Lack of mitochondrial trifunctional protein in mice causes neonatal hypoglycemia and sudden death

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works

Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,240 · see citing works

Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues

Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311 · see citing works

Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction

Chomczyński, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90021-2 · Cited by 47,092 · see citing works

A Fetal Fatty-Acid Oxidation Disorder as a Cause of Liver Disease in Pregnant Women

Ibdah, J. A., Bennett, M. J., Rinaldo, P., Zhao, Y., Gibson, B., Sims, H. F., & Strauss, A. W. (1999) · New England Journal of Medicine · doi:10.1056/nejm199906033402204 · Cited by 489 · see citing works

Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein.

Uchida, Y., Izai, K., Orii, T., & Hashimoto, T. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48391-3 · Cited by 339 · see citing works

Recognition and management of fatty acid oxidation defects: A series of 107 patients

Saudubray, J., Martin, D., de Lonlay, P., Touati, G., Poggi-Travert, F., Bonnet, D., Jouvet, P. A., Boutron, M. C., Slama, A., Vianey‐Saban, C., et al. (1999) · Journal of Inherited Metabolic Disease · doi:10.1023/a:1005556207210 · Cited by 330 · see citing works

Arrhythmias and Conduction Defects as Presenting Symptoms of Fatty Acid Oxidation Disorders in Children

Bonnet, D., Martin, D., de Lonlay, P., Villain, E., Jouvet, P. A., Rabier, D., Brivet, M., & Saudubray, J. (1999) · Circulation · doi:10.1161/01.cir.100.22.2248 · Cited by 309 · see citing works

Disorders of mitochondrial fatty acyl‐CoA β‐oxidation

Wanders, R. J. A., Vreken, P., den Boer, M. E. J., Wijburg, F. A., Van Gennip, A. H., & IJlst, L. (1999) · Journal of Inherited Metabolic Disease · doi:10.1023/a:1005504223140 · Cited by 257 · see citing works

Targeted disruption of mouse long-chain acyl-CoA dehydrogenase gene reveals crucial roles for fatty acid oxidation

Kurtz, D. M., Rinaldo, P., Rhead, W. J., Tian, L., Millington, D. S., Vockley, J. E., Hamm, D. A., Brix, A. E., Lindsey, J. R., Pinkert, C. A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15592 · Cited by 248 · see citing works

The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy.

Sims, H. F., Brackett, J. C., Powell, C. K., Treem, W. R., Hale, D. E., Bennett, M. J., Gibson, B., Shapiro, S. D., & Strauss, A. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.841 · Cited by 222 · see citing works

Pregnancy and fetal long-chain 3-hydroxyacyl coenzyme A dehydrogenase deficiency

Wilcken, B., Leung, K.-C., Hammond, J., Wilcken, B., Kamath, R., & Leonard, J. V. (1993) · The Lancet · doi:10.1016/0140-6736(93)92993-4 · Cited by 214 · see citing works

Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein alpha subunit gene.

IJlst, L., Ruiter, J. P. N., Hoovers, J. M. N., Jakobs, M. E., & Wanders, R. J. A. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118863 · Cited by 163 · see citing works

Human trifunctional protein deficiency: A new disorder of mitochondrial fatty acid β-oridation

Wanders, R. J. A., IJlst, L., Poggi, F., Bonnefont, J., Münnich, A., Brivet, M., Rabier, D., & Saudubray, J. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91350-y · Cited by 152 · see citing works

Pregnancy complications are frequent in long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency

Tyni, T. A., Ekholm, E. M. K., & Pihko, H. S. (1998) · American Journal of Obstetrics and Gynecology · doi:10.1016/s0002-9378(98)70446-6 · Cited by 138 · see citing works

SUDDEN INFANT DEATH AND LONG-CHAIN 3-HYDROXYACYL-CoA DEHYDROGENASE

Wanders, R. J. A., Durán, M., IJlst, L., de Jager, J. P., Gennip, A. H., Jakobs, C., DORLAND, L., & van Sprang, F. J. (1989) · The Lancet · doi:10.1016/s0140-6736(89)90300-0 · Cited by 130 · see citing works

Combined enzyme defect of mitochondrial fatty acid oxidation.

Jackson, S., Kler, R. S., Bartlett, K., Briggs, H. L., Bindoff, L. A., Pourfarzam, M., Gardner‐Medwin, D., & Turnbull, D. M. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115983 · Cited by 127 · see citing works

Liver Disease in Pregnancy and Fetal Fatty Acid Oxidation Defects

Ibdah, J. A., Yang, Z. F., & Bennett, M. J. (2000) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2000.3065 · Cited by 113 · see citing works

Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits.

Ushikubo, S., Aoyama, T., Kamijo, T., Wanders, R. J. A., Rinaldo, P., Vockley, J. E., & Hashimoto, T. (1996) · PubMed Central · Cited by 104 · see citing works

Structural Analysis of cDNAs for Subunits of Human Mitochondrial Fatty Acid β-Oxidation Trifunctional Protein

Kamijo, T., Aoyama, T., Komiyama, A., & Hashimoto, T. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1302 · Cited by 98 · see citing works

Two alpha subunit donor splice site mutations cause human trifunctional protein deficiency.

Brackett, J. C., Sims, H. F., Rinaldo, P., Shapiro, S., Powell, C. K., Bennett, M. J., & Strauss, A. W. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117894 · Cited by 95 · see citing works

Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients.

Kamijo, T., Wanders, R. J. A., Saudubray, J., Aoyama, T., Komiyama, A., & Hashimoto, T. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117158 · Cited by 80 · see citing works

Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation.

Ibdah, J. A., Tein, I., Dionisi‐Vici, C., Bennett, M. J., IJlst, L., Gibson, B., Wanders, R. J. A., & Strauss, A. W. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2091 · Cited by 77 · see citing works

Biochemical diagnosis of fatty acid oxidation disorders by metabolite analysis of postmortem liver

Boles, R. G., Martin, S. K., Blitzer, M. G., & Rinaldo, P. (1994) · Human Pathology · doi:10.1016/0046-8177(94)90240-2 · Cited by 57 · see citing works

Long‐chain 3‐hydroxyacyl‐CoA dehydrogenase deficiency: Variable expressivity of maternal illness during pregnancy and unusual presentation with infantile cholestasis and hypocalcaemia

Ibdah, J. A., Dasouki, M., & Strauss, A. W. (1999) · Journal of Inherited Metabolic Disease · doi:10.1023/a:1005506024055 · Cited by 41 · see citing works

Clinical and biochemical presentation of long‐chain 3‐hydroxyacyl‐CoA dehydrogenase deficiency

Hagenfeldt, L., Venizelos, N., & von Döbeln, U. (1995) · Journal of Inherited Metabolic Disease · doi:10.1007/bf00711779 · Cited by 38 · see citing works

[Mitochondrial trifunctional protein (TP) deficiency].

Uchiyama, A., & Yamaguchi, S. (1998) · PubMed · Cited by 19 · see citing works

A general introduction to the biochemistry of mitochondrial fatty acid β‐oxidation

Houten, S. M., & Wanders, R. J. A. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9061-2 · Cited by 1,020 · see citing works

The Biochemistry and Physiology of Mitochondrial Fatty Acid β-Oxidation and Its Genetic Disorders

Houten, S. M., Violante, S. N., Ventura, F. V., & Wanders, R. J. A. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105045 · Cited by 938 · see citing works

Lipotoxicity: when tissues overeat

Schaffer, J. E. (2003) · Current Opinion in Lipidology · doi:10.1097/00041433-200306000-00008 · Cited by 914 · see citing works

Mouse models in non‐alcoholic fatty liver disease and steatohepatitis research

Anstee, Q. M., & Goldin, R. D. (2006) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2006.00465.x · Cited by 714 · see citing works

Fatty Acid Oxidation Disorders

Rinaldo, P., Matern, D., & Bennett, M. J. (2002) · Annual Review of Physiology · doi:10.1146/annurev.physiol.64.082201.154705 · Cited by 483 · see citing works

Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways

Rardin, M. J., Newman, J. C., Held, J. M., Cusack, M. P., Sorensen, D. J., Li, B., Schilling, B., Mooney, S. D., Kahn, C. R., Verdin, E. M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302961110 · Cited by 446 · see citing works

Control of mitochondrial β-oxidation flux

Eaton, S. D. (2002) · Progress in Lipid Research · doi:10.1016/s0163-7827(01)00024-8 · Cited by 410 · see citing works

Expression of miR-33 from an SREBP2 Intron Inhibits Cholesterol Export and Fatty Acid Oxidation*

Gerin, I., Clerbaux, L.-A., Haumont, O., Lanthier, N., Das, A. K., Burant, C. F., Leclercq, I. A., MacDougald, O. A., & Bommer, G. T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.152090 · Cited by 382 · see citing works

Nonalcoholic fatty liver disease and mitochondrial dysfunction

Wei, Y., Rector, R. S., Thyfault, J. P., & Ibdah, J. A. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.193 · Cited by 370 · see citing works

Role of Mitochondria in Nonalcoholic Fatty Liver Disease

Nassir, F., & Ibdah, J. A. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15058713 · Cited by 359 · see citing works

PGC-1 Coactivators in Cardiac Development and Disease

Rowe, G. C., Jiang, A., & Arany, Z. P. (2010) · Circulation Research · doi:10.1161/circresaha.110.223818 · Cited by 355 · see citing works

Hepatic Steatosis in Leptin-Deficient Mice Is Promoted by the PPARγ Target Gene Fsp27

Matsusue, K., Kusakabe, T., Noguchi, T., Takiguchi, S., Suzuki, T., Yamano, S., & Gonzalez, F. J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.03.003 · Cited by 348 · see citing works

Mitochondrial deficiency and cardiac sudden death in mice lacking the MEF2A transcription factor

Naya, F. J., Black, B. L., Wu, H., Bassel‐Duby, R., Richardson, J. A., Hill, J. A., & Olson, E. N. (2002) · Nature Medicine · doi:10.1038/nm789 · Cited by 325 · see citing works

Peroxisome Proliferator–Activated Receptor γ Coactivator-1 (PGC-1) Regulatory Cascade in Cardiac Physiology and Disease

Finck, B. N., & Kelly, D. P. (2007) · Circulation · doi:10.1161/circulationaha.107.670588 · Cited by 281 · see citing works

MYC inhibition induces metabolic changes leading to accumulation of lipid droplets in tumor cells

Zirath, H., Frenzel, A., Oliynyk, G., Segerström, L., Westermark, U., Larsson, K., Persson, M. M., Hultenby, K. R., Lehtiö, J., Einvik, C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222404110 · Cited by 229 · see citing works

Mitochondrial dysfunction in fatty acid oxidation disorders: insights from human and animal studies

Wajner, M., & Amaral, A. U. (2015) · Bioscience Reports · doi:10.1042/bsr20150240 · Cited by 230 · see citing works

The PPAR regulatory system in cardiac physiology and disease

Finck, B. N. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.08.023 · Cited by 222 · see citing works

Maternal and fetal lipid metabolism under normal and gestational diabetic conditions

Herrera, E., & Desoyé, G. (2015) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2015-0025 · Cited by 202 · see citing works

Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors

Gispert, S., Parganlija, D., Klinkenberg, M., Dröse, S., Wittig, I., Mittelbronn, M. G. A., Grzmil, P., Koob, S., Hamann, A., Walter, M. J., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt338 · Cited by 188 · see citing works

Mice Heterozygous for a Defect in Mitochondrial Trifunctional Protein Develop Hepatic Steatosis and Insulin Resistance

Ibdah, J. A., Perlegas, P., Zhao, Y., Angdisen, J., Borgerink, H., Shadoan, M. K., Wagner, J. D., Matern, D., Rinaldo, P., & Cline, J. M. (2005) · Gastroenterology · doi:10.1053/j.gastro.2005.02.001 · Cited by 186 · see citing works

Autophagy and ubiquitin–proteasome system contribute to sperm mitophagy after mammalian fertilization

Song, W., Yi, Y., Sutovsky, M., Meyers, S. A., & Šutovský, P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605844113 · Cited by 178 · see citing works

Mitochondrial Dysfunction Plays Central Role in Nonalcoholic Fatty Liver Disease

Ramanathan, R., Ali, A. H., & Ibdah, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137280 · Cited by 179 · see citing works

Strategies, models and biomarkers in experimental non-alcoholic fatty liver disease research

Willebrords, J., Pereira, I. V. A., Maes, M., Yanguas, S. C., Colle, I. O., Bossche, B. V. D., da Silva, T. C., de Oliveira, C. P. M. S., Andraus, W., Alves, V. A. F., et al. (2015) · Progress in Lipid Research · doi:10.1016/j.plipres.2015.05.002 · Cited by 172 · see citing works

Human placenta metabolizes fatty acids: implications for fetal fatty acid oxidation disorders and maternal liver diseases

Shekhawat, P., Bennett, M. J., Sadovsky, Y., Nelson, D. M., Rakheja, D., & Strauss, A. W. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00481.2002 · Cited by 170 · see citing works

Carnitine homeostasis, mitochondrial function and cardiovascular disease

Sharma, S., & Black, S. M. (2009) · Drug Discovery Today Disease Mechanisms · doi:10.1016/j.ddmec.2009.02.001 · Cited by 164 · see citing works

TMAVA, a Metabolite of Intestinal Microbes, Is Increased in Plasma From Patients With Liver Steatosis, Inhibits γ-Butyrobetaine Hydroxylase, and Exacerbates Fatty Liver in Mice

Zhao, M., Zhao, L., Xiong, X., He, Y. M., Huang, W., Liu, Z., Liang, J., Pan, B., Guo, X., Wang, L., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.02.033 · Cited by 131 · see citing works

Methyl donor deficiency induces cardiomyopathy through altered methylation/acetylation of PGC‐1α by PRMT1 and SIRT1

Garcia, M. M., Guéant‐Rodriguez, R., Pooya, S., Brachet, P., Alberto, J., Jeannesson, É., Maskali, F., Guéguen, N., Marie, P., Lacolley, P. J., et al. (2011) · The Journal of Pathology · doi:10.1002/path.2881 · Cited by 127 · see citing works

Adipose tissue development and lipid metabolism in the human fetus: The 2020 perspective focusing on maternal diabetes and obesity

Desoyé, G., & Herrera, E. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101082 · Cited by 126 · see citing works

Mechanisms of Lipoapoptosis

Listenberger, L. L., & Schaffer, J. E. (2002) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(02)00152-4 · Cited by 123 · see citing works

Mitochondrial long chain fatty acid β-oxidation in man and mouse

Chegary, M., Brinke, H. T., Ruiter, J. P. N., Wijburg, F. A., Stoll, M. S. K., Minkler, P. E., van Weeghel, M., Schulz, H., Hoppel, C. L., Wanders, R. J. A., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.05.006 · Cited by 123 · see citing works

Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to ?-subunit mutations

Spiekerkoetter, U., Sun, B., Khuchua, Z. A., Bennett, M. J., & Strauss, A. W. (2003) · Human Mutation · doi:10.1002/humu.10211 · Cited by 118 · see citing works

TFPa/HADHA is required for fatty acid beta-oxidation and cardiolipin re-modeling in human cardiomyocytes

Miklas, J. W., Clark, E. C., Levy, S., Detraux, D., Leonard, A., Beussman, K. M., Showalter, M. R., Smith, A. S. T., Hofsteen, P., Yang, X., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12482-1 · Cited by 116 · see citing works

Gut microbiota production of trimethyl-5-aminovaleric acid reduces fatty acid oxidation and accelerates cardiac hypertrophy

Zhao, M., Wei, H., Li, C., Zhan, R., Liu, C., Gao, J., Yi, Y., Cui, X. B., Shan, W., Liang, J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29060-7 · Cited by 115 · see citing works

Diminished Hepatic Gluconeogenesis via Defects in Tricarboxylic Acid Cycle Flux in Peroxisome Proliferator-activated Receptor γ Coactivator-1α (PGC-1α)-deficient Mice

Burgess, S. C., Leone, T. C., Wende, A. R., Croce, M. A., Chen, Z., Sherry, A. D., Malloy, C. R., & Finck, B. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600050200 · Cited by 111 · see citing works

Fetal Fatty Acid Oxidation Disorders, Their Effect on Maternal Health and Neonatal Outcome: Impact of Expanded Newborn Screening on Their Diagnosis and Management

Shekhawat, P., Matern, D., & Strauss, A. W. (2005) · Pediatric Research · doi:10.1203/01.pdr.0000159631.63843.3e · Cited by 109 · see citing works

Understanding the impact of mitochondrial defects in cardiovascular disease: A review

Marı́n-Garcı́a, J., & Goldenthal, M. J. (2002) · Journal of Cardiac Failure · doi:10.1054/jcaf.2002.127774 · Cited by 109 · see citing works

Long-Chain Fatty Acid Oxidation during Early Human Development

Oey, N. A., den Boer, M. E. J., Wijburg, F. A., Vekemans, M. J. J., Augé, J., Steiner, C., Wanders, R. J. A., Waterham, H. R., Ruiter, J. P. N., & Attié‐Bitach, T. (2005) · Pediatric Research · doi:10.1203/01.pdr.0000161413.42874.74 · Cited by 98 · see citing works

CLUH regulates mitochondrial metabolism by controlling translation and decay of target mRNAs

Schatton, D., Pla‐Martín, D., Marx, M., Hansen, H., Mourier, A., Nemazanyy, I., Pessia, A., Zentis, P., Corona, T., Kondylis, V., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201607019 · Cited by 96 · see citing works

Mitochondrial trifunctional protein deficiency: A severe fatty acid oxidation disorder with cardiac and neurologic involvement

den Boer, M. E. J., Dionisi‐Vici, C., Chakrapani, A., van Thuijl, A. O. J., Wanders, R. J. A., & Wijburg, F. A. (2003) · The Journal of Pediatrics · doi:10.1067/mpd.2003.231 · Cited by 90 · see citing works

Transcriptional analysis of abdominal fat in genetically fat and lean chickens reveals adipokines, lipogenic genes and a link between hemostasis and leanness

Resnyk, C., Carré, W., Wang, X., Porter, T. E., Simon, J., Bihan-Duval, É. L., Duclos, M. J. M. J., Aggrey, S. E., & Cogburn, L. A. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-557 · Cited by 90 · see citing works

Myocardial recovery from ischemia is impaired in CD36-null mice and restored by myocyte CD36 expression or medium-chain fatty acids

Irie, H., Krukenkamp, I. B., Brinkmann, J. F. F., Gaudette, G. R., Saltman, A. E., Jou, W., Glatz, J. F. C., Abumrad, N. A., & Ibrahimi, A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1132094100 · Cited by 85 · see citing works

Fetal genotypes and pregnancy outcomes in 35 families with mitochondrial trifunctional protein mutations

Yang, Z., Zhao, Y., Bennett, M. J., Strauss, A. W., & Ibdah, J. A. (2002) · American Journal of Obstetrics and Gynecology · doi:10.1067/mob.2002.125893 · Cited by 83 · see citing works

Sexual Dimorphism in the Expression of Mitochondria-Related Genes in Rat Heart at Different Ages

Vijay, V., Han, T., Moland, C. L., Kwekel, J. C., Fuscoe, J. C., & Desai, V. G. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117047 · Cited by 80 · see citing works

Genetically modified mouse models for the study of nonalcoholic fatty liver disease

Nagarajan, P. (2012) · World Journal of Gastroenterology · doi:10.3748/wjg.v18.i11.1141 · Cited by 79 · see citing works

Acetylation of Mitochondrial Trifunctional Protein α-Subunit Enhances Its Stability To Promote Fatty Acid Oxidation and Is Decreased in Nonalcoholic Fatty Liver Disease

Guo, L., Zhou, S.-R., Wei, X.-B., Liu, Y., Chang, X., Liu, Y., Ge, X., Dou, X., Huang, H.-Y., Qian, S.-W., et al. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00227-16 · Cited by 78 · see citing works

The mitochondrial pyruvate carrier mediates high fat diet-induced increases in hepatic TCA cycle capacity

Rauckhorst, A. J., Gray, L. R., Sheldon, R. D., Fu, X., Pewa, A. D., Feddersen, C. R., Dupuy, A. J., Gibson-Corley, K. N., Cox, J. E., Burgess, S. C., et al. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.09.002 · Cited by 74 · see citing works

Rescue of enzyme deficiency in embryonic diaphragm in a mouse model of metabolic myopathy: Pompe disease

Rucker, M., Fraites, T. J., Porvasnik, S., Lewis, M. A., Zolotukhin, I., Cloutier, D. A., & Byrne, B. J. (2004) · Development · doi:10.1242/dev.01169 · Cited by 73 · see citing works

Peripheral neuropathy, episodic myoglobinuria, and respiratory failure in deficiency of the mitochondrial trifunctional protein

Spiekerkoetter, U., Bennett, M. J., Ben‐Zeev, B., Strauss, A. W., & Tein, I. (2003) · Muscle & Nerve · doi:10.1002/mus.10500 · Cited by 72 · see citing works

Mitochondria and Redox Signaling in Steatohepatitis

Morris, E. M., Rector, R. S., Thyfault, J. P., & Ibdah, J. A. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3795 · Cited by 71 · see citing works

Mitochondrial fatty acid oxidation disorders: pathophysiological studies in mouse models

Spiekerkoetter, U., & Wood, P. A. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9121-7 · Cited by 71 · see citing works

Pptc7 is an essential phosphatase for promoting mammalian mitochondrial metabolism and biogenesis

Niemi, N. M., Wilson, G. M., Overmyer, K. A., Vögtle, F. ‐., Myketin, L., Lohman, D. C., Schueler, K. L., Attie, A., Meisinger, C., Coon, J. J., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11047-6 · Cited by 71 · see citing works

The biochemistry and physiology of long-chain dicarboxylic acid metabolism

Ranea‐Robles, P., & Houten, S. M. (2023) · Biochemical Journal · doi:10.1042/bcj20230041 · Cited by 70 · see citing works

Stimulation of astrocyte fatty acid oxidation by thyroid hormone is protective against ischemic stroke-induced damage

Sayre, N. L., Sifuentes, M. M., Holstein, D. M., Cheng, S.-Y., Zhu, X., & Lechleiter, J. D. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16629153 · Cited by 69 · see citing works

Selective hepatic insulin resistance in a murine model heterozygous for a mitochondrial trifunctional protein defect

Rector, R. S., Morris, E. M., Ridenhour, S. E., Meers, G. M.-E., Hsu, F., TURK, J. W., & Ibdah, J. A. (2013) · Hepatology · doi:10.1002/hep.26285 · Cited by 69 · see citing works

Lack of Myoglobin Causes a Switch in Cardiac Substrate Selection

Flögel, U., Laußmann, T., Gödecke, A., Abanador-Kamper, N., Schäfers, M. A., Fingas, C. D., Metzger, S. U., Levkau, B., Jacoby, C., & Schrader, J. (2005) · Circulation Research · doi:10.1161/01.res.0000165481.36288.d2 · Cited by 64 · see citing works

Role of 3-Hydroxy Fatty Acid-Induced Hepatic Lipotoxicity in Acute Fatty Liver of Pregnancy

Natarajan, S. K., & Ibdah, J. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010322 · Cited by 63 · see citing works

Maternal nutrition modulates fetal development by inducing placental efficiency changes in gilts

Che, L., Yang, Z., Xu, M., Xu, S., Che, L., Lin, Y., Fang, Z., Feng, B., Li, J., Chen, D., et al. (2017) · BMC Genomics · doi:10.1186/s12864-017-3601-1 · Cited by 65 · see citing works

Functional, proteomic and bioinformatic analyses of Nrf2- and Keap1- null skeletal muscle

Gao, L., Kumar, V., Vellichirammal, N. N., Park, S., Rudebush, T. L., Yu, L., Son, W., Pekas, E. J., Wafi, A. M., Hong, J., et al. (2020) · The Journal of Physiology · doi:10.1113/jp280176 · Cited by 58 · see citing works

Fatty acid metabolism in cardiac failure: biochemical, genetic and cellular analysis

Marı́n-Garcı́a, J. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(01)00552-1 · Cited by 61 · see citing works

Mitochondrial trifunctional protein defects: Clinical implications and therapeutic approaches

Rector, R. S., Payne, R. M., & Ibdah, J. A. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2008.04.014 · Cited by 56 · see citing works

Alterations of Mitochondrial Enzymes Contribute to Cardiac Hypertrophy before Hypertension Development in Spontaneously Hypertensive Rats

Meng, C., Jin, X., Li, X., Shen, S.-M., Wang, X., Cai, J., Chen, G., Wang, L., & Fang, N. (2009) · Journal of Proteome Research · doi:10.1021/pr801059u · Cited by 56 · see citing works

Mouse Models for Disorders of Mitochondrial Fatty Acid -Oxidation

Schuier, A. M., & Wood, P. A. (2002) · ILAR Journal · doi:10.1093/ilar.43.2.57 · Cited by 54 · see citing works

Deletion of mouse Alkbh7 leads to obesity

Solberg, A., Robertson, A. B., Aronsen, J. M., Rognmo, Ø., Sjaastad, I., Wisløff, U., & Klungland, A. (2013) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjt012 · Cited by 56 · see citing works

Partial Resistance to Peroxisome Proliferator–Activated Receptor-α Agonists in ZDF Rats Is Associated With Defective Hepatic Mitochondrial Metabolism

Satapati, S., He, T., Inagaki, T., Potthoff, M. J., Merritt, M. E., Esser, V., Mangelsdorf, D. J., Kliewer, S. A., Browning, J. D., & Burgess, S. C. (2008) · Diabetes · doi:10.2337/db08-0226 · Cited by 52 · see citing works

Glucocorticoid receptor-PPARα axis in fetal mouse liver prepares neonates for milk lipid catabolism

Rando, G., Tan, C. K., Khaled, N., Montagner, A., Leuenberger, N., Bertrand‐Michel, J., Paramalingam, E., Guillou, H., & Wahli, W. (2016) · eLife · doi:10.7554/elife.11853 · Cited by 51 · see citing works

l-Carnitine is Synthesized in the Human Fetal–Placental Unit: Potential Roles in Placental and Fetal Metabolism

Oey, N. A., van Vlies, N., Wijburg, F. A., Wanders, R. J. A., Attié‐Bitach, T., & Vaz, F. M. (2005) · Placenta · doi:10.1016/j.placenta.2005.10.002 · Cited by 51 · see citing works

Epoxyeicosatrienoic Acid as Therapy for Diabetic and Ischemic Cardiomyopathy

Romashko, M. D., Schragenheim, J., Abraham, N. G., & McClung, J. A. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.08.001 · Cited by 50 · see citing works

Deletion of Cyclophilin D Impairs β-Oxidation and Promotes Glucose Metabolism

Tavecchio, M., Lisanti, S., Bennett, M. J., Languino, L. R., & Altieri, D. C. (2015) · Scientific Reports · doi:10.1038/srep15981 · Cited by 49 · see citing works

Regulation of mitochondrial trifunctional protein modulates nonalcoholic fatty liver disease in mice

Nassir, F., Arndt, J. J., Johnson, S. A., & Ibdah, J. A. (2018) · Journal of Lipid Research · doi:10.1194/jlr.m080952 · Cited by 49 · see citing works

Mice with an Oncogenic HRAS Mutation are Resistant to High-Fat Diet-Induced Obesity and Exhibit Impaired Hepatic Energy Homeostasis

Oba, D., Inoue, S., Miyagawa‐Tomita, S., Nakashima, Y., Niihori, T., Yamaguchi, S., Matsubara, Y., & Aoki, Y. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.11.029 · Cited by 48 · see citing works

Impact of selected inborn errors of metabolism on prenatal and neonatal development

Illsinger, S., & Das, A. M. (2010) · IUBMB Life · doi:10.1002/iub.336 · Cited by 48 · see citing works

Chromosome instability and tumor predisposition inversely correlate with BLM protein levels

McDaniel, L. D., Chester, N., Watson, M. L., Borowsky, A. D., Leder, P., & Schultz, R. A. (2003) · DNA repair · doi:10.1016/j.dnarep.2003.08.006 · Cited by 46 · see citing works

ENU mutagenesis identifies mice with cardiac fibrosis and hepatic steatosis caused by a mutation in the mitochondrial trifunctional protein β-subunit

Kao, H.-J., Cheng, C.-F., Chen, Y.-H., Hung, S.-I., Huang, C.-C., Millington, D., Kikuchi, T., Wu, J.-Y., & Chen, Y.-T. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl433 · Cited by 47 · see citing works

Deficiency of 3‐hydroxybutyrate dehydrogenase (BDH1) in mice causes low ketone body levels and fatty liver during fasting

Otsuka, H., Kimura, T., Ago, Y., Nakama, M., Aoyama, Y., Abdelkreem, E., Matsumoto, H., Ohnishi, H., Sasai, H., Osawa, M., et al. (2020) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12243 · Cited by 46 · see citing works

La mitocondria y el corazón

Marı́n-Garcı́a, J., & Goldenthal, M. J. (2002) · Revista Española de Cardiología · doi:10.1016/s0300-8932(02)76802-4 · Cited by 44 · see citing works

Differential expression of adipose tissue proteins between obesity‐susceptible and ‐resistant rats fed a high‐fat diet

Joo, J. I., Oh, T. S., Kim, D. H., Choi, D. K., Wang, X., Choi, J., & Yun, J. W. (2011) · PROTEOMICS · doi:10.1002/pmic.201000515 · Cited by 44 · see citing works

Dietary fat impacts fetal growth and metabolism: uptake of chylomicron remnant core lipids by the placenta

Rebholz, S. L., Burke, K. T., Yang, Q., Tso, P., & Woollett, L. A. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00619.2010 · Cited by 43 · see citing works

Fatty acid oxidation in the human fetus: Implications for fetal and adult disease

Oey, N. A., Ruiter, J. P. N., Attié‐Bitach, T., IJlst, L., Wanders, R. J. A., & Wijburg, F. A. (2006) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-006-0199-x · Cited by 42 · see citing works

Role of short-chain hydroxyacyl CoA dehydrogenases in SCHAD deficiency

Filling, C., Keller, B., Hirschberg, D., Marschall, H., Jörnvall, H., Bennett, M. J., & Oppermann, U. C. T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.10.188 · Cited by 39 · see citing works

Hepatitis C Virus Attenuates Mitochondrial Lipid β-Oxidation by Downregulating Mitochondrial Trifunctional-Protein Expression

Amako, Y., Munakata, T., Kohara, M., Siddiqui, A., Peers, C., & Harris, M. (2015) · Journal of Virology · doi:10.1128/jvi.01653-14 · Cited by 37 · see citing works

Proteomic mapping of differentially vulnerable pre-synaptic populations identifies regulators of neuronal stability in vivo

Hurtado, M. L., Fuller, H. R., Wong, A. M. S., Eaton, S. L., Gillingwater, T. H., Pennetta, G., Cooper, J. D., & Wishart, T. M. (2017) · Scientific Reports · doi:10.1038/s41598-017-12603-0 · Cited by 36 · see citing works

GRK5 – A Functional Bridge Between Cardiovascular and Neurodegenerative Disorders

Hendrickx, J. O., van Gastel, J., Leysen, H., Santos‐Otte, P., Premont, R. T., Martin, B., & Maudsley, S. R. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01484 · Cited by 36 · see citing works

Impaired fatty acid oxidation in a Drosophila model of mitochondrial trifunctional protein (MTP) deficiency

Kishita, Y., Tsuda, M., & Aigaki, T. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.02.026 · Cited by 34 · see citing works

Proteomics Analysis to Identify and Characterize the Molecular Signatures of Hepatic Steatosis in Ovariectomized Rats as a Model of Postmenopausal Status

Liao, C.-C., Chiu, Y., Chiu, W., Tung, Y., Chuang, H.-L., Wu, J., & Huang, C. (2015) · Nutrients · doi:10.3390/nu7105434 · Cited by 33 · see citing works

Phospholipids: Identification and Implication in Muscle Pathophysiology

Bargui, R., Solgadi, A., Prost, B., Chester, M., Ferreiro, A., Piquereau, J., & Moulin, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158176 · Cited by 32 · see citing works

Impaired fatty acid oxidation as a cause of liver disease associated with hyperemesis gravidarum

Outlaw, W. M., & Ibdah, J. A. (2005) · Medical Hypotheses · doi:10.1016/j.mehy.2005.05.035 · Cited by 30 · see citing works

Inhibition of Estrogen-Related Receptor α Blocks Liver Steatosis and Steatohepatitis and Attenuates Triglyceride Biosynthesis

Chen, C.-Y., Li, Y., Zeng, N., He, L., Zhang, X., Tu, T., Tang, Q., Alba, M. M., Mir, S., Stiles, E. X., et al. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.04.007 · Cited by 28 · see citing works

Label-free quantitative proteomic analysis of milk fat globule membrane proteins in porcine colostrum and mature milk

Zhao, H., Li, M., Zhu, Q., Liu, A., Bi, J., Quan, Z., Luo, X. G., Zheng, Y., Yang, N., Yue, X., et al. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.136447 · Cited by 28 · see citing works

Carnitine Content and Expression of Mitochondrial β-Oxidation Enzymes in Placentas of Wild-Type (OCTN2+/+) and OCTN2 Null (OCTN2−/−) Mice

Shekhawat, P., Yang, H.-S., Bennett, M. J., Carter, A. L., Matern, D., Tamai, I., & Ganapathy, V. (2004) · Pediatric Research · doi:10.1203/01.pdr.0000134252.02876.55 · Cited by 28 · see citing works

Disruption of Slc52a3 gene causes neonatal lethality with riboflavin deficiency in mice

Yoshimatsu, H., Yonezawa, A., Yamanishi, K., Yao, Y., Sugano, K., Nakagawa, S., Imai, S., Omura, T., Nakagawa, T., Yano, I., et al. (2016) · Scientific Reports · doi:10.1038/srep27557 · Cited by 28 · see citing works

The Trifunctional Protein Mediates Thyroid Hormone Receptor-Dependent Stimulation of Mitochondria Metabolism

Chocrón, E. S., Sayre, N. L., Holstein, D. M., Saelim, N., Ibdah, J. A., Dong, L., Zhu, X., Cheng, S.-Y., & Lechleiter, J. D. (2012) · Molecular Endocrinology · doi:10.1210/me.2011-1348 · Cited by 27 · see citing works

Modeling Disorders of Fatty Acid Metabolism in the Mouse

Goetzman, E. S. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-384878-9.00010-8 · Cited by 26 · see citing works

Maternal heterozygosity for a mitochondrial trifunctional protein mutation as a cause for liver disease in pregnancy

Blish, K. R., & Ibdah, J. A. (2004) · Medical Hypotheses · doi:10.1016/j.mehy.2004.06.005 · Cited by 26 · see citing works

HADHA, the alpha subunit of the mitochondrial trifunctional protein, is involved in long-chain fatty acid-induced autophagy in intestinal epithelial cells

Maeyashiki, C., Oshima, S., Otsubo, K., Kobayashi, M., Nibe, Y., Matsuzawa, Y., Onizawa, M., Nemoto, Y., Nagaishi, T., Okamoto, R., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.01.159 · Cited by 25 · see citing works

Recent Advances in the Pathophysiology of Fatty Acid Oxidation Defects: Secondary Alterations of Bioenergetics and Mitochondrial Calcium Homeostasis Caused by the Accumulating Fatty Acids

Amaral, A. U., & Wajner, M. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.598976 · Cited by 24 · see citing works

Effect of High-Fat Diet on Hepatic Proteomics of Hamsters

Liao, C.-C., Lin, Y.-L., & Kuo, C.-F. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf506118j · Cited by 23 · see citing works

Mitochondrial peptide Mtln contributes to oxidative metabolism in mice

Averina, O. A., Permyakov, O. A., Emelianova, M. A., Grigoryeva, O. O., Gulyaev, M. V., Pavlova, O. S., Mariasina, S. S., Frolova, O., Kurkina, M. V., Baydakova, G., et al. (2022) · Biochimie · doi:10.1016/j.biochi.2022.09.009 · Cited by 22 · see citing works

Characterization of l-aminocarnitine, an inhibitor of fatty acid oxidation

Chegary, M., Brinke, H. T., Doolaard, M., IJlst, L., Wijburg, F. A., Wanders, R. J. A., & Houten, S. M. (2008) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2007.11.001 · Cited by 22 · see citing works

Deciphering the gene expression profile of peroxisome proliferator-activated receptor signaling pathway in the left atria of patients with mitral regurgitation

Chen, M., Chang, J.-P., Lin, Y., Pan, K., Ho, W., Liu, W.-H., Chang, T., Huang, Y., Fang, C.-Y., & Chen, C. (2016) · Journal of Translational Medicine · doi:10.1186/s12967-016-0871-3 · Cited by 22 · see citing works

Functions of mammalian SIRT4 in cellular metabolism and research progress in human cancer (Review)

Wang, C., Liu, Y., Zhu, Y., & Kong, C. (2020) · Oncology Letters · doi:10.3892/ol.2020.11872 · Cited by 22 · see citing works

Complete deficiency of mitochondrial trifunctional protein due to a novel mutation within the β-subunit of the mitochondrial trifunctional protein gene leads to failure of long-chain fatty acid β-oxidation with fatal outcome

Schwab, K. O., Ensenauer, R. E., Matern, D., Uyanık, G., Schnieders, B., Wanders, R. J. A., & Lehnert, W. (2003) · European Journal of Pediatrics · doi:10.1007/s00431-002-1035-4 · Cited by 24 · see citing works

Using Mitochondrial Trifunctional Protein Deficiency to Understand Maternal Health

Miklas, J. W., & Ruohola‐Baker, H. (2020) · Journal of Cellular Signaling · doi:10.33696/signaling.1.018 · Cited by 1 · see citing works

Impaired fatty acid oxidation in a Drosophila model of mitochondrial trifunctional protein (MTP) deficiency

Kishita, Y., Tsuda, M., & Aigaki, T. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.02.026 · Cited by 34 · see citing works

Fatal cardiomyopathy and hepatic dysfunction with acute onset due to mitochondrial trifunctional protein deficiency diagnosed by whole exome sequencing

Brătilă, E. (2015) · Gineco eu · doi:10.18643/gieu.2015.8

Mitochondrial trifunctional protein deficiency: A severe fatty acid oxidation disorder with cardiac and neurologic involvement

den Boer, M. E. J., Dionisi‐Vici, C., Chakrapani, A., van Thuijl, A. O. J., Wanders, R. J. A., & Wijburg, F. A. (2003) · The Journal of Pediatrics · doi:10.1067/mpd.2003.231 · Cited by 90 · see citing works