Parasites, Hosts and Diseases

"inhibitor"

Brief Communication

Partial characterization of a cysteine protease inhibitor of Plasmodium vivax: Tuấn Cường Võ, Jung-Mi Kang, Hương Giang Lê, Byoung-Kuk Na; Parasites Hosts Dis 2025;63(4):354-359.
Published online November 19, 2025; DOI: https://doi.org/10.3347/PHD.25043

Abstract
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Cysteine proteases play key roles in the biology of Plasmodium parasites and are recognized as antimalarial drug targets. Because these enzymes are involved in diverse biological functions, precise regulation is required to prevent unnecessary damage to both parasites and hosts. In this study, we identified an endogenous inhibitor of cysteine protease of Plasmodium vivax (PvICP) and characterized its biochemical properties. PvICP was found to share highly similar structural characteristics with orthologous proteins from other Plasmodium species. Recombinant PvICP (rPvICP) expressed in Escherichia coli showed a broad range of inhibitory activity against falcipain family cysteine proteases, including vivapain-3, vivapain-4, falcipain-3, malapain-2, and malapain-4, with more potent inhibitory activity against vivapain-3 and vivapain-4. rPvICP’s inhibitory activity was not significantly affected by pH, suggesting its broad biological functions. These findings provide new insights into PvICP and lay the groundwork for future studies exploring its biological significance and potential as a therapeutic target in malaria research.

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Original Articles

Identification of the protease inhibitory domain of Trichinella spiralis novel cystatin (TsCstN): Thassanee Yuthithum, Orawan Phuphisut, Onrapak Reamtong, Nathamon Kosoltanapiwat, Salisa Chaimon, Porntida Kobpornchai, Charin Thawornkuno, Preeyarat Malaithong, Orathai Sawatdichaikul, Poom Adisakwattana; Parasites Hosts Dis 2024;62(3):330-341.
Published online August 26, 2024; DOI: https://doi.org/10.3347/PHD.24026

The Trichinella spiralis novel cystatin (TsCstN) inhibits cathepsin L (CatL) activity and inflammation of macrophages during lipopolysaccharide (LPS) induction. To identify the protease inhibitory region, this study applied an in silico modeling approach to simulate truncation sites of TsCstN (Ts01), which created four truncated forms, including TsCstN^∆1-39 (Ts02), TsCstN^∆1-71 (Ts03), TsCstN^{∆1-20, ∆73-117} (Ts04), and TsCstN^{∆1-20, ∆42-117} (Ts05). The superimposition of these truncates modeled with AlphaFold Colab indicated that their structures were more akin to Ts01 than those modeled with I-TASSER. Moreover, Ts04 exhibited the closest resemblance to the structure of Ts01. The recombinant Ts01 (rTs01) and truncated proteins (rTs02, rTs03, and rTs04) were successfully expressed in a prokaryotic expression system while Ts05 was synthesized, with sizes of approximately 14, 12, 8, 10, and 2.5 kDa, respectively. When determining the inhibition of CatL activity, both rTs01 and rTs04 effectively reduced CatL activity in vitro. Thus, the combination of the α1 and L1 regions may be sufficient to inhibit CatL. This study provides comprehensive insights into TsCstN, particularly regarding its protein function and inhibitory domains against CatL.

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Systems biology of Haemonchus contortus – Advancing biotechnology for parasitic nematode control
Yuanting Zheng, Neil D. Young, Tao Wang, Bill C.H. Chang, Jiangning Song, Robin B. Gasser
Biotechnology Advances.2025; 81: 108567. CrossRef
Therapeutic potentials of Trichinella spiralis in immune disorders: From allergy to autoimmunity
Minkyoung Cho, Hak Sun Yu
Parasites, Hosts and Diseases.2025; 63(2): 123. CrossRef

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Genome-wide identification of histone lysine methyltransferases and their implications in the epigenetic regulation of eggshell formation-related genes in a trematode parasite Clonorchis sinensis: Min-Ji Park, Woon-Mok Sohn, Young-An Bae; Parasites Hosts Dis 2024;62(1):98-116.
Published online February 23, 2024; DOI: https://doi.org/10.3347/PHD.23116

Epigenetic writers including DNA and histone lysine methyltransferases (DNMT and HKMT, respectively) play an initiative role in the differentiation and development of eukaryotic organisms through the spatiotemporal regulation of functional gene expressions. However, the epigenetic mechanisms have long been suspected in helminth parasites lacking the major DNA methyltransferases DNMT1 and DNMT3a/3b. Very little information on the evolutionary status of the epigenetic tools and their role in regulating chromosomal genes is currently available in the parasitic trematodes. We previously suggested the probable role of a DNMT2-like protein (CsDNMT2) as a genuine epigenetic writer in a trematode parasite Clonorchis sinensis. Here, we analyzed the phylogeny of HKMT subfamily members in the liver fluke and other platyhelminth species. The platyhelminth genomes examined conserved genes for the most of SET domain-containing HKMT and Disruptor of Telomeric Silencing 1 subfamilies, while some genes were expanded specifically in certain platyhelminth genomes. Related to the high gene dosages for HKMT activities covering differential but somewhat overlapping substrate specificities, variously methylated histones were recognized throughout the tissues/organs of C. sinensis adults. The temporal expressions of genes involved in eggshell formation were gradually decreased to their lowest levels proportionally to aging, whereas those of some epigenetic tool genes were re-boosted in the later adult stages of the parasite. Furthermore, these expression levels were significantly affected by treatment with DNMT and HKMT inhibitors. Our data strongly suggest that methylated histones are potent epigenetic markers that modulate the spatiotemporal expressions of C. sinensis genes, especially those involved in sexual reproduction.

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Secretome Analysis of Host Cells Infected with Toxoplasma gondii after Treatment of Human Epidermal Growth Factor Receptor 2/4 Inhibitors: Hye-Jung Kim, Hye-Jin Ahn, Hyeweon Kang, Jaehui Park, Seul gi Oh, Saehae Choi, Won-Kyu Lee, Ho-Woo Nam; Korean J Parasitol 2020;58(3):249-255.
Published online June 26, 2020; DOI: https://doi.org/10.3347/kjp.2020.58.3.249

Abstract
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Toxoplasma gondii, a ubiquitous, intracellular parasite of the phylum Apicomplexa, infects an estimated one-third of the human population as well as a broad range of warm-blooded animals. We have observed that some tyrosine kinase inhibitors suppressed the growth of T. gondii within host ARPE-10 cells. Among them, afatinib, human epithermal growth factor receptor 2 and 4 (HER2/4) inhibitor, may be used as a therapeutic agent for inhibiting parasite growth with minimal adverse effects on host. In this report, we conducted a proteomic analysis to observe changes in host proteins that were altered via infection with T. gondii and the treatment of HER2/4 inhibitors. Secreting proteins were subjected to a procedure of micor basic reverse phase liquid chromatography, nano-liquid chromatography-mass spectrometry, and ingenuity pathway analysis serially. As a result, the expression level of heterogeneous nuclear ribonucleoprotein K, semaphorin 7A, a GPI membrane anchor, serine/threonine-protein phosphatase 2A, and calpain small subunit 1 proteins were significantly changed, and which were confirmed further by western blot analysis. Changes in various proteins, including these 4 proteins, can be used as a basis for explaining the effects of T. gondii infections and HER2/4 inhibitors.

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Host cell proteins modulated upon Toxoplasma infection identified using proteomic approaches: a molecular rationale
Sajad Rashidi, Carmen Vieira, Reza Mansouri, Mohammad Ali-Hassanzadeh, Esmaeel Ghani, Mohammadreza Karimazar, Paul Nguewa, Raúl Manzano-Román
Parasitology Research.2022; 121(7): 1853. CrossRef

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Afatinib Reduces STAT6 Signaling of Host ARPE-19 Cells Infected with Toxoplasma gondii: Zhaoshou Yang, Hye-Jin Ahn, Young-Hoon Park, Ho-Woo Nam; Korean J Parasitol 2016;54(1):31-38.
Published online February 26, 2016; DOI: https://doi.org/10.3347/kjp.2016.54.1.31

Abstract
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Specific gene expressions of host cells by spontaneous STAT6 phosphorylation are major strategy for the survival of intracellular Toxoplasma gondii against parasiticidal events through STAT1 phosphorylation by infection provoked IFN-γ. We determined the effects of small molecules of tyrosine kinase inhibitors (TKIs) on the growth of T. gondii and on the relationship with STAT1 and STAT6 phosphorylation in ARPE-19 cells. We counted the number of T. gondii RH tachyzoites per parasitophorous vacuolar membrane (PVM) after treatment with TKIs at 12-hr intervals for 72 hr. The change of STAT6 phosphorylation was assessed via western blot and immunofluorescence assay. Among the tested TKIs, Afatinib (pan ErbB/EGFR inhibitor, 5 ?M) inhibited 98.0% of the growth of T. gondii, which was comparable to pyrimethamine (5 ?M) at 96.9% and followed by Erlotinib (ErbB1/EGFR inhibitor, 20 ?M) at 33.8% and Sunitinib (PDGFR or c-Kit inhibitor, 10 ?M) at 21.3%. In the early stage of the infection (2, 4, and 8 hr after T. gondii challenge), Afatinib inhibited the phosphorylation of STAT6 in western blot and immunofluorescence assay. Both JAK1 and JAK3, the upper hierarchical kinases of cytokine signaling, were strongly phosphorylated at 2 hr and then disappeared entirely after 4 hr. Some TKIs, especially the EGFR inhibitors, might play an important role in the inhibition of intracellular replication of T. gondii through the inhibition of the direct phosphorylation of STAT6 by T. gondii.

Citations

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Small molecule kinase inhibitor altiratinib inhibits brain cyst forming bradyzoites of Toxoplasma gondii
Yeong Hoon Kim, Hye-Jin Ahn, Hwa Sun Kim, Ho-Woo Nam
Journal of Microbiology.2025; 63(2): e2409001. CrossRef
iTRAQ-Based Phosphoproteomic Analysis Exposes Molecular Changes in the Small Intestinal Epithelia of Cats after Toxoplasma gondii Infection
Bintao Zhai, Yu-Meng Meng, Shi-Chen Xie, Jun-Jie Peng, Yang Liu, Yanhua Qiu, Lu Wang, Jiyu Zhang, Jun-Jun He
Animals.2023; 13(22): 3537. CrossRef
Secretome Analysis of Host Cells Infected with Toxoplasma gondii after Treatment of Human Epidermal Growth Factor Receptor 2/4 Inhibitors
Hye-Jung Kim, Hye-Jin Ahn, Hyeweon Kang, Jaehui Park, Seul gi Oh, Saehae Choi, Won-Kyu Lee, Ho-Woo Nam
The Korean Journal of Parasitology.2020; 58(3): 249. CrossRef
A Human Proteome Array Approach to Identifying Key Host Proteins Targeted by Toxoplasma Kinase ROP18
Zhaoshou Yang, Yongheng Hou, Taofang Hao, Hee-Sool Rho, Jun Wan, Yizhao Luan, Xin Gao, Jianping Yao, Aihua Pan, Zhi Xie, Jiang Qian, Wanqin Liao, Heng Zhu, Xingwang Zhou
Molecular & Cellular Proteomics.2017; 16(3): 469. CrossRef
Adverse Event Profile of Pyrimethamine-Based Therapy in Toxoplasmosis: A Systematic Review
Ruben R. Ben-Harari, Elizabeth Goodwin, Julio Casoy
Drugs in R&D.2017; 17(4): 523. CrossRef
Suppressors for Human Epidermal Growth Factor Receptor 2/4 (HER2/4): A New Family of Anti-Toxoplasmic Agents in ARPE-19 Cells
Yeong Hoon Kim, Lokraj Bhatt, Hye-Jin Ahn, Zhaoshou Yang, Won-Kyu Lee, Ho-Woo Nam
The Korean Journal of Parasitology.2017; 55(5): 491. CrossRef

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Effect of Farnesyltransferase Inhibitor R115777 on Mitochondria of Plasmodium falciparum: Young Ran Ha, Bae-Geun Hwang, Yeonchul Hong, Hye-Won Yang, Sang Joon Lee; Korean J Parasitol 2015;53(4):421-430.
Published online August 25, 2015; DOI: https://doi.org/10.3347/kjp.2015.53.4.421

Abstract
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The parasite Plasmodium falciparum causes severe malaria and is the most dangerous to humans. However, it exhibits resistance to their drugs. Farnesyltransferase has been identified in pathogenic protozoa of the genera Plasmodium and the target of farnesyltransferase includes Ras family. Therefore, the inhibition of farnesyltransferase has been suggested as a new strategy for the treatment of malaria. However, the exact functional mechanism of this agent is still unknown. In addition, the effect of farnesyltransferase inhibitor (FTIs) on mitochondrial level of malaria parasites is not fully understood. In this study, therefore, the effect of a FTI R115777 on the function of mitochondria of P. falciparum was investigated experimentally. As a result, FTI R115777 was found to suppress the infection rate of malaria parasites under in vitro condition. It also reduces the copy number of mtDNA-encoded cytochrome c oxidase III. In addition, the mitochondrial membrane potential (ΔΨm) and the green fluorescence intensity of MitoTracker were decreased by FTI R115777. Chloroquine and atovaquone were measured by the mtDNA copy number as mitochondrial non-specific or specific inhibitor, respectively. Chloroquine did not affect the copy number of mtDNA-encoded cytochrome c oxidase III, while atovaquone induced to change the mtDNA copy number. These results suggest that FTI R115777 has strong influence on the mitochondrial function of P. falciparum. It may have therapeutic potential for malaria by targeting the mitochondria of parasites.

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Promising Molecular Targets of Plasmodium Falciparum, the Deadliest Parasite and Their Synthetic Inhibitors: A Review
Raksha Kardam, Ashok Jangra, Dinesh Kumar, Vinod Kumar, Vikas Sharma
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Recent Advances in Diagnostics and Therapeutic Interventions for Drug-Resistant Malaria
Kangkana Barman, Pranab Goswami
ACS Infectious Diseases.2025; 11(6): 1296. CrossRef
Novel Therapeutics for Malaria
Haitham Alaithan, Nirbhay Kumar, Mohammad Z. Islam, Angelike P. Liappis, Victor E. Nava
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Vivek K. Vyas, Sapna Bhati, Shivani Patel, Manjunath Ghate
Journal of Biomolecular Structure and Dynamics.2022; 40(20): 10481. CrossRef
Characterization of the promoter of the human farnesyltransferase beta subunit and the impact of the transcription factor OCT-1 on its expression
Henning Verhasselt, Patrick Stelmach, Marie Domin, Dominik Jung, Anna Hagemann, Iris Manthey, Hagen S. Bachmann
Genomics.2022; 114(2): 110314. CrossRef
A comprehensive review on classifying fast-acting and slow-acting antimalarial agents based on time of action and target organelle of Plasmodium sp
Monika Mariebernard, Abhinab Mohanty, Vinoth Rajendran
Pathogens and Disease.2022;[Epub] CrossRef
Disentangling the therapeutic tactics in GBM: From bench to bedside and beyond
S. Daisy Precilla, Shreyas S. Kuduvalli, Anitha Thirugnanasambandhar Sivasubramanian
Cell Biology International.2021; 45(1): 18. CrossRef
The Repurposing of the Antimalaria Drug, Primaquine, as a Photosensitizer to Inactivate Cryptococcal Cells
Uju L. Madu, Adepemi O. Ogundeji, Olufemi S. Folorunso, Jacobus Albertyn, Carolina H. Pohl, Olihile M. Sebolai
Photochem.2021; 1(2): 275. CrossRef
Live and Let Dye: Visualizing the Cellular Compartments of the Malaria Parasite Plasmodium falciparum
Marleen Linzke, Sun Liu Rei Yan, Attila Tárnok, Henning Ulrich, Matthew R. Groves, Carsten Wrenger
Cytometry Part A.2020; 97(7): 694. CrossRef
Drug targets for resistant malaria: Historic to future perspectives
Sahil Kumar, T.R. Bhardwaj, D.N. Prasad, Rajesh K. Singh
Biomedicine & Pharmacotherapy.2018; 104: 8. CrossRef
The Prenylated Proteome of Plasmodium falciparum Reveals Pathogen-specific Prenylation Activity and Drug Mechanism-of-action
Jolyn E. Gisselberg, Lichao Zhang, Joshua E. Elias, Ellen Yeh
Molecular & Cellular Proteomics.2017; 16(4): S54. CrossRef
Exploring the putative self‐binding property of the human farnesyltransferase alpha‐subunit
Anna Hagemann, Grit Müller, Iris Manthey, Hagen S. Bachmann
FEBS Letters.2017; 591(21): 3637. CrossRef

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Brief Communication

Partial Purification and Characterization of a Cysteine Protease Inhibitor from the Plerocercoid of Spirometra erinacei: Young-Bae Chung, Hyun-Jong Yang; Korean J Parasitol 2008;46(3):183-186.
Published online September 20, 2008; DOI: https://doi.org/10.3347/kjp.2008.46.3.183

Abstract
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Helminthic cysteine proteases are well known to play critical roles in tissue invasion, nutrient uptake, and immune evasion of the parasites. In the same manner, the sparganum, the plerocercoid of Spirometra mansoni, is also known to secrete a large amount of cysteine proteases. However, cysteine protease inhibitors regulating the proteolytic activities of the cysteine protease are poorly illustrated. In this regard, we partially purified an endogenous cysteine protease inhibitor from spargana and characterized its biochemical properties. The cysteine protease inhibitor was purified by sequential chromatographies using Resource Q anion exchanger and Superdex 200 HR gel filtration from crude extracts of spargana. The molecular weight of the purified protein was estimated to be about 11 kD on SDS-PAGE. It was able to inhibit papain and 27 kDa cysteine protease of spargana with the ratio of 25.7% and 49.1%, respectively, while did not inhibit chymotrypsin. This finding suggests that the cysteine protease inhibitor of spargana may be involved in regulation of endogenous cysteine proteases of the parasite, rather than interact with cysteine proteases from their hosts.

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Identification, molecular profiling and immune functions of cystatin M in silver pomfret (Pampus argenteus)
Yadong Xue, Xiumei Liu, Yajun Wang, Jing Chang, Xubo Wang
Fish & Shellfish Immunology.2024; 153: 109844. CrossRef
Bioinformatics analysis and prokaryotic expression of a cystatin analogue from Spirometra erinaceieuropaei
Lin Huang, Ling Mai, Gang Lv, Xinjun Chen
Biotechnology & Biotechnological Equipment.2023;[Epub] CrossRef
Characterization of Spirometra erinaceieuropaei Plerocercoid Cysteine Protease and Potential Application for Serodiagnosis of Sparganosis
Li Na Liu, Zhong Quan Wang, Xi Zhang, Peng Jiang, Xin Qi, Ruo Dan Liu, Zi Fang Zhang, Jing Cui, Xiao-Nong Zhou
PLOS Neglected Tropical Diseases.2015; 9(6): e0003807. CrossRef
Analysis of Structures, Functions, and Epitopes of Cysteine Protease fromSpirometra erinaceieuropaeiSpargana
Li Na Liu, Jing Cui, Xi Zhang, Tong Wei, Peng Jiang, Zhong Quan Wang
BioMed Research International.2013; 2013: 1. CrossRef
Differential protein expression in Spirometra erinacei according to its development in its final host
Jae-Hwan Kim, Young Ju Kim, Woon-Mok Sohn, Young Mee Bae, Sung-Tae Hong, Min-Ho Choi
Parasitology Research.2009; 105(6): 1549. CrossRef

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Original Article

Degradation of immunoglobulins, protease inhibitors, and interleukin-1 by a secretory proteinase of Acanthamoeba castellanii: Byoung-Kuk Na, Jong-Hwa Cho, Chul-Yong Song, Tong-Soo Kim; Korean J Parasitol 2002;40(2):93-99.
Published online June 30, 2002; DOI: https://doi.org/10.3347/kjp.2002.40.2.93

Abstract
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The effect of a secretory proteinase from the pathogenic amoebae Acanthamoeba castellanii on host's defense-oriented or regulatory proteins such as immunoglobulins, interleukin-1, and protease inhibitors was investigated. The enzyme was found to degrade secretory immunoglobulin A (sIgA), IgG, and IgM. It also degraded interleukin-1α (IL-1α) and IL-1β. Its activity was not inhibited by endogenous protease inhibitors, such as α2-macroglobulin, α1-trypsin inhibitor, and α2-antiplasmin. Furthermore, the enzyme rapidly degraded those endogenous protease inhibitors as well. The degradation of host's defense-oriented or regulatory proteins by the Acanthamoeba proteinase suggested that the enzyme might be an important virulence factor in the pathogenesis of Acanthamoeba infection.

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Bianca Prado-Costa, Larissa Fagundes Pinto, Mariana Fernandes Fonseca, Denise de Freitas, Larissa Magalhães Alvarenga
Cornea.2025; 44(1): 118. CrossRef
Biological characteristics and pathogenicity of Acanthamoeba
Yuehua Wang, Linzhe Jiang, Yitong Zhao, Xiaohong Ju, Le Wang, Liang Jin, Ryan D. Fine, Mingguang Li
Frontiers in Microbiology.2023;[Epub] CrossRef
Genetic Background Affects the Mucosal Secretory IgA Levels, Parasite Burden, Lung Inflammation, and Mouse Susceptibility toAscaris suumInfection
Luciana Maria Oliveira, Denise Silva Nogueira, Ricardo Marcelo Geraldi, Fernando Sérgio Barbosa, Chiara Cássia Oliveira Amorim, Ana Clara Gazzinelli-Guimarães, Nathália Maria Resende, Natália Pinheiro-Rosa, Lucas Rocha Kraemer, Matheus Silvério Mattos, Li
Infection and Immunity.2022;[Epub] CrossRef
Identification and characterization of a secreted M28 aminopeptidase protein in Acanthamoeba
Jian-Ming Huang, Yao-Tsung Chang, Min-Hsiu Shih, Wei-Chen Lin, Fu-Chin Huang
Parasitology Research.2019; 118(6): 1865. CrossRef
Acanthamoeba Keratitis: Current Status and Urgent Research Priorities
Naveed Ahmed Khan, Ayaz Anwar, Ruqaiyyah Siddiqui
Current Medicinal Chemistry.2019; 26(30): 5711. CrossRef
Comparison of Proteins Secreted into Extracellular Space of Pathogenic and Non-pathogenic Acanthamoeba castellanii
Eun-Kyung Moon, Hyun-Seo Choi, So-Min Park, Hyun-Hee Kong, Fu-Shi Quan
The Korean Journal of Parasitology.2018; 56(6): 553. CrossRef
Human antimicrobial peptides in ocular surface defense
Imran Mohammed, Dalia G. Said, Harminder S. Dua
Progress in Retinal and Eye Research.2017; 61: 1. CrossRef
Evaluation of the immunodiagnostic potential of a recombinant surface protein domain fromAcanthamoeba castellanii
ALEMAO G. CARPINTEYRO SÁNCHEZ, VERIDIANA GOMES VIRGINIO, VINICIUS JOSÉ MASCHIO, HENRIQUE BUNSELMEYER FERREIRA, MARILISE BRITTES ROTT
Parasitology.2016; 143(12): 1656. CrossRef
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Experimental Parasitology.2010; 126(1): 73. CrossRef
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Jenica L. Harrison, Gabriela A. Ferreira, Erinn S. Raborn, Audrey D. Lafrenaye, Francine Marciano-Cabral, Guy A. Cabral
Infection and Immunity.2010; 78(9): 4001. CrossRef
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R. S. SACRAMENTO, R. M. MARTINS, A. MIRANDA, A. S. S. DOBROFF, S. DAFFRE, A. S. FORONDA, D. DE FREITAS, S. SCHENKMAN
Parasitology.2009; 136(8): 813. CrossRef
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Marion Blaschitz, Martina Köhsler, Horst Aspöck, Julia Walochnik
Experimental Parasitology.2006; 114(1): 26. CrossRef
Acanthamoeba: biology and increasing importance in human health
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FEMS Microbiology Reviews.2006; 30(4): 564. CrossRef
Pathogenic free-living amoebae in Korea
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The Korean Journal of Parasitology.2004; 42(3): 93. CrossRef