Cited by 1,089Erythrocyte Function and PathophysiologyLipid Membrane Structure and BehaviorHemoglobinopathies and Related Disorders

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 access

Mohandas, Narla, Gallagher, Patrick G.·2008·Blood

DOI 10.1182/blood-2008-07-161166PMC PMC2582001

Open this paper in CoChat — free account

Abstract

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.

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

Crossref · 10.1182/blood-2008-07-161166

Cites

106 of 106 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy
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
Mechanical Properties of the Red Cell Membrane in Relation to Molecular Structure and Genetic Defects
Mohandas, N., & Evans, E. (1994) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.23.060194.004035 · Cited by 563
Self-citation
Increased erythrocyte phosphatidylserine exposure in sickle cell disease: flow-cytometric measurement and clinical associations
Wood, 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

Show all 104 references

Research works printed but not linked: 1

Gulliver, 1862, Blood of Vertebrata.

Sorted by citations

Items 301–400 of 1,000

The influence of extracellular matrix proteins and mesenchymal stem cells on erythropoietic cell maturation
Lazar‐Karsten, P., Dorn, I., Meyer, G. A., Lindner, U., Driller, B., & Schlenke, P. (2010) · Vox Sanguinis · doi:10.1111/j.1423-0410.2010.01453.x · Cited by 33
C4d Deposits on the Surface of RBCs in Trauma Patients and Interferes With Their Function*
Muroya, T., Kannan, L., Ghiran, I. C., Shevkoplyas, S. S., Paz, Z., Tsokos, M., Lucca, J. J. D., Shapiro, N. I., & Tsokos, G. C. (2014) · Critical Care Medicine · doi:10.1097/ccm.0000000000000231 · Cited by 33
Effects of acute and chronic exercise on the osmotic stability of erythrocyte membrane of competitive swimmers
Paraíso, L. F., Gonçalves-e-Oliveira, A. F. M., Cunha, L. M., Neto, O. P. D. A., Pacheco, A. G., Araujo, K. B. G., Garrote-Filho, M. D. S., Neto, M. B., & Penha‐Silva, N. (2017) · PLoS ONE · doi:10.1371/journal.pone.0171318 · Cited by 32
Caspase-3 activation decreases lipid order in the outer plasma membrane leaflet during apoptosis: A fluorescent probe study
Pyrshev, K. A., Yesylevskyy, S. O., Mély, Y., Demchenko, A. P., & Klymchenko, A. S. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.08.002 · Cited by 32
Molecular mechanisms of deformability of Plasmodium -infected erythrocytes
Lavazec, C. (2017) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.11.011 · Cited by 32
Bottom up design of nanoparticles for anti-cancer diapeutics: “put the drug in the cancer’s food”
Needham, D., Arslanagic, A., Glud, K., Hervella, P., Karimi, L., Høeilund-Carlsen, P.-F., Kinoshita, K., Mollenhauer, J., Parra‐Ortiz, E., Utoft, A., et al. (2016) · Journal of drug targeting · doi:10.1080/1061186x.2016.1238092 · Cited by 31
Cation Channels in Erythrocytes - Historical and Future Perspective
Kaestner, L. (2011) · The Open Biology Journal · doi:10.2174/1874196701104010027 · Cited by 31
Multifunctional manipulation of red blood cells using optical tweezers
Xie, Y., & Liu, X. (2021) · Journal of Biophotonics · doi:10.1002/jbio.202100315 · Cited by 31
Red blood cell lingering modulates hematocrit distribution in the microcirculation
Rashidi, Y., Simionato, G., Zhou, Q., John, T., Kihm, A., Bendaoud, M., Krüger, T., Bernabéu, M. O., Kaestner, L., Laschke, M. W., et al. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.03.020 · Cited by 31
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin
Velásquez, F. C., Maté, S. M., Bakás, L. S., & Herlax, V. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.08.012 · Cited by 31
Mechanical Modeling of Red Blood Cells During Optical Stretching
Tan, Y., Sun, D. B., & Huang, W. (2010) · Journal of Biomechanical Engineering · doi:10.1115/1.4001042 · Cited by 31
ATP, an extracellular signaling molecule in red blood cells: A messenger for malaria?
Langsley, G., & Ramdani, G. (2014) · Biomedical Journal · doi:10.4103/2319-4170.132910 · Cited by 33
Chronic training increases blood oxidative damage but promotes health in elderly men
de Gonzalo‐Calvo, D., Fernández‐Garcia, B., de Luxán‐Delgado, B., Rodríguez‐González, S., Macia, M. G., Suárez, F. M., Solano, J. J., Rodríguez‐Colunga, M. J., & Coto‐Montes, A. M. (2012) · AGE · doi:10.1007/s11357-011-9358-6 · Cited by 31
Effects of flaxseed oil on anti-oxidative system and membrane deformation of human peripheral blood erythrocytes in high glucose level
Yang, W. Q., Fu, J., Yu, M., Huang, Q., Wang, D., Xu, J., Deng, Q., Yao, P., Huang, F., & Liu, L. (2012) · Lipids in Health and Disease · doi:10.1186/1476-511x-11-88 · Cited by 31
Aluminum Trichloride Induces Hypertension and Disturbs the Function of Erythrocyte Membrane in Male Rats
Zhang, Q., Cao, Z., Sun, X., Zhuang, C., Huang, W., & Li, Y. (2015) · Biological Trace Element Research · doi:10.1007/s12011-015-0504-3 · Cited by 31
The Impact of Two Combined Oral Contraceptives Containing Ethinyl Estradiol and Drospirenone on Whole Blood Clot Viscoelasticity and the Biophysical and Biochemical Characteristics of Erythrocytes
Emmerson, O., Bester, J., Lindeque, B. G., & Swanepoel, A. C. (2018) · Microscopy and Microanalysis · doi:10.1017/s1431927618015453 · Cited by 30
Effective 3D viscoelasticity of red blood cells measured by diffraction phase microscopy
Wang, R., Ding, H., Mir, M., Tangella, K. V., & Popescu, G. (2011) · Biomedical Optics Express · doi:10.1364/boe.2.000485 · Cited by 30
Structure Governs the Deformability of Polymer Particles in a Microfluidic Blood Capillary Model
Sun, H., Björnmalm, M., Cui, J., Wong, E. H. H., Dai, Y., Dai, Q., Qiao, G. G., & Caruso, F. (2015) · ACS Macro Letters · doi:10.1021/acsmacrolett.5b00591 · Cited by 31
Interpreting and Integrating Clinical and Anatomic Pathology Results
Ramaiah, L., Hinrichs, M. J., Skuba, E., Iverson, W. O., & Ennulat, D. (2016) · Toxicologic Pathology · doi:10.1177/0192623316677068 · Cited by 30
Spatial Relationship and Functional Relevance of Three Lipid Domain Populations at the Erythrocyte Surface
Conrard, L., Stommen, A., Cloos, A., Steinkühler, J., Dimova, R., Pollet, H., & Tyteca, D. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000495645 · Cited by 31
Blood rheology biomarkers in sickle cell disease
Lu, M., Rab, M. A. E., Shevkoplyas, S. S., & Sheehan, V. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370219900494 · Cited by 30
Syk Kinase Inhibitors Synergize with Artemisinins by Enhancing Oxidative Stress in Plasmodium falciparum-Parasitized Erythrocytes
Tsamesidis, I., Reybier, K., Marchetti, G., Pau, M. C., Virdis, P., Fozza, C., Nepveu, F., Low, P. S., Turrini, F. M., & Pantaleo, A. (2020) · Antioxidants · doi:10.3390/antiox9080753 · Cited by 30
Bioinspired Perfluorocarbon‐Based Oxygen Carriers with Concave Shape and Deformable Shell
Fu, X., Ohta, S., Kawakatsu, T., Kamihira, M., Sakai, Y., & Ito, T. (2021) · Advanced Materials Technologies · doi:10.1002/admt.202100573 · Cited by 30
Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins
Barshtein, G., Gural, A., Arbell, D., Barkan, R. B., Livshits, L., Pajić‐Lijaković, I., & Yedgar, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612755 · Cited by 32
Concise Review: Production of Cultured Red Blood Cells from Stem Cells
Bouhassira, E. E. (2012) · Stem Cells Translational Medicine · doi:10.5966/sctm.2012-0097 · Cited by 30
Essential Function of Protein 4.1G in Targeting of Membrane Protein Palmitoylated 6 into Schmidt-Lanterman Incisures in Myelinated Nerves
Terada, N., Saitoh, Y., Ohno, N., Komada, M., Saitoh, S., Peles, E., & Ohno, S. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05945-11 · Cited by 30
Red Blood Cell Homeostasis: Pharmacological Interventions to Explore Biochemical, Morphological and Mechanical Properties
Cluitmans, J. C. A., Gevi, F., Siciliano, A., Mattè, A., Leal, J. K. F., Franceschi, L. D., Zolla, L., Brock, R. E., Adjobo-Hermans, M. J. W., & Bosman, G. J. G. C. M. (2016) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2016.00010 · Cited by 30
Dielectric Response of Cytoplasmic Water and Its Connection to the Vitality of Human Red Blood Cells: I. Glucose Concentration Influence
Levy, E., Barshtein, G., Livshits, L., Ishai, P. B., & Feldman, Y. D. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b06996 · Cited by 30
Cdk6 contributes to cytoskeletal stability in erythroid cells
Uras, I. Z., Scheicher, R., Kollmann, K., Glösmann, M., Prchal‐Murphy, M., Tigan, A.-S., Fux, D. A., Altamura, S., Neves, J., Muckenthaler, M. U., et al. (2017) · Haematologica · doi:10.3324/haematol.2016.159947 · Cited by 31
Biomimetic Virulomics for Capture and Identification of Cell-Type Specific Effector Proteins
Lapek, J. D., Fang, R. H., Wei, X., Li, P., Wang, B., Zhang, L., & Gonzalez, D. J. (2017) · ACS Nano · doi:10.1021/acsnano.7b02650 · Cited by 30
Extraction methods of red blood cell membrane proteins for Multidimensional Protein Identification Technology (MudPIT) analysis
Palma, A. D., Roveri, A., Zaccarin, M., Benazzi, L., Daminelli, S., Pantano, G., Buttarello, M., Ursini, F., Gion, M., & Mauri, P. (2010) · Journal of Chromatography A · doi:10.1016/j.chroma.2010.06.045 · Cited by 29
The Pleiotropic Effects of GATA1 and KLF1 in Physiological Erythropoiesis and in Dyserythropoietic Disorders
Barbarani, G., Fugazza, C., Strouboulis, J., & Ronchi, A. E. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00091 · Cited by 26
From myofibril to membrane; the transitional junction at the intercalated disc
Pauline, M. (2011) · Frontiers in bioscience · doi:10.2741/3972 · Cited by 29
Mechanically Encoded Cellular Shapes for Synthesis of Anisotropic Mesoporous Particles
Meyer, K. C., Coker, E. N., Bolintineanu, D., & Kaehr, B. (2014) · Journal of the American Chemical Society · doi:10.1021/ja506718z · Cited by 29
Erythrocyte-based drug delivery in Transfusion Medicine: Wandering questions seeking answers
Tzounakas, V. L., Karadimas, D. G., Papassideri, I. S., Seghatchian, J., & Antonelou, M. H. (2017) · Transfusion and Apheresis Science · doi:10.1016/j.transci.2017.07.015 · Cited by 29
Metabolite and protein shifts in mature erythrocyte under hypoxia
Jin, X., Zhang, Y., Wang, D., Zhang, X., Li, Y., Wang, D., Liang, Y., Wang, J., Zheng, L., Song, H., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109315 · Cited by 28
Enhanced delivery of CRISPR/Cas9 system based on biomimetic nanoparticles for hepatitis B virus therapy
Wu, K., He, M., Mao, B., Xing, Y., Wei, S., Jiang, D., Wang, S., Alkuhali, A. A., Guo, J., Gan, Z., et al. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.08.019 · Cited by 28
Precision‐Guided Stealth Missiles in Biomedicine: Biological Carrier‐Mediated Nanomedicine Hitchhiking Strategy
Zhou, Y., Wang, X., Zhang, D., Cui, H., Tian, X., Du, W., Yang, Z., Wan, D., Qiu, Z., Liu, C., et al. (2025) · Advanced Science · doi:10.1002/advs.202504672 · Cited by 28
Involvement of membrane tubulin in erythrocyte deformability and blood pressure
Amaiden, M. R., Monesterolo, N. E., Santander, V. S., Campetelli, A. N., Arce, C. A., Pié, J., Hope, S. I., Vatta, M. S., & Casale, C. H. (2012) · Journal of Hypertension · doi:10.1097/hjh.0b013e328353b19a · Cited by 28
The neuronal and actin commitment: Why do neurons need rings?
Leite, S. C., & Sousa, M. M. (2016) · Cytoskeleton · doi:10.1002/cm.21273 · Cited by 28
Exome sequencing for diagnosis of congenital hemolytic anemia
Mansour‐Hendili, L., Aissat, A., Badaoui, B., Sakka, M., Gameiro, C., Ortonne, V., Wagner‐Ballon, O., Pissard, S., Picard, V., Ghazal, K., et al. (2020) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-020-01425-5 · Cited by 28
A Dynamic Membrane‐Active Glycopeptide for Enhanced Protection of Human Red Blood Cells against Freeze‐Stress
Gao, S., Niu, Q., Wang, Y., Ren, L., Chong, J., Zhu, K., & Yuan, X. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202202516 · Cited by 28
In-plane elasticity controls the full dynamics of red blood cells in shear flow
Mendez, S., & Abkarian, M. (2018) · Physical Review Fluids · doi:10.1103/physrevfluids.3.101101 · Cited by 28
Erythroid glucose transport in health and disease
Guizouarn, H., & Allegrini, B. (2020) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-020-02406-0 · Cited by 30
Congenital Hemolytic Anemias: Is There a Role for the Immune System?
Zaninoni, A., Fermo, E., Vercellati, C., Marcello, A. P., Barcellini, W., & Bianchi, P. I. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01309 · Cited by 27
Red Blood Cell Metabolism in Pyruvate Kinase Deficient Patients
Roy, M. K., Cendali, F. I., Ooyama, G., Gamboni, F., Morton, H. D., & D’Alessandro, A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.735543 · Cited by 27
Abnormal erythroid maturation leads to microcytic anemia in the TSAP6/Steap3 null mouse model
Blanc, L., Papoin, J., Debnath, G., Vidal, M., Amson, R. B., Telerman, A., An, X., & Mohandas, N. (2014) · American Journal of Hematology · doi:10.1002/ajh.23920 · Cited by 26
Self-citation
A synbiotic containing Lactobacillus acidophilus CHO-220 and inulin improves irregularity of red blood cells
Ooi, L.-G., Bhat, R., Rosma, A., Yuen, K. H., & Liong, M. (2010) · Journal of Dairy Science · doi:10.3168/jds.2010-3330 · Cited by 27
Rotation and deformation of human red blood cells with light from tapered fiber probes
Liu, X., Huang, J., Li, Y., Zhang, Y., & Li, B. (2016) · Nanophotonics · doi:10.1515/nanoph-2016-0115 · Cited by 27
Lipopeptisomes: Anticancer peptide-assembled particles for fusolytic oncotherapy
Aronson, M. R., Simonson, A. W., Orchard, L., Llinás, M., & Medina, S. H. (2018) · Acta Biomaterialia · doi:10.1016/j.actbio.2018.09.025 · Cited by 27
Evolution of the spectrin-based membrane skeleton
Baines, A. J. (2010) · Transfusion Clinique et Biologique · doi:10.1016/j.tracli.2010.06.008 · Cited by 26
A robust mass spectrometry method for rapid profiling of erythrocyte ghost membrane proteomes
Fye, H. K. S., Mrosso, P., Bruce, L. J., Thézénas, M., Davis, S. A., Fischer, R., Rwegasira, G. L., Makani, J., & Kessler, B. M. (2018) · Clinical Proteomics · doi:10.1186/s12014-018-9190-4 · Cited by 26
Are There Differences in the Anthropometric, Hemodynamic, Hematologic, and Biochemical Profiles between Late- and Early-Onset Preeclampsia?
de Freitas, M. A. R., da Costa, A. V., de Medeiros, L. A., Garrote-Filho, M. D. S., Diniz, A. L. D., & Penha‐Silva, N. (2018) · Obstetrics and Gynecology International · doi:10.1155/2018/9628726 · Cited by 28
Deformation behaviour of stomatocyte, discocyte and echinocyte red blood cell morphologies during optical tweezers stretching
Geekiyanage, N. M., Sauret, E., Saha, S. C., Flower, R. L., & Gu, Y. (2020) · Biomechanics and Modeling in Mechanobiology · doi:10.1007/s10237-020-01311-w · Cited by 26
Role Ca2+ in Mechanisms of the Red Blood Cells Microrheological Changes
Muravyov, A. V., & Tikhomirova, I. A. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2888-2_47 · Cited by 26
Alterations of the Erythrocyte Membrane during Sepsis
Serroukh, Y. I. M., Djebara, S., Lelubre, C., Boudjeltia, K. Z., Biston, P., & Piagnerelli, M. (2012) · Critical Care Research and Practice · doi:10.1155/2012/702956 · Cited by 26
Abnormal red cell features associated with hereditary neurodegenerative disorders
Franceschi, L. D., Bosman, G. J. C. G. M., & Mohandas, N. (2014) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000035 · Cited by 26
Self-citation
Lateral migration of a capsule in a parabolic flow
Nix, S., Imai, Y., & Ishikawa, T. (2015) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2015.11.038 · Cited by 26
Biphasic impairment of erythrocyte deformability in response to repeated, short duration exposures of supraphysiological, subhaemolytic shear stress
McNamee, A. P., Tansley, G. D., Sabapathy, S., & Simmonds, M. J. (2016) · Biorheology · doi:10.3233/bir-15108 · Cited by 26
Multimodal analysis ofPlasmodium knowlesi‐infected erythrocytes reveals large invaginations, swelling of the host cell, and rheological defects
Liu, B., Blanch, A. J., Namvar, A., Carmo, O. M. S., Tiash, S., Andrew, D. W., Hanssen, E. G., Rajagopal, V., Dixon, M. W. A., & Tilley, L. M. (2019) · Cellular Microbiology · doi:10.1111/cmi.13005 · Cited by 26
Cellular microdomains for nitric oxide signaling in endothelium and red blood cells
Leo, F., Hutzler, B., Ruddiman, C. A., Isakson, B. E., & Cortese-Krott, M. M. (2020) · Nitric Oxide · doi:10.1016/j.niox.2020.01.002 · Cited by 28
Antioxidant comparative effects of two grape pomace Mexican extracts from vineyards on erythrocytes
García-Becerra, L., Mitjans, M., Rivas-Morales, C., Verde‐Star, M. J., Oranday-Cárdenas, A., & Vinardell, M. P. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.08.131 · Cited by 26
Renitrosylation of banked human red blood cells improves deformability and reduces adhesivity
Riccio, D. A., Zhu, H., Foster, M. W., Huang, B., Hofmann, C. L., Palmer, G. M., & McMahon, T. (2015) · Transfusion · doi:10.1111/trf.13189 · Cited by 25
Red blood cell shape and deformability in the context of the functional evolution of its membrane structure
Svetina, S. (2012) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-012-0001-z · Cited by 25
Effect of Radiographic Contrast Media on the Spectrin/Band3-Network of the Membrane Skeleton of Erythrocytes
Franke, R., Scharnweber, T., Fuhrmann, R., Wenzel, F., Krüger, A., Mrowietz, C., & Jung, F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089512 · Cited by 25
Continuous noninvasive glucose monitoring; water as a relevant marker of glucose uptake in vivo
Caduff, A., Ishai, P. B., & Feldman, Y. D. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00601-7 · Cited by 25
Modelling of Red Blood Cell Morphological and Deformability Changes during In-Vitro Storage
Geekiyanage, N. M., Sauret, E., Saha, S. C., Flower, R. L., & Gu, Y. (2020) · Applied Sciences · doi:10.3390/app10093209 · Cited by 25
Red Blood Cell Stiffness and Adhesion Are Species-Specific Properties Strongly Affected by Temperature and Medium Changes in Single Cell Force Spectroscopy
Baier, D., Müller, T., Mohr, T. T., & Windberger, U. B. (2021) · Molecules · doi:10.3390/molecules26092771 · Cited by 25
Persistent red blood cells retain their ability to move in microcapillaries under high levels of oxidative stress
Besedina, N. A., Skverchinskaya, E. A., Shmakov, S. V., Ivanov, A. S., Викторович, М. И., & Bukatin, A. (2022) · Communications Biology · doi:10.1038/s42003-022-03620-5 · Cited by 25
Alterations of hemorheological parameters and tubulin content in erythrocytes from diabetic subjects
Nigra, A. D., Monesterolo, N. E., Rivelli, J. F., Amaiden, M. R., Campetelli, A. N., Casale, C. H., & Santander, V. S. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.02.016 · Cited by 25
Insights into the morphological pattern of erythrocytes' aging: Coupling quantitative AFM data to microcalorimetry and Raman spectroscopy
Dinarelli, S., Longo, G., Krumova, S., Todinova, S. J., Danailova, A., Taneva, S. G., Lenzi, E., Mussi, V., & Girasole, M. (2018) · Journal of Molecular Recognition · doi:10.1002/jmr.2732 · Cited by 25
Intravital Vascular Phototheranostics and Real-Time Circulation Dynamics of Micro- and Nanosized Erythrocyte-Derived Carriers
Jia, W., Burns, J. M., Villantay, B., Tang, J. C., Vankayala, R., Lertsakdadet, B. S., Choi, B., Nelson, J. S., & Anvari, B. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b18624 · Cited by 25
Core–Shell Microfiber Encapsulation Enables Glycerol-Free Cryopreservation of RBCs with High Hematocrit
Qin, X., Chen, Z., Shen, L., Liu, H., Ouyang, X., & Zhao, G. (2023) · Nano-Micro Letters · doi:10.1007/s40820-023-01213-3 · Cited by 24
Spectrin Tetramer Formation Is Not Required for Viable Development in Drosophila
Khanna, M. R., Mattie, F. J., Browder, K. C., Radyk, M. D., Crilly, S. E., Bakerink, K. J., Harper, S. L., Speicher, D. W., & Thomas, G. H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.615427 · Cited by 24
Biomechanics of Ex Vivo-Generated Red Blood Cells Investigated by Optical Tweezers and Digital Holographic Microscopy
Bernecker, C., Lima, M. A. R. B. F., Ciubotaru, C. D., Schlenke, P., Dorn, I., & Cojoc, D. (2021) · Cells · doi:10.3390/cells10030552 · Cited by 24
Nanomechanics of Blood Clot and Thrombus Formation
Domingues, M. M., Carvalho, F. A., & Santos, N. C. (2022) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111821-072110 · Cited by 24
Nanoscale dynamics of actin filaments in the red blood cell membrane skeleton
Nowak, R. B., Alimohamadi, H., Pestonjamasp, K. N., Rangamani, P., & Fowler, V. M. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-03-0107 · Cited by 24
Knobs, Adhesion, and Severe Falciparum Malaria
Wiser, M. F. (2023) · Tropical Medicine and Infectious Disease · doi:10.3390/tropicalmed8070353 · Cited by 24
Genetic disarray follows mutant KLF1-E325K expression in a congenital dyserythropoietic anemia patient
Varricchio, L., Planutis, A., Manwani, D. G., Jaffray, J., Mitchell, W. B., Migliaccio, A. R., & Bieker, J. J. (2019) · Haematologica · doi:10.3324/haematol.2018.209858 · Cited by 24
A model for coordinating nuclear mechanics and membrane remodeling to support nuclear integrity
King, M. C., & Lusk, C. P. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.03.009 · Cited by 23
Impact of the membrane viscosity on the tank-treading behavior of red blood cells
Mattéoli, P., Nicoud, F., & Mendez, S. (2021) · Physical Review Fluids · doi:10.1103/physrevfluids.6.043602 · Cited by 23
AAPH-induced oxidative damage reduced anion exchanger 1 (SLC4A1/AE1) activity in human red blood cells: protective effect of an anthocyanin-rich extract
Remigante, A., Spinelli, S., Patanè, G. T., Barreca, D., Straface, E., Gambardella, L., Bozzuto, G., Caruso, D., Falliti, G., Dossena, S., et al. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1303815 · Cited by 23
Biophysical investigation of living monocytes in flow by collaborative coherent imaging techniques
Dannhauser, D., Rossi, D., Memmolo, P., Fińizio, A., Ferraro, P., Netti, P. A., & Causa, F. (2018) · Biomedical Optics Express · doi:10.1364/boe.9.005194 · Cited by 23
The role of the erythrocyte in the outcome of pregnancy with preeclampsia
de Freitas, M. A. R., da Costa, A. V., de Medeiros, L. A., Cunha, L. M., Filho, U. C., Garrote-Filho, M. D. S., Diniz, A. L. D., & Penha‐Silva, N. (2019) · PLoS ONE · doi:10.1371/journal.pone.0212763 · Cited by 23
Membrane skeleton modulates erythroid proteome remodeling and organelle clearance
Liu, Y., Mei, Y., Han, X., Korobova, F. V., Prado, M. A., Yang, J. C., Peng, Z., Paulo, J. A., Gygi, S. P., Finley, D. J., et al. (2020) · Blood · doi:10.1182/blood.2020006673 · Cited by 24
Surface-functionalized bacteria: Frontier explorations in next-generation live biotherapeutics
Jiang, J.-N., Kong, F., Lei, Q., & Zhang, X. (2024) · Biomaterials · doi:10.1016/j.biomaterials.2024.123029 · Cited by 24
Evolution of surface area and membrane shear modulus of matured human red blood cells during mechanical fatigue
Wei, Q., Wang, X., Zhang, C., Dao, M., & Gong, X. (2023) · Scientific Reports · doi:10.1038/s41598-023-34605-x · Cited by 22
Activation of pyruvate kinase as therapeutic option for rare hemolytic anemias: Shedding new light on an old enzyme
van Dijk, M. J., de Wilde, J. R. A., Bartels, M., Kuo, K. H. M., Glenthøj, A. B., Rab, M. A. E., van Beers, E. J., & van Wijk, R. (2023) · Blood Reviews · doi:10.1016/j.blre.2023.101103 · Cited by 22
Chapter 4 Cytoskeletal Control of Red Blood Cell Shape
Gov, N. S., Cluitmans, J. C. A., Sens, P., & Bosman, G. J. C. G. M. (2009) · Elsevier eBooks · doi:10.1016/s1554-4516(09)10004-2 · Cited by 23
Single Particle Electron Microscopy Analysis of the Bovine Anion Exchanger 1 Reveals a Flexible Linker Connecting the Cytoplasmic and Membrane Domains
Jiang, J., Magilnick, N., Tsirulnikov, K., Abuladze, N. K., Atanasov, I. C., Ge, P., Mohandas, N., Pushkin, A., Zhou, Z. H., & Kurtz, I. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055408 · Cited by 22
Self-citation
Characterizing osmotic lysis kinetics under microfluidic hydrodynamic focusing for erythrocyte fragility studies
Zhan, Y., Loufakis, D. N., Bao, N., & Lu, C. (2012) · Lab on a Chip · doi:10.1039/c2lc40522a · Cited by 22
Validated hemoglobin‐depletion approach for red blood cell lysate proteome analysis by means of 2 D PAGE and O rbitrap MS
Walpurgis, K., Kohler, M., Thomas, A., Wenzel, F., Geyer, H., Schänzer, W., & Thevis, M. (2012) · Electrophoresis · doi:10.1002/elps.201200151 · Cited by 22
Hemin induces autophagy in a leukemic erythroblast cell line through the LRP1 receptor
Grosso, R. A., Subirada, P. V., Sanchez, M. C., Chiabrando, G. A., Colombo, M. I., & Fader, C. M. (2018) · Bioscience Reports · doi:10.1042/bsr20181156 · Cited by 21
Phosphinate-based mitochondria-targeted fluorescent probe for imaging and detection of endogenous superoxide in live cells and in vivo
Huang, S., Zhang, X., Liu, Y., Gui, J., Wang, R., Han, L., Jia, H., & Du, L. (2019) · Talanta · doi:10.1016/j.talanta.2018.12.080 · Cited by 22
Computational Identification of Phospho-Tyrosine Sub-Networks Related to Acanthocyte Generation in Neuroacanthocytosis
Franceschi, L. D., Scardoni, G., Tomelleri, C., Danek, A., Walker, R. H., Jung, H. H., Bader, B., Mazzucco, S., Dotti, M. T., Siciliano, A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031015 · Cited by 21
Clinical Diagnosis of Red Cell Membrane Disorders: Comparison of Osmotic Gradient Ektacytometry and Eosin Maleimide (EMA) Fluorescence Test for Red Cell Band 3 (AE1, SLC4A1) Content for Clinical Diagnosis
Zaidi, A. U., Buck, S. A., Gadgeel, M., Herrera‐Martinez, M., Mohan, A., JOHNSON, K. E. E., Bagla, S., Johnson, R. M., & Ravindranath, Y. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00636 · Cited by 21
Erythrocyte flow through the interendothelial slits of the splenic venous sinus
Dao, M., Macdonald, I. A., & Asaro, R. J. (2021) · Biomechanics and Modeling in Mechanobiology · doi:10.1007/s10237-021-01503-y · Cited by 21
Red blood cell triglycerides—a unique pool that incorporates plasma-free fatty acids and relates to metabolic health
Song, Y., & Jensen, M. D. (2021) · Journal of Lipid Research · doi:10.1016/j.jlr.2021.100131 · Cited by 21
Shape-directed drug release and transport of erythrocyte-like nanodisks augment chemotherapy
Wang, N., Li, J., Wang, J., Nie, D., Jiang, X., Zhuo, Y., & Yu, M. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.09.005 · Cited by 21
Recent developments in the use of pyruvate kinase activators as a new approach for treating sickle cell disease
Parekh, D. S., Eaton, W. A., & Thein, S. L. (2023) · Blood · doi:10.1182/blood.2023021167 · Cited by 23

Authors: Mohandas, N., & Gallagher, P. G.
Affiliations: New York Blood Center (US)
Yale University (US)
ORCID: Mohandas, Narla
Gallagher, Patrick G.
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
DOI: 10.1182/blood-2008-07-161166
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

Red cell membrane: past, present, and future

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks