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Interference with the Host Haemostatic System by Schistosomes
Open accessAbstract
Schistosomes, parasitic flatworms that cause the tropical disease schistosomiasis, are still a threat. They are responsible for 200 million infections worldwide and an estimated 280,000 deaths annually in sub-Saharan Africa alone. The adult parasites reside as pairs in the mesenteric or perivesicular veins of their human host, where they can survive for up to 30 years. The parasite is a potential activator of blood coagulation according to Virchow's triad, because it is expected to alter blood flow and endothelial function, leading to hypercoagulability. In contrast, hepatosplenic schistosomiasis patients are in a hypocoagulable and hyperfibrinolytic state, indicating that schistosomes interfere with the haemostatic system of their host. In this review, the interactions of schistosomes with primary haemostasis, secondary haemostasis, fibrinolysis, and the vascular tone will be discussed to provide insight into the reduction in coagulation observed in schistosomiasis patients. Interference with the haemostatic system by pathogens is a common mechanism and has been described for other parasitic worms, bacteria, and fungi as a mechanism to support survival and spread or enhance virulence. Insight into the mechanisms used by schistosomes to interfere with the haemostatic system will provide important insight into the maintenance of the parasitic life cycle within the host. This knowledge may reveal new potential anti-schistosome drug and vaccine targets. In addition, some of the survival mechanisms employed by schistosomes might be used by other pathogens, and therefore, these mechanisms that interfere with host haemostasis might be a broad target for drug development against blood-dwelling pathogens. Also, schistosome antithrombotic or thrombolytic molecules could form potential new drugs in the treatment of haemostatic disorders.
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Helminth entry is facilitated by inhibiting coagulation, particularly prominent in blood-dwelling helminths like schistosomes with multiple strategies to manipulate host vasodilation, fibrinolysis, and coagulation.
“Their entry is also facilitated by inhibiting coagulation, particularly prominent in blood-dwelling helminths like schistosomes with multiple strategies to manipulate host vasodilation, fibrinolysis, and coagulation (Mebius et al., 2013).”
From Modulation of Host Immunity by Helminths: The Expanding Repertoire of Parasite Effector Molecules (2018) · cites this paper as Mebius et al., 2013
The Introduction and Concluding Remarks (page numbers unavailable) describe schistosomes inhibiting coagulation and manipulating fibrinolysis and vascular tone to survive in the host bloodstream. They do not say that inhibiting coagulation facilitates helminth entry into the host; that entry claim is unsupported by this source. (LLM, conf=0.88)
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Citations
Cites
Aggregation of Blood Platelets by Adenosine Diphosphate and its Reversal
Born, G. V. R. (1962) · Nature · doi:10.1038/194927b0 · Cited by 4,296
Gryseels, B., Polman, K., Clerinx, J., & Kestens, L. (2006) · The Lancet · doi:10.1016/s0140-6736(06)69440-3 · Cited by 2,122
The aggregation of blood platelets
Born, G. V. R., & Cross, M. J. (1963) · The Journal of Physiology · doi:10.1113/jphysiol.1963.sp007185 · Cited by 2,111
Modulation of endothelial cell hemostatic properties by tumor necrosis factor.
Nawroth, P. P., & Stern, D. (1986) · The Journal of Experimental Medicine · doi:10.1084/jem.163.3.740 · Cited by 1,310
Defective thrombus formation in mice lacking coagulation factor XII
Renné, T., Požgajová, M., Grüner, S., Schuh, K., Pauer, H., Burfeind, P., Gailani, D., & Nieswandt, B. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050664 · Cited by 684
Virchow and his triad: a question of attribution
Bagot, C. N., & Arya, R. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07323.x · Cited by 681
Millán, J. L. (2006) · Purinergic Signalling · doi:10.1007/s11302-005-5435-6 · Cited by 610
Identification and Characterization of CD39/Vascular ATP Diphosphohydrolase
Kaczmarek, E., Koziak, K., Sévigny, J., Siegel, J. B., Anrather, J., Beaudoin, A. R., Bach, F. H., & Robson, S. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.33116 · Cited by 582
Review: Role of Blood Platelets in Infection and Inflammation
Klinger, M. H. F., & JELKMANN, W. E. B. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/10799900260286623 · Cited by 506
Fluid Flow Stimulates Tissue Plasminogen Activator Secretion by Cultured Human Endothelial Cells
Diamond, S. L., Eskin, S. G., & McIntire, L. V. (1989) · Science · doi:10.1126/science.2467379 · Cited by 464
Jin, Z., Ueba, H., Tanimoto, T., Lungu, A. O., Frame, M. D. S., & Berk, B. C. (2003) · Circulation Research · doi:10.1161/01.res.0000089257.94002.96 · Cited by 380
Renné, T., Schmaier, A. H., Nickel, K. F., Blombäck, M., & Maas, C. (2012) · Blood · doi:10.1182/blood-2012-07-292094 · Cited by 342
Procoagulant Activity in Hemostasis and Thrombosis
Wolberg, A. S., Aleman, M. M., Leiderman, K., & Machlus, K. R. (2011) · Anesthesia & Analgesia · doi:10.1213/ane.0b013e31823a088c · Cited by 314
Virchow’s Triad Revisited: Abnormal Flow
Lowe, G. D. O. (2003) · Pathophysiology of Haemostasis and Thrombosis · doi:10.1159/000083845 · Cited by 278
Angéli, V., Faveeuw, C., Roye, O., Fontaine, J., Teissier, E., Capron, A., Wolowczuk, I., Capron, M., & Trottein, F. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.10.1135 · Cited by 274
Measured Turbulence and Its Effect on Thrombus Formation
Stein, P. D., & Sabbah, H. N. (1974) · Circulation Research · doi:10.1161/01.res.35.4.608 · Cited by 273
Activation of the classical pathway of complement by Hageman factor fragment.
Ghebrehiwet, B., Silverberg, M., & Kaplan, A. P. (1981) · The Journal of Experimental Medicine · doi:10.1084/jem.153.3.665 · Cited by 248
Sévigny, J., Sundberg, C., Braun, N., Guckelberger, O., Csizmadia, E., Qawi, I., Imai, M., Zimmermann, H., & Robson, S. C. (2002) · Blood · doi:10.1182/blood.v99.8.2801 · Cited by 233
Activation of hageman factor by collagen
Wilner, G. D., Nossel, H. L., & LeRoy, E. C. (1968) · Journal of Clinical Investigation · doi:10.1172/jci105943 · Cited by 219
Making Sense of the Schistosome Surface
Skelly, P. J., & Wilson, R. A. (2006) · Advances in Parasitology/Advances in parasitology · doi:10.1016/s0065-308x(06)63003-0 · Cited by 213
New topics in bradykinin research
Maurer, M., Bader, M., Bas, M., Bossi, F., Cicardi, M., Cugno, M., Howarth, P., Kaplan, A., Kojda, G., Leeb‐Lundberg, F., et al. (2011) · Allergy · doi:10.1111/j.1398-9995.2011.02686.x · Cited by 176
The Interaction Between Pathogens and the Host Coagulation System
Sun, H. (2006) · Physiology · doi:10.1152/physiol.00059.2005 · Cited by 163
Fluid Shear Stress Modulates von Willebrand Factor Release From Human Vascular Endothelium
Galbusera, M., Zoja, C., Donadelli, R., Paris, S., Morigi, M., Benigni, A., Figliuzzi, M., Remuzzi, G., & Remuzzi, A. (1997) · Blood · doi:10.1182/blood.v90.4.1558 · Cited by 152
Mechanotransduction of shear in the endothelium: Basic studies and clinical implications
Johnson, B. D., Mather, K. J., & Wallace, J. P. (2011) · Vascular Medicine · doi:10.1177/1358863x11422109 · Cited by 145
Mann, K. G., Brummel‐Ziedins, K. E., Orfeo, T., & Butenas, S. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.12.034 · Cited by 136
Ramajo-Hernández, A., Pérez–Sánchez, R., Ramajo, V., & Oleaga, A. (2006) · Experimental Parasitology · doi:10.1016/j.exppara.2006.07.003 · Cited by 106
The annexin A2 system and vascular homeostasis
Flood, E. C., & Hajjar, K. A. (2011) · Vascular Pharmacology · doi:10.1016/j.vph.2011.03.003 · Cited by 103
Norris, L. (2003) · Best Practice & Research Clinical Obstetrics & Gynaecology · doi:10.1016/s1521-6934(03)00014-2 · Cited by 101
Overview on fibrinolysis: Plasminogen activation pathways on fibrin and cell surfaces
Anglés‐Cano, E. (1994) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(94)90157-0 · Cited by 94
Miles, L. A., Greengard, J. S., & Griffin, J. H. (1983) · Thrombosis Research · doi:10.1016/0049-3848(83)90244-x · Cited by 87
Vasconcelos, E. G., Nascimento, P. S., Nazareth, M. R., Meirelles, L., Verjovski‐Almeida, S., & Ferreira, S. T. (1993) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(93)90042-v · Cited by 86
Interactions between Coagulation and Inflammation
Opal, S. M. (2003) · Scandinavian Journal of Infectious Diseases · doi:10.1080/00365540310015638 · Cited by 83
Interaction of von Willebrand Factor withStaphylococcus aureus
Herrmann, M., Hartleib, J., Kehrel, B. E., Montgomery, R. R., Sixma, J. J., & Peters, G. (1997) · The Journal of Infectious Diseases · doi:10.1086/516502 · Cited by 80
de la Torre-Escudero, E., Manzano-Román, R., Pérez–Sánchez, R., Siles‐Lucas, M., & Oleaga, A. (2010) · Veterinary Parasitology · doi:10.1016/j.vetpar.2010.06.011 · Cited by 75
Purinergic signaling and immune modulation at the schistosome surface?
Bhardwaj, R., & Skelly, P. J. (2009) · Trends in Parasitology · doi:10.1016/j.pt.2009.03.004 · Cited by 73
Cesari, I. M., Simpson, A. J. G., & Evans, W. H. (1981) · Biochemical Journal · doi:10.1042/bj1980467 · Cited by 70
Cloning of a developmentally regulated tegument antigen of Schistosoma mansoni
Stein, L. D., & DAVID, J. (1986) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(86)90106-4 · Cited by 67
Molecular characterization and immunolocalization of Schistosoma mansoni ATP-diphosphohydrolase
Demarco, R. C., Kowaltowski, A. T., Mortara, R. A., & Verjovski‐Almeida, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01268-3 · Cited by 63
Protease specificity and heparin binding and activation of recombinant protease nexin I.
Evans, D. L. I., McGrogan, M. P., Scott, R. W., & Carrell, R. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54571-3 · Cited by 62
Schistosoma mansoni: Topochemical features of cercariae, schistosomula, and adults
Stein, P. C., & Lumsden, R. D. (1973) · Experimental Parasitology · doi:10.1016/0014-4894(73)90118-5 · Cited by 60
Blanton, R. E., Licate, L. S., & Aman, R. A. (1994) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(94)90003-5 · Cited by 57
Tissue Factor Activity Is Upregulated in Human Endothelial Cells Exposed to Oscillatory Shear Stress
Silacci, P., Bouzourène, K., Daniel, F., Brunner, H. R., Hayoz, D., & Mazzolai, L. (2002) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1613133 · Cited by 56
Walshe, T. E., Ferguson, G., Connell, P., O'Brien, C. J., & Cahill, P. A. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-0806 · Cited by 47
Salafsky, B. P., & Fusco, A. (1987) · Experimental Parasitology · doi:10.1016/0014-4894(87)90048-8 · Cited by 47
Yang, J., Qiu, C., Xia, Y., Lixiao, Y., Fu, Z., Yuan, C., Feng, X., & Lin, J. (2010) · Parasitology Research · doi:10.1007/s00436-010-1913-z · Cited by 46
Araujo-Montoya, B. O., Rofatto, H. K., Tararam, C. A., Farias, L. P., Oliveira, K. C., Verjovski‐Almeida, S., Wilson, R. A., & Leite, L. C. C. (2011) · Experimental Parasitology · doi:10.1016/j.exppara.2011.07.008 · Cited by 42
Interaction of Schistosome Eggs with Vascular Endothelium
File, S. K. (1995) · Journal of Parasitology · doi:10.2307/3283925 · Cited by 40
A Schistosomiasis Research Agenda
Colley, D. G., & Secor, W. E. (2007) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000032 · Cited by 38
de la Torre-Escudero, E., Manzano-Román, R., Siles‐Lucas, M., Pérez–Sánchez, R., Moyano, J. C., Barrera, I., & Oleaga, A. (2011) · Veterinary Parasitology · doi:10.1016/j.vetpar.2011.08.013 · Cited by 37
España, F., & Ratnoff, O. D. (1983) · PubMed · Cited by 37
Manipulation of vascular function by blood flukes?
Da’dara, A. A., & Skelly, P. J. (2011) · Blood Reviews · doi:10.1016/j.blre.2011.04.002 · Cited by 35
Schistosoma mansoni: Wandering Capacity of a Worm Couple
Pellegrino, J., & Coelho, P. M. Z. (1978) · Journal of Parasitology · doi:10.2307/3279647 · Cited by 32
Haemostatic abnormalities in hepatosplenic schistosomiasis mansoni
Tanabe, M. (2003) · Parasitology International · doi:10.1016/s1383-5769(03)00051-5 · Cited by 31
Wu, Y., Lenting, P. J., Tielens, A. G. M., de Groot, P. G., & van Hellemond, J. J. (2007) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2007.02725.x · Cited by 30
Self-citationSm22.6 antigen is an inhibitor to human thrombin
Lin, Y., & He, S. (2006) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2006.01.012 · Cited by 30
Schistosoma mansoni and Haematoloechus medioplexus: Nucleosidediphosphatase localization in tegument
Bogitsh, B. J., & Krupa, P. L. (1971) · Experimental Parasitology · doi:10.1016/0014-4894(71)90106-8 · Cited by 30
Tsang, V. C., & Damian, R. (1977) · Blood · doi:10.1182/blood.v49.4.619.619 · Cited by 28
Coagulation Factor XIIa (Activated Hageman Factor) Inhibitor from Adult Schistosoma Mansoni
Tsang, V. C. W., Hubbard, W. J., & Damian, R. T. (1977) · American Journal of Tropical Medicine and Hygiene · doi:10.4269/ajtmh.1977.26.243 · Cited by 28
Oliveira, S. D., Quintas, L. E. M., Amaral, L. S., Noël, F., Farsky, S. H. P., & Silva, C. L. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023547 · Cited by 27
Correia, M. C. B., Domingues, A. L. C., Lacerda, H. R., dos Santos, E. M., Machado, C. G., Hora, V., Neves, M. A., Brito, A., Coêlho, M. R. C. D., & Silva, J. L. A. (2009) · Transactions of the Royal Society of Tropical Medicine and Hygiene · doi:10.1016/j.trstmh.2008.11.017 · Cited by 25
CARVALHO, W. S., LOPES, C. T., Juliano, L., Coelho, P. M. Z., Cunha-Melo, J. R., Beraldo, W. T., & Pesquero, J. L. (1998) · Parasitology · doi:10.1017/s0031182098003175 · Cited by 21
Silva, C., Lenzi, H. L., Silva, V., Paulo, F. L., & l, F. N. X. E. (2002) · Parasitology Research · doi:10.1007/s00436-002-0711-7 · Cited by 20
Cocude, C., Pierrot, C., Cêtre, C., Fontaine, J., GODIN, C., Capron, A., & Khalife, J. (1999) · Parasitology · doi:10.1017/s0031182098003874 · Cited by 19
Esterre, RAOBELISON, Ramarokoto, C. É., Ravaoalimalala, V. E., BOISIER, & Roux (1998) · Parasite Immunology · doi:10.1046/j.1365-3024.1998.00168.x · Cited by 19
Isolation and characterization of glycosaminoglycans from Schistosoma mansoni
Robertson, N. P., & Cain, G. D. (1985) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(85)90245-7 · Cited by 19
Sun, R., Muller, S., Wang, X., Zhuang, F. Y., & Stoltz, J. F. (2000) · PubMed · Cited by 18
The coagulation profile in hepatosplenic schistosomiasis
El-Bassiouni, N. E., Bassiouny, A. E. E., Hussein, N. A., El-Sayed, H. H., Mostafa, I., Lotfy, M., & Omran, S. A. (1998) · Blood Coagulation & Fibrinolysis · doi:10.1097/00001721-199803000-00011 · Cited by 17
Inhibition of the activation of Hageman factor (factor XII) by extracts of Schistosoma mansoni.
Foster, C. B., Flanigan, T., DeStigter, K. K., Blanton, R. E., Dumenco, L. L., Gallagher, C., & Ratnoff, O. D. (1992) · PubMed · Cited by 14
Hyperfibrinolysis in hepatosplenic schistosomiasis.
El-Bassiouni, N. E., Bassiouny, A. E. E., El‐Khayat, H. R., Akl, M., & Omran, S. A. (1996) · Journal of Clinical Pathology · doi:10.1136/jcp.49.12.990 · Cited by 13
Disseminated Intravascular Coagulation in Endemic Hepatosplenic Schistosomiasis
Omran, S. A., El-Bassiouni, N. E., Hussein, N. A., Akl, M., Hussein, A. T., & Mohamed, A. A. (2009) · Haemostasis · doi:10.1159/000217164 · Cited by 12
Schistosoma mansoni-induced thrombocytopenia in mice
Ngaiza, J. R., & Doenhoff, M. J. (1987) · Transactions of the Royal Society of Tropical Medicine and Hygiene · doi:10.1016/0035-9203(87)90444-5 · Cited by 11
Silva, C., Morel, N., & Noël, F. (1998) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/s0074-02761998000700021 · Cited by 8
Enhanced monocyte tissue factor expression in hepatosplenic Schistosomiasis
Amer, A. S., & Amer, M. E. (2002) · Blood Coagulation & Fibrinolysis · doi:10.1097/00001721-200201000-00006 · Cited by 5
Assessment of Factors II, VII, IX, X, and Protein C in Hepatosplenic Schistosomiasis
Amin, H. M., Omran, S. A., El-Bassuoni, N. E., El-Kaliouby, A. H., & El-Ashmawy, S. A. (2009) · Haemostasis · doi:10.1159/000217076 · Cited by 5
Ferriani, M. D. G. C., de Mello, R. T., Soares, A. L., Bicalho, R. S., Silva, F. D. C. L. E., & Coelho, P. M. Z. (2005) · Blood Coagulation & Fibrinolysis · doi:10.1097/01.mbc.0000179911.73032.d5 · Cited by 4
Flagged first, then by citations
Research works printed but not linked: 1
- Beck WS (1985) Hematology. Cambridge: The MIT Press. 496 p.
Cited by
Sorted by citations
Modulation of Host Immunity by Helminths: The Expanding Repertoire of Parasite Effector Molecules
Maizels, R. M., Smits, H. H., & McSorley, H. J. (2018) · Immunity · doi:10.1016/j.immuni.2018.10.016 · Cited by 435
Schistosome Egg Migration: Mechanisms, Pathogenesis and Host Immune Responses
Costain, A. H., MacDonald, A. S., & Smits, H. H. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.03042 · Cited by 231
Patrolling the vascular borders: platelets in immunity to infection and cancer
Gaertner, F., & Maßberg, S. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0202-z · Cited by 194
Innate immune receptors in platelets and platelet-leukocyte interactions
Dib, P. R. B., Quirino-Teixeira, A. C., Merij, L. B., Pinheiro, M. B. M., Rozini, S. V., Andrade, F. B., & Hottz, E. D. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.4mr0620-701r · Cited by 174
Samoil, V., Dagenais, M., Ganapathy, V., Aldridge, J. R., Glebov, A., Jardim, A., & Ribeiro, P. (2018) · Scientific Reports · doi:10.1038/s41598-018-21587-4 · Cited by 148
Anderson, L., Amaral, M. S., Beckedorff, F., Silva, L. F., Dazzani, B., Oliveira, K. C., Almeida, G. T., Gomes, M. R., Pires, D. S., Setúbal, J. C., et al. (2015) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0004334 · Cited by 85
Karkowska‐Kuleta, J., & Kozik, A. (2014) · Molecular Oral Microbiology · doi:10.1111/omi.12078 · Cited by 79
Ranasinghe, S. L., Fischer, K., Gobert, G. N., & McManus, D. P. (2015) · Parasites & Vectors · doi:10.1186/s13071-015-1022-z · Cited by 75
Ariyaratne, A., & Finney, C. A. M. (2019) · Infection and Immunity · doi:10.1128/iai.00127-19 · Cited by 68
Morais, S. B., Figueiredo, B. C.-P., Assis, N. R. G., Alvarenga, D. M., de Magalhães, M. T. Q., Ferreira, R. S., Vieira, A. T., Menezes, G. B., & Oliveira, S. C. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006870 · Cited by 67
Schistosomes Enhance Plasminogen Activation: The Role of Tegumental Enolase
Figueiredo, B. C.-P., Da’dara, A. A., Oliveira, S. C., & Skelly, P. J. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005335 · Cited by 65
González‐Miguel, J., Valero, M. A., Reguera-Gómez, M., Mas‐Bargues, C., Bargues, M. D., Simón, F., & Mas‐Coma, S. (2018) · Parasitology · doi:10.1017/s0031182018001464 · Cited by 53
Wang, Q., Da’dara, A. A., & Skelly, P. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-13141-5 · Cited by 51
Leontovyč, A., Ulrychová, L., O’Donoghue, A. J., Vondrášek, J., Marešová, L., Hubálek, M., Fajtová, P., Chanová, M., Jiang, Z., Craik, C. S., et al. (2018) · PLOS Neglected Tropical Diseases · doi:10.1371/journal.pntd.0006446 · Cited by 45
Ziniel, P. D., Karumudi, B., Barnard, A. H., Fisher, E. M. S., Thatcher, G. R. J., Podust, L. M., & Williams, D. L. (2015) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0004279 · Cited by 43
Retra, K., deWalick, S., Schmitz, M., Yazdanbakhsh, M., Tielens, A. G. M., Brouwers, J. F. H. M., & van Hellemond, J. J. (2015) · International Journal for Parasitology · doi:10.1016/j.ijpara.2015.03.011 · Cited by 43
Self-citationTranscriptome of the parasitic flatworm Schistosoma mansoni during intra-mammalian development
Wangwiwatsin, A., Protasio, A. V., Wilson, S., Owusu, C. K., Holroyd, N. E., Sanders, M. J., Keane, J. A., Doenhoff, M. J., Rinaldi, G., & Berriman, M. (2020) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0007743 · Cited by 41
Da’dara, A. A., & Skelly, P. J. (2014) · Thrombosis Research · doi:10.1016/j.thromres.2014.09.032 · Cited by 41
Protease inhibitors of parasitic flukes: emerging roles in parasite survival and immune defence
Ranasinghe, S. L., & McManus, D. P. (2017) · Trends in Parasitology · doi:10.1016/j.pt.2016.12.013 · Cited by 38
A novel coagulation inhibitor fromSchistosoma japonicum
Ranasinghe, S. L., Fischer, K., Gobert, G. N., & McManus, D. P. (2015) · Parasitology · doi:10.1017/s0031182015001328 · Cited by 29
Femoe, U. M., Jatsa, H. B., Greigert, V., Brunet, J., Cannet, C., Kenfack, M. C., Feussom, N. G., Fassi-Kadji, J. B., Nkondo, E. T., Abou‐Bacar, A., et al. (2022) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0010382 · Cited by 29
González‐Miguel, J., Morchón, R., Siles‐Lucas, M., Oleaga, A., & Simón, F. (2015) · Acta Tropica · doi:10.1016/j.actatropica.2015.01.010 · Cited by 28
González‐Miguel, J., Morchón, R., Siles‐Lucas, M., & Simón, F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124445 · Cited by 26
Molecular characterization of serine protease inhibitor isoform 3, SmSPI, from Schistosoma mansoni
Pakchotanon, P., Molee, P., Nuamtanong, S., Limpanont, Y., Chusongsang, P., Limsomboon, J., Chusongsang, Y., Maneewatchararangsri, S., Chaisri, U., & Adisakwattana, P. (2016) · Parasitology Research · doi:10.1007/s00436-016-5053-y · Cited by 26
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Zhu, B., Luo, F., Shen, Y., Yang, W., Sun, C., Wang, J., Li, J., Mo, X., Xu, B., Zhang, X., et al. (2020) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0008810 · Cited by 26
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Dvořák, J., & Horn, M. (2018) · International Journal for Parasitology · doi:10.1016/j.ijpara.2018.01.001 · Cited by 24
Mebius, M. M., Adégnika, A. A., Zinsou, J. F., Agobe, J. C. D., Honkpéhèdji, Y. J., Yazdanbakhsh, M., van Dam, G. J., Corstjens, P. L. A. M., Tielens, A. G. M., de Groot, P. G., et al. (2019) · Journal of Helminthology · doi:10.1017/s0022149x19000798 · Cited by 22
Self-citationGillis-Germitsch, N., Kockmann, T., Asmis, L. M., Tritten, L., & Schnyder, M. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.753320 · Cited by 22
Leontovyč, A., Ulrychová, L., Horn, M., & Dvořák, J. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0635-3_5 · Cited by 21
Daily rhythms in gene expression of the human parasite Schistosoma mansoni
Rawlinson, K. A., Reid, A. J., Lu, Z., Driguez, P., Wawer, A., Coghlan, A., Sankaranarayanan, G., Buddenborg, S. K., Soria, C. D., McCarthy, C. A., et al. (2021) · BMC Biology · doi:10.1186/s12915-021-01189-9 · Cited by 21
Pirovich, D. B., Da’dara, A. A., & Skelly, P. J. (2020) · Biology Open · doi:10.1242/bio.050385 · Cited by 20
Influence of schistosomiasis on host vaccine responses
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Self-citationTritten, L., Gillis-Germitsch, N., Kockmann, T., & Schnyder, M. (2021) · Scientific Reports · doi:10.1038/s41598-020-79459-9 · Cited by 19
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Janssen, L., Santos, G. L. S., Muller, H. S., Vieira, A. R. A., de Campos, T. A., & Martins, V. D. P. (2016) · Journal of Immunology Research · doi:10.1155/2016/5267485 · Cited by 17
Zhang, Y., Guo, J., He, L., Zong, H.-Y., & Cai, G.-B. (2018) · Parasitology International · doi:10.1016/j.parint.2018.04.002 · Cited by 17
Wang, Q., Da’dara, A. A., & Skelly, P. J. (2018) · Parasites & Vectors · doi:10.1186/s13071-018-2704-0 · Cited by 16
Eyayu, T., Zeleke, A. J., Seyoum, M., & Worku, L. (2020) · Research and Reports in Tropical Medicine · doi:10.2147/rrtm.s244912 · Cited by 15
Diosdado, A., Simón, F., Morchón, R., & González‐Miguel, J. (2020) · Parasitology · doi:10.1017/s0031182020000104 · Cited by 15
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Nation, C. S., Da’dara, A. A., & Skelly, P. J. (2020) · Virulence · doi:10.1080/21505594.2020.1770481 · Cited by 15
Gillis-Germitsch, N., Kockmann, T., Kapel, C. M. O., Thamsborg, S. M., Webster, P., Tritten, L., & Schnyder, M. (2021) · Pathogens · doi:10.3390/pathogens10111513 · Cited by 14
Diosdado, A., Simón, F., Serrat, J., & González‐Miguel, J. (2022) · Parasite · doi:10.1051/parasite/2022034 · Cited by 13
Bexkens, M. L., van Gestel, R. A., van Breukelen, B., Urbanus, R. T., Brouwers, J. F. H. M., Nieuwland, R., Tielens, A. G. M., & van Hellemond, J. J. (2020) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2020.111296 · Cited by 13
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NAD-catabolizing ectoenzymes of Schistosoma mansoni
Nation, C. S., Da’dara, A. A., & Skelly, P. J. (2022) · Biochemical Journal · doi:10.1042/bcj20210784 · Cited by 11
Yeh, Y., Skinner, D., Criado-Hidalgo, E., Chen, N. S., Garcia‐Herreros, A., El‐Sakkary, N., Liu, L. J., Zhang, S., Kandasamy, A., Chien, S., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010309 · Cited by 10
Li, D., Shu, Z., Hao, J., Luo, X., Ye, X., Zhu, W., Duan, W., & Chen, Z. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.03.005 · Cited by 9
Gava, S. G., Tavares, N. C., Falcone, F. H., Oliveira, G., & Mourão, M. D. M. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.01036 · Cited by 8
Chimponda, T. N., Mushayi, C., Osakunor, D. N. M., Vengesai, A., Eyoh, E., Amanfo, S., Murray, J., Tshuma, C., Mutapi, F., & Mduluza, T. (2019) · BMC Infectious Diseases · doi:10.1186/s12879-019-4690-z · Cited by 7
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Diosdado, A., Simón, F., Morchón, R., & González‐Miguel, J. (2021) · Animals · doi:10.3390/ani11030804 · Cited by 6
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Ibrahim, U. A., & Ahmed, S. G. (2018) · Egyptian Journal of Medical Human Genetics · doi:10.1016/j.ejmhg.2018.01.003 · Cited by 5
Gillis-Germitsch, N., Kockmann, T., Schnyder, M., & Tritten, L. (2025) · PLoS ONE · doi:10.1371/journal.pone.0316217 · Cited by 4
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Wu, Z., Nagano, I., Khueangchiangkhwang, S., & Maekawa, Y. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821209-7.00009-3 · Cited by 3
Ibrahim, U. A., & Ahmed, S. G. (2017) · Egyptian Journal of Medical Human Genetics · doi:10.1016/j.ejmhg.2017.10.004 · Cited by 3
Zhang, Y., He, L., Zong, H.-Y., & Cai, G.-B. (2019) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2019.111220 · Cited by 3
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Silva, C. L. M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801078-5.00015-7 · Cited by 3
Collado-Cuadrado, M., Alarcón-Torrecillas, C., la Puente, A. B., Rodríguez-Escolar, I., González-Mohino, E. I., Pericacho, M., & Morchón, R. (2024) · Animals · doi:10.3390/ani14233371 · Cited by 2
Liu, Y., Juma, S., Xue, Q., He, M., Ali, S. M., Khamis, K. S., Suleiman, M. M. A., Hamad, M. S., Khamis, M. A., Zhao, H., et al. (2025) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0013429 · Cited by 2
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Sridhar, G. R., Botta, S., & Lakshmi, G. (2026) · Academia Biology · doi:10.20935/acadbiol8088 · Cited by 2
Abebe, W., Asmare, Z., Alamaw, A. W., Awoke, M., Tesema, A. A., Derso, A., & Lemma, W. (2024) · Scientific Reports · doi:10.1038/s41598-024-56529-w · Cited by 2
Vieira, L. G. M. D. S., Souza, A. F. P., Vital, C. E., Silva, D. R. P., Marques, F. D. S., Silva, G. G., Vieira, P. M. D. A., Wilson, R. A., & Castro‐Borges, W. (2026) · Proteomes · doi:10.3390/proteomes14030039 · Cited by 1
تاثیر شیستوزوما بویس (Schistosoma bovis) در بیان فاکتورهای آنژیوژنزیس بر سلول های ماکروفاژ رت
شریفی, ف. ش., & آلوارز, آ. م. (2016) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.22088/jbums.18.8.61 · Cited by 1
Banerjee, A., Widmer, K., Caffrey, C. R., & Abagyan, R. A. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/116921
Coagulation system in horses in the aspect of comparative pathology
Abramowicz, B., Milczak, A., Kaczmarek, B., Kurek, Ł., Riha, T., & Lutnicki, K. (2018) · Medycyna Weterynaryjna · doi:10.21521/mw.6000
MESENTERIC ISCHEMIA AS A CAUSE OF EARLY DEATH AMONG MICE INFECTED BY Schistosoma mansoni
de Carvalho, T. P. V., Loyo, R. M., do Nascimento, W. R. C., de Paiva, I. H. R., Júnior, F. C. A. D. A., Gomes, E. C. D. S., & Barbosa, C. S. (2018) · Revista de Patologia Tropical / Journal of Tropical Pathology · doi:10.5216/rpt.v47i3.55269
INVOLVEMENT OF SCHISTOSOMA HAEMATOBIUM IN HEPATIC INJURY IN PAPA VILLAGE, SOUTHWEST NIGERIA.
Oladapo, A. A. (2019) · International Journal of Advanced Research · doi:10.21474/ijar01/9485
Sulbarán, G., Costa, G., Losada, S., Peralta, J. M., & Cesari, I. M. (2021) · Pathogens · doi:10.3390/pathogens11010022
Ahmed, S. G., & Ibrahim, U. A. (2022) · African Journal of Clinical and Experimental Microbiology · doi:10.4314/ajcem.v23i2.1
Adedze-Kpodo, R. K. (2023) · Central European Management Journal · doi:10.57030/23364890.cemj.31.1.77
An update on proteases and protease inhibitors from trematodes
Horn, M., Bieliková, L., Vostoupalová, A., Švéda, J., & Mareš, M. (2024) · Advances in Parasitology/Advances in parasitology · doi:10.1016/bs.apar.2024.07.002
Konečný, L., Peterková, K., Hrachovinová, I., Loukas, A. C., Macháček, T., Dvořák, J., & Jedličková, L. (2026) · International Journal for Parasitology · doi:10.1016/j.ijpara.2026.104808
Collado-Cuadrado, M., Rodríguez-Escolar, I., la Puente, A. B., Montero‐Calle, A., Vázquez-Ávila, S., Macchioni, F., Barderas, R., Sotillo, J., Pericacho, M., & Morchón, R. (2026) · Animals · doi:10.3390/ani16060926
Structural and interaction study of MEG family proteins and their role in liver fibrosis onset
Nedvědová, Š. (2023) · theses.fr (ABES) · doi:10.70675/8633d2c6zc9eaz4b4ezb86ez0bb8d3371901
Yimgoua, E. S., Nkondo, E. T., Femoe, U. M., Fassi-Kadji, J. B., Kenfack, M. C., Feussom, N. G., Vázquez, S., Tchuenté, L.-A. T., Sotillo, J., & Jatsa, H. B. (2026) · BMC Infectious Diseases · doi:10.1186/s12879-026-13894-3
Metadata
- Authors
- Mebius, M. M., van Genderen, P. J. J., Urbanus, R. T., Tielens, A. G. M., de Groot, P. G., & van Hellemond, J. J.
- Affiliations
- Erasmus MC (NL)
- University Medical Center Utrecht (NL)
- Corresponding author
- van Hellemond, Jaap J.
- ORCID
- Venue
- PLoS Pathogens
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-12-26
- Volume
- 9
- Issue
- 12
- Pages
- e1003781
- ISSN
- 1553-7366 (ISSN-L)
- 1553-7374
- PMC
- PMC3873443
- OpenAlex
- W2142245213
- Cited by
- 83
- References
- 75
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 3 · 2023: 3 · 2022: 7 · 2021: 9 · 2020: 10 · 2019: 7 · 2018: 13 · 2017: 4 · 2016: 7 · 2015: 9 · 2014: 2
- FWCI
- 0.75
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS Pathogens (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (publishedVersion, other-oa)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion, other-oa)
- RePub (Erasmus University Rotterdam) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Immunology and Microbiology › Parasitology › Parasites and Host Interactions
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Health Sciences › Medicine › Hematology › Blood properties and coagulation
- Keywords
- schistosomes, schistosomiasis, hemostasis, hypercoagulability, hypocoagulability, fibrinolysis, primary hemostasis, vascular tone, endothelial function, host-parasite interactions, thrombolysis, therapeutic target, vaccine targets
- MeSH terms
- Animals, Blood Coagulation, Blood Coagulation Disorders, Fibrinolysis, Hemostasis, Host-Parasite Interactions, Humans, Schistosoma, Schistosomiasis
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