{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T07:48:06Z","timestamp":1767944886035,"version":"3.49.0"},"reference-count":157,"publisher":"Walter de Gruyter GmbH","issue":"10-12","license":[{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["ER178\/17-1"],"award-info":[{"award-number":["ER178\/17-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Ruhr University Bochum, InnovationsFoRUM\u00a0\u2013\u00a0Host Microbe Interactions","award":["IF-009N-22"],"award-info":[{"award-number":["IF-009N-22"]}]},{"name":"Ruhr University Bochum, InnovationsFoRUM\u00a0\u2013\u00a0Host Microbe Interactions","award":["IF-018N-22"],"award-info":[{"award-number":["IF-018N-22"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,12,17]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The phylum Euglenozoa, within the Eukaryote domain, includes diverse protists such as the medically significant kinetoplastids, characterized by their unique kinetoplast DNA. Both kinetoplastids and their sister class Diplonemea possess glycosomes\u00a0\u2013\u00a0specialized microbodies that compartmentalize glycolysis and other metabolic pathways. Glycosomes likely evolved in a common ancestor of kinetoplastid and diplonemids, conferring metabolic flexibility and reducing cellular toxicity. These organelles are essential for parasite survival and thus, represent promising drug targets for treating kinetoplastid diseases. While the basic principles of peroxisome and glycosome biogenesis are conserved, distinct features in glycosome biogenesis machinery and a lower level of sequence conservation enables pathogen specific drug design for developing new therapies. This review summarizes our current knowledge on glycosome biogenesis, recent advances, and therapeutic potential for treating trypanosomatid infections.<\/jats:p>","DOI":"10.1515\/hsz-2025-0183","type":"journal-article","created":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T07:12:47Z","timestamp":1764573167000},"page":"457-476","source":"Crossref","is-referenced-by-count":0,"title":["Recent advances in glycosome biogenesis and its implications for drug discovery"],"prefix":"10.1515","volume":"406","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6859-6467","authenticated-orcid":false,"given":"Lisa","family":"Hohnen","sequence":"first","affiliation":[{"name":"Department of Systems Biochemistry, Faculty of Medicine , Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , Universit\u00e4tsstr. 150, D-44780 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0002-3161-4075","authenticated-orcid":false,"given":"Chethan K.","family":"Krishna","sequence":"additional","affiliation":[{"name":"Department of Systems Biochemistry, Faculty of Medicine , Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , Universit\u00e4tsstr. 150, D-44780 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lewis","family":"Walker","sequence":"additional","affiliation":[{"name":"Department of Systems Biochemistry, Faculty of Medicine , Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , Universit\u00e4tsstr. 150, D-44780 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8380-0342","authenticated-orcid":false,"given":"Ralf","family":"Erdmann","sequence":"additional","affiliation":[{"name":"Department of Systems Biochemistry, Faculty of Medicine , Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , Universit\u00e4tsstr. 150, D-44780 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6023-7454","authenticated-orcid":false,"given":"Vishal C.","family":"Kalel","sequence":"additional","affiliation":[{"name":"Department of Systems Biochemistry, Faculty of Medicine , Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum , Universit\u00e4tsstr. 150, D-44780 Bochum , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"374","published-online":{"date-parts":[[2025,12,1]]},"reference":[{"key":"2026010906004188945_j_hsz-2025-0183_ref_001","doi-asserted-by":"crossref","unstructured":"Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A.J., Bambrick, J., et al.. (2024). Accurate structure prediction of biomolecular interactions with AlphaFold 3. Nature 630: 493\u2013500, https:\/\/doi.org\/10.1038\/s41586-024-07487-w.","DOI":"10.1038\/s41586-024-07487-w"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_002","doi-asserted-by":"crossref","unstructured":"Acosta, H., Burchmore, R., Naula, C., Gualdr\u00f3n-L\u00f3pez, M., Quintero-Troconis, E., C\u00e1ceres, A.J., Michels, P.A.M., Concepci\u00f3n, J.L., and Qui\u00f1ones, W. (2019). Proteomic analysis of glycosomes from Trypanosoma cruzi epimastigotes. Mol. Biochem. Parasitol. 229: 62\u201374, https:\/\/doi.org\/10.1016\/j.molbiopara.2019.02.008.","DOI":"10.1016\/j.molbiopara.2019.02.008"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_003","doi-asserted-by":"crossref","unstructured":"Ali, B.A., Judy, R.M., Chowdhury, S., Jacobsen, N.K., Castanzo, D.T., Carr, K.L., Richardson, C.D., Lander, G.C., Martin, A., and Gardner, B.M. (2024). The N1 domain of the peroxisomal AAA-ATPase Pex6 is required for Pex15 binding and proper assembly with Pex1. J.\u00a0Biol. Chem. 300: 105504, https:\/\/doi.org\/10.1016\/j.jbc.2023.105504.","DOI":"10.1016\/j.jbc.2023.105504"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_004","doi-asserted-by":"crossref","unstructured":"Allmann, S. and Bringaud, F. (2017). Glycosomes: a comprehensive view of their metabolic roles in T. brucei. Int. J.\u00a0Biochem. Cell Biol. 85: 85\u201390, https:\/\/doi.org\/10.1016\/j.biocel.2017.01.015.","DOI":"10.1016\/j.biocel.2017.01.015"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_005","doi-asserted-by":"crossref","unstructured":"Andrade-Alvi\u00e1rez, D., Bonive-Boscan, A.D., C\u00e1ceres, A.J., Qui\u00f1ones, W., Gualdr\u00f3n-L\u00f3pez, M., Ginger, M.L., and Michels, P.A.M. (2022). Delineating transitions during the evolution of specialised peroxisomes: glycosome formation in kinetoplastid and diplonemid protists. Front. Cell Dev. Biol. 10: 979269, https:\/\/doi.org\/10.3389\/fcell.2022.979269.","DOI":"10.3389\/fcell.2022.979269"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_006","doi-asserted-by":"crossref","unstructured":"Bakker, B.M., Mensonides, F.I., Teusink, B., van Hoek, P., Michels, P.A., and Westerhoff, H.V. (2000). Compartmentation protects trypanosomes from the dangerous design of glycolysis. Proc. Natl. Acad. Sci. U.S.A. 97: 2087\u20132092, https:\/\/doi.org\/10.1073\/pnas.030539197.","DOI":"10.1073\/pnas.030539197"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_007","doi-asserted-by":"crossref","unstructured":"Banasik, M., Napolitano, V., Blat, A., Abdulkarim, K., Plewka, J., Czaplewski, C., Gieldon, A., Kozak, M., Wladyka, B., Popowicz, G., et al.. (2024). Structural dynamics of the TPR domain of the peroxisomal cargo receptor Pex5 in Trypanosoma. Int. J.\u00a0Biol. Macromol. 280: 135510, https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.135510.","DOI":"10.1016\/j.ijbiomac.2024.135510"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_008","doi-asserted-by":"crossref","unstructured":"Banerjee, S.K., Kessler, P.S., Saveria, T., and Parsons, M. (2005). Identification of trypanosomatid PEX19: functional characterization reveals impact on cell growth and glycosome size and number. Mol. Biochem. Parasitol. 142: 47\u201355, https:\/\/doi.org\/10.1016\/j.molbiopara.2005.03.008.","DOI":"10.1016\/j.molbiopara.2005.03.008"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_009","doi-asserted-by":"crossref","unstructured":"Banerjee, H., Knoblach, B., and Rachubinski, R.A. (2019). The early-acting glycosome biogenic protein Pex3 is essential for trypanosome viability. Life Sci. Alliance 2: e201900421, https:\/\/doi.org\/10.26508\/lsa.201900421.","DOI":"10.26508\/lsa.201900421"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_010","doi-asserted-by":"crossref","unstructured":"Banerjee, H., LaPointe, P., Eitzen, G., and Rachubinski, R.A. (2021). A small molecule inhibitor of Pex3-Pex19 interaction disrupts glycosome biogenesis and causes lethality in Trypanosoma brucei. Front. Cell Dev. Biol. 9: 703603, https:\/\/doi.org\/10.3389\/fcell.2021.703603.","DOI":"10.3389\/fcell.2021.703603"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_011","doi-asserted-by":"crossref","unstructured":"Banerjee, H. and Rachubinski, R.A. (2017). Involvement of SNARE protein Ykt6 in glycosome biogenesis in Trypanosoma brucei. Mol. Biochem. Parasitol. 218: 28\u201337, https:\/\/doi.org\/10.1016\/j.molbiopara.2017.10.003.","DOI":"10.1016\/j.molbiopara.2017.10.003"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_012","doi-asserted-by":"crossref","unstructured":"Barros-Alvarez, X., Gualdr\u00f3n-L\u00f3pez, M., Acosta, H., C\u00e1ceres, A.J., Graminha, M.A.S., Michels, P.A.M., Concepci\u00f3n, J.L., and Qui\u00f1ones, W. (2014). Glycosomal targets for anti-trypanosomatid drug discovery. Curr. Med. Chem. 21: 1679\u20131706, https:\/\/doi.org\/10.2174\/09298673113209990139.","DOI":"10.2174\/09298673113209990139"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_013","doi-asserted-by":"crossref","unstructured":"Bauer, S.T., McQueeney, K.E., Patel, T., and Morris, M.T. (2017). Localization of a trypanosome peroxin to the endoplasmic reticulum. J.\u00a0Eukaryot. Microbiol. 64: 97\u2013105, https:\/\/doi.org\/10.1111\/jeu.12343.","DOI":"10.1111\/jeu.12343"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_014","doi-asserted-by":"crossref","unstructured":"Bauer, S. and Morris, M.T. (2017). Glycosome biogenesis in trypanosomes and the de novo dilemma. PLoS Negl. Trop. Dis. 11: e0005333, https:\/\/doi.org\/10.1371\/journal.pntd.0005333.","DOI":"10.1371\/journal.pntd.0005333"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_015","doi-asserted-by":"crossref","unstructured":"Bauer, S., Morris, J.C., and Morris, M.T. (2013). Environmentally regulated glycosome protein composition in the African trypanosome. Eukaryot. Cell 12: 1072\u20131079, https:\/\/doi.org\/10.1128\/ec.00086-13.","DOI":"10.1128\/EC.00086-13"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_016","doi-asserted-by":"crossref","unstructured":"Birschmann, I., Stroobants, A.K., van den Berg, M., Sch\u00e4fer, A., Rosenkranz, K., Kunau, W.-H., and Tabak, H.F. (2003). Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes. Mol. Biol. Cell 14: 2226\u20132236, https:\/\/doi.org\/10.1091\/mbc.e02-11-0752.","DOI":"10.1091\/mbc.e02-11-0752"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_017","doi-asserted-by":"crossref","unstructured":"Brennand, A., Gualdr\u00f3n-L\u00f3pez, M., Coppens, I., Rigden, D.J., Ginger, M.L., and Michels, P.A.M. (2011). Autophagy in parasitic protists: unique features and drug targets. Mol. Biochem. Parasitol. 177: 83\u201399, https:\/\/doi.org\/10.1016\/j.molbiopara.2011.02.003.","DOI":"10.1016\/j.molbiopara.2011.02.003"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_018","doi-asserted-by":"crossref","unstructured":"Brennand, A., Rigden, D.J., and Michels, P.A.M. (2012). Trypanosomes contain two highly different isoforms of peroxin PEX13 involved in glycosome biogenesis. FEBS Lett. 586: 1765\u20131771, https:\/\/doi.org\/10.1016\/j.febslet.2012.05.019.","DOI":"10.1016\/j.febslet.2012.05.019"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_019","doi-asserted-by":"crossref","unstructured":"Brocard, C. and Hartig, A. (2006). Peroxisome targeting signal 1: is it really a simple tripeptide? Biochim. Biophys. Acta 1763: 1565\u20131573, https:\/\/doi.org\/10.1016\/j.bbamcr.2006.08.022.","DOI":"10.1016\/j.bbamcr.2006.08.022"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_020","doi-asserted-by":"crossref","unstructured":"Brown, A.I., Kim, P.K., and Rutenberg, A.D. (2014). PEX5 and ubiquitin dynamics on mammalian peroxisome membranes. PLoS Comput. Biol. 10: e1003426, https:\/\/doi.org\/10.1371\/journal.pcbi.1003426.","DOI":"10.1371\/journal.pcbi.1003426"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_021","doi-asserted-by":"crossref","unstructured":"Carmichael, R.E., Islinger, M., and Schrader, M. (2022). Fission impossible (?)-New insights into disorders of peroxisome dynamics. Cells 11, https:\/\/doi.org\/10.3390\/cells11121922.","DOI":"10.3390\/cells11121922"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_022","doi-asserted-by":"crossref","unstructured":"Cavalier-Smith, T. (2016). Higher classification and phylogeny of Euglenozoa. Eur. J.\u00a0Protistol. 56: 250\u2013276, https:\/\/doi.org\/10.1016\/j.ejop.2016.09.003.","DOI":"10.1016\/j.ejop.2016.09.003"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_023","doi-asserted-by":"crossref","unstructured":"Chen, W.W., Rodrigues, T.A., Wendscheck, D., Pedrosa, A.G., Yang, C., Francisco, T., M\u00f6cklinghoff, T., Zografakis, A., Nunes-Silva, B., Avraham, R.E., et al.. (2025). PEX39 facilitates the peroxisomal import of PTS2-containing proteins. Nat. Cell Biol. 27: 1256\u20131271, https:\/\/doi.org\/10.1038\/s41556-025-01711-z.","DOI":"10.1038\/s41556-025-01711-z"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_024","doi-asserted-by":"crossref","unstructured":"Choe, J., Moyersoen, J., Roach, C., Carter, T.L., Fan, E., Michels, P.A.M., and Hol, W.G.J. (2003). Analysis of the sequence motifs responsible for the interactions of peroxins 14 and 5, which are involved in glycosome biogenesis in Trypanosoma brucei. Biochem. 42: 10915\u201310922, https:\/\/doi.org\/10.1021\/bi034248n.","DOI":"10.1021\/bi034248n"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_025","doi-asserted-by":"crossref","unstructured":"Chou, S.-E., Kalel, V.C., and Erdmann, R. (2024). An inhibitor targeting glycosome membrane biogenesis kills Leishmania parasites. bioRxiv, https:\/\/doi.org\/10.1101\/2024.09.13.612636.","DOI":"10.1101\/2024.09.13.612636"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_026","doi-asserted-by":"crossref","unstructured":"Colasante, C., Ellis, M., Ruppert, T., and Voncken, F. (2006). Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei. Proteomics 6: 3275\u20133293, https:\/\/doi.org\/10.1002\/pmic.200500668.","DOI":"10.1002\/pmic.200500668"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_027","doi-asserted-by":"crossref","unstructured":"Colasante, C., Voncken, F., Manful, T., Ruppert, T., Tielens, A.G.M., van Hellemond, J.J., and Clayton, C. (2013). Proteins and lipids of glycosomal membranes from Leishmania tarentolae and Trypanosoma brucei. F1000Res 2: 27, https:\/\/doi.org\/10.3410\/f1000research.2-27.v1.","DOI":"10.12688\/f1000research.2-27.v1"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_028","doi-asserted-by":"crossref","unstructured":"Cronin, C.N. and Tipton, K.F. (1985). Purification and regulatory properties of phosphofructokinase from Trypanosoma (Trypanozoon) brucei brucei. Biochem. J. 227: 113\u2013124, https:\/\/doi.org\/10.1042\/bj2270113.","DOI":"10.1042\/bj2270113"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_029","doi-asserted-by":"crossref","unstructured":"Crowe, L.P. and Morris, M.T. (2021). Glycosome heterogeneity in kinetoplastids. Biochem. Soc. Trans. 49: 29\u201339, https:\/\/doi.org\/10.1042\/bst20190517.","DOI":"10.1042\/BST20190517"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_030","doi-asserted-by":"crossref","unstructured":"Crowe, L.P., Wilkinson, C.L., Nicholson, K.R., and Morris, M.T. (2020). Trypanosoma brucei Pex13.2 is an accessory peroxin that functions in the import of peroxisome targeting sequence type 2 proteins and localizes to subdomains of the glycosome. mSphere 5, https:\/\/doi.org\/10.1128\/msphere.00744-19.","DOI":"10.1128\/mSphere.00744-19"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_031","doi-asserted-by":"crossref","unstructured":"Cyr, N., Madrid, K.P., Strasser, R., Aurousseau, M., Finn, R., Ausio, J., and Jardim, A. (2008). Leishmania donovani peroxin 14 undergoes a marked conformational change following association with peroxin 5. J.\u00a0Biol. Chem. 283: 31488\u201331499, https:\/\/doi.org\/10.1074\/jbc.m803529200.","DOI":"10.1074\/jbc.M803529200"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_032","doi-asserted-by":"crossref","unstructured":"d\u2019Avila-Levy, C.M., Boucinha, C., Kostygov, A., Santos, H.L.C., Morelli, K.A., Grybchuk-Ieremenko, A., Duval, L., Vot\u00fdpka, J., Yurchenko, V., Grellier, P., et al.. (2015). Exploring the environmental diversity of kinetoplastid flagellates in the high-throughput DNA sequencing era. Mem. Inst. Oswaldo Cruz 110, 956\u2013965, https:\/\/doi.org\/10.1590\/0074-02760150253.","DOI":"10.1590\/0074-02760150253"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_033","doi-asserted-by":"crossref","unstructured":"Dammai, V. and Subramani, S. (2001). The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol. Cell 105: 187\u2013196, https:\/\/doi.org\/10.1016\/s0092-8674(01)00310-5.","DOI":"10.1016\/S0092-8674(01)00310-5"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_034","doi-asserted-by":"crossref","unstructured":"Dawidowski, M., Emmanouilidis, L., Kalel, V.C., Tripsianes, K., Schorpp, K., Hadian, K., Kaiser, M., M\u00e4ser, P., Kolonko, M., Tanghe, S., et al.. (2017). Inhibitors of PEX14 disrupt protein import into glycosomes and kill Trypanosoma parasites. Science 355: 1416\u20131420, https:\/\/doi.org\/10.1126\/science.aal1807.","DOI":"10.1126\/science.aal1807"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_035","doi-asserted-by":"crossref","unstructured":"Dawidowski, M., Kalel, V.C., Napolitano, V., Fino, R., Schorpp, K., Emmanouilidis, L., Lenhart, D., Ostertag, M., Kaiser, M., Kolonko, M., et al.. (2020). Structure-activity relationship in pyrazolo[4,3-c]pyridines, first inhibitors of PEX14-PEX5 protein-protein interaction with Trypanocidal activity. J.\u00a0Med. Chem. 63: 847\u2013879, https:\/\/doi.org\/10.1021\/acs.jmedchem.9b01876.","DOI":"10.1021\/acs.jmedchem.9b01876"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_036","doi-asserted-by":"crossref","unstructured":"Debelyy, M.O., Platta, H.W., Saffian, D., Hensel, A., Thoms, S., Meyer, H.E., Warscheid, B., Girzalsky, W., and Erdmann, R. (2011). Ubp15p, a ubiquitin hydrolase associated with the peroxisomal export machinery. J.\u00a0Biol. Chem. 286: 28223\u201328234, https:\/\/doi.org\/10.1074\/jbc.m111.238600.","DOI":"10.1074\/jbc.M111.238600"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_037","doi-asserted-by":"crossref","unstructured":"Deori, N.M. and Nagotu, S. (2022). Peroxisome biogenesis and inter-organelle communication: an indispensable role for Pex11 and Pex30 family proteins in yeast. Current genetics 68: 537\u2013550, https:\/\/doi.org\/10.1007\/s00294-022-01254-y.","DOI":"10.1007\/s00294-022-01254-y"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_038","doi-asserted-by":"crossref","unstructured":"Durrani, H., Hampton, M., Rumbley, J.N., and Zimmer, S.L. (2020). A global analysis of enzyme compartmentalization to glycosomes. Pathogens 9, https:\/\/doi.org\/10.3390\/pathogens9040281.","DOI":"10.3390\/pathogens9040281"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_039","doi-asserted-by":"crossref","unstructured":"Emmanouilidis, L., Sch\u00fctz, U., Tripsianes, K., Madl, T., Radke, J., Ruckt\u00e4schel, R., Wilmanns, M., Schliebs, W., Erdmann, R., and Sattler, M. (2017). Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19. Nat. Commun. 8: 14635, https:\/\/doi.org\/10.1038\/ncomms14635.","DOI":"10.1038\/ncomms14635"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_040","doi-asserted-by":"crossref","unstructured":"Erdmann, R. and Schliebs, W. (2005). Peroxisomal matrix protein import: the transient pore model. Nat. Rev. Mol. Cell Biol. 6: 738\u2013742, https:\/\/doi.org\/10.1038\/nrm1710.","DOI":"10.1038\/nrm1710"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_041","doi-asserted-by":"crossref","unstructured":"Fino, R., Lenhart, D., Kalel, V.C., Softley, C.A., Napolitano, V., Byrne, R., Schliebs, W., Dawidowski, M., Erdmann, R., Sattler, M., et al.. (2021). Computer-aided design and synthesis of a new class of PEX14 inhibitors: substituted 2,3,4,5-tetrahydrobenzo[F] [1,4]oxazepines as potential new trypanocidal agents. J.\u00a0Chem. Inf. Model. 61: 5256\u20135268, https:\/\/doi.org\/10.1021\/acs.jcim.1c00472.","DOI":"10.1021\/acs.jcim.1c00472"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_042","doi-asserted-by":"crossref","unstructured":"Flaspohler, J.A., Lemley, K., and Parsons, M. (1999). A dominant negative mutation in the GIM1 gene of Leishmania donovani is responsible for defects in glycosomal protein localization. Mol. Biochem. Parasitol. 99: 117\u2013128, https:\/\/doi.org\/10.1016\/s0166-6851(99)00005-5.","DOI":"10.1016\/S0166-6851(99)00005-5"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_043","doi-asserted-by":"crossref","unstructured":"Flaspohler, J.A., Rickoll, W.L., Beverley, S.M., and Parsons, M. (1997). Functional identification of a Leishmania gene related to the peroxin 2 gene reveals common ancestry of glycosomes and peroxisomes. Mol. Cell. Biol. 17: 1093\u20131101, https:\/\/doi.org\/10.1128\/mcb.17.3.1093.","DOI":"10.1128\/MCB.17.3.1093"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_044","doi-asserted-by":"crossref","unstructured":"Fransen, M., Vastiau, I., Brees, C., Brys, V., Mannaerts, G.P., and van Veldhoven, P.P. (2005). Analysis of human Pex19p\u2019s domain structure by pentapeptide scanning mutagenesis. J.\u00a0Mol. Biol. 346: 1275\u20131286, https:\/\/doi.org\/10.1016\/j.jmb.2005.01.013.","DOI":"10.1016\/j.jmb.2005.01.013"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_045","doi-asserted-by":"crossref","unstructured":"Furuya, T., Kessler, P., Jardim, A., Schnaufer, A., Crudder, C., and Parsons, M. (2002). Glucose is toxic to glycosome-deficient trypanosomes. Proc. Natl. Acad. Sci. U.S.A. 99: 14177\u201314182, https:\/\/doi.org\/10.1073\/pnas.222454899.","DOI":"10.1073\/pnas.222454899"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_046","doi-asserted-by":"crossref","unstructured":"Galland, N., Demeure, F., Hannaert, V., Verplaetse, E., Vertommen, D., van der Smissen, P., Courtoy, P.J., and Michels, P.A.M. (2007). Characterization of the role of the receptors PEX5 and PEX7 in the import of proteins into glycosomes of Trypanosoma brucei. Biochim. Biophys. Acta 1773: 521\u2013535, https:\/\/doi.org\/10.1016\/j.bbamcr.2007.01.006.","DOI":"10.1016\/j.bbamcr.2007.01.006"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_047","doi-asserted-by":"crossref","unstructured":"Galland, N., Walque, S.de, Voncken, F.G.J., Verlinde, C.L.M.J., and Michels, P.A.M. (2010). An internal sequence targets Trypanosoma brucei triosephosphate isomerase to glycosomes. Mol. Biochem. Parasitol. 171: 45\u201349, https:\/\/doi.org\/10.1016\/j.molbiopara.2010.01.002.","DOI":"10.1016\/j.molbiopara.2010.01.002"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_048","doi-asserted-by":"crossref","unstructured":"Gao, Y., Skowyra, M.L., Feng, P., and Rapoport, T.A. (2022). Protein import into peroxisomes occurs through a nuclear pore-like phase. Science 378: eadf3971, https:\/\/doi.org\/10.1126\/science.adf3971.","DOI":"10.1126\/science.adf3971"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_049","doi-asserted-by":"crossref","unstructured":"Gardner, B.M., Castanzo, D.T., Chowdhury, S., Stjepanovic, G., Stefely, M.S., Hurley, J.H., Lander, G.C., and Martin, A. (2018). The peroxisomal AAA-ATPase Pex1\/Pex6 unfolds substrates by processive threading. Nat. Commun. 9, https:\/\/doi.org\/10.1038\/s41467-017-02474-4.","DOI":"10.1038\/s41467-017-02474-4"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_050","doi-asserted-by":"crossref","unstructured":"Gaussmann, S., Peschel, R., Ott, J., Zak, K.M., Sastre, J., Delhommel, F., Popowicz, G.M., Boekhoven, J., Schliebs, W., Erdmann, R., et al.. (2024). Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif. Nat. Commun. 15: 3317, https:\/\/doi.org\/10.1038\/s41467-024-47605-w.","DOI":"10.1038\/s41467-024-47605-w"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_051","doi-asserted-by":"crossref","unstructured":"Gerber, M., Suppanz, I., Oeljeklaus, S., Niemann, M., K\u00e4ser, S., Warscheid, B., Schneider, A., and Dewar, C.E. (2023). A Msp1-containing complex removes orphaned proteins in the mitochondrial outer membrane of T. brucei. Life Sci. Alliance 6, https:\/\/doi.org\/10.26508\/lsa.202302004.","DOI":"10.1101\/2023.03.07.531462"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_052","doi-asserted-by":"crossref","unstructured":"Giannopoulou, E.-A., Emmanouilidis, L., Sattler, M., Dodt, G., and Wilmanns, M. (2016). Towards the molecular mechanism of the integration of peroxisomal membrane proteins. Biochim. Biophys. Acta 1863: 863\u2013869, https:\/\/doi.org\/10.1016\/j.bbamcr.2015.09.031.","DOI":"10.1016\/j.bbamcr.2015.09.031"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_053","doi-asserted-by":"crossref","unstructured":"Goto, S., Mano, S., Nakamori, C., and Nishimura, M. (2011). Arabidopsis ABERRANT PEROXISOME MORPHOLOGY9 is a peroxin that recruits the PEX1-PEX6 complex to peroxisomes. Plant Cell 23: 1573\u20131587, https:\/\/doi.org\/10.1105\/tpc.110.080770.","DOI":"10.1105\/tpc.110.080770"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_054","doi-asserted-by":"crossref","unstructured":"Goto-Yamada, S., Oikawa, K., Yamato, K.T., Kanai, M., Hikino, K., Nishimura, M., and Mano, S. (2022). Image-based analysis revealing the molecular mechanism of peroxisome dynamics in plants. Front. Cell Dev. Biol. 10: 883491, https:\/\/doi.org\/10.3389\/fcell.2022.883491.","DOI":"10.3389\/fcell.2022.883491"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_055","doi-asserted-by":"crossref","unstructured":"Grimm, I., Saffian, D., Girzalsky, W., and Erdmann, R. (2016). Nucleotide-dependent assembly of the peroxisomal receptor export complex. Sci. Rep. 6: 19838, https:\/\/doi.org\/10.1038\/srep19838.","DOI":"10.1038\/srep19838"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_056","doi-asserted-by":"crossref","unstructured":"Grou, C.P., Francisco, T., Rodrigues, T.A., Freitas, M.O., Pinto, M.P., Carvalho, A.F., Domingues, P., Wood, S.A., Rodr\u00edguez-Borges, J.E., S\u00e1-Miranda, C., et al.. (2012). Identification of ubiquitin-specific protease 9X (USP9X) as a deubiquitinase acting on ubiquitin-peroxin 5 (PEX5) thioester conjugate. J.\u00a0Biol. Chem. 287: 12815\u201312827, https:\/\/doi.org\/10.1074\/jbc.m112.340158.","DOI":"10.1074\/jbc.M112.340158"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_057","doi-asserted-by":"crossref","unstructured":"Gualdr\u00f3n-L\u00f3pez, M., Brennand, A., Avil\u00e1n, L., and Michels, P.A.M. (2013a). Translocation of solutes and proteins across the glycosomal membrane of trypanosomes; possibilities and limitations for targeting with trypanocidal drugs. Parasitology 140: 1\u201320, https:\/\/doi.org\/10.1017\/s0031182012001278.","DOI":"10.1017\/S0031182012001278"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_058","doi-asserted-by":"crossref","unstructured":"Gualdr\u00f3n-L\u00f3pez, M., Brennand, A., Hannaert, V., Qui\u00f1ones, W., C\u00e1ceres, A.J., Bringaud, F., Concepci\u00f3n, J.L., and Michels, P.A.M. (2012). When, how and why glycolysis became compartmentalised in the Kinetoplastea. A new look at an ancient organelle. Int. J.\u00a0Parasitol. 42: 1\u201320, https:\/\/doi.org\/10.1016\/j.ijpara.2011.10.007.","DOI":"10.1016\/j.ijpara.2011.10.007"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_059","doi-asserted-by":"crossref","unstructured":"Gualdr\u00f3n-L\u00f3pez, M., Chevalier, N., van der Smissen, P., Courtoy, P.J., Rigden, D.J., and Michels, P.A.M. (2013b). Ubiquitination of the glycosomal matrix protein receptor PEX5 in Trypanosoma brucei by PEX4 displays novel features. Biochim. Biophys. Acta 1833: 3076\u20133092, https:\/\/doi.org\/10.1016\/j.bbamcr.2013.08.008.","DOI":"10.1016\/j.bbamcr.2013.08.008"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_060","doi-asserted-by":"crossref","unstructured":"Guerra-Giraldez, C., Quijada, L., and Clayton, C.E. (2002). Compartmentation of enzymes in a microbody, the glycosome, is essential in Trypanosoma brucei. J.\u00a0Cell Sci. 115: 2651\u20132658, https:\/\/doi.org\/10.1242\/jcs.115.13.2651.","DOI":"10.1242\/jcs.115.13.2651"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_061","doi-asserted-by":"crossref","unstructured":"G\u00fcther, M.L.S., Urbaniak, M.D., Tavendale, A., Prescott, A., and Ferguson, M.A.J. (2014). High-confidence glycosome proteome for procyclic form Trypanosoma brucei by epitope-tag organelle enrichment and SILAC proteomics. J.\u00a0Proteome Res. 13: 2796\u20132806, https:\/\/doi.org\/10.1021\/pr401209w.","DOI":"10.1021\/pr401209w"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_062","doi-asserted-by":"crossref","unstructured":"Haanstra, J.R., Gonz\u00e1lez-Marcano, E.B., Gualdr\u00f3n-L\u00f3pez, M., and Michels, P.A.M. (2016). Biogenesis, maintenance and dynamics of glycosomes in trypanosomatid parasites. Biochim. Biophys. Acta 1863: 1038\u20131048, https:\/\/doi.org\/10.1016\/j.bbamcr.2015.09.015.","DOI":"10.1016\/j.bbamcr.2015.09.015"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_063","doi-asserted-by":"crossref","unstructured":"Haanstra, J.R., van Tuijl, A., Kessler, P., Reijnders, W., Michels, P.A.M., Westerhoff, H.V., Parsons, M., and Bakker, B.M. (2008). Compartmentation prevents a lethal turbo-explosion of glycolysis in trypanosomes. Proc. Natl. Acad. Sci. U.S.A. 105: 17718\u201317723, https:\/\/doi.org\/10.1073\/pnas.0806664105.","DOI":"10.1073\/pnas.0806664105"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_064","doi-asserted-by":"crossref","unstructured":"Hagedorn, N., Fradera-Sola, A., Mitnacht, M., Gold, T., Schleicher, U., Butter, F., and Janzen, C.J. (2025). Quantitative proteomics of infected macrophages reveals novel Leishmania virulence factors. bioRxiv, https:\/\/doi.org\/10.1101\/2025.01.17.633565.","DOI":"10.1101\/2025.01.17.633565"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_065","doi-asserted-by":"crossref","unstructured":"Herman, M., P\u00e9rez-Morga, D., Schtickzelle, N., and Michels, P.A.M. (2008). Turnover of glycosomes during life-cycle differentiation of Trypanosoma brucei. Autophagy 4: 294\u2013308, https:\/\/doi.org\/10.4161\/auto.5443.","DOI":"10.4161\/auto.5443"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_066","doi-asserted-by":"crossref","unstructured":"Hettema, E.H., Girzalsky, W., van den Berg, M., Erdmann, R., and Distel, B. (2000). Saccharomyces cerevisiae pex3p and pex19p are required for proper localization and stability of peroxisomal membrane proteins. EMBO J. 19: 223\u2013233, https:\/\/doi.org\/10.1093\/emboj\/19.2.223.","DOI":"10.1093\/emboj\/19.2.223"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_067","doi-asserted-by":"crossref","unstructured":"Hojjat, H. and Jardim, A. (2015). The Leishmania donovani peroxin 14 binding domain accommodates a high degeneracy in the pentapeptide motifs present on peroxin 5. Biochim. Biophys. Acta 1850: 2203\u20132212, https:\/\/doi.org\/10.1016\/j.bbagen.2015.07.006.","DOI":"10.1016\/j.bbagen.2015.07.006"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_068","doi-asserted-by":"crossref","unstructured":"Jamdhade, M.D., Pawar, H., Chavan, S., Sathe, G., Umasankar, P.K., Mahale, K.N., Dixit, T., Madugundu, A.K., Prasad, T.S.K., Gowda, H., et al.. (2015). Comprehensive proteomics analysis of glycosomes from Leishmania donovani. OMICS 19: 157\u2013170, https:\/\/doi.org\/10.1089\/omi.2014.0163.","DOI":"10.1089\/omi.2014.0163"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_069","doi-asserted-by":"crossref","unstructured":"Jansen, R.L.M., Santana-Molina, C., van den Noort, M., Devos, D.P., and van der Klei, I.J. (2021). Comparative genomics of peroxisome biogenesis proteins: making sense of the PEX proteins. Front. Cell Dev. Biol. 9: 654163, https:\/\/doi.org\/10.3389\/fcell.2021.654163.","DOI":"10.3389\/fcell.2021.654163"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_070","doi-asserted-by":"crossref","unstructured":"Jardim, A., Hardie, D.B., Boitz, J., and Borchers, C.H. (2018). Proteomic profiling of Leishmania donovani promastigote subcellular organelles. J.\u00a0Proteome Res. 17: 1194\u20131215, https:\/\/doi.org\/10.1021\/acs.jproteome.7b00817.","DOI":"10.1021\/acs.jproteome.7b00817"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_071","doi-asserted-by":"crossref","unstructured":"Jardim, A., Liu, W., Zheleznova, E., and Ullman, B. (2000). Peroxisomal targeting signal-1 receptor protein PEX5 from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization. J.\u00a0Biol. Chem. 275: 13637\u201313644, https:\/\/doi.org\/10.1074\/jbc.275.18.13637.","DOI":"10.1074\/jbc.275.18.13637"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_072","doi-asserted-by":"crossref","unstructured":"Jardim, A., Rager, N., Liu, W., and Ullman, B. (2002). Peroxisomal targeting protein 14 (PEX14) from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization. Mol. Biochem. Parasitol. 124: 51\u201362, https:\/\/doi.org\/10.1016\/s0166-6851(02)00164-0.","DOI":"10.1016\/S0166-6851(02)00164-0"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_073","doi-asserted-by":"crossref","unstructured":"Jones, J.M., Morrell, J.C., and Gould, S.J. (2004). PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins. J.\u00a0Cell Biol. 164: 57\u201367, https:\/\/doi.org\/10.1083\/jcb.200304111.","DOI":"10.1083\/jcb.200304111"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_074","doi-asserted-by":"crossref","unstructured":"Judy, R.M., Sheedy, C.J., and Gardner, B.M. (2022). Insights into the structure and function of the Pex1\/Pex6\u00a0AAA-ATPase in peroxisome homeostasis. Cells. 11, https:\/\/doi.org\/10.3390\/cells11132067.","DOI":"10.3390\/cells11132067"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_075","doi-asserted-by":"crossref","unstructured":"Kalel, V.C., Li, M., Gaussmann, S., Delhommel, F., Sch\u00e4fer, A.-B., Tippler, B., Jung, M., Maier, R., Oeljeklaus, S., Schliebs, W., et al.. (2019). Evolutionary divergent PEX3 is essential for glycosome biogenesis and survival of trypanosomatid parasites. Biochim. Biophys. Acta 1866: 118520, https:\/\/doi.org\/10.1016\/j.bbamcr.2019.07.015.","DOI":"10.1016\/j.bbamcr.2019.07.015"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_076","doi-asserted-by":"crossref","unstructured":"Kalel, V.C., M\u00e4ser, P., Sattler, M., Erdmann, R., and Popowicz, G.M. (2018). Come, sweet death: targeting glycosomal protein import for antitrypanosomal drug development. Curr. Opin. Microbiol. 46: 116\u2013122, https:\/\/doi.org\/10.1016\/j.mib.2018.11.003.","DOI":"10.1016\/j.mib.2018.11.003"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_077","doi-asserted-by":"crossref","unstructured":"Kalel, V.C., Schliebs, W., and Erdmann, R. (2015). Identification and functional characterization of Trypanosoma brucei peroxin 16. Biochim. Biophys. Acta 1853: 2326\u20132337, https:\/\/doi.org\/10.1016\/j.bbamcr.2015.05.024.","DOI":"10.1016\/j.bbamcr.2015.05.024"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_078","doi-asserted-by":"crossref","unstructured":"Kiel, J.A.K.W., Emmrich, K., Meyer, H.E., and Kunau, W.-H. (2005). Ubiquitination of the peroxisomal targeting signal type 1 receptor, Pex5p, suggests the presence of a quality control mechanism during peroxisomal matrix protein import. J.\u00a0Biol. Chem. 280: 1921\u20131930, https:\/\/doi.org\/10.1074\/jbc.m403632200.","DOI":"10.1074\/jbc.M403632200"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_079","doi-asserted-by":"crossref","unstructured":"Kragt, A., Voorn-Brouwer, T., van den Berg, M., and Distel, B. (2005). The Saccharomyces cerevisiae peroxisomal import receptor Pex5p is monoubiquitinated in wild type cells. J.\u00a0Biol. Chem. 280: 7867\u20137874, https:\/\/doi.org\/10.1074\/jbc.m413553200.","DOI":"10.1074\/jbc.M413553200"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_080","doi-asserted-by":"crossref","unstructured":"Krazy, H. and Michels, P.A.M. (2006). Identification and characterization of three peroxins--PEX6, PEX10 and PEX12--involved in glycosome biogenesis in Trypanosoma brucei. Biochim. Biophys. Acta 1763: 6\u201317, https:\/\/doi.org\/10.1016\/j.bbamcr.2005.11.002.","DOI":"10.1016\/j.bbamcr.2005.11.002"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_081","doi-asserted-by":"crossref","unstructured":"Krishna, C.K., Das, H., Hohnen, L., Schliebs, W., Oeljeklaus, S., Warscheid, B., Kalel, V.C., and Erdmann, R. (2025a). High-confidence glycosomal membrane protein inventory unveils trypanosomal peroxin PEX15. Cell Rep. 44: 115614, https:\/\/doi.org\/10.1016\/j.celrep.2025.115614.","DOI":"10.1016\/j.celrep.2025.115614"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_082","doi-asserted-by":"crossref","unstructured":"Krishna, C.K., Gaussmann, S., Das, H., Jung, M., Oeljeklaus, S., Sattler, M., Warscheid, B., Kalel, V.C., and Erdmann, R. (2025b). Evolutionary remodelling of a remnant GET-pathway factor into PEX38, a novel and essential peroxin in Euglenozoa. bioRxiv. https:\/\/doi.org\/10.1101\/2025.11.03.686288.","DOI":"10.1101\/2025.11.03.686288"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_083","doi-asserted-by":"crossref","unstructured":"Krishna, C.K., Schmidt, N., Tippler, B.G., Schliebs, W., Jung, M., Winklhofer, K.F., Erdmann, R., and Kalel, V.C. (2023). Molecular basis of the glycosomal targeting of PEX11 and its mislocalization to mitochondrion in trypanosomes. Front. Cell Dev. Biol. 11: 1213761, https:\/\/doi.org\/10.3389\/fcell.2023.1213761.","DOI":"10.3389\/fcell.2023.1213761"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_084","doi-asserted-by":"crossref","unstructured":"Krshnan, L., van de Weijer, M.L., and Carvalho, P. (2022). Endoplasmic reticulum-associated protein degradation. Cold Spring Harb. Perspect. Biol. 14: a041247, https:\/\/doi.org\/10.1101\/cshperspect.a041247.","DOI":"10.1101\/cshperspect.a041247"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_085","doi-asserted-by":"crossref","unstructured":"Kumar, A., Roach, C., Hirsh, I.S., Turley, S., deWalque, S., Michels, P.A., and Hol, W.G. (2001). An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei. J.\u00a0Mol. Biol. 307: 271\u2013282, https:\/\/doi.org\/10.1006\/jmbi.2000.4465.","DOI":"10.1006\/jmbi.2000.4465"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_086","doi-asserted-by":"crossref","unstructured":"Law, K.B., Bronte-Tinkew, D., Di Pietro, E., Snowden, A., Jones, R.O., Moser, A., Brumell, J.H., Braverman, N., and Kim, P.K. (2017). The peroxisomal AAA ATPase complex prevents pexophagy and development of peroxisome biogenesis disorders. Autophagy 13: 868\u2013884, https:\/\/doi.org\/10.1080\/15548627.2017.1291470.","DOI":"10.1080\/15548627.2017.1291470"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_087","doi-asserted-by":"crossref","unstructured":"Lazarow, P.B. and Fujiki, Y. (1985). Biogenesis of peroxisomes. Annu. Rev. Cell. Biol. 1: 489\u2013530, https:\/\/doi.org\/10.1146\/annurev.cb.01.110185.002421.","DOI":"10.1146\/annurev.cb.01.110185.002421"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_088","doi-asserted-by":"crossref","unstructured":"Lejon, V., Lindner, A.K., and Franco, J.R. (2025). Human African trypanosomiasis. Lancet 405: 937\u2013950, https:\/\/doi.org\/10.1016\/s0140-6736(25)00107-2.","DOI":"10.1016\/S0140-6736(25)00107-2"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_089","doi-asserted-by":"crossref","unstructured":"L\u00e9on, S., Zhang, L., McDonald, W.H., Yates, J., Cregg, J.M., and Subramani, S. (2006). Dynamics of the peroxisomal import cycle of PpPex20p: ubiquitin-dependent localization and regulation. J.\u00a0Cell Biol. 172: 67\u201378, https:\/\/doi.org\/10.1083\/jcb.200508096.","DOI":"10.1083\/jcb.200508096"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_090","doi-asserted-by":"crossref","unstructured":"Li, M., Gaussmann, S., Tippler, B., Ott, J., Popowicz, G.M., Schliebs, W., Sattler, M., Erdmann, R., and Kalel, V.C. (2021). Novel trypanocidal inhibitors that block glycosome biogenesis by targeting PEX3-PEX19 interaction. Front. Cell Dev. Biol. 9: 737159, https:\/\/doi.org\/10.3389\/fcell.2021.737159.","DOI":"10.3389\/fcell.2021.737159"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_091","doi-asserted-by":"crossref","unstructured":"Lorenz, P., Maier, A.G., Baumgart, E., Erdmann, R., and Clayton, C. (1998). Elongation and clustering of glycosomes in Trypanosoma brucei\u00a0overexpressing the glycosomal Pex11p. EMBO J. 17: 3542\u20133555, https:\/\/doi.org\/10.1093\/emboj\/17.13.3542.","DOI":"10.1093\/emboj\/17.13.3542"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_092","doi-asserted-by":"crossref","unstructured":"Mahadevan, L., Arya, H., Droste, A., Schliebs, W., Erdmann, R., and Kalel, V.C. (2024). PEX1 is essential for glycosome biogenesis and trypanosomatid parasite survival. Front. Cell. Infect. Microbiol. 14: 1274506, https:\/\/doi.org\/10.3389\/fcimb.2024.1274506.","DOI":"10.3389\/fcimb.2024.1274506"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_093","doi-asserted-by":"crossref","unstructured":"Maier, A., Lorenz, P., Voncken, F., and Clayton, C. (2001). An essential dimeric membrane protein of trypanosome glycosomes. Mol. Microbiol. 39: 1443\u20131451, https:\/\/doi.org\/10.1046\/j.1365-2958.2001.02333.x.","DOI":"10.1046\/j.1365-2958.2001.02333.x"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_094","doi-asserted-by":"crossref","unstructured":"Mannion-Henderson, J., Flaspohler, J.A., Lemley, K.R., Rickoll, W.L., and Parsons, M. (2000). Isolation and characterization of Leishmania mutants defective in glycosomal protein import. Mol. Biochem. Parasitol. 106: 225\u2013237, https:\/\/doi.org\/10.1016\/s0166-6851(99)00215-7.","DOI":"10.1016\/S0166-6851(99)00215-7"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_095","doi-asserted-by":"crossref","unstructured":"Mano, S., Nakamori, C., Nito, K., Kondo, M., and Nishimura, M. (2006). The Arabidopsis pex12 and pex13 mutants are defective in both PTS1- and PTS2-dependent protein transport to peroxisomes. Plant J. 47: 604\u2013618, https:\/\/doi.org\/10.1111\/j.1365-313x.2006.02809.x.","DOI":"10.1111\/j.1365-313X.2006.02809.x"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_096","doi-asserted-by":"crossref","unstructured":"Marciniak, M., Mr\u00f3z, P., Napolitano, V., Kalel, V.C., Fino, R., Pykacz, E., Schliebs, W., Plettenburg, O., Erdmann, R., Sattler, M., et al.. (2023). Development of novel PEX5-PEX14 protein-protein interaction (PPI) inhibitors based on an oxopiperazine template. Eur. J.\u00a0Med. Chem. 258: 115587, https:\/\/doi.org\/10.1016\/j.ejmech.2023.115587.","DOI":"10.1016\/j.ejmech.2023.115587"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_097","doi-asserted-by":"crossref","unstructured":"Mathison, B.A. and Bradley, B.T. (2023). Review of the clinical presentation, pathology, diagnosis, and treatment of Leishmaniasis. Lab. Med. 54: 363\u2013371, https:\/\/doi.org\/10.1093\/labmed\/lmac134.","DOI":"10.1093\/labmed\/lmac134"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_098","doi-asserted-by":"crossref","unstructured":"Matsumoto, N., Tamura, S., and Fujiki, Y. (2003). The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes. Nat. Cell Biol. 5: 454\u2013460, https:\/\/doi.org\/10.1038\/ncb982.","DOI":"10.1038\/ncb982"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_099","doi-asserted-by":"crossref","unstructured":"Meinecke, M., Cizmowski, C., Schliebs, W., Kr\u00fcger, V., Beck, S., Wagner, R., and Erdmann, R. (2010). The peroxisomal importomer constitutes a large and highly dynamic pore. Nat. Cell Biol. 12: 273\u2013277, https:\/\/doi.org\/10.1038\/ncb2027.","DOI":"10.1038\/ncb2027"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_100","doi-asserted-by":"crossref","unstructured":"Michels, P.A.M. and Gualdr\u00f3n-L\u00f3pez, M. (2022). Biogenesis and metabolic homeostasis of trypanosomatid glycosomes: new insights and new questions. J.\u00a0Eukaryot. Microbiol. 69: e12897, https:\/\/doi.org\/10.1111\/jeu.12897.","DOI":"10.1111\/jeu.12897"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_101","doi-asserted-by":"crossref","unstructured":"Mindthoff, S., Grunau, S., Steinfort, L.L., Girzalsky, W., Hiltunen, J.K., Erdmann, R., and Antonenkov, V.D. (2016). Peroxisomal Pex11 is a pore-forming protein homologous to TRPM channels. Biochimica et biophysica acta 1863: 271\u2013283, https:\/\/doi.org\/10.1016\/j.bbamcr.2015.11.013.","DOI":"10.1016\/j.bbamcr.2015.11.013"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_102","doi-asserted-by":"crossref","unstructured":"Miyata, N. and Fujiki, Y. (2005). Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export. Mol. Cell. Biol. 25: 10822\u201310832, https:\/\/doi.org\/10.1128\/mcb.25.24.10822-10832.2005.","DOI":"10.1128\/MCB.25.24.10822-10832.2005"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_103","doi-asserted-by":"crossref","unstructured":"Montes, I.D., Amirthagunanathan, S., Ganji, R., Paulo, J.A., Ahlstedt, B.A., Nguyen, L., Joshi, A.S., and Raman, M. (2025). The p97 ATPase and its adaptor UBXD8 maintain peroxisome pools by preventing pexophagy. J.\u00a0Cell Biol. 224, https:\/\/doi.org\/10.1083\/jcb.202409024.","DOI":"10.1083\/jcb.202409024"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_104","doi-asserted-by":"crossref","unstructured":"Moyersoen, J., Choe, J., Kumar, A., Voncken, F.G.J., Hol, W.G.J., and Michels, P.A.M. (2003). Characterization of Trypanosoma brucei PEX14 and its role in the import of glycosomal matrix proteins. Eur. J.\u00a0Biochem. 270: 2059\u20132067, https:\/\/doi.org\/10.1046\/j.1432-1033.2003.03582.x.","DOI":"10.1046\/j.1432-1033.2003.03582.x"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_105","doi-asserted-by":"crossref","unstructured":"Nair, D.M., Purdue, P.E., and Lazarow, P.B. (2004). Pex7p translocates in and out of peroxisomes in Saccharomyces cerevisiae. J.\u00a0Cell Biol. 167: 599\u2013604, https:\/\/doi.org\/10.1083\/jcb.200407119.","DOI":"10.1083\/jcb.200407119"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_106","doi-asserted-by":"crossref","unstructured":"Napolitano, V., Mr\u00f3z, P., Marciniak, M., Kalel, V.C., Softley, C.A., Janna Olmos, J.D., Tippler, B.G., Schorpp, K., Rioton, S., Fr\u00f6hlich, T., et al.. (2022a). Structure-based design, synthesis and evaluation of a novel family of PEX5-PEX14 interaction inhibitors against Trypanosoma. Eur. J.\u00a0Med. Chem. 243: 114778, https:\/\/doi.org\/10.1016\/j.ejmech.2022.114778.","DOI":"10.1016\/j.ejmech.2022.114778"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_107","doi-asserted-by":"crossref","unstructured":"Napolitano, V., Softley, C.A., Blat, A., Kalel, V.C., Schorpp, K., Siebenmorgen, T., Hadian, K., Erdmann, R., Sattler, M., Popowicz, G.M., et al.. (2022b). Small molecule mediated inhibition of protein cargo recognition by peroxisomal transport receptor PEX5 is toxic to Trypanosoma. Sci. Rep. 12: 14705, https:\/\/doi.org\/10.1038\/s41598-022-18841-1.","DOI":"10.1038\/s41598-022-18841-1"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_108","doi-asserted-by":"crossref","unstructured":"Nashiro, C., Kashiwagi, A., Matsuzaki, T., Tamura, S., and Fujiki, Y. (2011). Recruiting mechanism of the AAA peroxins, Pex1p and Pex6p, to Pex26p on the peroxisomal membrane. Traffic 12: 774\u2013788, https:\/\/doi.org\/10.1111\/j.1600-0854.2011.01182.x.","DOI":"10.1111\/j.1600-0854.2011.01182.x"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_109","doi-asserted-by":"crossref","unstructured":"Nordgren, M., Francisco, T., Lismont, C., Hennebel, L., Brees, C., Wang, B., van Veldhoven, P.P., Azevedo, J.E., and Fransen, M. (2015). Export-deficient monoubiquitinated PEX5 triggers peroxisome removal in SV40 large T antigen-transformed mouse embryonic fibroblasts. Autophagy 11: 1326\u20131340, https:\/\/doi.org\/10.1080\/15548627.2015.1061846.","DOI":"10.1080\/15548627.2015.1061846"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_110","doi-asserted-by":"crossref","unstructured":"Nuebel, E., Morgan, J.T., Fogarty, S., Winter, J.M., Lettlova, S., Berg, J.A., Chen, Y.-C., Kidwell, C.U., Maschek, J.A., Clowers, K.J., et al.. (2021). The biochemical basis of mitochondrial dysfunction in Zellweger Spectrum Disorder. EMBO Rep. 22: e51991, https:\/\/doi.org\/10.15252\/embr.202051991.","DOI":"10.15252\/embr.202051991"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_111","doi-asserted-by":"crossref","unstructured":"Nuttall, J.M., Motley, A.M., and Hettema, E.H. (2014). Deficiency of the exportomer components Pex1, Pex6, and Pex15 causes enhanced pexophagy in Saccharomyces cerevisiae. Autophagy 10: 835\u2013845, https:\/\/doi.org\/10.4161\/auto.28259.","DOI":"10.4161\/auto.28259"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_112","unstructured":"Nwagwu, M. and Opperdoes, F.R. (1982). Regulation of glycolysis in Trypanosoma brucei: hexokinase and phosphofructokinase activity. Acta Trop. 39: 61\u201372."},{"key":"2026010906004188945_j_hsz-2025-0183_ref_113","doi-asserted-by":"crossref","unstructured":"Opperdoes, F.R. (1987). Compartmentation of carbohydrate metabolism in trypanosomes. Annu. Rev. Microbiol. 41: 127\u2013151, https:\/\/doi.org\/10.1146\/annurev.mi.41.100187.001015.","DOI":"10.1146\/annurev.mi.41.100187.001015"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_114","doi-asserted-by":"crossref","unstructured":"Opperdoes, F.R. and Szikora, J.-P. (2006). In silico prediction of the glycosomal enzymes of Leishmania major and trypanosomes. Mol. Biochem. Parasitol. 147: 193\u2013206, https:\/\/doi.org\/10.1016\/j.molbiopara.2006.02.010.","DOI":"10.1016\/j.molbiopara.2006.02.010"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_115","doi-asserted-by":"crossref","unstructured":"Ott, J., Sehr, J., Lindemann, C., Barkovits, K., Bader, V., Winklhofer, K., Marcus, K., Schliebs, W., and Erdmann, R. (2022). Peroxisomal ATPase ATAD1 acts in quality control of the protein import machinery. bioRxiv, https:\/\/doi.org\/10.1101\/2025.10.14.682039.","DOI":"10.1101\/2022.04.22.489171"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_116","doi-asserted-by":"crossref","unstructured":"Pedra-Rezende, Y., Bomba\u00e7a, A.C.S., and Menna-Barreto, R.F.S. (2022). Is the mitochondrion a promising drug target in trypanosomatids? Mem. Inst. Oswaldo Cruz 117: e210379, https:\/\/doi.org\/10.1590\/0074-02760210379.","DOI":"10.1590\/0074-02760210379"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_117","doi-asserted-by":"crossref","unstructured":"Penha, L.L., Sant\u2019Anna, C.B., Mendon\u00e7a-Previato, L., Cunha-e-Silva, N.L., Previato, J.O., and Lima, A.P.C.A. (2009). Sorting of phosphoglucomutase to glycosomes in Trypanosoma cruzi is mediated by an internal domain. Glycobiology 19: 1462\u20131472, https:\/\/doi.org\/10.1093\/glycob\/cwp121.","DOI":"10.1093\/glycob\/cwp121"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_118","doi-asserted-by":"crossref","unstructured":"Petriv, O.I., Tang, L., Titorenko, V.I., and Rachubinski, R.A. (2004). A new definition for the consensus sequence of the peroxisome targeting signal type 2. J.\u00a0Mol. Biol. 341: 119\u2013134, https:\/\/doi.org\/10.1016\/j.jmb.2004.05.064.","DOI":"10.1016\/j.jmb.2004.05.064"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_119","doi-asserted-by":"crossref","unstructured":"Phan, T.-N., Park, K.-H.P., Shum, D., and No, J.H. (2024). Identification of Leishmania donovani PEX5-PTS1 interaction inhibitors through fluorescence polarization-based high-throughput screening. Molecules 29, https:\/\/doi.org\/10.3390\/molecules29081835.","DOI":"10.3390\/molecules29081835"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_120","doi-asserted-by":"crossref","unstructured":"Pilar, A.V.C., Madrid, K.P., and Jardim, A. (2008). Interaction of Leishmania PTS2 receptor peroxin 7 with the glycosomal protein import machinery. Mol. Biochem. Parasitol. 158: 72\u201381, https:\/\/doi.org\/10.1016\/j.molbiopara.2007.11.013.","DOI":"10.1016\/j.molbiopara.2007.11.013"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_121","doi-asserted-by":"crossref","unstructured":"Pilar, A.V.C., Strasser, R., McLean, J., Quinn, E., Cyr, N., Hojjat, H., Kottarampatel, A.H., and Jardim, A. (2014). Analysis of the Leishmania peroxin 7 interactions with peroxin 5, peroxin 14 and PTS2 ligands. Biochem. J. 460: 273\u2013282, https:\/\/doi.org\/10.1042\/bj20131628.","DOI":"10.1042\/BJ20131628"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_122","doi-asserted-by":"crossref","unstructured":"Platta, H.W., Girzalsky, W., and Erdmann, R. (2004). Ubiquitination of the peroxisomal import receptor Pex5p. Biochem. J. 384: 37\u201345, https:\/\/doi.org\/10.1042\/bj20040572.","DOI":"10.1042\/BJ20040572"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_123","doi-asserted-by":"crossref","unstructured":"Platta, H.W., Grunau, S., Rosenkranz, K., Girzalsky, W., and Erdmann, R. (2005). Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nat. Cell Biol. 7: 817\u2013822, https:\/\/doi.org\/10.1038\/ncb1281.","DOI":"10.1038\/ncb1281"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_124","doi-asserted-by":"crossref","unstructured":"Ravanelli, S., Brave, F.den, and Hoppe, T. (2020). Mitochondrial quality control governed by ubiquitin. Front. Cell Dev. Biol. 8: 270, https:\/\/doi.org\/10.3389\/fcell.2020.00270.","DOI":"10.3389\/fcell.2020.00270"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_125","doi-asserted-by":"crossref","unstructured":"Ravindran, R., Bacellar, I.O.L., Castellanos-Girouard, X., Wahba, H.M., Zhang, Z., Omichinski, J.G., Kisley, L., and Michnick, S.W. (2023). Peroxisome biogenesis initiated by protein phase separation. Nature 617: 608\u2013615, https:\/\/doi.org\/10.1038\/s41586-023-06044-1.","DOI":"10.1038\/s41586-023-06044-1"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_126","doi-asserted-by":"crossref","unstructured":"Rodrigues, T.A., Alencastre, I.S., Francisco, T., Brites, P., Fransen, M., Grou, C.P., and Azevedo, J.E. (2014). A PEX7-centered perspective on the peroxisomal targeting signal type 2-mediated protein import pathway. Mol. Cell. Biol. 34: 2917\u20132928, https:\/\/doi.org\/10.1128\/mcb.01727-13.","DOI":"10.1128\/MCB.01727-13"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_127","doi-asserted-by":"crossref","unstructured":"Romano, P.S., Akematsu, T., Besteiro, S., Bindschedler, A., Carruthers, V.B., Chahine, Z., Coppens, I., Descoteaux, A., Alberto Duque, T.L., He, C.Y., et al.. (2023). Autophagy in protists and their hosts: when, how and why? Autophagy Rep 2, https:\/\/doi.org\/10.1080\/27694127.2022.2149211.","DOI":"10.1080\/27694127.2022.2149211"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_128","doi-asserted-by":"crossref","unstructured":"Rottensteiner, H., Kramer, A., Lorenzen, S., Stein, K., Landgraf, C., Volkmer-Engert, R., and Erdmann, R. (2004). Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Mol. Biol. Cell 15: 3406\u20133417, https:\/\/doi.org\/10.1091\/mbc.e04-03-0188.","DOI":"10.1091\/mbc.e04-03-0188"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_129","doi-asserted-by":"crossref","unstructured":"Ruckt\u00e4schel, R., Thoms, S., Sidorovitch, V., Halbach, A., Pechlivanis, M., Volkmer, R., Alexandrov, K., Kuhlmann, J., Rottensteiner, H., and Erdmann, R. (2009). Farnesylation of pex19p is required for its structural integrity and function in peroxisome biogenesis. J.\u00a0Biol. Chem. 284: 20885\u201320896, https:\/\/doi.org\/10.1074\/jbc.m109.016584.","DOI":"10.1074\/jbc.M109.016584"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_130","doi-asserted-by":"crossref","unstructured":"R\u00fcttermann, M., Koci, M., Lill, P., Geladas, E.D., Kaschani, F., Klink, B.U., Erdmann, R., and Gatsogiannis, C. (2023). Structure of the peroxisomal Pex1\/Pex6 ATPase complex bound to a substrate. Nat. Commun. 14: 5942, https:\/\/doi.org\/10.1038\/s41467-023-41640-9.","DOI":"10.1038\/s41467-023-41640-9"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_131","doi-asserted-by":"crossref","unstructured":"Sampathkumar, P., Roach, C., Michels, P.A.M., and Hol, W.G.J. (2008). Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5. J.\u00a0Mol. Biol. 381: 867\u2013880, https:\/\/doi.org\/10.1016\/j.jmb.2008.05.089.","DOI":"10.1016\/j.jmb.2008.05.089"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_132","doi-asserted-by":"crossref","unstructured":"Saveria, T., Halbach, A., Erdmann, R., Volkmer-Engert, R., Landgraf, C., Rottensteiner, H., and Parsons, M. (2007a). Conservation of PEX19-binding motifs required for protein targeting to mammalian peroxisomal and trypanosome glycosomal membranes. Eukaryot. Cell 6: 1439\u20131449, https:\/\/doi.org\/10.1128\/ec.00084-07.","DOI":"10.1128\/EC.00084-07"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_133","doi-asserted-by":"crossref","unstructured":"Saveria, T., Kessler, P., Jensen, B.C., and Parsons, M. (2007b). Characterization of glycosomal RING finger proteins of trypanosomatids. Exp. Parasitol. 116: 14\u201324, https:\/\/doi.org\/10.1016\/j.exppara.2006.11.004.","DOI":"10.1016\/j.exppara.2006.11.004"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_134","doi-asserted-by":"crossref","unstructured":"Schueller, N., Holton, S.J., Fodor, K., Milewski, M., Konarev, P., Stanley, W.A., Wolf, J., Erdmann, R., Schliebs, W., Song, Y.-H., et al.. (2010). The peroxisomal receptor Pex19p forms a helical mPTS recognition domain. EMBO J. 29: 2491\u20132500, https:\/\/doi.org\/10.1038\/emboj.2010.115.","DOI":"10.1038\/emboj.2010.115"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_135","doi-asserted-by":"crossref","unstructured":"Shakya, A.K. and Pratap, J.V. (2020). The coiled-coil domain of glycosomal membrane-associated Leishmania donovani PEX14: cloning, overexpression, purification and preliminary crystallographic analysis. Acta Cryst 76: 464\u2013468, https:\/\/doi.org\/10.1107\/s2053230x20011127.","DOI":"10.1107\/S2053230X20011127"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_136","doi-asserted-by":"crossref","unstructured":"Shpilka, T., Weidberg, H., Pietrokovski, S., and Elazar, Z. (2011). Atg8: an autophagy-related ubiquitin-like protein family. Genome Biol. 12: 226, https:\/\/doi.org\/10.1186\/gb-2011-12-7-226.","DOI":"10.1186\/gb-2011-12-7-226"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_137","doi-asserted-by":"crossref","unstructured":"Singh, T., Hayashi, M., Mano, S., Arai, Y., Goto, S., and Nishimura, M. (2009). Molecular components required for the targeting of PEX7 to peroxisomes in Arabidopsis thaliana. Plant J. 60: 488\u2013498, https:\/\/doi.org\/10.1111\/j.1365-313x.2009.03970.x.","DOI":"10.1111\/j.1365-313X.2009.03970.x"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_138","doi-asserted-by":"crossref","unstructured":"Singh, R., Manivannan, S., Krikken, A.M., Boer, R.de, Bordin, N., Devos, D.P., and van der Klei, I.J. (2020). Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation. FEBS J. 287: 1742\u20131757, https:\/\/doi.org\/10.1111\/febs.15123.","DOI":"10.1111\/febs.15123"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_139","doi-asserted-by":"crossref","unstructured":"Skowyra, M.L., Feng, P., and Rapoport, T.A. (2024). Towards solving the mystery of peroxisomal matrix protein import. Trends Cell Biol. 34: 388\u2013405, https:\/\/doi.org\/10.1016\/j.tcb.2023.08.005.","DOI":"10.1016\/j.tcb.2023.08.005"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_140","doi-asserted-by":"crossref","unstructured":"Skowyra, M.L. and Rapoport, T.A. (2025). Import mechanism of peroxisomal proteins with an N-terminal signal sequence. Nat. Cell Biol. 27: 948\u2013958, https:\/\/doi.org\/10.1038\/s41556-025-01662-5.","DOI":"10.1038\/s41556-025-01662-5"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_141","doi-asserted-by":"crossref","unstructured":"Steverding, D. (2017). Sleeping sickness and Nagana disease caused by Trypanosoma brucei. In: Marcondes, C.B. (Ed.). Arthropod borne diseases. Springer International Publishing, Cham, pp.\u00a0277\u2013297.","DOI":"10.1007\/978-3-319-13884-8_18"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_142","doi-asserted-by":"crossref","unstructured":"Swett, M.C., Rayes, D.L., Campos, S.V., and Kumar, R.N. (2024). Chagas disease: epidemiology, diagnosis, and treatment. Curr. Cardiol. Rep. 26: 1105\u20131112, https:\/\/doi.org\/10.1007\/s11886-024-02113-7.","DOI":"10.1007\/s11886-024-02113-7"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_143","doi-asserted-by":"crossref","unstructured":"Sz\u00f6\u00f6r, B., Haanstra, J.R., Gualdr\u00f3n-L\u00f3pez, M., and Michels, P.A.M. (2014). Evolution, dynamics and specialized functions of glycosomes in metabolism and development of trypanosomatids. Curr. Opin. Microbiol. 22: 79\u201387, https:\/\/doi.org\/10.1016\/j.mib.2014.09.006.","DOI":"10.1016\/j.mib.2014.09.006"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_144","doi-asserted-by":"crossref","unstructured":"Tamura, S., Yasutake, S., Matsumoto, N., and Fujiki, Y. (2006). Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p. J.\u00a0Biol. Chem. 281: 27693\u201327704, https:\/\/doi.org\/10.1074\/jbc.m605159200.","DOI":"10.1074\/jbc.M605159200"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_145","doi-asserted-by":"crossref","unstructured":"Theodoulou, F.L., Bernhardt, K., Linka, N., and Baker, A. (2013). Peroxisome membrane proteins: multiple trafficking routes and multiple functions? Biochem. J. 451: 345\u2013352, https:\/\/doi.org\/10.1042\/bj20130078.","DOI":"10.1042\/BJ20130078"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_146","doi-asserted-by":"crossref","unstructured":"Urbina, J.A. and Crespo, A. (1984). Regulation of energy metabolism in Trypanosoma (Schizotrypanum) cruzi epimastigotes. I. Hexokinase and phosphofructokinase. Mol. Biochem. Parasitol. 11: 225\u2013239, https:\/\/doi.org\/10.1016\/0166-6851(84)90068-9.","DOI":"10.1016\/0166-6851(84)90068-9"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_147","doi-asserted-by":"crossref","unstructured":"van Ael, E. and Fransen, M. (2006). Targeting signals in peroxisomal membrane proteins. Biochim. Biophys. Acta 1763: 1629\u20131638, https:\/\/doi.org\/10.1016\/j.bbamcr.2006.08.020.","DOI":"10.1016\/j.bbamcr.2006.08.020"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_148","doi-asserted-by":"crossref","unstructured":"Verplaetse, E., Gualdr\u00f3n-L\u00f3pez, M., Chevalier, N., and Michels, P.A.M. (2012). Studies on the organization of the docking complex involved in matrix protein import into glycosomes of Trypanosoma brucei. Biochem. Biophys. Res. Commun. 424: 781\u2013785, https:\/\/doi.org\/10.1016\/j.bbrc.2012.07.035.","DOI":"10.1016\/j.bbrc.2012.07.035"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_149","doi-asserted-by":"crossref","unstructured":"Verplaetse, E., Rigden, D.J., and Michels, P.A.M. (2009). Identification, characterization and essentiality of the unusual peroxin 13 from Trypanosoma brucei. Biochim. Biophys. Acta 1793: 516\u2013527, https:\/\/doi.org\/10.1016\/j.bbamcr.2008.12.020.","DOI":"10.1016\/j.bbamcr.2008.12.020"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_150","doi-asserted-by":"crossref","unstructured":"Vertommen, D., van Roy, J., Szikora, J.-P., Rider, M.H., Michels, P.A.M., and Opperdoes, F.R. (2008). Differential expression of glycosomal and mitochondrial proteins in the two major life-cycle stages of Trypanosoma brucei. Mol. Biochem. Parasitol. 158: 189\u2013201, https:\/\/doi.org\/10.1016\/j.molbiopara.2007.12.008.","DOI":"10.1016\/j.molbiopara.2007.12.008"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_151","doi-asserted-by":"crossref","unstructured":"Voncken, F., van Hellemond, J.J., Pfisterer, I., Maier, A., Hillmer, S., and Clayton, C. (2003). Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes. J.\u00a0Biol. Chem. 278: 35299\u201335310, https:\/\/doi.org\/10.1074\/jbc.m301811200.","DOI":"10.1074\/jbc.M301811200"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_152","doi-asserted-by":"crossref","unstructured":"Weller, S., Cajigas, I., Morrell, J., Obie, C., Steel, G., Gould, S.J., and Valle, D. (2005). Alternative splicing suggests extended function of PEX26 in peroxisome biogenesis. Am. J.\u00a0Hum. Genet. 76: 987\u20131007, https:\/\/doi.org\/10.1086\/430637.","DOI":"10.1086\/430637"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_153","doi-asserted-by":"crossref","unstructured":"Williams, R.A.M., Woods, K.L., Juliano, L., Mottram, J.C., and Coombs, G.H. (2009). Characterization of unusual families of ATG8-like proteins and ATG12 in the protozoan parasite Leishmania major. Autophagy 5: 159\u2013172, https:\/\/doi.org\/10.4161\/auto.5.2.7328.","DOI":"10.4161\/auto.5.2.7328"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_154","doi-asserted-by":"crossref","unstructured":"Wu, J., Lv, S., Xu, P., Yue, S., and Zhuang, M. (2025). PEX14 condensates recruit receptor and cargo pairs for peroxisomal protein import. Nat. Struct. Mol. Biol. 32: 1644\u20131656, https:\/\/doi.org\/10.1038\/s41594-025-01601-w.","DOI":"10.1038\/s41594-025-01601-w"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_155","doi-asserted-by":"crossref","unstructured":"Wyllie, S. and Fairlamb, A.H. (2011). Methylglyoxal metabolism in trypanosomes and leishmania. Semin. Cell. Dev. Biol. 22: 271\u2013277, https:\/\/doi.org\/10.1016\/j.semcdb.2011.02.001.","DOI":"10.1016\/j.semcdb.2011.02.001"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_156","doi-asserted-by":"crossref","unstructured":"Yernaux, C., Fransen, M., Brees, C., Lorenzen, S., and Michels, P.A.M. (2006). Trypanosoma brucei glycosomal ABC transporters: identification and membrane targeting. Mol. Membr. Biol. 23: 157\u2013172, https:\/\/doi.org\/10.1080\/09687860500460124.","DOI":"10.1080\/09687860500460124"},{"key":"2026010906004188945_j_hsz-2025-0183_ref_157","doi-asserted-by":"crossref","unstructured":"Yusuf, I.F., Jeziorek, T., Droste, A., Girzalsky, W., and Erdmann, R. (2025). Role of AAA-ATPase Cdc48p in peroxisomal quality control. Cell Rep 44: 116405, https:\/\/doi.org\/10.1016\/j.celrep.2025.116405.","DOI":"10.1016\/j.celrep.2025.116405"}],"container-title":["Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/hsz-2025-0183\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/hsz-2025-0183\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T06:01:29Z","timestamp":1767938489000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/hsz-2025-0183\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,1]]},"references-count":157,"journal-issue":{"issue":"10-12","published-online":{"date-parts":[[2026,1,1]]},"published-print":{"date-parts":[[2025,12,17]]}},"alternative-id":["10.1515\/hsz-2025-0183"],"URL":"https:\/\/doi.org\/10.1515\/hsz-2025-0183","relation":{},"ISSN":["1431-6730","1437-4315"],"issn-type":[{"value":"1431-6730","type":"print"},{"value":"1437-4315","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,12,1]]}}}