeletal defects in hereditary and acquired hemolytic anemias.
Palek, J., & Se, L. (1983) · PubMed · Cited by 168
Marfatia, S. M., Lue, R. A., Branton, D., & Chishti, A. H. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37012-6 · Cited by 166
Bruce, L. J., Robinson, H. C., Guizouarn, H., Borgèse, F., Harrison, P. J., King, M., Goede, J. S., Coles, S. E., Gore, D. M., Lutz, H. U., et al. (2005) · Nature Genetics · doi:10.1038/ng1656 · Cited by 165
Erythrocyte G Protein-Coupled Receptor Signaling in Malarial Infection
Harrison, T., Samuel, B. U., Akompong, T., Hamm, H. E., Mohandas, N., Lomasney, J. W., & Haldar, K. (2003) · Science · doi:10.1126/science.1089324 · Cited by 159
Self-citationRegulation of actin filament length in erythrocytes and striated muscle
Fowler, V. M. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80052-4 · Cited by 152
Murphy, S. C., Samuel, B. U., Harrison, T., Speicher, K. D., Speicher, D. W., Reid, M. E., Prohaska, R., Low, P. S., Tanner, M. J., Mohandas, N., et al. (2003) · Blood · doi:10.1182/blood-2003-09-3165 · Cited by 151
Self-citationOhanian, V., Wolfe, L. C., John, K. M., Pinder, J. C., Lux, S. E., & Gratzer, W. B. (1984) · Biochemistry · doi:10.1021/bi00314a027 · Cited by 148
Embury, S., Clark, M. R., Monroy, G., & Mohandas, N. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111181 · Cited by 145
Self-citationMohandas, N., Winardi, R., Knowles, D., Leung, A., Parra, M., George, E., Conboy, J. G., & Chasis, J. A. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115636 · Cited by 142
Self-citationRegulation of phospholipid asymmetry in the erythrocyte membrane
Daleke, D. L. (2008) · Current Opinion in Hematology · doi:10.1097/moh.0b013e3282f97af7 · Cited by 136
Nicolas, V., Kim, C. L. V., Gane, P., Birkenmeier, C. S., Cartron, J., Colin, Y., & Mouro-Chanteloup, I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302816200 · Cited by 134
Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency
Jarolı́m, P., Murray, J., Rubin, H., Taylor, W., Prchal, J., Ballas, S., Snyder, L., Chrobák, L., Melrose, W., Brabec, V., et al. (1996) · Blood · doi:10.1182/blood.v88.11.4366.4366 · Cited by 130
Spectrin tetramer–dimer equilibrium and the stability of erythrocyte membrane skeletons
Liu, S., & Palek, J. (1980) · Nature · doi:10.1038/285586a0 · Cited by 129
The identification and sequence of the actin-binding domain of human red blood cell beta-spectrin.
Karinch, A. M., Zimmer, W. E., & Goodman, S. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38474-1 · Cited by 125
Yasin, Z., Witting, S. R., Palascak, M. B., Joiner, C. H., Rucknagel, D. L., & Franco, R. S. (2003) · Blood · doi:10.1182/blood-2002-11-3416 · Cited by 121
Rigid membranes of Malayan ovalocytes: a likely genetic barrier against malaria
Mohandas, N., Lie-Injo, L., Friedman, M. J., & Mak, J. W. (1984) · Blood · doi:10.1182/blood.v63.6.1385.1385 · Cited by 117
Self-citationStructural and functional diversity of blood group antigens
Cartron, J., & Colin, Y. (2001) · Transfusion Clinique et Biologique · doi:10.1016/s1246-7820(01)00142-2 · Cited by 113
An, X., Guo, X., Sum, H., Morrow, J. S., Gratzer, W. B., & Mohandas, N. (2003) · Biochemistry · doi:10.1021/bi035653h · Cited by 111
Self-citationShear-Response of the Spectrin Dimer-Tetramer Equilibrium in the Red Blood Cell Membrane
An, X., Lecomte, M., Chasis, J. A., Mohandas, N., & Gratzer, W. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204567200 · Cited by 110
Self-citationGlycophorin C content of human erythrocyte membrane is regulated by protein 4.1
Reid, M., Takakuwa, Y., Conboy, J., Tchernia, G., & Mohandas, N. (1990) · Blood · doi:10.1182/blood.v75.11.2229.2229 · Cited by 110
Self-citationSiegel, D. L., & Branton, D. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.3.775 · Cited by 108
Spectrin: a structural mediator between diverse plasma membrane proteins and the cytoplasm
Bennett, V. (1990) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(05)80030-4 · Cited by 104
Speicher, D. W., DeSilva, T. M., Speicher, K. D., Ursitti, J. A., Hembach, P., & Węglarz, L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53600-0 · Cited by 103
Basis of unique red cell membrane properties in hereditary ovalocytosis
Schofield, A. E., Tanner, M. J. A., Pinder, J. C., Clough, B., Bayley, P. M., Nash, G. B., Dluzewski, A. R., Reardon, D. M., Cox, T. M., Wilson, R. J., et al. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90254-h · Cited by 100
Tropomodulins: life at the slow end
Fischer, R. S., & Fowler, V. M. (2003) · Trends in Cell Biology · doi:10.1016/j.tcb.2003.09.007 · Cited by 96
Delaunay, J. (2004) · Seminars in Hematology · doi:10.1053/j.seminhematol.2004.02.005 · Cited by 95
Red blood cell membrane defects.
Iolascon, A., Perrotta, S., & Stewart, G. W. (2003) · PubMed · Cited by 88
Khan, A., Hanada, T., Mohseni, M., Jeong, J., Zeng, L., Gaetani, M., Li, D., Reed, B. C., Speicher, D. W., & Chishti, A. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707818200 · Cited by 88
Delaunay, J., & Dhermy, D. (1993) · PubMed · Cited by 84
Liu, S., Jarolim, P., Rubin, H., Palek, J., Amato, D., Hassan, K., Zaik, M., & Sapak, P. (1994) · Blood · doi:10.1182/blood.v84.10.3590.bloodjournal84103590 · Cited by 80
Human erythrocyte protein 4.1 is a phosphatidylserine binding protein.
Rybicki, A. C., Heath, R., Lubin, B. H., & Schwartz, R. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113303 · Cited by 80
Hassoun, H., Vassiliadis, J., Murray, J. M., Njølstad, P. R., Rogus, J. J., Ballas, S., Schaffer, F., Jarolı́m, P., Brabec, V., & Palek, J. (1997) · PubMed · doi:10.1182/blood.v90.1.398 · Cited by 79
An, X., Debnath, G., Guo, X., Liu, S., Lux, S. E., Baines, A. J., Gratzer, W. B., & Mohandas, N. (2005) · Biochemistry · doi:10.1021/bi047331z · Cited by 70
Self-citationDeSilva, T. M., Peng, K. C., Speicher, K. D., & Speicher, D. W. (1992) · Biochemistry · doi:10.1021/bi00159a030 · Cited by 69
An, X., Guo, X., Zhang, X., Baines, A. J., Debnath, G., Moyo, D., Salomao, M. A., Bhasin, N., Johnson, C. P., Discher, D. E., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513725200 · Cited by 68
Self-citationErythrocyte membrane transport physiology
Brugnara, C. (1997) · Current Opinion in Hematology · doi:10.1097/00062752-199704020-00008 · Cited by 68
An, X., Zhang, X., Debnath, G., Baines, A. J., & Mohandas, N. (2006) · Biochemistry · doi:10.1021/bi060015v · Cited by 61
Self-citationTurrini, F., Mannu, F., Arese, P., Yuan, J., & Low, P. S. (1993) · Blood · doi:10.1182/blood.v81.11.3146.3146 · Cited by 60
New insights into erythrocyte membrane organization and microelasticity
Discher, D. E. (2000) · Current Opinion in Hematology · doi:10.1097/00062752-200003000-00008 · Cited by 58
Hereditary ovalocytosis in Melanesians.
Amato, D., & Pb, B. (1977) · PubMed · Cited by 56
Bookchin, R. M., Etzion, Z., Sorette, M. P., Mohandas, N., Skepper, J. N., & Lew, V. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130198797 · Cited by 56
Self-citationGaetani, M., Mootien, S., Harper, S. L., Gallagher, P. G., & Speicher, D. W. (2008) · Blood · doi:10.1182/blood-2007-11-122457 · Cited by 54
Self-citationErythrocyte blood group antigens: not so simple after all [editorial; comment]
Telen, M. J. (1995) · Blood · doi:10.1182/blood.v85.2.299.299 · Cited by 54
Spectrin-based skeleton in red blood cells and malaria
Dhermy, D., Schrével, J., & Lecomte, M. (2007) · Current Opinion in Hematology · doi:10.1097/moh.0b013e3280d21afd · Cited by 48
Partial spectrin deficiency in hereditary pyropoikilocytosis
Coetzer, T., & Palek, J. (1986) · Blood · doi:10.1182/blood.v67.4.919.919 · Cited by 48
Some aspects of the pathophysiology of homozygous Hb CC erythrocytes.
Fabry, M. E., Kaul, D. K., Raventos, C., Baez, S., Rieder, R. F., & Nagel, R. L. (1981) · Journal of Clinical Investigation · doi:10.1172/jci110156 · Cited by 41
Johnson, C. P., Gaetani, M., Ortiz, V., Bhasin, N., Harper, S. L., Gallagher, P. G., Speicher, D. W., & Discher, D. E. (2006) · Blood · doi:10.1182/blood-2006-07-038588 · Cited by 40
Self-citationGiorgi, M., Cianci, C. D., Gallagher, P. G., & Morrow, J. S. (2001) · Experimental and Molecular Pathology · doi:10.1006/exmp.2001.2377 · Cited by 38
Self-citationMarchesi, S. L., Conboy, J. G., Agre, P. C., Letsinger, J. T., Marchesi, V. T., Speicher, D. W., & Mohandas, N. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114738 · Cited by 33
Self-citationMolecular basis for red cell membrane viscoelastic properties
Mohandas, N. (1992) · Biochemical Society Transactions · doi:10.1042/bst0200776 · Cited by 29
Self-citationIntegral Protein Linkage and the Bilayer-Skeletal Separation Energy in Red Blood Cells
Butler, J. T., Mohandas, N., & Waugh, R. E. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.129163 · Cited by 28
Self-citationUnique alpha-spectrin mutant in a kindred with common hereditary elliptocytosis.
Lane, P. A., Shew, R. L., Iarocci, T., Mohandas, N., Hays, T. S., & Mentzer, W. C. (1987) · Journal of Clinical Investigation · doi:10.1172/jci112911 · Cited by 26
Self-citationMohandas, N., & An, X. (2006) · Transfusion Clinique et Biologique · doi:10.1016/j.tracli.2006.02.017 · Cited by 25
Self-citationBESSIS, M. C., & Delpech, G. (1981) · PubMed · Cited by 25
Ion Transport and Volume Regulation in Red Blood Cells
Milanick, M. A., & Hoffman, J. F. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb46556.x · Cited by 22
Molecular basis of erythrocyte membrane disorders
Gallagher, P. G., & Ferriera, J. D. S. (1997) · Current Opinion in Hematology · doi:10.1097/00062752-199704020-00009 · Cited by 21
Self-citationLecomte, M., Nicolas, G., Dhermy, D., Pinder, J. C., & Gratzer, W. B. (1999) · European Biophysics Journal · doi:10.1007/s002490050201 · Cited by 19
Ion Transport and Volume Regulation in Red Blood Cells
Milanick, M. A., & Hoffman, J. F. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb54402.x · Cited by 19
Blood group antigens defined by the amino acid sequences of red cell surface proteins
Anstee, D. J. (1995) · Transfusion Medicine · doi:10.1111/j.1365-3148.1995.tb00179.x · Cited by 18
Rigid membranes of Malayan ovalocytes: a likely genetic barrier against malaria
Mohandas, N., Lie-Injo, L., Friedman, M. J., et al. (1984) · Blood · doi:10.1182/blood.v63.6.1385.bloodjournal6361385 · Cited by 14
Self-citation(1675) · Philosophical Transactions of the Royal Society of London · doi:10.1098/rstl.1675.0033 · Cited by 11
Research works printed but not linked: 1
- Gulliver, 1862, Blood of Vertebrata.
Cited by
Sorted by citations
A Review of Cell Adhesion Studies for Biomedical and Biological Applications
Khalili, A. A., & Ahmad, M. R. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160818149 · Cited by 999
Nicolson, G. L. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.10.019 · Cited by 790
Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging
Mohanty, J. G., Nagababu, E., & Rifkind, J. M. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00084 · Cited by 595
“This region of band 3 binds competitively both Hb, and a number of glycolytic enzymes (Mohandas and Gallagher, 2008).”
BackgroundGao, M., Liang, C., Song, X., Chen, Q., Jin, Q., Wang, C., & Liu, Z. (2017) · Advanced Materials · doi:10.1002/adma.201701429 · Cited by 593
Chen, K., Liu, J., Heck, S., Chasis, J. A., An, X., & Mohandas, N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909296106 · Cited by 516
Self-citation
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review