The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
Extracellular hemin crisis triggers acute chest syndrome in sickle mice
Open accessAbstract
The prevention and treatment of acute chest syndrome (ACS) is a major clinical concern in sickle cell disease (SCD).However, the mechanism underlying the pathogenesis of ACS remains elusive.We tested the hypothesis that the hemolysis byproduct hemin elicits events that induce ACS.Infusion of a low dose of hemin caused acute intravascular hemolysis and autoamplification of extracellular hemin in transgenic sickle mice, but not in sickle-trait littermates.The sickle mice developed multiple symptoms typical of ACS and succumbed rapidly.Pharmacologic inhibition of TLR4 and hemopexin replacement therapy prior to hemin infusion protected sickle mice from developing ACS.Replication of the ACS-like phenotype in nonsickle mice revealed that the mechanism of lung injury due to extracellular hemin is independent of SCD.Using genetic and bone marrow chimeric tools, we confirmed that TLR4 expressed in nonhematopoietic vascular tissues mediated this lethal type of acute lung injury.Respiratory failure was averted after the onset of ACS-like symptoms in sickle mice by treating them with recombinant hemopexin.Our results reveal a mechanism that helps to explain the pathogenesis of ACS, and we provide proof of principle for therapeutic strategies to prevent and treat this condition in mice. Results Extracellular hemin elevation causes a lethal hemolytic crisis in sickle mice.To mimic acute extracellular hemin release, transgenic Townes sickle mice (referred to herein as SS mice; see Methods) and control sickletrait (AS) and wild-type human Hb (AA) mice were infused with a relatively low dose of purified hemin (35 μmol/kg).No adverse effects were seen in the control mice, but a majority of SS mice developed labored breathing and died within 2 hours (Figure 1A).We confirmed these acute adverse effects in a second murine model of SCD (Berkeley sickle mice; see Methods) and showed that the lethality rate was dependent on the dose of hemin (Figure 1B).A previous study had shown that 40 μmol/kg hemin given i.p. did not cause any fatalities in the Berkeley sickle mouse (26).A higher dose (70 μmol/kg) given i.v. had no adverse effects in wild-type mice (17, 27); moreover, the SS mouse deaths occurred 24 hours before hepatic failure onset, due to hemin overload in septic mice (28).Thus, our results in the SS mice revealed an unusual effect of extracellular hemin that had not previously been described.Plasma hemopexin (Hx) levels decreased sharply in all animals, coincident with nearly 50% clearance of the hemin bolus within Conflict of interest: The authors have declared that no conflict of interest exists.
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?
The cited source says what the claim attributes to it.
In the citing paper
“animal models showing that heme is directly responsible for acute lung injury in SCD mouse models (89).”
From Pathophysiology of Sickle Cell Disease (2019) · cites this paper as [89]
The cited source says what the claim attributes to it.
In the citing paper
“high levels of hemopexin, the enzyme that scavenges heme, can rescue acute lung injury (89), while HO-1 deficiency potentiates it (57).”
From Pathophysiology of Sickle Cell Disease (2019) · cites this paper as [89]
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
Mortality in sickle cell disease. Life expectancy and risk factors for early death
Platt, O. S., Brambilla, D. J., Rosse, W. F., Milner, P. F., Castro, O., Steinberg, M. H., & Klug, P. P. (1994) · New England Journal of Medicine · doi:10.1056/nejm199406093302303 · Cited by 3,320 · cited 1×
“Acute chest syndrome (ACS) is the second most common reason for hospital admission of SCD patients (2) and the leading cause of referral to intensive care units (3), and it is associated with a high mortality rate (4).”
Animal models of acute lung injury
Matute‐Bello, G., Frevert, C. W., & Martin, T. R. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00010.2008 · Cited by 1,762
Endotoxin-tolerant Mice Have Mutations in Toll-like Receptor 4 ( Tlr4 )
Qureshi, S. T., Larivière, L., Leveque, G., Clermont, S., Moore, K. J., Gros, P., & Malo, D. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.4.615 · Cited by 1,532
Causes and Outcomes of the Acute Chest Syndrome in Sickle Cell Disease
Vichinsky, E. P., Neumayr, L. D., Earles, A. N., Williams, R., Lennette, E. T., Dean, D., Nickerson, B., Orringer, E., McKie, V., Bellevue, R., et al. (2000) · New England Journal of Medicine · doi:10.1056/nejm200006223422502 · Cited by 1,234
Opal, S. M., Laterre, P.-F., Francois, B., LaRosa, S. P., Angus, D. C., Mira, J.-P., Wittebole, X., Dugernier, T., Perrotin, D., Tidswell, M., et al. (2013) · JAMA · doi:10.1001/jama.2013.2194 · Cited by 812
Castro, O. L., Brambilla, D. J., Thorington, B. D., Reindorf, C. A., Scott, R., GILLETTE, P. N., Vera, J., & Levy, P. S. (1994) · Blood · doi:10.1182/blood.v84.2.643.643 · Cited by 805
Pro-oxidant and cytotoxic effects of circulating heme
Jeney, V., Balla, J., Yachie, A., Varga, Z., Vercellotti, G. M., Eaton, J. W., & Balla, G. (2002) · Blood · doi:10.1182/blood.v100.3.879 · Cited by 633
Castro, O. L., Brambilla, D. J., Thorington, B. D., et al. (1994) · Blood · doi:10.1182/blood.v84.2.643.bloodjournal842643 · Cited by 615
Characterization of Heme as Activator of Toll-like Receptor 4
Figueiredo, R. T., Fernandez, P. L., Mourao-Sa, D. S., Porto, B. N., Dutra, F. F., Alves, L. S., Oliveira, M. F., Oliveira, P. L., Graça-Souza, A. V., & Bozza, M. T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610737200 · Cited by 576
Hemmi, H., Takeuchi, O., Sato, S., Yamamoto, M., Kaisho, T., Sanjo, H., Kawai, T., Hoshino, K., Takeda, K., & Akira, S. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040520 · Cited by 576
Flagged first, then by citations
Research works printed but not linked: 1
- Sprinkle, 1986, Am J Pediatr Hematol Oncol., 8, 105
Cited by
Sorted by citations
Items 101–200 of 282
The clinical relevance of heme detoxification by the macrophage heme oxygenase system
Yeudall, S., Upchurch, C. M., & Leitinger, N. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1379967 · Cited by 36
Pain in sickle cell disease: current and potential translational therapies
Sagi, V., Mittal, A., Tran, H., & Gupta, K. (2021) · Translational research · doi:10.1016/j.trsl.2021.03.007 · Cited by 38
Mouse models of sickle cell disease: Imperfect and yet very informative
Kamimura, S., Smith, M. L., Vogel, S., Almeida, L. E. F., Thein, S. L., & Quezado, Z. (2023) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2023.102776 · Cited by 37
Tang, A., Strat, A. N., Rahman, M., Zhang, H., Bao, W., Liu, Y., Shi, D., An, X., Manwani, D. G., Shi, P. A., et al. (2021) · Blood · doi:10.1182/blood.2021012663 · Cited by 33
Heme metabolism in nonerythroid cells
Dunaway, L. S., Loeb, S. A., Petrillo, S., Tolosano, E., & Isakson, B. E. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107132 · Cited by 37
Nonhematopoietic Nrf2 dominantly impedes adult progression of sickle cell anemia in mice
Ghosh, S., Ihunnah, C. A., Hazra, R., Walker, A. L., Hansen, J. M., Archer, D. R., Owusu-Ansah, A. T., & Ofori-Acquah, S. F. (2016) · JCI Insight · doi:10.1172/jci.insight.81090 · Cited by 33
Self-citationThere is blood in the water: hemolysis, hemoglobin, and heme in acute lung injury
Gaggar, A., & Patel, R. P. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00312.2016 · Cited by 31
Inflammatory and oxidative stress phenotypes in transgenic sickle cell mice
Charrin, E., Ofori-Acquah, S. F., Nader, É., Skinner, S. C., Connes, P., Pialoux, V., Joly, P., & Martin, C. (2016) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2016.10.020 · Cited by 31
Self-citationP-selectin–deficient mice to study pathophysiology of sickle cell disease
Bennewitz, M. F., Tütüncüoğlu, E., Gudapati, S., Brzóska, T., Watkins, S. C., Monga, S. P., Pradhan‐Sundd, T., & Sundd, P. (2020) · Blood Advances · doi:10.1182/bloodadvances.2019000603 · Cited by 32
Belcher, J. D., Chen, C., Nguyen, J., Abdulla, F. A., Nguyen, P., Nguyen, T. M., Okeley, N. M., Benjamin, D. R., Senter, P. D., & Vercellotti, G. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117772 · Cited by 31
Prestes, E. B., Alves, L. S., Rodrigues, D. A. S., Dutra, F. F., Fernández, P. L., Paiva, C. N., Kagan, J. C., & Bozza, M. T. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1900886 · Cited by 29
Hemopexin dosing improves cardiopulmonary dysfunction in murine sickle cell disease
Buehler, P. W., Swindle, D. C., Pak, D. I., Ferguson, S. K., Majka, S. M., Karoor, V., Moldovan, R., Sintas, C., Black, J., Gentinetta, T., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.08.238 · Cited by 29
Nyffenegger, N., Zennadi, R., Kalleda, N., Flace, A., Ingoglia, G., Buzzi, R. M., Doucerain, C., Buehler, P. W., Schaer, D. J., Dürrenberger, F., et al. (2022) · Blood · doi:10.1182/blood.2021014716 · Cited by 30
Complement in sickle cell disease and targeted therapy: I know one thing, that I know nothing
Tampaki, A., Gavriilaki, E., Varelas, C., Anagnostopoulos, Α., & Vlachaki, E. (2021) · Blood Reviews · doi:10.1016/j.blre.2021.100805 · Cited by 29
Sickle cell vaso-occlusion: The dialectic between red cells and white cells
Conran, N., & Embury, S. H. (2021) · Experimental Biology and Medicine · doi:10.1177/15353702211005392 · Cited by 31
Association of plasma CD40L with acute chest syndrome in sickle cell anemia
Garrido, V. T., Sonzogni, L., Nkya, S. W., Costa, F. F., Conran, N., & Thein, S. L. (2017) · Cytokine · doi:10.1016/j.cyto.2017.05.017 · Cited by 27
Sickle cell disease as a vascular disorder
Ofori-Acquah, S. F. (2020) · Expert Review of Hematology · doi:10.1080/17474086.2020.1758555 · Cited by 28
Self-citationHeme Induces IL-6 and Cardiac Hypertrophy Genes Transcripts in Sickle Cell Mice
Gbotosho, O. T., Kapetanaki, M. G., Ghosh, S., Villanueva, F. S., Ofori-Acquah, S. F., & Kato, G. J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01910 · Cited by 27
Self-citationRole of complement in alloimmunization and hyperhemolysis
Chonat, S., Mener, A., Verkerke, H., & Stowell, S. R. (2020) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000610 · Cited by 27
Identification of oxidative modifications of hemopexin and their predicted physiological relevance
Hahl, P., Hunt, R., Bjes, E. S., Skaff, D. A., Keightley, A., & Smith, A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.783951 · Cited by 26
Louie, J. E., Anderson, C., Fomani, K., Henry, A., Killeen, T. F., Mohandas, N., Yazdanbakhsh, K., Belcher, J. D., Vercellotti, G. M., & Shi, P. A. (2017) · Transfusion · doi:10.1111/trf.14407 · Cited by 26
Vasculopathy in Sickle Cell Disease: From Red Blood Cell Sickling to Vascular Dysfunction
Nader, É., Conran, N., Romana, M., & Connes, P. (2021) · Comprehensive physiology · doi:10.1002/cphy.c200024 · Cited by 35
The NLRP3 inflammasome fires up heme-induced inflammation in hemolytic conditions
Salgar, S., Bolívar, B. E., Flanagan, J. M., Anum, S. J., & Bouchier‐Hayes, L. (2022) · Translational research · doi:10.1016/j.trsl.2022.08.011 · Cited by 28
P‐selectin plays a role in haem‐induced acute lung injury in sickle mice
Ghosh, S., Flage, B., Weidert, F. L., & Ofori-Acquah, S. F. (2019) · British Journal of Haematology · doi:10.1111/bjh.15807 · Cited by 25
Self-citationChonat, S., Jones, J. A., Patel, S. R., Briones, W., Schoettler, M. L., Maarouf, M., Jeffers, L. A., Adisa, O. A., Tan, F., Fields, E. J., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adl4922 · Cited by 24
Self-citationRevisiting the hyperhemolysis paradigm
Gladwin, M. T. (2015) · Blood · doi:10.1182/blood-2015-06-649491 · Cited by 24
Telen, M. J. (2020) · Blood Advances · doi:10.1182/bloodadvances.2020001469 · Cited by 23
Gonzales, J., Holbert, K., Czysz, K., George, J. T., Fernandes, C., & Fraidenburg, D. R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094763 · Cited by 23
cGMP modulation therapeutics for sickle cell disease
Conran, N., & Torres, L. S. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219827276 · Cited by 23
Xi, C., Pang, J., Xue, W., Cui, Y., Jiang, N., Zhi, W., Shi, H., Horuzsko, A., Pace, B. S., & Zhu, X. (2025) · Communications Biology · doi:10.1038/s42003-024-07424-7 · Cited by 26
Advances in Sickle Cell Therapies in the Hydroxyurea Era
Field, J. J., & Nathan, D. G. (2014) · Molecular Medicine · doi:10.2119/molmed.2014.00187 · Cited by 24
Immune regulation of sickle cell alloimmunization
Yazdanbakhsh, K., Shaz, B. H., & Hillyer, C. D. (2016) · ISBT Science Series · doi:10.1111/voxs.12296 · Cited by 22
Nader, É., Garnier, Y., Connes, P., & Romana, M. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.728693 · Cited by 23
Oxidative stress in sickle cell disease; more than a DAMP squib
van Beers, E. J., & van Wijk, R. (2018) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-189010 · Cited by 23
Sickle cell nephropathy: insights into the pediatric population
Adebayo, O. C., van den Heuvel, L. P., Olowu, W. A., Levtchenko, E. N., & Labarque, V. (2021) · Pediatric Nephrology · doi:10.1007/s00467-021-05126-4 · Cited by 21
Multiple inducers of endothelial NOS ( eNOS ) dysfunction in sickle cell disease
Hebbel, R. P., & Vercellotti, G. M. (2021) · American Journal of Hematology · doi:10.1002/ajh.26308 · Cited by 22
Allali, S., de Montalembert, M., Rignault‐Bricard, R., Taylor, M., Brice, J., Brousse, V. A. M., Talbot, J.-M., Moulin, F., Heilbronner, C., Hermine, O., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2020003519 · Cited by 21
Zhang, P., Nguyen, J., Abdulla, F. A., Nelson, A. T., Beckman, J. D., Vercellotti, G. M., & Belcher, J. D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.632709 · Cited by 20
The heart in sickle cell disease, a model for heart failure with preserved ejection fraction
Wood, J. C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611899113 · Cited by 20
Epidemiology, Pathogenesis, and Clinical Approach in Group 5 Pulmonary Hypertension
Al‐Qadi, M. O., LeVarge, B. L., & Ford, H. J. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2020.616720 · Cited by 21
Augmented NRF 2 activation protects adult sickle mice from lethal acute chest syndrome
Ghosh, S., Hazra, R., Ihunnah, C. A., Weidert, F. L., Flage, B., & Ofori-Acquah, S. F. (2018) · British Journal of Haematology · doi:10.1111/bjh.15401 · Cited by 19
Self-citationHopp, M.-T., Holze, J., Lauber, F., Holtkamp, L., Rathod, D., Miteva, M. A., Prestes, E. B., Geyer, M., Manoury, B., Merle, N. S., et al. (2023) · Immunology · doi:10.1111/imm.13708 · Cited by 18
Complement in Sickle Cell Disease: Are We Ready for Prime Time?
Varelas, C., Tampaki, A., Sakellari, I., Anagnostopoulos, Α., Gavriilaki, E., & Vlachaki, E. (2021) · Journal of Blood Medicine · doi:10.2147/jbm.s287301 · Cited by 20
SARS-CoV-2, hemoglobin and protoporphyrin IX: Interactions and perspectives
Courrol, L. C., Silva, F. R. D. O., & Masilamani, V. (2021) · Photodiagnosis and Photodynamic Therapy · doi:10.1016/j.pdpdt.2021.102324 · Cited by 18
Haptoglobin gene polymorphisms and interleukin-6 and -8 levels in patients with sickle cell anemia
Pierrot-Gallo, B. S., Vicari, P., Matsuda, S. S., Adegoke, S. A., Mecabô, G., & Figueiredo, M. S. (2015) · Revista Brasileira de Hematologia e Hemoterapia · doi:10.1016/j.bjhh.2015.07.006 · Cited by 18
Bilan, V. P., Schneider, F., Novelli, E. M., Kelley, E. E., Shiva, S., Gladwin, M. T., Jackson, E. K., & Tofovic, S. P. (2018) · Pulmonary Circulation · doi:10.1177/2045894018791557 · Cited by 17
The cause and pathogenesis of hemolytic transfusion reactions in sickle-cell disease
Pirenne, F. (2019) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000546 · Cited by 17
The role of redox-dependent mechanisms in heme release from hemoglobin and erythrocyte hemolysates
Oh, J., Williams, A., & Patel, R. P. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.12.005 · Cited by 16
Sickle Cell Disease and Acute Chest Syndrome: Epidemiology, Diagnosis, Management, Outcomes
Sysol, J. R., & Machado, R. F. (2016) · Respiratory medicine · doi:10.1007/978-3-319-41912-1_4 · Cited by 19
Schmidt, H. M., DeVallance, E., Lewis, S. E., Wood, K. C., Annarapu, G. K., Carreño, M., Hahn, S. A., Seman, M., Maxwell, B. A., Hileman, E. A., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102636 · Cited by 18
Cell-free hemoglobin triggers macrophage cytokine production via TLR4 and MyD88
Schaaf, K., Landstreet, S. R., Pugazenthi, S., Qian, E. Y., Putz, N. D., Siderova, T., Owen, A. M., Bohannon, J. K., Ware, L. B., Bastarache, J. A., et al. (2023) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00123.2023 · Cited by 16
Kang, B., Park, K., Kleinhenz, J., Murphy, T. C., Sutliff, R. L., Archer, D. R., & Hart, C. M. (2016) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2016-0166oc · Cited by 16
Self-citationSantaterra, V. A. G., Fiusa, M. M. L., Hounkpe, B. W., Chénou, F., Tonassé, W. V., da Costa, L. N. G., Garcia-Weber, D., Domingos, I. F., de Lima, F., Borba-Junior, I. T., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.535147 · Cited by 16
Assessment of total and unbound cell-free heme in plasma of patients with sickle cell disease
Vissa, M., Larkin, S. K., Vichinsky, E. P., Kuypers, F. A., & Soupène, E. (2023) · Experimental Biology and Medicine · doi:10.1177/15353702231157920 · Cited by 15
Chloroquine inhibits pro-inflammatory effects of heme on macrophages and in vivo
Silva, R. C. M. C., Tan, L. B., Rodrigues, D. A., Prestes, E. B., Gomes, C. P., Gama, A. M. D. S., de Oliveira, P. L., Paiva, C., Manoury, B., & Bozza, M. T. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.028 · Cited by 16
Avondt, K. V., Schimmel, M., Bulder, I., van Mierlo, G. J., Nur, E., van Bruggen, R., Biemond, B. J., Luken, B. M., & Zeerleder, S. S. (2023) · Transfusion Medicine and Hemotherapy · doi:10.1159/000526760 · Cited by 15
Day, M. E., Rodeghier, M., & DeBaun, M. R. (2018) · Pediatric Blood & Cancer · doi:10.1002/pbc.27352 · Cited by 16
Free heme regulates placenta growth factor through NRF2-antioxidant response signaling
Kapetanaki, M. G., Gbotosho, O. T., Sharma, D., Weidert, F. L., Ofori-Acquah, S. F., & Kato, G. J. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.08.009 · Cited by 15
Self-citationInterleukin-1 receptor inhibition reduces stroke size in a murine model of sickle cell disease
Venugopal, J., Wang, J., Mawri, J., Guo, C., & Eitzman, D. T. (2020) · Haematologica · doi:10.3324/haematol.2020.252395 · Cited by 15
Acute Hemolysis and Heme Suppress Anti-CD40 Antibody-Induced Necro-Inflammatory Liver Disease
Pfefferlé, M., Ingoglia, G., Schaer, C. A., Hansen, K., Schulthess, N., Humar, R., Schaer, D. J., & Vallelian, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.680855 · Cited by 16
Prospects for early investigational therapies for sickle cell disease
Conran, N. (2015) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2015.1012292 · Cited by 15
Gbotosho, O. T., Gollamudi, J., & Hyacinth, H. I. (2023) · Biomolecules · doi:10.3390/biom13020381 · Cited by 15
Kaminski, T. W., Brzóska, T., Li, X., Vats, R., Katoch, O., Dubey, R. K., Bagale, K., Watkins, S. C., McVerry, B. J., Pradhan‐Sundd, T., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.167299 · Cited by 14
Dagur, P. K., McCoy, J. P., Nichols, J., Mendelsohn, L., Seamon, C. A., Kato, G. J., & van Beers, E. J. (2017) · British Journal of Haematology · doi:10.1111/bjh.14663 · Cited by 14
Zaidi, G. Z., Rosentsveyg, J., Fomani, K., Louie, J. E., & Koenig, S. J. (2019) · Journal of Intensive Care Medicine · doi:10.1177/0885066619874041 · Cited by 14
Emokpae, M. A., Fatimehin, E. B., & Obazelu, P. A. (2019) · African Health Sciences · doi:10.4314/ahs.v19i3.56 · Cited by 14
Nguyen, K., Mattè, A., Foresti, R., Federti, E., Kiger, L., Lefebvre, C., Hocini, H., Pelinski, Y., Kitagishi, H., Bencheikh, L., et al. (2024) · Blood · doi:10.1182/blood.2023023165 · Cited by 13
Differential role of adenosine signaling cascade in acute and chronic pain
Adebiyi, M. G., Manalo, J. M., Kellems, R. E., & Xia, Y. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.134483 · Cited by 15
Nyakundi, B. B., Erdei, J., Tóth, A., Balogh, E., Nagy, A., Nagy, B., Novák, L., Bognár, L., Paragh, G., Kappelmayer, J., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8929020 · Cited by 14
Mishra, S., Sonter, S., Dwivedi, M. K., & Singh, P. K. (2021) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2021.103539 · Cited by 13
Atteintes pulmonaires au cours de la drépanocytose chez l’enfant
Pincez, T., Calamy, L., Germont, Z., Lemoine, A., Lopes, A., Massiot, A., Tencer, J., Thivent, C., & Hadchouel, A. (2016) · Archives de Pédiatrie · doi:10.1016/j.arcped.2016.06.014 · Cited by 13
Silva, M., & Faustino, P. (2023) · Antioxidants · doi:10.3390/antiox12111977 · Cited by 17
Chen, Q., Hazra, R., Crosby, D. E., Lenhart, D., Lenhart, S. C., Mondal, P., Zhang, Y., Nouraie, M. S., Tan, R. J., Esmon, C. T., et al. (2024) · Blood · doi:10.1182/blood.2023023528 · Cited by 12
Self-citationAggarwal, S., DeBerry, J. J., Ahmad, I., Lynn, P., DeWitte, C., Malik, S., Merlin, J. S., Goodin, B. R., Heath, S. L., & Matalon, S. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101684 · Cited by 12
Heme Burden and Ensuing Mechanisms That Protect the Kidney: Insights from Bench and Bedside
Balla, J., & Zarjou, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158174 · Cited by 12
The invisible string of coagulation, complement, iron, and inflammation in sickle cell disease
Beckman, J. D., & Sparkenbaugh, E. (2023) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000773 · Cited by 12
Mechanisms of Pain in Sickle Cell Disease
Aich, A., Beitz, A. J., & Gupta, K. (2016) · InTech eBooks · doi:10.5772/64647 · Cited by 11
Adebiyi, M. G., Zhao, Z., Ye, Y., Manalo, J. M., Hong, Y., Lee, C. C., Xian, W., McKeon, F., Culp‐Hill, R., D’Alessandro, A., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900246rr · Cited by 11
Gotardo, É. M. F., Brito, P. L., Gushiken, L. F. S., Chweih, H., Leonardo, F. C., Costa, F. F., & Conran, N. (2023) · Vascular Pharmacology · doi:10.1016/j.vph.2023.107176 · Cited by 10
The ongoing challenge of RBC alloimmunization in the management of patients with sickle cell disease
Chang, D. Y., Wankier, Z., Arthur, C. M., & Stowell, S. R. (2023) · La Presse Médicale · doi:10.1016/j.lpm.2023.104211 · Cited by 10
Inflammatory pathways and anti‐inflammatory therapies in sickle cell disease
Tozatto‐Maio, K., Rós, F. A., Weinlich, R., & Rocha, V. (2024) · HemaSphere · doi:10.1002/hem3.70032 · Cited by 10
Sickle cell disease mice have cerebral oxidative stress and vascular and white matter abnormalities
Khaibullina, A., Almeida, L. E. F., Kamimura, S., Zerfas, P. M., Smith, M. L., Vogel, S., Wakim, P., Vasconcelos, O. M., Quezado, M., Horkayne‐Szakaly, I., et al. (2020) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2020.102493 · Cited by 11
Oxidized hemoglobin triggers polyreactivity and autoreactivity of human IgG via transfer of heme
Planchais, C., Noé, R., Gilbert, M., Lecerf, M., Kaveri, S. V., Lacroix‐Desmazes, S., Roumenina, L. T., & Dimitrov, J. D. (2023) · Communications Biology · doi:10.1038/s42003-023-04535-5 · Cited by 13
Tan, F., Ghosh, S., Mosunjac, M. I., Manci, E. A., & Ofori-Acquah, S. F. (2016) · Experimental Biology and Medicine · doi:10.1177/1535370216642046 · Cited by 10
Self-citationPecker, L. H., & Ackerman, H. C. (2016) · Springer eBooks · doi:10.1007/978-3-319-06713-1_7 · Cited by 10
Mechanisms of haem toxicity in haemolysis and protection by the haem‐binding protein, haemopexin
Smith, A. L., & McCulloh, R. J. (2017) · ISBT Science Series · doi:10.1111/voxs.12340 · Cited by 9
Alishlash, A. S., Sapkota, M., Ahmad, I., Maclin, K. M., Ahmed, N. A., Molyvdas, A., Doran, S. F., Albert, C. J., Aggarwal, S., Ford, D. A., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102009 · Cited by 8
Inflammation and Sickle Cell Anemia
Almeida, C. B., Kato, G. J., & Conran, N. (2016) · Springer eBooks · doi:10.1007/978-3-319-06713-1_8 · Cited by 9
Chatterjee, T., Arora, I., Underwood, L., Lewis, T. L., Juncos, J. X. M., Heath, S. L., Goodin, B. R., & Aggarwal, S. (2023) · Cells · doi:10.3390/cells12121565 · Cited by 8
Bourne, J. H., Perrella, G., El-Awaisi, J., Terry, L. V., Tinkova, V. V., Hogg, R. L., Gant, P., Grygielska, B., Kalia, N., Kavanagh, D. P. J., et al. (2024) · Journal of Thrombosis and Haemostasis · doi:10.1016/j.jtha.2024.04.008 · Cited by 10
Kaminski, T. W., Katoch, O., Li, Z., Hanway, C. B., Dubey, R. K., Alagbe, A. E., Brzóska, T., Zhang, H., Sundd, P., Kato, G. J., et al. (2023) · Haematologica · doi:10.3324/haematol.2023.283792 · Cited by 8
Vasculopathy in Sickle Cell Disease: From Red Blood Cell Sickling to Vascular Dysfunction
Nader, É., Conran, N., Romana, M., & Connes, P. (2021) · Comprehensive physiology · doi:10.1002/j.2040-4603.2021.tb00164.x · Cited by 8
van Vuren, A. J., van Straaten, S., Mokrý, M., van Wijk, R., & van Beers, E. J. (2021) · HemaSphere · doi:10.1097/hs9.0000000000000531 · Cited by 8
Changes in Heme Levels During Acute Vaso-occlusive Crisis in Sickle Cell Anemia
Cardoso, E. C., Silva-Neto, P. V. D., Hounkpe, B. W., Chénou, F., Albuquerque, C. C. M. X., Garcia, N. P., Silva-Junior, A. L., Malheiro, A., Cesar, P., de Lima, F., et al. (2021) · Hematology/Oncology and Stem Cell Therapy · doi:10.1016/j.hemonc.2021.08.002 · Cited by 10
Transfusion‐transmitted malaria masquerading as sickle cell crisis with multisystem organ failure
Maier, C. L., Gross, P. J., Dean, C. L., Chonat, S., Ip, A., McLemore, M. L., Rassi, F. A. E., Stowell, S. R., Josephson, C. D., & Fasano, R. M. (2018) · Transfusion · doi:10.1111/trf.14566 · Cited by 8
Ademolue, T. W., Amodu, O. K., & Awandare, G. A. (2017) · Clinical & Experimental Immunology · doi:10.1111/cei.12936 · Cited by 11
HMGB1 takes a “Toll” in sickle cell disease
Gupta, K. (2014) · Blood · doi:10.1182/blood-2014-11-608984 · Cited by 7
Karlsson, E. A., Oguin, T. H., Meliopoulos, V., Iverson, A., Broadnax, A., Yoon, S., Pestina, T. I., Thomas, P. G., Webby, R. J., Schultz‐Cherry, S., et al. (2017) · Scientific Reports · doi:10.1038/srep43308 · Cited by 6
de Azevedo, J. T. C., Costa, T. C. D. M., Lima, K. C., Maciel, T. T., Palma, P. V. B., Darrigo, L. G., Grecco, C. E. S., Stracieri, A. B. P. L., Elias, J., Pieroni, F., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.774442 · Cited by 8
Dosunmu-Ogunbi, A. M., Yuan, S. S., Shiwarski, D. J., Tashman, J. W., Reynolds, M. J., Feinberg, A. W., Novelli, E. M., Shiva, S., & Straub, A. C. (2022) · Function · doi:10.1093/function/zqac005 · Cited by 9
Metadata
- Authors
- Ghosh, S., Adisa, O. A., Chappa, P., Tan, F., Jackson, K. A., Archer, D. R., & Ofori-Acquah, S. F.
- Affiliations
- Emory University (US)
- Venue
- Journal of Clinical Investigation
- Published
- 2013-10-01
- Volume
- 123
- Issue
- 11
- Pages
- 4809-4820
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC3809772
- OpenAlex
- W2100360129
- Cited by
- 282
- References
- 72
- Citations by year
- 2026: 18 · 2025: 14 · 2024: 14 · 2023: 23 · 2022: 17 · 2021: 29 · 2020: 24 · 2019: 19 · 2018: 25 · 2017: 19 · 2016: 37 · 2015: 23 · 2014: 18 · 2013: 2
- FWCI
- 13.13
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- Emory University
- National Heart, Lung, and Blood Institute (R01HL106192, K02HL088026, U01HL117721)
- Topics
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Health Sciences › Medicine › Hematology › Blood groups and transfusion
- Keywords
- acute chest syndrome, sickle cell disease, hemolysis, TLR4, hemopexin, acute lung injury, respiratory failure, TLR4 inhibition, lung injury pathogenesis, bone marrow chimeras
- MeSH terms
- Anemia, Sickle Cell, Animals, Disease Models, Animal, Extracellular Space, Hemin, Hemoglobin, Sickle, Hemolysis, Hemopexin, Humans, Mice, Inbred C3H, Mice, Inbred C57BL, Mice, Mutant Strains, Mice, Transgenic, Recombinant Proteins, Sickle Cell Trait, Sulfonamides, Mice, Knockout, Toll-Like Receptor 4, Mice, Acute Chest Syndrome
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