Hemoglobin S gelation and sickle cell disease

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

Monod, J., Wyman, J., & Changeux, J. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 7,681

The number and distribution of capillaries in muscles with calculations of the oxygen pressure head necessary for supplying the tissue

Krogh, A. (1919) · The Journal of Physiology · doi:10.1113/jphysiol.1919.sp001839 · Cited by 1,433

Hydroxyurea enhances fetal hemoglobin production in sickle cell anemia.

Platt, O., Orkin, S. H., Dover, G., Beardsley, G. P., Miller, B. A., & Nathan, D. G. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111464 · Cited by 532

Kinetics and Mechanism of Deoxyhemoglobin S Gelation: A New Approach to Understanding Sickle Cell Disease

Hofrichter, J., Ross, P. D., & Eaton, W. A. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.12.4864 · Cited by 520

Erythrocyte Adherence to Endothelium in Sickle-Cell Anemia

Hebbel, R. P., Boogaerts, M., Eaton, J. W., & Steinberg, M. H. (1980) · New England Journal of Medicine · doi:10.1056/nejm198005013021803 · Cited by 518

Kinetics of sickle hemoglobin polymerization

Ferrone, F. A., Hofrichter, J., & Eaton, W. A. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90175-5 · Cited by 505

Abnormal Adherence of Sickle Erythrocytes to Cultured Vascular Endothelium

Hebbel, R. P., Yamada, O., Moldow, C. F., Jacob, H. S., White, J. G., & Eaton, J. W. (1980) · Journal of Clinical Investigation · doi:10.1172/jci109646 · Cited by 421

Abnormal rheology of oxygenated blood in sickle cell anemia

Chien, S., Usami, S., & Bertles, J. F. (1970) · Journal of Clinical Investigation · doi:10.1172/jci106273 · Cited by 358

Is there a threshold level of fetal hemoglobin that ameliorates morbidity in sickle cell anemia?

Powars, D., Weiss, J., Chan, L., & Schroeder, W. (1984) · Blood · doi:10.1182/blood.v63.4.921.921 · Cited by 314

Hemoglobin as a receptor of drugs and peptides: x-ray studies of the stereochemistry of binding

Perutz, M. F., Fermi, G., Abraham, D. J., Poyart, C., & Bursaux, E. (1986) · Journal of the American Chemical Society · doi:10.1021/ja00265a036 · Cited by 299

Association of plasma homocysteine level with vaso-occlusive crisis in sickle cell anemia patients of Odisha, India

Meher, S., Patel, S., Das, K., Dehury, S., Jit, B. P., Maske, M. M., Das, P., Dash, B. P., & Mohanty, P. K. (2019) · Annals of Hematology · doi:10.1007/s00277-019-03776-x · Cited by 22

Impact of hemoglobin biophysical studies on molecular pathogenesis and drug therapy for sickle cell disease

Eaton, W. A. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.100971 · Cited by 22

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

Mesoscopic Adaptive Resolution Scheme toward Understanding of Interactions between Sickle Cell Fibers

Lu, L., Li, H., Bian, X., Li, X., & Karniadakis, G. E. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.05.050 · Cited by 19

Targeting βCys93 in hemoglobin S with an antisickling agent possessing dual allosteric and antioxidant effects

Kassa, T., Strader, M. B., Nakagawa, A., Zapol, W. M., & Alayash, A. I. (2017) · Metallomics · doi:10.1039/c7mt00104e · Cited by 20

Sickling of Anoxic Red Blood Cells in Fish

Hárosi, F. I., von Herbing, I. H., & van Keuren, J. R. (1998) · Biological Bulletin · doi:10.2307/1542769 · Cited by 20

Perfluorocarbon emulsion improves oxygen transport of normal and sickle cell human blood in vitro

Filho, I. P. T., Pedro, J. R. P., Narayanan, S., Nguyen, N. M., Roseff, S. D., & Spiess, B. D. (2013) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.34885 · Cited by 20

Hemoglobin polymerization in sickle cells studied by circular polarized light scattering

Gross, C. T., Salamon, H., Hunt, A. J., Macey, R. I., Orme, F. W., & Quintanilha, A. T. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90120-o · Cited by 20

Kinetics of domain formation by sickle hemoglobin polymers

Basak, S., Ferrone, F. A., & Wang, J. T. (1988) · Biophysical Journal · doi:10.1016/s0006-3495(88)83020-0 · Cited by 20

GBT440 Inhibits Sickling of Sickle Cell Trait Blood under In Vitro Conditions Mimicking Strenuous Exercise

Dufu, K., Lehrer‐Graiwer, J., Ramos, E. L., & Oksenberg, D. (2016) · Hematology Reports · doi:10.4081/hr.2016.6637 · Cited by 19

A non‐electrolyte haemolysis assay for diagnosis and prognosis of sickle cell disease

Milligan, C., Rees, D. C., Ellory, J. C., Osei, A., Browning, J., Hannemann, A., & Gibson, J. S. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2012.246579 · Cited by 19

Pathophysiology of Red Cell Volume

Browning, J., Ellory, J. C., & Gibson, J. S. (2006) · KARGER eBooks · doi:10.1159/000096327 · Cited by 19

Nonblack Patients With Sickle Cell Disease Have African βs Gene Cluster Haplotypes

Rogers, Z. R. (1989) · JAMA · doi:10.1001/jama.1989.03420200081042 · Cited by 19

Image analysis studies of the degree of irreversible deformation of sickle cells in relation to cell density and Hb F level

Horiuchi, K., Stephens, M. J., Adachi, K., Asakura, T., Schwartz, E., & Ohene‐Frempong, K. (1993) · British Journal of Haematology · doi:10.1111/j.1365-2141.1993.tb03179.x · Cited by 19

Supersaturation-Dependent Formation of Amyloid Fibrils

Goto, Y., Noji, M., Nakajima, K., & Yamaguchi, K. (2022) · Molecules · doi:10.3390/molecules27144588 · Cited by 18

Metastable Polymerization of Sickle Hemoglobin in Droplets

Aprelev, A. M., Weng, W., Zakharov, M. N., Rotter, M. A., Yosmanovich, D. A., Kwong, S., Briehl, R. W., & Ferrone, F. A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.030 · Cited by 18

Nucleation of Sickle Hemoglobin Mixed with Hemoglobin A: Experimental and Theoretical Studies of Hybrid-Forming Mixtures

Rotter, M. A., Yosmanovich, D. A., Briehl, R. W., Kwong, S., & Ferrone, F. A. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.10.027 · Cited by 18

The Physical Foundation of Vasoocclusion in Sickle Cell Disease

Aprelev, A. M., Stephenson, W., Noh, H. “., Meier, M., & Ferrone, F. A. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.09.003 · Cited by 18

Effect of Intracellular Magnesium and Oxygen Tension on K+-Cl- Cotransport in Normal and Sickle Human Red Cells

Muzyamba, M. C., Campbell, E., & Gibson, J. S. (2006) · Cellular Physiology and Biochemistry · doi:10.1159/000092073 · Cited by 18

Ion Content and Transport and the Regulation of Volume in Sickle Cellsa

Brugnara, C., Bunn, H. F., & Tosteson, D. C. (1989) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1989.tb24155.x · Cited by 18

Evaluation of 24-Second Cyanide-Containing and Cyanide-Free Methods for Whole Blood Hemoglobin on the Technicon H*1™ Analyzer with Normal and Abnormal Blood Samples

Malin, M. J., Sclafani, L., & Wyatt, J. L. (1989) · American Journal of Clinical Pathology · doi:10.1093/ajcp/92.3.286 · Cited by 18

Spectral domain optical coherence tomography findings in Turkish sickle-cell disease and beta thalassemia major patients

Ulusoy, M. O., Türk, H., & Kıvanç, S. A. (2019) · Journal of Current Ophthalmology · doi:10.1016/j.joco.2019.01.012 · Cited by 17

Management of the oral and maxillofacial surgery patient with sickle cell disease and related hemoglobinopathies

Sansevere, J. J., & Milles, M. (1993) · Journal of Oral and Maxillofacial Surgery · doi:10.1016/s0278-2391(10)80114-4 · Cited by 17

The polymerization of sickle hemoglobin in solutions and cells

Ferrone, F. A. (1993) · Cellular and Molecular Life Sciences · doi:10.1007/bf01989414 · Cited by 16

Beneficial Effects of Soluble Guanylyl Cyclase Stimulation and Activation in Sickle Cell Disease Are Amplified by Hydroxyurea: In Vitro and In Vivo Studies

Ferreira, W. A., Chweih, H., Lanaro, C., Almeida, C. B., Brito, P. L., Gotardo, É. M. F., Torres, L. S., Miguel, L. I., Franco‐Penteado, C. F., Leonardo, F. C., et al. (2020) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.119.264606 · Cited by 15

Hydrodynamics of Hemostasis in Sickle-Cell Disease

Cohen, S. I. A., & Mahadevan, L. (2013) · Physical Review Letters · doi:10.1103/physrevlett.110.138104 · Cited by 16

In vivored blood cell sickling and mechanism of recovery in whiting,Merlangius merlangus

Koldkjær, P., & Berenbrink, M. (2007) · Journal of Experimental Biology · doi:10.1242/jeb.008524 · Cited by 16

Red Blood Cells of a Transgenic Mouse Expressing High Levels of Human Hemoglobin S Exhibit Deoxy-stimulated Cation Flux

Romero, J. R., Fabry, M. E., Suzuka, S. M., Nagel, R. L., & CANESSA, M. L. (1997) · The Journal of Membrane Biology · doi:10.1007/s002329900282 · Cited by 16

Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease

Bonaventura, C., Godette, G., Ferruzzi, G., Tesh, S., Stevens, R. D., & Henkens, R. W. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00092-3 · Cited by 15

Sudden death in sickle trait

Charache, S. (1988) · The American Journal of Medicine · doi:10.1016/0002-9343(88)90266-5 · Cited by 15

Alpha Thalassemiaa

Embury, S. H. (1989) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1989.tb24169.x · Cited by 15

Association of fetal hemoglobin level with frequency of acute pain episodes in sickle cell disease (HbS-only phenotype) patients

Jit, B. P., Mohanty, P. K., Purohit, P., Das, K., Patel, S., Meher, S., Mohanty, J. R., Sinha, S., Behera, R. K., & Das, P. (2018) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2018.12.003 · Cited by 15

Differential sensitivity to hypoxia enables shape‐based classification of sickle cell disease and trait blood samples at point of care

D’Costa, C., Sharma, O., Manna, R., Singh, M., Singh, S., Singh, S., Mahto, A., Govil, P., Satti, S., Mehendale, N. D., et al. (2023) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10643 · Cited by 14

Rate of deoxygenation modulates rheologic behavior of sickle red blood cells at a given mean corpuscular hemoglobin concentration.

Kaul, D. K., & Liu, X. D. (1999) · PubMed · Cited by 14

The role of β93 Cys in the inhibition of Hb S fiber formation

Knee, K. M., Roden, C. K., Flory, M. R., & Mukerji, I. (2007) · Biophysical Chemistry · doi:10.1016/j.bpc.2007.02.002 · Cited by 14

Molecular dynamics of sickle and normal hemoglobins

Prabhakaran, M., & Johnson, M. E. (1993) · Biopolymers · doi:10.1002/bip.360330503 · Cited by 14

Alterações hemostáticas em pacientes com doença falciforme

Stypulkowski, J. B., & Manfredini, V. (2010) · Revista Brasileira de Hematologia e Hemoterapia · doi:10.1590/s1516-84842010005000001 · Cited by 14

Mass Spectral Analysis of Asymmetric Hemoglobin Hybrids: Demonstration of Hb FS (α2γβS) in Sickle Cell Disease

Ofori-Acquah, S. F., Green, B. N., Davies, S. C., Nicolaides, K. H., Serjeant, G. R., & Layton, D. M. (2001) · Analytical Biochemistry · doi:10.1006/abio.2001.5358 · Cited by 14

Monomer diffusion into polymer domains in sickle hemoglobin

Cho, M., & Ferrone, F. A. (1990) · Biophysical Journal · doi:10.1016/s0006-3495(90)82449-8 · Cited by 14

Effect of dimethyl adipimidate on K+ transport and shape change in red blood cells from sickle cell patients

Gibson, J. S., Stewart, G. W., & Ellory, J. C. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01930-x · Cited by 14

The management of two pediatric patients with sickle cell trait and sickle cell disease during cardiopulmonary bypass

Baxter, M. R. N., Bevan, J. C., Esseltine, D. W., & Bernstein, M. (1989) · Journal of Cardiothoracic Anesthesia · doi:10.1016/s0888-6296(89)97891-5 · Cited by 14

Kinetic Models and the Pathophysiology of Sickle Cell Diseasea

Ferrone, F. A. (1989) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1989.tb24151.x · Cited by 14

An integrated therapeutic approach to sickle cell disease management beyond infancy

Ribeil, J., Pollock, G., Frangoul, H., & Steinberg, M. H. (2023) · American Journal of Hematology · doi:10.1002/ajh.26956 · Cited by 13

The Relationship of Oxygen Transport and Cardiac Index for the Prevention of Sickle Cell Crises

Farrell, K., Dent, L., Nguyen, M. L., Buchowski, M. S., Bhatt, A., & Aguinaga, M. D. P. (2010) · Journal of the National Medical Association · doi:10.1016/s0027-9684(15)30726-4 · Cited by 13

Bepridil protects sickle cells against the adverse rheological effects of cyclical deoxygenation

Johnston, M. N., Ellory, J. C., & Stuart, J. (1989) · British Journal of Haematology · doi:10.1111/j.1365-2141.1989.tb00291.x · Cited by 13

Pluripotent Stem Cells in Research and Treatment of HemoglobinopathiesPreprint

Arora, N., & Daley, G. Q. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011841 · Cited by 14

Gene therapy and gene editing strategies in inherited blood disorders

Song, X., Liu, J., Chen, T., Zheng, T., Wang, X., & Guo, X. (2024) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2024.07.004 · Cited by 13

Heterogeneity of fetal hemoglobin production in adult red blood cells

Khandros, E., & Blobel, G. A. (2021) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000640 · Cited by 12

Hydroxyurea and fetal hemoglobin effect on leg ulcers in patients with sickle cell disease

Tolu, S. S., Crouch, A. S., Choi, J., Gao, Q., Reyes-Gil, M., Ogu, U. O., Vinces, G., & Minniti, C. P. (2022) · Annals of Hematology · doi:10.1007/s00277-021-04635-4 · Cited by 12

Combinatorial targeting of epigenome-modifying enzymes with decitabine and RN-1 synergistically increases HbF

Ibañez, V., Vaitkus, K., Zhang, X., Jagadeeswaran, R., Rivers, A. E., Saunthararajah, Y., Molokie, R. E., & Lavelle, D. (2023) · Blood Advances · doi:10.1182/bloodadvances.2022009558 · Cited by 12

Effect of inositol hexaphosphate–loaded red blood cells (RBCs) on the rheology of sickle RBCs

Lamarre, Y., Bourgeaux, V., Pichon, A., Hardeman, M. R., Campion, Y., Hardeman‐Zijp, M., Martin, C., Richalet, J., Bernaudin, F., Driss, F., et al. (2012) · Transfusion · doi:10.1111/j.1537-2995.2012.03779.x · Cited by 12

Substitutions in the β subunits of sickle-cell hemoglobin improve oxidative stability and increase the delay time of sickle-cell fiber formation

Meng, F., Kassa, T., Strader, M. B., Soman, J., Olson, J. S., & Alayash, A. I. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006452 · Cited by 12

Hb S-São Paulo: A new sickling hemoglobin with stable polymers and decreased oxygen affinity

Jorge, S. E., Petruk, A. A., Kimura, E. M., de Oliveira, D. M., da Silva, L. C., Suemasu, C. N., Silveira, P. A. A., de Albuquerque, D. M., Costa, F. F., Skaf, M. S., et al. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.01.001 · Cited by 12

The effect of the antisickling compound GBT 1118 on the permeability of red blood cells from patients with sickle cell anemia

Balushi, H. W. M. A., Dufu, K., Rees, D. C., Brewin, J. N., Hannemann, A., Oksenberg, D., Lu, D. C. ‐., & Gibson, J. S. (2019) · Physiological Reports · doi:10.14814/phy2.14027 · Cited by 12

A recombinant bisphosphoglycerate mutase variant with acid phosphatase homology degrades 2,3-diphosphoglycerate.

Garel, M. C., Arous, N., Calvin, M., Craescu, C. T., Rosa, J., & Rosa, R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.9.3593 · Cited by 12

K+ efflux in deoxygenated sickle cells in the presence or absence of DIOA, a specific inhibitor of the [K+, Cl‐] cotransport system

Olivieri, O., Vitoux, D., Bachir, D., & Beuzard, Y. (1991) · British Journal of Haematology · doi:10.1111/j.1365-2141.1991.tb07957.x · Cited by 12

HB Shelby [β131(H9)GLN→LYS] in Association with HB S [β6(A3)GLU→VAL]: Characterization, Stability, and Effects on HB S Polymerization

Adachi, K., Surrey, S., Tamary, H., Kim, J., Eck, H. S., Rappaport, E. F., & Ohene‐Frempong, K. (1993) · Hemoglobin · doi:10.3109/03630269308997486 · Cited by 12

New Insights Into Hemolytic Anemias: Ultrastructural and Nanomechanical Investigation of Red Blood Cells Showed Early Morphological Changes

Amorim, M. D. S. D. N., Batista, J. A., Maia, F. E. N., Fontes, A., Santos‐Oliveira, R., & Alencar, L. M. R. (2021) · Journal of Biomedical Nanotechnology · doi:10.1166/jbn.2022.3267 · Cited by 11

TNFSF/TNFRSF cytokine gene expression in sickle cell anemia: Up-regulated TNF-like cytokine 1A (TL1A) and its decoy receptor (DcR3) in peripheral blood mononuclear cells and plasma

Safaya, S., Alfarhan, M. F. A., Sulaiman, A., Alsulaiman, A. A., & Al‐Ali, A. K. (2019) · Cytokine · doi:10.1016/j.cyto.2019.154744 · Cited by 11

Dynamics of oxygen unloading from sickle erythrocytes

Makhijani, V. B., Cokelet, G. R., & Clark, A. (1990) · Biophysical Journal · doi:10.1016/s0006-3495(90)82446-2 · Cited by 11

Vainillina: agente inhibidor de la polimerización de la hemoglobina S

García, G. D. T., Dieguez, J. E. F., Geli, Y. A., Rodríguez, Y. C. V., & Mirabal, C. A. C. (2003) · Bioquimia · Cited by 11

Anion Transport in Sickle Red Blood Cells

Joiner, C. H., Gunn, R. B., & Fröhlich, O. (1990) · Pediatric Research · doi:10.1203/00006450-199012000-00008 · Cited by 11

Resolving the chromatin impact of mosaic variants with targeted Fiber-seqPreprint

Bohaczuk, S. C., Amador, Z. J., Li, C. L., Mallory, B. J., Swanson, E. G., Ranchalis, J., Vollger, M. R., Munson, K. M., Walsh, T., Hamm, M. O., et al. (2024) · Genome Research · doi:10.1101/gr.279747.124 · Cited by 12

In vivo measurement of RBC survival in patients with sickle cell disease before or after hematopoietic stem cell transplantation

Leonard, A. K., Furstenau, D. K., Inam, Z. S., Luckett, C., Chu, R., Demirci, S., Essawi, K., Gudmundsdottir, B., Hinds, M., DiNicola, J., et al. (2024) · Blood Advances · doi:10.1182/bloodadvances.2023011397 · Cited by 13

How does protein aggregate structure affect mechanisms of disaggregation?

Yang, Y., & Rye, H. S. (2025) · Biochemical Society Transactions · doi:10.1042/bst20253077 · Cited by 10

Faster Sickling Kinetics and Sickle Cell Shape Evolution during Repeated Deoxygenation and Oxygenation Cycles

Du, E., & Dao, M. (2018) · Experimental Mechanics · doi:10.1007/s11340-018-00444-5 · Cited by 10

On the Nonaggregation of Normal Adult Hemoglobin and the Aggregation of Sickle Cell Hemoglobin

Galamba, N. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b09727 · Cited by 10

Assessment of functional shunting in patients with sickle cell disease

Afzali‐Hashemi, L., Václavů, L., Wood, J. C., Biemond, B. J., Nederveen, A. J., Mutsaerts, H. J. M. M., & Schrantee, A. (2022) · Haematologica · doi:10.3324/haematol.2021.280183 · Cited by 10

Laboratory Methods for Diagnosis and Evaluation of Hemoglobin Disorders

Steinberg, M. H., Fabry, M. E., & Old, J. (2009) · Cambridge University Press eBooks · doi:10.1017/cbo9780511596582.038 · Cited by 10

Renal Vascular Resistance in Sickle Cell Painful Crisis

Güvenç, B., Aikimbaev, K. S., Ünsal, Ç., Akgül, E., Akgul, A. E., Binokay, F., & Beşen, A. A. (2005) · International Journal of Hematology · doi:10.1532/ijh97.e0412 · Cited by 10

Innovative Therapies for Hemoglobin Disorders

Sii-Felice, K., Nègre, O., Brendel, C., Tubsuwan, A., Morel-à-l’Huissier, E., Filardo, C., & Payen, E. (2020) · BioDrugs · doi:10.1007/s40259-020-00439-6 · Cited by 10

Emerging drug targets for sickle cell disease: shedding light on new knowledge and advances at the molecular level

Gibson, J. S., & Rees, D. C. (2023) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2023.2179484 · Cited by 12

MetAP2 inhibition modifies hemoglobin S to delay polymerization and improves blood flow in sickle cell disease

Demers, M., Sturtevant, S., Guertin, K. R., Gupta, D., Desai, K., Vieira, B. F., Li, W., Hicks, A., Ismail, A., Gonçalves, B. P., et al. (2021) · Blood Advances · doi:10.1182/bloodadvances.2020003670 · Cited by 9

Gene editing for sickle cell disease and transfusion dependent thalassemias- A cure within reach

Eckrich, M. J., & Frangoul, H. (2022) · Seminars in Hematology · doi:10.1053/j.seminhematol.2022.12.001 · Cited by 9

Review on pharmacology activities of Justicia Gendarussa Burm F.

Jain, T., Singh, M. P., Bhardwaj, H., & Gohil, K. J. (2023) · Pharmacological Research - Modern Chinese Medicine · doi:10.1016/j.prmcm.2023.100339 · Cited by 9

Can new optical techniques for in vivo imaging and flow cytometry of the microcirculation benefit sickle cell disease research?

Morgan, S. P. (2011) · Cytometry Part A · doi:10.1002/cyto.a.21101 · Cited by 9

The super sickling haemoglobin HbS‐Oman: a study of red cell sickling, K+ permeability and associations with disease severity in patients heterozygous for HbA and HbS‐Oman (HbA/S‐Oman genotype)

Balushi, H. W. M. A., Wali, Y. A. M. S., Awadi, M. A., Subhi, T. A., Rees, D. C., Brewin, J. N., Hannemann, A., & Gibson, J. S. (2017) · British Journal of Haematology · doi:10.1111/bjh.14851 · Cited by 9

Microvascular and systemic responses to novel PEGylated carboxyhaemoglobin-based oxygen carrier in a rat model of vaso-occlusive crisis

Nugent, W. H., Jubin, R., Buontempo, P. J., Kazo, F., & Song, B. K. (2019) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2018.1543197 · Cited by 9

Protein aggregation-inhibition: a therapeutic route from Parkinson’s disease to sickle cell anemia

Martins, G. F., & Galamba, N. (2023) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2023.2201406 · Cited by 9

Oxygen-Sensitive Cation Transport in Sickle Cells

Gibson, J. S. (2001) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2000.0361 · Cited by 9

Case 2—1996 Anesthetic management of a patient with hemoglobin SS disease and mitral insufficiency for mitral valve repair

Kingsley, C. P., Chronister, T., Cohen, D. J., Parrish, J. M., Drew, R., & Bongiovanni, M. B. (1996) · Journal of Cardiothoracic and Vascular Anesthesia · doi:10.1016/s1053-0770(96)80108-x · Cited by 9

Drépanocytose de l'adulte

Lionnet, F., Stankovic, K., & Girot, R. (2009) · Encyclopédie médico-chirurgicale. Hématologie · doi:10.1016/s1155-1984(09)49949-7 · Cited by 9

Calpain-1 regulates platelet function in a humanized mouse model of sickle cell disease

Nwankwo, J. O., Gremmel, T., Gerrits, A. J., Mithila, F. J., Warburton, R. R., Hill, N. S., Lu, Y., Richey, L. J., Jakubowski, J. A., Frelinger, A. L., et al. (2017) · Thrombosis Research · doi:10.1016/j.thromres.2017.10.018 · Cited by 9

Prenatal Diagnosis of Hemoglobinopathies

Fischel‐Ghodsian, N. (1990) · Clinics in Perinatology · doi:10.1016/s0095-5108(18)30547-5 · Cited by 9

Prevention of Red Cell Dehydration: A Possible New Treatment for Sickle Cell Disease

Mueller, B. U., & Brugnara, C. (2001) · Fetal and Pediatric Pathology · doi:10.1080/15513810109168815 · Cited by 9

Location of potential binding sites on deoxy hemoglobin for the design of antigelling agents

Manavalan, P., Prabhakaran, M., & Johnson, M. E. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90990-2 · Cited by 9

The Use of Radioisotopes to Characterise the Abnormal Permeability of Red Blood Cells from Sickle Cell Patients

Hannemann, A., Cytlak, U., Robert, J., Clive, J., David, C., & John, S. (2011) · InTech eBooks · doi:10.5772/24426 · Cited by 7

Hemoglobin S Polymerizationa

Briehl, R. W., & Mann, E. (1989) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1989.tb24177.x · Cited by 8

Can the surgical tourniquet be used in patients with sickle cell disease or trait? A review of the literature

Pignatti, M., Zanella, S., & Borgna‐Pignatti, C. (2016) · Expert Review of Hematology · doi:10.1080/17474086.2017.1273765 · Cited by 8

Sickle Cell Disease in the Sudan: Clinical and Biochemical Aspects

Mohamed, A. O. (1992) · Upsala Journal of Medical Sciences · doi:10.3109/03009739209179297 · Cited by 9

Ischemic Colitis Sustained by Sickle Cell Trait in Young Adult Patient

Sada, S., Benini, L., Pavan, C., Favalli, N. M., Mansueto, G., Capelli, P., Corrocher, R., & Franceschi, L. D. (2005) · The American Journal of Gastroenterology · doi:10.1111/j.1572-0241.2005.00309_7.x · Cited by 8

Current Perspectives on the Kinetics of Hemoglobin S Gelation

Biagio, P. L. S., Hofrichter, J., Mozzarelli, A., Henry, E. R., & Eaton, W. A. (1989) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1989.tb24150.x · Cited by 8

Calculations of scattered light from rigid polymers by Shifrin and Rayleigh-Debye approximations

Bishop, M. F. (1989) · Biophysical Journal · doi:10.1016/s0006-3495(89)82737-7 · Cited by 8

Relationship between the nicotinamide adenine dinucleotide redox potential and the 2,3‐diphosphoglycerate content in the erythrocyte in sickle cell disease

Lachant, N. A., Zerez, C. R., & Tanaka, K. R. (1989) · British Journal of Haematology · doi:10.1111/j.1365-2141.1989.tb07693.x · Cited by 9

Reversing Ontogeny

Bunn, H. F. (1993) · New England Journal of Medicine · doi:10.1056/nejm199301143280210 · Cited by 8

Pharmacologic Manipulation of Fetal Hemoglobin Levels in Sickle Cell Diseases and Thalassemia: Promise and Reality

Pearson, H. A. (1996) · Advances in Pediatrics · doi:10.1016/s0065-3101(24)00077-x · Cited by 7

The paradox of the serrated sickle erythrocyte: The importance of the red blood cell membrane topography

Ballas, S. K., & Connes, P. (2016) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-152014 · Cited by 7

In-vitro anti-sickling potential of baicalin and naringenin isolated from Oroxylum indicum and Citrus aurantium on human sickle red blood cells

Lone, B. A., Sharma, N., Kour, D., Bhushan, A., Rani, D., Kumar, A., Gupta, P. K., & Gupta, P. (2022) · Natural Product Research · doi:10.1080/14786419.2022.2158330 · Cited by 8

Histidine Protonation Behaviors on Structural Properties and Aggregation Properties of Aβ(1–42) Mature Fibril: Approaching by Edge Effects

Sun, Y., Shi, Y., Li, C., & Shi, H. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c02343 · Cited by 7

The role of WNK in modulation of KCl cotransport activity in red cells from normal individuals and patients with sickle cell anaemia

Lu, D. C. ‐., Hannemann, A., Wadud, R., Rees, D. C., Brewin, J. N., Low, P. S., & Gibson, J. S. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02327-7 · Cited by 7

Effect of other hemoglobins on gelation of sickle cell hemoglobin.

Sunshine, H. R. (1982) · PubMed · Cited by 3

Solidity of sickle hemoglobin gels: relevance to pathophysiology of sickling disorders

Danish, E. H., Harris, J. W., & Oh, K. (1989) · Cleveland Clinic Journal of Medicine · doi:10.3949/ccjm.56.8.793 · Cited by 1

Hemoglobin gelation.

Adachi, K., & Asakura, T. (1980) · PubMed · Cited by 1

The physical chemistry of the gelation of sickle hemoglobin.

Rw, B. (1982) · PubMed · Cited by 2

[The hemoglobins of sickle-cell blood].

Roche, J., Derrien, Y., Gallais, P., & Roques, M. (1952) · PubMed · Cited by 1