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695 results on '"Tilley, Leann"'

1. Reaction hijacking inhibition of Plasmodium falciparum asparagine tRNA synthetase.

Author

Xie, Stanley, Wang, Yinuo, Morton, Craig, Metcalfe, Riley, Dogovski, Con, Pasaje, Charisse, Dunn, Elyse, Luth, Madeline, Kumpornsin, Krittikorn, Istvan, Eva, Park, Joon, Fairhurst, Kate, Ketprasit, Nutpakal, Yeo, Tomas, Yildirim, Okan, Bhebhe, Mathamsanqa, Klug, Dana, Rutledge, Peter, Godoy, Luiz, Dey, Sumanta, De Souza, Mariana, Siqueira-Neto, Jair, Du, Yawei, Puhalovich, Tanya, Amini, Mona, Shami, Gerry, Loesbanluechai, Duangkamon, Nie, Shuai, Williamson, Nicholas, Jana, Gouranga, Maity, Bikash, Thomson, Patrick, Foley, Thomas, Tan, Derek, Niles, Jacquin, Han, Byung, Goldberg, Daniel, Burrows, Jeremy, Fidock, David, Lee, Marcus, Griffin, Michael, Todd, Matthew, Tilley, Leann, and Winzeler, Elizabeth

Subjects
Animals, Humans, Plasmodium falciparum, Asparagine, Aspartate-tRNA Ligase, RNA, Transfer, Amino Acyl, Antimalarials, Mammals
Abstract

Malaria poses an enormous threat to human health. With ever increasing resistance to currently deployed drugs, breakthrough compounds with novel mechanisms of action are urgently needed. Here, we explore pyrimidine-based sulfonamides as a new low molecular weight inhibitor class with drug-like physical parameters and a synthetically accessible scaffold. We show that the exemplar, OSM-S-106, has potent activity against parasite cultures, low mammalian cell toxicity and low propensity for resistance development. In vitro evolution of resistance using a slow ramp-up approach pointed to the Plasmodium falciparum cytoplasmic asparaginyl-tRNA synthetase (PfAsnRS) as the target, consistent with our finding that OSM-S-106 inhibits protein translation and activates the amino acid starvation response. Targeted mass spectrometry confirms that OSM-S-106 is a pro-inhibitor and that inhibition of PfAsnRS occurs via enzyme-mediated production of an Asn-OSM-S-106 adduct. Human AsnRS is much less susceptible to this reaction hijacking mechanism. X-ray crystallographic studies of human AsnRS in complex with inhibitor adducts and docking of pro-inhibitors into a model of Asn-tRNA-bound PfAsnRS provide insights into the structure-activity relationship and the selectivity mechanism.

Published
2024

3. Reaction hijacking of tyrosine tRNA synthetase as a new whole-of-life-cycle antimalarial strategy.

Author

Xie, Stanley, Metcalfe, Riley, Dunn, Elyse, Morton, Craig, Huang, Shih-Chung, Puhalovich, Tanya, Du, Yawei, Wittlin, Sergio, Nie, Shuai, Luth, Madeline, Ma, Liting, Kim, Mi-Sook, Pasaje, Charisse, Kumpornsin, Krittikorn, Giannangelo, Carlo, Houghton, Fiona, Churchyard, Alisje, Famodimu, Mufuliat, Barry, Daniel, Gillett, David, Dey, Sumanta, Kosasih, Clara, Newman, William, Niles, Jacquin, Lee, Marcus, Baum, Jake, Ottilie, Sabine, Winzeler, Elizabeth, Creek, Darren, Williamson, Nicholas, Parker, Michael, Brand, Stephen, Langston, Steven, Dick, Lawrence, Griffin, Michael, Gould, Alexandra, and Tilley, Leann

Subjects
Adenosine, Animals, Antimalarials, Crystallography, X-Ray, Humans, Malaria, Falciparum, Mice, Molecular Targeted Therapy, Plasmodium falciparum, Protein Biosynthesis, Protein Conformation, Protozoan Proteins, Sulfonic Acids, Tyrosine-tRNA Ligase
Abstract

Aminoacyl transfer RNA (tRNA) synthetases (aaRSs) are attractive drug targets, and we present class I and II aaRSs as previously unrecognized targets for adenosine 5-monophosphate-mimicking nucleoside sulfamates. The target enzyme catalyzes the formation of an inhibitory amino acid-sulfamate conjugate through a reaction-hijacking mechanism. We identified adenosine 5-sulfamate as a broad-specificity compound that hijacks a range of aaRSs and ML901 as a specific reagent a specific reagent that hijacks a single aaRS in the malaria parasite Plasmodium falciparum, namely tyrosine RS (PfYRS). ML901 exerts whole-life-cycle-killing activity with low nanomolar potency and single-dose efficacy in a mouse model of malaria. X-ray crystallographic studies of plasmodium and human YRSs reveal differential flexibility of a loop over the catalytic site that underpins differential susceptibility to reaction hijacking by ML901.

Published
2022

4. Design of proteasome inhibitors with oral efficacy in vivo against Plasmodium falciparum and selectivity over the human proteasome.

Author

Xie, Stanley, Metcalfe, Riley, Mizutani, Hirotake, Puhalovich, Tanya, Hanssen, Eric, Morton, Craig, Du, Yawei, Dogovski, Con, Huang, Shih-Chung, Ciavarri, Jeffrey, Hales, Paul, Griffin, Robert, Cohen, Lawrence, Chuang, Bei-Ching, Wittlin, Sergio, Deni, Ioanna, Yeo, Tomas, Ward, Kurt, Barry, Daniel, Liu, Boyin, Gillett, David, Crespo-Fernandez, Benigno, Ottilie, Sabine, Mittal, Nimisha, Churchyard, Alisje, Ferguson, Daniel, Aguiar, Anna, Guido, Rafael, Baum, Jake, Hanson, Kirsten, Winzeler, Elizabeth, Gamo, Francisco-Javier, Fidock, David, Baud, Delphine, Parker, Michael, Brand, Stephen, Dick, Lawrence, Griffin, Michael, Gould, Alexandra, and Tilley, Leann

Subjects
Plasmodium, antimalarial drug, cryo-EM, peptide boronate, proteasome, Administration, Oral, Animals, Boron Compounds, Catalytic Domain, Humans, Malaria, Falciparum, Mice, Mice, Inbred NOD, Mice, SCID, Models, Molecular, Plasmodium falciparum, Proteasome Endopeptidase Complex, Proteasome Inhibitors
Abstract

The Plasmodium falciparum proteasome is a potential antimalarial drug target. We have identified a series of amino-amide boronates that are potent and specific inhibitors of the P. falciparum 20S proteasome (Pf20S) β5 active site and that exhibit fast-acting antimalarial activity. They selectively inhibit the growth of P. falciparum compared with a human cell line and exhibit high potency against field isolates of P. falciparum and Plasmodium vivax They have a low propensity for development of resistance and possess liver stage and transmission-blocking activity. Exemplar compounds, MPI-5 and MPI-13, show potent activity against P. falciparum infections in a SCID mouse model with an oral dosing regimen that is well tolerated. We show that MPI-5 binds more strongly to Pf20S than to human constitutive 20S (Hs20Sc). Comparison of the cryo-electron microscopy (EM) structures of Pf20S and Hs20Sc in complex with MPI-5 and Pf20S in complex with the clinically used anti-cancer agent, bortezomib, reveal differences in binding modes that help to explain the selectivity. Together, this work provides insights into the 20S proteasome in P. falciparum, underpinning the design of potent and selective antimalarial proteasome inhibitors.

Published
2021

8. A mechanistic model quantifies artemisinin-induced parasite growth retardation in blood-stage Plasmodium falciparum infection

Author

Cao, Pengxing, Klonis, Nectarios, Zaloumis, Sophie, Khoury, David S., Cromer, Deborah, Davenport, Miles P., Tilley, Leann, Simpson, Julie A., and McCaw, James M.

Subjects
Quantitative Biology - Populations and Evolution, 92B05
Abstract

Falciparum malaria is a major parasitic disease causing widespread morbidity and mortality globally. Artemisinin derivatives---the most effective and widely-used antimalarials that have helped reduce the burden of malaria by 60% in some areas over the past decade---have recently been found to induce growth retardation of blood-stage Plasmodium falciparum when applied at clinically relevant concentrations. To date, no model has been designed to quantify the growth retardation effect and to predict the influence of this property on in vivo parasite killing. Here we introduce a mechanistic model of parasite growth from the ring to trophozoite stage of the parasite's life cycle, and by modelling the level of staining with an RNA-binding dye, we demonstrate that the model is able to reproduce fluorescence distribution data from in vitro experiments using the laboratory 3D7 strain. We quantify the dependence of growth retardation on drug concentration and demonstrate the model's utility as a platform to propose experimentally-testable mechanisms of growth retardation. Furthermore we illustrate that a drug-induced delay in growth may significantly influence in vivo parasite dynamics, demonstrating the importance of considering growth retardation in the design of optimal artemisinin-based dosing regimens., Comment: 44 pages, 20 figures (including 8 supplementary figures), 8 tables (including 6 supplementary tables)

Published
2017
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9. A dynamic stress model explains the delayed drug effect in artemisinin treatment of Plasmodium falciparum

Author

Cao, Pengxing, Klonis, Nectarios, Zaloumis, Sophie, Dogovski, Con, Xie, Stanley C., Saralamba, Sompob, White, Lisa J., Fowkes, Freya J. I., Tilley, Leann, Simpson, Julie A., and McCaw, James M.

Subjects
Quantitative Biology - Populations and Evolution, 92B05
Abstract

Artemisinin resistance constitutes a major threat to the continued success of control programs for malaria. With alternative antimalarial drugs not yet available, improving our understanding of how artemisinin-based drugs act and how resistance manifests is essential to enable optimisation of dosing regimens in order to prolong the lifespan of current first-line treatment options. Here, through introduction of a novel model of the dynamics of the parasites' response to drug, we explore how artemisinin-based therapies may be adjusted to maintain efficacy and how artemisinin resistance may manifest and be overcome. We introduce a dynamic mathematical model, extending on the traditional pharmacokinetic-pharmacodynamic framework, to capture the time-dependent development of a stress response in parasites. We fit the model to in vitro data and establish that the parasites' stress response explains the recently identified complex interplay between drug concentration, exposure time and parasite viability. Our model demonstrates that the previously reported hypersensitivity of early ring stage parasites of the 3D7 strain to dihydroartemisinin (DHA) is primarily due to the rapid development of stress, rather than any change in the maximum achievable killing rate. Of direct clinical relevance, we demonstrate that the complex temporal features of artemisinin action observed in vitro have a significant impact on predictions of in vivo parasite clearance using PK-PD models. Given the important role that such models play in the design and evaluation of clinical trials for alternative drug dosing regimens, our model contributes an enhanced predictive platform for the continued efforts to minimise the burden of malaria., Comment: 24 Pages, 9 figures, 2 tables

Published
2016
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11. Safety, infectivity and immunogenicity of a genetically attenuated blood-stage malaria vaccine

Author

Webster, Rebecca, Sekuloski, Silvana, Odedra, Anand, Woolley, Stephen, Jennings, Helen, Amante, Fiona, Trenholme, Katharine R., Healer, Julie, Cowman, Alan F., Eriksson, Emily M., Sathe, Priyanka, Penington, Jocelyn, Blanch, Adam J., Dixon, Matthew W. A., Tilley, Leann, Duffy, Michael F., Craig, Alister, Storm, Janet, Chan, Jo-Anne, Evans, Krystal, Papenfuss, Anthony T., Schofield, Louis, Griffin, Paul, Barber, Bridget E., Andrew, Dean, Boyle, Michelle J., de Labastida Rivera, Fabian, Engwerda, Christian, and McCarthy, James S.

Published
2021
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13. Structure- and function-based design of Plasmodium-selective proteasome inhibitors

Author

Li, Hao, O’Donoghue, Anthony J, van der Linden, Wouter A, Xie, Stanley C, Yoo, Euna, Foe, Ian T, Tilley, Leann, Craik, Charles S, da Fonseca, Paula CA, and Bogyo, Matthew

Subjects
Medical Microbiology, Biomedical and Clinical Sciences, Clinical Sciences, Good Health and Well Being, Animals, Antimalarials, Artemisinins, Catalytic Domain, Cryoelectron Microscopy, Dose-Response Relationship, Drug, Drug Design, Drug Resistance, Drug Synergism, Enzyme Activation, Female, Humans, Mice, Mice, Inbred BALB C, Models, Molecular, Plasmodium, Plasmodium chabaudi, Plasmodium falciparum, Proteasome Endopeptidase Complex, Proteasome Inhibitors, Protein Subunits, Species Specificity, Substrate Specificity, General Science & Technology
Abstract

The proteasome is a multi-component protease complex responsible for regulating key processes such as the cell cycle and antigen presentation. Compounds that target the proteasome are potentially valuable tools for the treatment of pathogens that depend on proteasome function for survival and replication. In particular, proteasome inhibitors have been shown to be toxic for the malaria parasite Plasmodium falciparum at all stages of its life cycle. Most compounds that have been tested against the parasite also inhibit the mammalian proteasome, resulting in toxicity that precludes their use as therapeutic agents. Therefore, better definition of the substrate specificity and structural properties of the Plasmodium proteasome could enable the development of compounds with sufficient selectivity to allow their use as anti-malarial agents. To accomplish this goal, here we use a substrate profiling method to uncover differences in the specificities of the human and P. falciparum proteasome. We design inhibitors based on amino-acid preferences specific to the parasite proteasome, and find that they preferentially inhibit the β2-subunit. We determine the structure of the P. falciparum 20S proteasome bound to the inhibitor using cryo-electron microscopy and single-particle analysis, to a resolution of 3.6 Å. These data reveal the unusually open P. falciparum β2 active site and provide valuable information about active-site architecture that can be used to further refine inhibitor design. Furthermore, consistent with the recent finding that the proteasome is important for stress pathways associated with resistance of artemisinin family anti-malarials, we observe growth inhibition synergism with low doses of this β2-selective inhibitor in artemisinin-sensitive and -resistant parasites. Finally, we demonstrate that a parasite-selective inhibitor could be used to attenuate parasite growth in vivo without appreciable toxicity to the host. Thus, the Plasmodium proteasome is a chemically tractable target that could be exploited by next-generation anti-malarial agents.

Published
2016

15. Hijacking tRNA charging process: a novel approach to combat malaria

Author

Ketprasit, Nutpakal, primary, Xie, Stanley C., additional, Dogovski, Con, additional, Park, Joon Sung, additional, Morton, Craig J., additional, Hilko, David, additional, Dunn, Elyse, additional, Amini, Mona, additional, Nie, Shuai, additional, Williamson, Nicholas, additional, Poulsen, Sally-Ann, additional, Han, Byung Woo, additional, Griffin, Michael D. W., additional, and Tilley, Leann, additional

Published
2023
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18. Reaction hijacking inhibition of Plasmodium falciparum asparagine tRNA synthetase

Author

Tilley, Leann, primary, Xie, Stanley, additional, Wang, Yinuo, additional, Morton, Craig, additional, Metcalfe, Riley, additional, Dogovski, Con, additional, Pasaje, Charisse Flerida, additional, Dunn, Elyse, additional, Luth, Madeline, additional, Kumpornsin, Krittikorn, additional, Istvan, Eva, additional, Park, Joon, additional, Fairhurst, Katie, additional, Yeo, Tomas, additional, Yildirim, Okan, additional, Bhebhe, Mathamsanqa, additional, Klug, Dana, additional, Rutledge, Peter, additional, Godoy, Luiz, additional, Dey, Sumanta, additional, De Souza, Mariana, additional, Siqueira-Neto, Jair, additional, Ketprasit, Nutpakal, additional, Du, Yawei, additional, Amini, Mona, additional, Shami, Gerald, additional, Nie, Shuai, additional, Williamson, Nicholas, additional, Jana, Gouranga, additional, Maity, Bikash, additional, Thomson, Patrick, additional, Foley, Thomas, additional, Loesbanluechai, Duangkamon, additional, Puhalovich, Tanya, additional, Tan, Derek, additional, Niles, Jacquin, additional, Han, Byung Woo, additional, Goldberg, Daniel, additional, Burrows, Jeremy, additional, Fidock, David, additional, Lee, Marcus, additional, Winzeler, Elizabeth, additional, Griffin, Michael, additional, and Todd, Matthew, additional

Published
2023
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29. Deletion of the Plasmodium falciparum exported protein PTP7 leads to Maurer's clefts vesiculation, host cell remodeling defects, and loss of surface presentation of EMP1

Author

Carmo, Olivia MS, Shami, Gerald J, Cox, Dezerae, Liu, Boyin, Blanch, Adam J, Tiash, Snigdha, Tilley, Leann, Dixon, Matthew WA, Carmo, Olivia MS [0000-0002-0132-3843], Shami, Gerald J [0000-0003-2094-1740], Cox, Dezerae [0000-0002-5345-8360], Liu, Boyin [0000-0001-9242-0712], Blanch, Adam J [0000-0001-6565-2438], Dixon, Matthew WA [0000-0001-9732-9686], and Apollo - University of Cambridge Repository

Subjects
Organelles, Protein Transport, Erythrocytes, Virology, Immunology, Erythrocyte Membrane, Plasmodium falciparum, Genetics, Protozoan Proteins, Parasitology, Molecular Biology, Microbiology
Abstract

Presentation of the variant antigen, Plasmodium falciparum erythrocyte membrane protein 1 (EMP1), at knob-like protrusions on the surface of infected red blood cells, underpins the parasite’s pathogenicity. Here we describe a protein PF3D7_0301700 (PTP7), that functions at the nexus between the intermediate trafficking organelle, the Maurer’s cleft, and the infected red blood cell surface. Genetic disruption of PTP7 leads to accumulation of vesicles at the Maurer’s clefts, grossly aberrant knob morphology, and failure to deliver EMP1 to the red blood cell surface. We show that an expanded low complexity sequence in the C-terminal region of PTP7, identified only in the Laverania clade of Plasmodium, is critical for efficient virulence protein trafficking.

Published
2022

32. Fuzzy Classification of Secretory Signals in Proteins Encoded by the Plasmodium falciparum Genome

Author

Logan, Erica, Hall, Richard, Klonis, Nectarios, Herd, Susanna, Tilley, Leann, Hutchison, David, editor, Kanade, Takeo, editor, Kittler, Josef, editor, Kleinberg, Jon M., editor, Mattern, Friedemann, editor, Mitchell, John C., editor, Naor, Moni, editor, Nierstrasz, Oscar, editor, Pandu Rangan, C., editor, Steffen, Bernhard, editor, Sudan, Madhu, editor, Terzopoulos, Demetri, editor, Tygar, Dough, editor, Vardi, Moshe Y., editor, Weikum, Gerhard, editor, Carbonell, Jaime G., editor, Siekmann, Jörg, editor, Negoita, Mircea Gh., editor, Howlett, Robert J., editor, and Jain, Lakhmi C., editor

Published
2004
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45. High Throughput Screening to Identify Selective and Nonpeptidomimetic Proteasome Inhibitors As Antimalarials

Author

Mata-Cantero, Lydia, primary, Xie, Stanley C., additional, García, Mercedes, additional, Coyle, Joanne, additional, Fernandez, Raquel, additional, Cabrera, Alvaro Cortes, additional, Gillett, David L., additional, Crespo, Benigno, additional, Gamo, Francisco-Javier, additional, Fernández, Esther, additional, Tilley, Leann, additional, and Gomez-Lorenzo, Maria G., additional

Published
2021
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46. Additional file 2 of Safety, infectivity and immunogenicity of a genetically attenuated blood-stage malaria vaccine

Author

Webster, Rebecca, Sekuloski, Silvana, Odedra, Anand, Woolley, Stephen, Jennings, Helen, Amante, Fiona, Trenholme, Katharine R., Healer, Julie, Cowman, Alan F., Eriksson, Emily M., Sathe, Priyanka, Penington, Jocelyn, Blanch, Adam J., Dixon, Matthew W. A., Tilley, Leann, Duffy, Michael F., Craig, Alister, Storm, Janet, Chan, Jo-Anne, Evans, Krystal, Papenfuss, Anthony T., Schofield, Louis, Griffin, Paul, Barber, Bridget E., Andrew, Dean, Boyle, Michelle J., de Labastida Rivera, Fabian, Engwerda, Christian, and McCarthy, James S.

Abstract

Additional File 2. Supplementary methods and results for immunogenicity assessments of GAP vaccine. Text S1. Methodology for determining antibody mediated immune response to GAP vaccine. Text S2. Methodology for determining cell mediated immune response to GAP vaccine. Table S1. Antibodies used for flow cytometry. Figure S1. The gating strategy used to identify CD4+ T cells and subsets, as well as the expression of T cell activation markers. Figure S2. The anti-MSP2 IgM response over the course of the study in each subject. Figure S3. The IgG and IgM response to whole parasite lysate over the course of the study in each subject. Figure S4. The frequency of CD4+ T cells, Treg cells, Th1 cells and Tfh cells in peripheral blood mononuclear cells over the course of the study in each subject.

Published
2021
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47. Additional file 3 of Safety, infectivity and immunogenicity of a genetically attenuated blood-stage malaria vaccine

Author

Webster, Rebecca, Sekuloski, Silvana, Odedra, Anand, Woolley, Stephen, Jennings, Helen, Amante, Fiona, Trenholme, Katharine R., Healer, Julie, Cowman, Alan F., Eriksson, Emily M., Sathe, Priyanka, Penington, Jocelyn, Blanch, Adam J., Dixon, Matthew W. A., Tilley, Leann, Duffy, Michael F., Craig, Alister, Storm, Janet, Chan, Jo-Anne, Evans, Krystal, Papenfuss, Anthony T., Schofield, Louis, Griffin, Paul, Barber, Bridget E., Andrew, Dean, Boyle, Michelle J., de Labastida Rivera, Fabian, Engwerda, Christian, and McCarthy, James S.

Abstract

Additional File 3. Supplementary methods and results for in vitro assessments of GAP vaccine. Text S1. Methodology for parasite genotyping. Text S2. Methodology for cytoadherence assays. Text S3. Methodology for scanning electron microscopy. Text S4. Methodology for var gene expression analysis. Table S1. Duration of in vitro culture of P. falciparum prior to harvest for RNA extraction for var gene transcription analysis. Text S5. Results of parasite genotyping. Text S6. Results of scanning electron microscopy analysis of parasite-infected erythrocytes. Text S7. Results of cytoadherence assays. Text S8. Results of var gene expression analysis. Table S2. Most abundantly expressed var genes.

Published
2021
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48. Additional file 1 of Safety, infectivity and immunogenicity of a genetically attenuated blood-stage malaria vaccine

Author

Webster, Rebecca, Sekuloski, Silvana, Odedra, Anand, Woolley, Stephen, Jennings, Helen, Amante, Fiona, Trenholme, Katharine R., Healer, Julie, Cowman, Alan F., Eriksson, Emily M., Sathe, Priyanka, Penington, Jocelyn, Blanch, Adam J., Dixon, Matthew W. A., Tilley, Leann, Duffy, Michael F., Craig, Alister, Storm, Janet, Chan, Jo-Anne, Evans, Krystal, Papenfuss, Anthony T., Schofield, Louis, Griffin, Paul, Barber, Bridget E., Andrew, Dean, Boyle, Michelle J., de Labastida Rivera, Fabian, Engwerda, Christian, and McCarthy, James S.

Abstract

Additional File 1. Supplementary methods and results for subject eligibility and safety assessments. Text S1: Subject eligibility criteria. Table S1: Incidence of adverse events by subject. Table S2: Red blood cell alloantibody test results for Cohort 4 and phenotype of donor red blood cells used for GAP master cell bank manufacture.

Published
2021
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50. Violacein-Induced Chaperone System Collapse Underlies Multistage Antiplasmodial Activity

Author

Tavella, Tatyana Almeida, primary, da Silva, Noeli Soares Melo, additional, Spillman, Natalie, additional, Kayano, Ana Carolina Andrade Vitor, additional, Cassiano, Gustavo Capatti, additional, Vasconcelos, Adrielle Ayumi, additional, Camargo, Antônio Pedro, additional, da Silva, Djane Clarys Baia, additional, Fontinha, Diana, additional, Salazar Alvarez, Luis Carlos, additional, Ferreira, Letícia Tiburcio, additional, Peralis Tomaz, Kaira Cristina, additional, Neves, Bruno Junior, additional, Almeida, Ludimila Dias, additional, Bargieri, Daniel Youssef, additional, Lacerda, Marcus Vinicius Guimarães de, additional, Lemos Cravo, Pedro Vitor, additional, Sunnerhagen, Per, additional, Prudêncio, Miguel, additional, Andrade, Carolina Horta, additional, Pinto Lopes, Stefanie Costa, additional, Carazzolle, Marcelo Falsarella, additional, Tilley, Leann, additional, Bilsland, Elizabeth, additional, Borges, Júlio César, additional, and Maranhão Costa, Fabio Trindade, additional

Published
2021
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