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Mitochondrial Alterations Caused by Defective Peroxisomal Biogenesis in a Mouse Model for Zellweger Syndrome (PEX5 Knockout Mouse)
Open accessAbstract
Zellweger syndrome (cerebro-hepato-renal syndrome) is the most severe form of the peroxisomal biogenesis disorders leading to early death of the affected children. To study the pathogenetic mechanisms causing organ dysfunctions in Zellweger syndrome, we have recently developed a knockout-mouse model by disrupting the PEX5 gene, encoding the targeting receptor for most peroxisomal matrix proteins (M Baes, P Gressens, E Baumgart, P Carmeliet, M Casteels, M Fransen, P Evrard, D Fahimi, PE Declercq, D Collen, PP van Veldhoven, GP Mannaerts: A mouse model for Zellweger syndrome. Nat Genet 1997, 17:49-57). In this study, we present evidence that the absence of functional peroxisomes, causing a general defect in peroxisomal metabolism, leads to proliferation of pleomorphic mitochondria with severe alterations of the mitochondrial ultrastructure, changes in the expression and activities of mitochondrial respiratory chain complexes, and an increase in the heterogeneity of the mitochondrial compartment in various organs and specific cell types (eg, liver, proximal tubules of the kidney, adrenal cortex, heart, skeletal and smooth muscle cells, neutrophils). The changes of mitochondrial respiratory chain enzymes are accompanied by a marked increase of mitochondrial manganese-superoxide dismutase, as revealed by in situ hybridization and immunocytochemistry, suggesting increased production of reactive oxygen species in altered mitochondria. This increased oxidative stress induced probably by defective peroxisomal antioxidant mechanisms combined with accumulation of lipid intermediates of peroxisomal beta-oxidation system could contribute significantly to the pathogenesis of multiple organ dysfunctions in Zellweger syndrome.
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Cites
(1975) · Journal of AOAC INTERNATIONAL · doi:10.1093/jaoac/58.5.1085 · Cited by 20,078
Ashburner, M. (1989) · Cold Spring Harbor Laboratory eBooks · Cited by 6,756
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
(1985) · International Journal of Biochemistry · doi:10.1016/0020-711x(85)90098-9 · Cited by 3,494
Peroxisomes (microbodies and related particles).
De Duve, C., & Baudhuin, P. (1966) · Physiological Reviews · doi:10.1152/physrev.1966.46.2.323 · Cited by 1,666
Onset of Maternal Arterial Blood Flow and Placental Oxidative Stress
Jauniaux, E., Watson, A. L., Hempstock, J., Bao, Y.-P., Skepper, J. N., & Burton, G. J. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64849-3 · Cited by 1,057
Seligman, A. M., Karnovsky, M. J., Wasserkrug, H. L., & Hanker, J. S. (1968) · The Journal of Cell Biology · doi:10.1083/jcb.38.1.1 · Cited by 883
Reddy, J. K., Lalvvai, N. D., & Farber, E. (1983) · Critical Reviews in Toxicology · doi:10.3109/10408448309029317 · Cited by 879
Peroxisomal and Mitochondrial Defects in the Cerebro-Hepato-Renal Syndrome
Goldfischer, S. L., Moore, C. L., Johnson, T., Spiro, A. J., Valsamis, M. P., Wisniewski, H. K., Ritch, R. H., Norton, W. T., Rapin, I., & Gartner, L. M. (1973) · Science · doi:10.1126/science.182.4107.62 · Cited by 791
Leigh syndrome: Clinical features and biochemical and DNA abnormalities
Rahman, S., Blok, R. B., Dahl, H. ‐. M., Danks, D. M., Kirby, D. M., Chow, C. W., Christodoulou, J., & Thorburn, D. R. (1996) · Annals of Neurology · doi:10.1002/ana.410390311 · Cited by 776
Research works printed but not linked: 1
- Karnovsky, 1971, Use of ferrocyanide reduced osmium tetroxide in electron microscopy, J Cell Biol, 51, 146A
Cited by
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Sugiura, A., McLelland, G., Fon, E. A., & McBride, H. M. (2014) · The EMBO Journal · doi:10.15252/embj.201488104 · Cited by 862
Peroxisomes and oxidative stress
Schrader, M., & Fahimi, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.09.006 · Cited by 838
Self-citationRole of peroxisomes in ros/rns-metabolism: Implications for human disease
Fransen, M., Nordgren, M., Wang, B., & Apanasets, O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.001 · Cited by 644
Vanhorebeek, I., Vos, R. D., Mesotten, D., Wouters, P. J., Wolf‐Peeters, C. D., & den Berghe, G. V. (2005) · The Lancet · doi:10.1016/s0140-6736(04)17665-4 · Cited by 456
Self-citationThe Peroxisome-Mitochondria Connection: How and Why?
Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351
“, liver [57,113], proximal tubules of the kidney [109,113], adrenal cortex [113], spinal cord [111,112], heart [113], and brain [62]) and cell types (e.”
BackgroundReactive oxygen species and peroxisomes: Struggling for balance
Bonekamp, N. A., Völkl, A., Fahimi, H. D., & Schrader, M. (2009) · BioFactors · doi:10.1002/biof.48 · Cited by 279
Self-citationYoboue, E. D., Sitia, R., & Simmen, T. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0033-4 · Cited by 245
The ether lipid-deficient mouse: Tracking down plasmalogen functions
Gorgas, K., Teigler, A., Komljenovic, D., & Just, W. W. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.08.038 · Cited by 235
The physiological functions of human peroxisomes
Wanders, R. J. A., Baes, M., Ribeiro, D., Ferdinandusse, S., & Waterham, H. R. (2023) · Physiological Reviews · doi:10.1152/physrev.00051.2021 · Cited by 228
Self-citationPeroxisomes Are Oxidative Organelles
Antonenkov, V. D., Grunau, S., Ohlmeier, S., & Hiltunen, J. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2996 · Cited by 237
Peroxisomal disorders I: biochemistry and genetics of peroxisome biogenesis disorders
Wanders, R. J. A., & Waterham, H. R. (2004) · Clinical Genetics · doi:10.1111/j.1399-0004.2004.00329.x · Cited by 220
Peroxisome‐mitochondria interplay and disease
Schrader, M., Costello, J. L., Godinho, L. F., & Islinger, M. (2015) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-015-9819-7 · Cited by 232
Redox interplay between mitochondria and peroxisomes
Lismont, C., Nordgren, M., Van Veldhoven, P. P., & Fransen, M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00035 · Cited by 214
Peroxisome Biogenesis Disorders
Grønborg, S. W., Gould, S. J., & Valle, D. L. (2003) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.4.070802.110424 · Cited by 204
Hypoxia signaling pathways: modulators of oxygen-related organelles
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Peroxisomal metabolism and oxidative stress
Nordgren, M., & Fransen, M. (2013) · Biochimie · doi:10.1016/j.biochi.2013.07.026 · Cited by 201
van Zutphen, T., Čiapaitė, J., Bloks, V. W., Ackereley, C., Gerding, A., Jurdzinski, A., de Moraes, R. A., Zhang, L., Wolters, J. C., Bischoff, R., et al. (2016) · Journal of Hepatology · doi:10.1016/j.jhep.2016.05.046 · Cited by 190
Hein, S., Schonfeld, P., Kahlert, S., & Reiser, G. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn066 · Cited by 180
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Self-citationPlasmalogens and Chronic Inflammatory Diseases
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Absence of peroxisomes in mouse hepatocytes causes mitochondrial and ER abnormalities†
Dirkx, R., Vanhorebeek, I., Martens, K., Schad, A., Grabenbauer, M., Fahimi, D., Declercq, P., Van Veldhoven, P. P., & Baes, M. (2005) · Hepatology · doi:10.1002/hep.20628 · Cited by 174
Self-citationCatalase Deficiency Accelerates Diabetic Renal Injury Through Peroxisomal Dysfunction
Hwang, I., Lee, J., Huh, J. Y., Park, J., Lee, H. B., Ho, Y.-S., & Ha, H. (2012) · Diabetes · doi:10.2337/db11-0584 · Cited by 173
Dynamin‐related proteins and Pex11 proteins in peroxisome division and proliferation
Thoms, S., & Erdmann, R. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04939.x · Cited by 172
PEX11β Deficiency Is Lethal and Impairs Neuronal Migration but Does Not Abrogate Peroxisome Function
Li, X., Baumgart, E., Morrell, J. C., Jimenez-Sanchez, G., Valle, D., & Gould, S. J. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4358-4365.2002 · Cited by 165
Park, H.-S., Jang, J. E., Ko, M. S., Woo, S. H., Kim, B. J., Kim, H. S., Park, H. S., Park, I.-S., Koh, E. H., & Lee, K. (2016) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2016.40.5.376 · Cited by 161
Stępień, K. M., Heaton, R. A., Rankin, S., Murphy, A., Bentley, J., Sexton, D. W., & Hargreaves, I. P. (2017) · Journal of Clinical Medicine · doi:10.3390/jcm6070071 · Cited by 153
NFATc3 and NFATc4 Are Required for Cardiac Development and Mitochondrial Function
Bushdid, P. B., Osińska, H. E., Waclaw, R. R., Molkentin, J. D., & Yutzey, K. E. (2003) · Circulation Research · doi:10.1161/01.res.0000077045.84609.9f · Cited by 151
Galluzzi, L., Berghe, T. V., Vanlangenakker, N., Büttner, S., Eisenberg, T., Vandenabeele, P., Madeo, F., & Kroemer, G. (2011) · International review of cytology · doi:10.1016/b978-0-12-386039-2.00001-8 · Cited by 152
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Peroxisome quality control and dysregulated lipid metabolism in neurodegenerative diseases
Jo, D. S., Park, N. Y., & Cho, D. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00503-9 · Cited by 143
Eisenberg, T., Carmona‐Gutiérrez, D., Büttner, S., Tavernarakis, N., & Madeo, F. (2010) · APOPTOSIS · doi:10.1007/s10495-009-0453-4 · Cited by 141
Mitochondria and peroxisomes: Are the ‘Big Brother’ and the ‘Little Sister’ closer than assumed?
Schrader, M., & Yoon, Y. (2007) · BioEssays · doi:10.1002/bies.20659 · Cited by 136
Bile acids: the role of peroxisomes
Ferdinandusse, S., Denis, S. W., Faust, P. L., & Wanders, R. J. A. (2009) · Journal of Lipid Research · doi:10.1194/jlr.r900009-jlr200 · Cited by 137
Adreno-leukodystrophy: Oxidative Stress of Mice and Men
Powers, J. M., Pei, Z., Heinzer, A. K., Brose, R. D., Moser, A. B., Moser, H. W., Watkins, P. A., & Smith, K. D. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000190064.28559.a4 · Cited by 129
Bakovic, M., Fullerton, M. D., & Michel, V. (2007) · Biochemistry and Cell Biology · doi:10.1139/o07-006 · Cited by 129
López-Erauskin, J., Galino, J., Ruiz, M., Cuezva, J. M., Fabregat, I., Cacabelos, D., Boada, J., Martínez, J., Ferrer, I., Pamplona, R., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt186 · Cited by 125
Effects of peroxisomal catalase inhibition on mitochondrial function
Walton, P. A. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00108 · Cited by 114
Maxwell, M., Bjorkman, J., Nguyen, T., Sharp, P., Finnie, J., Paterson, C., Tonks, I., Paton, B. C., Kay, G. F., & Crane, D. I. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5947-5957.2003 · Cited by 110
Yano, T., Oku, M., Akeyama, N., Itoyama, A., Yurimoto, H., Kuge, S., Fujiki, Y., & Sakai, Y. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00121-10 · Cited by 117
Metherel, A. H., & Bazinet, R. P. (2019) · Progress in Lipid Research · doi:10.1016/j.plipres.2019.101008 · Cited by 112
Cholesterol biosynthesis and ER stress in peroxisome deficiency
Faust, P. L., & Kovacs, W. J. (2014) · Biochimie · doi:10.1016/j.biochi.2013.10.019 · Cited by 107
Ferrer, I., Kapfhammer, J. P., Hindelang, C., Kemp, S., Troffer-Charlier, N., Broccoli, V., Callyzot, N., Mooyer, P., Selhorst, J., Vreken, P., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi384 · Cited by 106
Progeric Effects of Catalase Inactivation in Human Cells
Koepke, J. I., Wood, C. S., Terlecky, L. J., Walton, P. A., & Terlecky, S. R. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.06.004 · Cited by 101
Peroxisomes and cancer: The role of a metabolic specialist in a disease of aberrant metabolism
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Paintlia, M. K., Paintlia, A. S., Contreras, M. A., Singh, I., & Singh, A. K. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2007.12.011 · Cited by 93
Organelle dynamics and dysfunction: A closer link between peroxisomes and mitochondria
Camões, F., Bonekamp, N. A., Delille, H. K., & Schrader, M. (2008) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-008-1018-3 · Cited by 93
Respiratory chain enzyme analysis in muscle and liver
Thorburn, D. R., Chow, C. W., & Kirby, D. M. (2004) · Mitochondrion · doi:10.1016/j.mito.2004.07.003 · Cited by 91
Krysko, O., Hulshagen, L., Janssen, A., Schütz, G., Klein, R., De Bruycker, M., Espeel, M., Gressens, P., & Baes, M. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21097 · Cited by 90
Self-citationGalino, J., Ruíz, M., Fourcade, S., Schlüter, A., López‐Erauskin, J., Guilera, C., Jové, M., Naudí, A., García‐Arumí, E., Andreu, A. L., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3877 · Cited by 85
Ahlemeyer, B., & Baumgart‐Vogt, E. (2005) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2005.05.022 · Cited by 82
Peroxisomes control mitochondrial dynamics and the mitochondrion-dependent apoptosis pathway
Tanaka, H., Okazaki, T., Aoyama-Ishiwatari, S., Yokota, M., Koike, M., Okada, Y., Fujiki, Y., & Gotoh, Y. (2019) · Journal of Cell Science · doi:10.1242/jcs.224766 · Cited by 84
Maintaining social contacts: The physiological relevance of organelle interactions
Silva, B. S. C., DiGiovanni, L. F., Kumar, R., Carmichael, R. E., Kim, P. K., & Schrader, M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118800 · Cited by 84
Redox Signaling from and to Peroxisomes: Progress, Challenges, and Prospects
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Peeters, A., Shinde, A. B., Dirkx, R., Smet, J., Bock, K. D., Espeel, M., Vanhorebeek, I., Vanlander, A. V., Coster, R. V., Carmeliet, P., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.11.017 · Cited by 85
Self-citationZarrouk, A., Véjux, A., Nury, T., Hajj, H. I. E., Haddad, M., Cherkaoui‐Malki, M., Riedinger, J., Hammami, M., & Lizard, G. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/623257 · Cited by 94
Debbabi, M., Nury, T., Zarrouk, A., Mekahli, N., Bezine, M., Sghaier, R., Gregoire, S., Martine, L., Durand, P., Prost-Camus, E., et al. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17121973 · Cited by 86
Peroxisome Interactions and Cross-Talk with Other Subcellular Compartments in Animal Cells
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Self-citationEmerging roles of mitochondria in the evolution, biogenesis, and function of peroxisomes
Mohanty, A., & McBride, H. M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00268 · Cited by 76
Fourcade, S., Ferrer, I., & Pujol, A. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.041 · Cited by 80
Zellweger syndrome and secondary mitochondrial myopathy
Salpietro, V., Phadke, R., Saggar, A. K., Hargreaves, I. P., Yates, R., Fokoloros, C., Mankad, K., Hertecant, J., Ruggieri, M., McCormick, D., et al. (2014) · European Journal of Pediatrics · doi:10.1007/s00431-014-2431-2 · Cited by 74
Organelle interplay in peroxisomal disorders
Thoms, S., Grønborg, S. W., & Gärtner, J. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.05.002 · Cited by 74
Keane, M. H., Overmars, H., Wikander, T. M., Ferdinandusse, S., Duran, M., Wanders, R. J. A., & Faust, P. L. (2007) · Hepatology · doi:10.1002/hep.21532 · Cited by 68
Ahlemeyer, B., Neubert, I., Kovacs, W. J., & Baumgart‐Vogt, E. (2007) · Journal of Comparative Neurology · doi:10.1002/cne.21448 · Cited by 68
Vijayan, V., Tumpara, S., Karnati, S., Garikapati, V., Linke, M., Kamalyan, L., Mali, S. R., Sudan, K., Kollas, A., Schmid, T., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601596 · Cited by 67
Müller, C. C., Nguyen, T. H., Ahlemeyer, B., Meshram, M., Santrampurwala, N., Cao, S., Sharp, P. C., Fietz, P. B., Baumgart‐Vogt, E., & Crane, D. I. (2010) · Disease Models & Mechanisms · doi:10.1242/dmm.004622 · Cited by 67
Kovacs, W. J., Tape, K. N., Shackelford, J. E., Wikander, T. M., Richards, M. J., Fliesler, S. J., Krisans, S. K., & Faust, P. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m809064200 · Cited by 67
Mouse models for peroxisome biogenesis defects and β-oxidation enzyme deficiencies
Baes, M. I., & Veldhoven, P. P. V. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.03.003 · Cited by 70
Self-citationNeuronal migration depends on intact peroxisomal function in brain and in extraneuronal tissues
Janssen, A., Gressens, P., Grabenbauer, M., Baumgart, E., Schad, A., Vanhorebeek, I., Brouwers, A., Declercq, P. E., Fahimi, D., Evrard, P., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-30-09732.2003 · Cited by 65
Self-citationDisturbed Cholesterol Homeostasis in a Peroxisome-Deficient PEX2 Knockout Mouse Model
Kovacs, W. J., Shackelford, J. E., Tape, K. N., Richards, M. J., Faust, P. L., Fliesler, S. J., & Krisans, S. K. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.1-13.2004 · Cited by 63
Hepatic dysfunction in peroxisomal disorders
Baes, M. I., & Veldhoven, P. P. V. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.09.035 · Cited by 64
Self-citationBonnet, C., Espagne, E., Zickler, D., Boisnard, S., Bourdais, A., & Berteaux‐Lecellier, V. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05353.x · Cited by 61
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Macrophage peroxisomes guide alveolar regeneration and limit SARS-CoV-2 tissue sequelae
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Peroxisomal participation in psychosine-mediated toxicity: Implications for Krabbe's disease
Khan, M., Haq, E., Giri, S., Singh, I., & Singh, A. K. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20529 · Cited by 58
Ahlemeyer, B., Gottwald, M., & Baumgart‐Vogt, E. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.007708 · Cited by 57
Peroxisomes in cardiomyocytes and the peroxisome / peroxisome proliferator-activated receptor-loop
Colasante, C., Chen, J., Ahlemeyer, B., & Baumgart‐Vogt, E. (2015) · Thrombosis and Haemostasis · doi:10.1160/th14-06-0497 · Cited by 59
Kruska, N., Schönfeld, P., Pujol, A., & Reiser, G. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.01.005 · Cited by 56
Fourcade, S., López-Erauskin, J., Ruiz, M., Ferrer, I., & Pujol, A. (2014) · Biochimie · doi:10.1016/j.biochi.2013.09.012 · Cited by 55
Pomatto, L. C. D., Raynes, R., & Davies, K. J. A. (2016) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12253 · Cited by 55
Peroxisomes Are Required for Lipid Metabolism and Muscle Function in Drosophila melanogaster
Faust, J. E., Manisundaram, A. D., Ivanova, P. T., Milne, S. B., Summerville, J. B., Brown, H. A., Wangler, M. F., Stern, M., & McNew, J. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100213 · Cited by 54
Jia, Y., Qi, C., Zhang, Z., Hashimoto, T., Rao, M. S., Huyghe, S., Suzuki, Y., Veldhoven, P. P. V., Baes, M. I., & Reddy, J. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306363200 · Cited by 55
Self-citationMendelian neurodegenerative disease genes involved in autophagy
Stamatakou, E., Wróbel, L., Hill, S. M., Puri, C., Son, S. M., Fujimaki, M., Zhu, Y., Siddiqi, F. H., Fernandez-Estévez, M., Manni, M. M., et al. (2020) · Cell Discovery · doi:10.1038/s41421-020-0158-y · Cited by 52
Nury, T., Sghaier, R., Zarrouk, A., Ménétrier, F., Uzun, T., Leoni, V., Caccia, C., Meddeb, W., Namsi, A., Sassi, K., et al. (2018) · Biochimie · doi:10.1016/j.biochi.2018.07.009 · Cited by 54
Revisiting the neuropathogenesis of Zellweger syndrome
Crane, D. I. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.02.007 · Cited by 51
Systems biology analysis reveals role of MDM2 in diabetic nephropathy
Saito, R., Arjó, A. R., You, Y.-H., Darshi, M., Espen, B. V., Miyamoto, S., Pham, J., Pu, M., Romoli, S., Natarajan, L., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.87877 · Cited by 49
Huang, K., Miao, T., Chang, K., Kim, J., Kang, P., Jiang, Q., Simmonds, A. J., Cara, F. D., & Bai, H. (2020) · Nature Communications · doi:10.1038/s41467-020-16781-w · Cited by 53
Plasmalogen loss caused by remodeling deficiency in mitochondria
Kimura, T., Kimura, A. K., Ren, M., Monteiro, V., Xu, Y., Berno, B., Schlame, M., & Epand, R. M. (2019) · Life Science Alliance · doi:10.26508/lsa.201900348 · Cited by 49
Molecular insights into peroxisome homeostasis and peroxisome biogenesis disorders
Fujiki, Y., Okumoto, K., Honsho, M., & Abe, Y. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119330 · Cited by 47
Cichocki, B. A., Krumpe, K., Vitali, D. G., & Rapaport, D. (2018) · Traffic · doi:10.1111/tra.12604 · Cited by 47
Generalised and conditional inactivation of Pex genes in mice
Baes, M. I., & Veldhoven, P. P. V. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.08.018 · Cited by 45
Self-citationWu, M.-X., Zou, Y., Yu, Y., Chen, B., Zheng, Q., Ye, Z., Wei, T., Ye, S., Guo, L., & Lin, J. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110540 · Cited by 45
Ruiz, M., Cuillerier, A., Daneault, C., Deschênes, S., Frayne, I. R., Bouchard, B., Forest, A., Legault, J. T., Vaz, F. M., Rioux, J. D., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.123231 · Cited by 46
Baarine, M., Ragot, K., Athias, A., Nury, T., Kattan, Z., Genin, E. C., Andreoletti, P., Ménétrier, F., Riedinger, J.-M., Bardou, M., et al. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2011.10.007 · Cited by 43
Paintlia, M. K., Paintlia, A. S., Khan, M., Singh, I., & Singh, A. K. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05199.x · Cited by 41
α‐Synuclein abnormalities in mouse models of peroxisome biogenesis disorders
Yakunin, E., Moser, A. B., Loeb, V., Saada, A., Faust, P. L., Crane, D. I., Baes, M. I., & Sharon, R. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22246 · Cited by 39
Self-citation
Metadata
- Authors
- Baumgart, E., Vanhorebeek, I., Grabenbauer, M., Borgers, M., Declercq, P. E., Fahimi, H. D., & Baes, M.
- Affiliations
- KU Leuven (BE)
- Heidelberg University (DE)
- Janssen (Belgium) (BE)
- Corresponding author
- Fahimi, H. Dariush
- Venue
- The American Journal of Pathology
- Publisher
- Elsevier BV
- Published
- 2001-10
- Volume
- 159
- Issue
- 4
- Pages
- 1477-1494
- ISSN
- 0002-9440 (ISSN-L)
- PMC
- PMC1850512
- OpenAlex
- W2151833520
- Cited by
- 210
- References
- 95
- Citations by year
- 2026: 4 · 2025: 11 · 2024: 10 · 2023: 5 · 2022: 11 · 2021: 8 · 2020: 10 · 2019: 12 · 2018: 11 · 2017: 6 · 2016: 11 · 2015: 8 · 2014: 10 · 2013: 10 · 2012: 8
- FWCI
- 3.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- American Journal Of Pathology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (Ba 1155/1-4, SFB 601-B1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Zellweger syndrome, peroxisome biogenesis disorders, mitochondrial ultrastructure, respiratory chain complexes, manganese superoxide dismutase, reactive oxygen species, oxidative stress, peroxisomal beta-oxidation, lipid intermediates, organ dysfunction
- MeSH terms
- Peroxisome-Targeting Signal 1 Receptor, Adenosine Triphosphate, Animals, Autophagy, Blood Cells, Electron Transport Complex IV, Cytoplasm, Disease Models, Animal, Electron Transport, Mitochondria, Mitochondria, Heart, Mitochondria, Liver, NADH, NADPH Oxidoreductases, Oxidation-Reduction, Superoxide Dismutase, Tissue Distribution, Zellweger Syndrome, Reactive Oxygen Species, Receptors, Cytoplasmic and Nuclear, Mice, Knockout, Peroxisomes, Hepatocytes, Electron Transport Complex I, Mice
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