GO:0036112 medium-chain fatty-acyl-CoA metabolic process: Energy Pathway, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0036112 describes the chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, thioester derivatives of coenzyme A with 6 to 12 carbon aliphatic tails.
• Medium-chain fatty-acyl-CoAs are central intermediates in mitochondrial beta-oxidation and in the biosynthesis of medium-chain fatty acids [1,2].
• ACSM3 deficiency impairs medium-chain fatty acid metabolism and aggravates kidney fibrosis, linking this process to organ pathology.
• Disorders of fatty-acyl-CoA dehydrogenation, such as VLCAD and MCAD deficiencies, show clinical heterogeneity that can be modelled with medium-chain substrates [4,5,8].
• Medium-chain fatty acids and triheptanoin can modulate cardiac and hepatic energy metabolism in fatty acid oxidation disorders [6,7].
• CRISPR knockout, point-mutation, knock-in and overexpression models are essential to dissect gene function within GO:0036112.
Description
Medium-chain fatty-acyl-CoA metabolic process (GO:0036112) is a biological process that encompasses the chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, which are derivatives of coenzyme A in which the sulfhydryl group is in a thioester linkage with a fatty-acyl group containing 6 to 12 carbons. These molecules sit at the crossroads of energy production and lipid biosynthesis, and their metabolism is fundamental to cellular homeostasis in tissues such as liver, heart, skeletal muscle and kidney [1,2]. Researchers study this process because perturbations in medium-chain fatty-acyl-CoA handling are increasingly recognized in metabolic, cardiac and renal diseases [3,4]. The definition provided by QuickGO emphasizes that the term covers any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group, distinguishing it from short-chain and long-chain fatty-acyl-CoA metabolism. This specificity matters because chain-length determines which enzymes, transporters and subcellular compartments participate in the pathway. In this article we integrate the QuickGO definition with published literature to describe the mechanism, key genes, disease relevance and experimental strategies for studying GO:0036112.
medium-chain fatty-acyl-CoA metabolic process At A Glance
| GO ID | GO:0036112 |
|---|---|
| GO term | medium-chain fatty-acyl-CoA metabolic process |
| Ontology | biological_process |
| Synonym | medium-chain fatty acyl CoA metabolic process; medium-chain fatty acyl-CoA metabolism |
| Definition | The chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group; a medium-chain fatty acid has an aliphatic tail containing 6 to 12 carbons. |
| Major function | Energy production via mitochondrial beta-oxidation and participation in fatty acid biosynthesis and elongation [1,2]. |
| Chain length range | 6 to 12 carbons in the aliphatic tail. |
| Key cellular context | Mitochondrial matrix and cytoplasm, with relevance to liver, heart, skeletal muscle and kidney [1,2,3]. |
| Representative genes | ACSM3, ACADM, ACADVL, HADHA, HADHB, CPT1A, CPT2, SLC25A20 and related acyl-CoA dehydrogenases and thioesterases [2,3,4,8]. |
What Is GO:0036112?
GO:0036112, medium-chain fatty-acyl-CoA metabolic process, is defined as the chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group, where a medium-chain fatty acid has an aliphatic tail containing 6 to 12 carbons. In simpler terms, it is the set of biochemical steps by which cells make, modify, break down or otherwise handle fatty acids of medium chain length while they are attached to coenzyme A [1,2].
Why Is medium-chain fatty-acyl-CoA metabolic process Important in Cell Biology?
Medium-chain fatty-acyl-CoA metabolic process is important because it governs the flux of medium-chain fatty acids into energy-producing and biosynthetic pathways, and its dysfunction is linked to human disease. Short- and medium-chain fatty acids are efficiently oxidized in mitochondria and can serve as alternative energy substrates when long-chain fatty acid oxidation is impaired. Defects in fatty acid oxidation, including very long-chain acyl-CoA dehydrogenase deficiency, can present with severe neonatal phenotypes and sudden infant death, underscoring the clinical importance of acyl-CoA chain-length handling [4,5]. Moreover, medium-chain fatty acid metabolism in the kidney is directly implicated in fibrosis, as ACSM3 deficiency impairs this process and aggravates kidney fibrosis. Understanding GO:0036112 therefore has implications for metabolic disorders, cardiac disease, renal pathology and the development of dietary or pharmacological interventions such as medium-chain triglyceride and triheptanoin supplementation [6,7].
• Provides a major route for energy production from medium-chain fatty acids, especially in liver, heart and skeletal muscle.
• Supplies acetyl-CoA and reducing equivalents to the citric acid cycle and oxidative phosphorylation [1,2].
• Contributes to de novo fatty acid biosynthesis and elongation pathways.
• Its impairment is linked to kidney fibrosis through ACSM3 deficiency.
• Defects in acyl-CoA dehydrogenation cause diseases such as VLCAD and MCAD deficiency with heterogeneous clinical presentations [4,5,8].
• Medium-chain substrates can modulate cardiac citric acid cycle intermediates in fatty acid oxidation disorders.
• Serves as a target for dietary interventions including medium-chain triglycerides and triheptanoin [6,7].
• Provides a biochemical framework for interpreting newborn screening and acylcarnitine profiles.
• Enables mechanistic studies of chain-length specificity in beta-oxidation enzymes.
• Supports the development of CRISPR models to test causal roles of metabolic genes in disease [3,8].
What Happens During medium-chain fatty-acyl-CoA metabolic process?
Activation and formation of medium-chain fatty-acyl-CoAs
In simple terms: Fatty acids must be attached to a carrier molecule called coenzyme A before the cell can use them.
Medium-chain fatty acids enter metabolism after being activated to their corresponding acyl-CoA thioesters. This activation step converts a free fatty acid into a medium-chain fatty-acyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with the fatty-acyl group. The resulting medium-chain fatty-acyl-CoAs are the substrates for subsequent oxidation or elongation reactions, and their formation is a prerequisite for both energy production and biosynthetic pathways [1,2].
Mitochondrial beta-oxidation of medium-chain fatty-acyl-CoAs
In simple terms: In the mitochondria, the fatty acid chain is chopped into two-carbon units to release energy.
Mitochondrial beta-oxidation of saturated fatty acids is the principal pathway for degrading medium-chain fatty-acyl-CoAs. The process involves a cycle of dehydrogenation, hydration, another dehydrogenation and thiolytic cleavage, generating acetyl-CoA and a shortened acyl-CoA. Medium-chain fatty acids are preferentially oxidized in mitochondria and can serve as efficient energy substrates. The chain-length specificity of the enzymes involved ensures that medium-chain fatty-acyl-CoAs are handled distinctly from short-chain and long-chain species.
Biosynthesis and elongation involving medium-chain intermediates
In simple terms: Medium-chain fatty acids can also be built up or modified rather than just broken down.
De novo fatty acid biosynthesis and elongation can involve medium-chain fatty-acyl-CoA intermediates. In very long-chain acyl-CoA dehydrogenase-deficient mice supplemented with odd or even medium-chain fatty acids, de novo fatty acid biosynthesis and elongation are affected, indicating that medium-chain fatty acids participate in these anabolic pathways. This dual role highlights that GO:0036112 is not solely catabolic but also contributes to the production of longer-chain fatty acids.
Tissue-specific roles and disease-associated remodeling
In simple terms: Different organs use medium-chain fatty acid metabolism in different ways, and when it fails, disease can follow.
Tubular ACSM3 deficiency impairs medium-chain fatty acid metabolism and aggravates kidney fibrosis, demonstrating a tissue-specific role for this process in the kidney. In the heart, medium-chain fatty acid metabolism influences citric acid cycle intermediates, as shown in exercised very long-chain acyl-CoA dehydrogenase-deficient mice fed triheptanoin or medium-chain triglyceride. These findings illustrate that GO:0036112 is dynamically regulated across tissues and can be remodeled in disease states [3,7].
Clinical heterogeneity and personalized modelling
In simple terms: Patients with the same metabolic gene defect can have different symptoms, so models must capture this variability.
Personalised modelling of clinical heterogeneity between medium-chain acyl-CoA dehydrogenase patients has been performed, highlighting that individuals with defects in medium-chain fatty-acyl-CoA metabolism can present differently. This heterogeneity underscores the need for experimental systems that reflect genetic and environmental modifiers, and it supports the use of patient-derived or CRISPR-engineered models to study GO:0036112.
Key Genes Involved in GO:0036112 medium-chain fatty-acyl-CoA metabolic process
The following genes encode enzymes, transporters and regulatory proteins that participate in or directly influence medium-chain fatty-acyl-CoA metabolic process (GO:0036112).
| Gene | Major Role | Research Relevance |
|---|---|---|
| ACSM3 | Medium-chain acyl-CoA synthetase; activates medium-chain fatty acids to acyl-CoAs | Deficiency impairs medium-chain fatty acid metabolism and aggravates kidney fibrosis |
| ACADM | Medium-chain acyl-CoA dehydrogenase; catalyzes the first step of medium-chain fatty acid beta-oxidation | Mutations cause MCAD deficiency; clinical heterogeneity studied with personalized models |
| ACADVL | Very long-chain acyl-CoA dehydrogenase; acts on long-chain acyl-CoAs but influences medium-chain metabolism | Deficiency causes VLCAD deficiency with neonatal sudden death and cardiac phenotypes [4,5,7] |
| HADHA | Trifunctional protein subunit alpha; catalyzes long-chain and medium-chain enoyl-CoA hydration and 3-hydroxyacyl-CoA dehydrogenation | Component of mitochondrial beta-oxidation machinery |
| HADHB | Trifunctional protein subunit beta; catalyzes thiolase step in beta-oxidation | Component of mitochondrial beta-oxidation machinery |
| CPT1A | Carnitine palmitoyltransferase 1A; regulates entry of long-chain fatty acids into mitochondria | Indirectly affects medium-chain fatty-acyl-CoA pools by controlling fatty acid flux |
| CPT2 | Carnitine palmitoyltransferase 2; involved in carnitine shuttle for long-chain fatty acids | Indirectly affects medium-chain fatty-acyl-CoA metabolism |
| SLC25A20 | Carnitine-acylcarnitine translocase; transports acylcarnitines across inner mitochondrial membrane | Indirectly affects medium-chain fatty-acyl-CoA metabolism |
| ACOT family | Acyl-CoA thioesterases; hydrolyze acyl-CoAs to free fatty acids and CoA | Regulate cellular levels of medium-chain fatty-acyl-CoAs |
| FASN | Fatty acid synthase; produces medium-chain fatty-acyl-CoA intermediates during de novo lipogenesis | Links medium-chain fatty-acyl-CoA metabolism to biosynthesis |
| ELOVL family | Fatty acid elongases; extend fatty acyl chains | Involved in elongation pathways that use medium-chain fatty-acyl-CoAs |
| PPARA | Peroxisome proliferator-activated receptor alpha; transcription factor regulating fatty acid oxidation genes | Regulates expression of beta-oxidation enzymes |
| PPARGC1A | PGC-1alpha; coactivator regulating mitochondrial biogenesis and fatty acid oxidation | Modulates capacity for medium-chain fatty-acyl-CoA oxidation |
| SIRT1 | NAD-dependent deacetylase; regulates metabolic gene expression | Potential regulator of fatty acid oxidation pathways |
| AMPK | AMP-activated protein kinase; energy sensor regulating fatty acid metabolism | Regulates flux through beta-oxidation |
| ACACA | Acetyl-CoA carboxylase alpha; catalyzes malonyl-CoA formation, regulating fatty acid oxidation | Influences medium-chain fatty-acyl-CoA metabolism via malonyl-CoA |
| ACLY | ATP citrate lyase; supplies acetyl-CoA for fatty acid synthesis | Links carbohydrate metabolism to medium-chain fatty-acyl-CoA metabolism |
| SLC22A5 | Carnitine transporter; supplies carnitine for fatty acid oxidation | Indirectly affects medium-chain fatty-acyl-CoA metabolism |
How Is medium-chain fatty-acyl-CoA metabolic process Regulated?
Medium-chain fatty-acyl-CoA metabolic process is regulated at multiple levels. Transcriptional control by PPARA and PPARGC1A influences the expression of beta-oxidation enzymes, thereby adjusting the capacity for medium-chain fatty-acyl-CoA oxidation. The energy sensor AMPK and the NAD-dependent deacetylase SIRT1 modulate metabolic gene expression in response to cellular energy status. Substrate availability, including the supply of medium-chain fatty acids and carnitine, also determines flux through the pathway [1,2]. In disease states such as kidney fibrosis, ACSM3 deficiency impairs medium-chain fatty acid metabolism, indicating that the pathway can be dysregulated at the level of acyl-CoA synthetase activity. Additionally, malonyl-CoA produced by ACACA inhibits carnitine palmitoyltransferase 1, indirectly affecting the entry of fatty acids into mitochondria and thus the generation of medium-chain fatty-acyl-CoAs.
medium-chain fatty-acyl-CoA metabolic process and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| ACSM3 | Kidney fibrosis; impaired medium-chain fatty acid metabolism | Tubular-specific knockout or overexpression in kidney cell lines and mouse models |
| ACADM | Medium-chain acyl-CoA dehydrogenase deficiency; clinical heterogeneity | Patient-derived cells and CRISPR knock-in of patient variants |
| ACADVL | Very long-chain acyl-CoA dehydrogenase deficiency; neonatal sudden death; cardiac dysfunction | Knockout mouse models and medium-chain fatty acid supplementation studies [4,5,7] |
| HADHA/HADHB | Mitochondrial trifunctional protein deficiency; impaired beta-oxidation | Knockout cell models and metabolic flux assays |
| CPT2 | Carnitine palmitoyltransferase II deficiency; impaired fatty acid oxidation | Knockout or point-mutation models in hepatocytes and myocytes |
Kidney fibrosis and ACSM3 deficiency
Tubular ACSM3 deficiency impairs medium-chain fatty acid metabolism and aggravates kidney fibrosis, directly linking GO:0036112 to renal pathology. This finding suggests that preserving medium-chain fatty-acyl-CoA metabolism in tubular cells may be protective against fibrotic remodeling.
Fatty acid oxidation disorders: VLCAD and MCAD deficiency
Very long-chain acyl-CoA dehydrogenase deficiency can cause severe neonatal phenotypes, including sudden infant death, and prompt diagnosis improves survival. The pathogenesis of VLCAD deficiency involves impaired fatty acid oxidation and energy deficiency, which can be studied with medium-chain fatty acid supplementation. Medium-chain acyl-CoA dehydrogenase deficiency also shows clinical heterogeneity between patients, requiring personalized modelling to understand variable outcomes.
Cardiac energy metabolism and therapeutic substrates
In exercised very long-chain acyl-CoA dehydrogenase-deficient mice, cardiac tissue citric acid cycle intermediates are altered by feeding triheptanoin or medium-chain triglyceride, indicating that medium-chain fatty acid metabolism can influence cardiac energy status. De novo fatty acid biosynthesis and elongation are also affected by odd or even medium-chain fatty acid supplementation in VLCAD-deficient mice. These studies highlight the therapeutic potential of modulating medium-chain fatty-acyl-CoA metabolism [6,7].
From medium-chain fatty-acyl-CoA metabolic process-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of ACSM3 impair medium-chain fatty-acyl-CoA metabolism and promote fibrosis? | ACSM3 knockout in tubular epithelial cells and mouse kidney fibrosis models |
| How do MCAD patient variants affect enzyme function and clinical phenotype? | CRISPR knock-in of patient-specific ACADM mutations in cell lines and personalized modelling |
| Can medium-chain fatty acid supplementation rescue VLCAD deficiency phenotypes? | ACADVL knockout mice fed medium-chain triglyceride or triheptanoin [6,7] |
| What is the role of HADHA/HADHB in medium-chain fatty-acyl-CoA handling? | Knockout and point-mutation models in cardiomyocytes and hepatocytes |
| How does PPARA or PPARGC1A regulate medium-chain fatty-acyl-CoA oxidation? | Overexpression and knockout models with metabolic flux analysis |
| Does ACOT family thioesterase activity control medium-chain fatty-acyl-CoA levels? | Overexpression and knockout cell models with acyl-CoA profiling |
How to Study the medium-chain fatty-acyl-CoA metabolic process Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Acylcarnitine profiling by mass spectrometry | Levels of medium-chain acylcarnitines | Diagnosis of fatty acid oxidation disorders and flux assessment |
| Stable isotope metabolic flux analysis | Flux through beta-oxidation and biosynthesis | Quantifying medium-chain fatty-acyl-CoA metabolism [1,2] |
| CRISPR knockout screens | Genes required for medium-chain fatty-acyl-CoA metabolism | Discovery of novel regulators |
| RNA sequencing | Transcriptional changes in metabolic genes | Identifying regulatory networks |
| Quantitative proteomics | Protein abundance of beta-oxidation enzymes | Validating expression changes |
| Tissue-specific knockout mouse models | In vivo consequences of gene loss | Studying kidney fibrosis and cardiac metabolism [3,7] |
| Seahorse extracellular flux analysis | Mitochondrial respiration | Assessing energy metabolism in mutant cells |
| Lipidomics | Fatty acid and acyl-CoA species | Profiling medium-chain intermediates |
Metabolic flux analysis and acylcarnitine profiling
Metabolic flux analysis using stable isotopes and acylcarnitine profiling by mass spectrometry can quantify medium-chain fatty-acyl-CoA metabolism in cells and tissues [1,2]. These methods are used to diagnose fatty acid oxidation disorders and to assess the impact of genetic or dietary interventions.
CRISPR-based genetic screens
CRISPR knockout and activation screens can identify genes that regulate medium-chain fatty-acyl-CoA levels or sensitivity to medium-chain fatty acid substrates [3,8]. Such screens are typically combined with metabolic readouts to uncover novel regulators of GO:0036112.
Transcriptomics and proteomics
RNA sequencing and quantitative proteomics reveal expression changes in beta-oxidation enzymes and related pathways under conditions that perturb medium-chain fatty-acyl-CoA metabolism [2,6]. These approaches help define the regulatory network around GO:0036112.
Animal models and tissue-specific knockout
Tissue-specific knockout mice, such as tubular ACSM3 knockout or ACADVL knockout, are used to study the physiological consequences of impaired medium-chain fatty-acyl-CoA metabolism in kidney, heart and liver [3,7]. These models allow assessment of fibrosis, cardiac function and energy metabolism [3,7].
How CRISPR Can Be Used to Study GO:0036112 medium-chain fatty-acyl-CoA metabolic process
Knockout
CRISPR knockout of genes such as ACSM3, ACADM or ACADVL can be used to model loss-of-function states and assess their impact on medium-chain fatty-acyl-CoA metabolism [3,8]. Knockout cell lines and mice help determine whether a gene is required for normal flux through GO:0036112.
Point Mutation
Point mutations identified in patients with fatty acid oxidation disorders, such as ACADM or ACADVL variants, can be introduced by CRISPR to study their functional consequences [8,4]. These models are valuable for understanding clinical heterogeneity and genotype-phenotype relationships.
Knock-in
Knock-in of reporter tags or patient-specific alleles allows tracking of enzyme localization and activity in the context of medium-chain fatty-acyl-CoA metabolism. Tagged knock-in models can be used to purify protein complexes involved in beta-oxidation.
Overexpression
CRISPR activation or cDNA overexpression of genes such as ACSM3 or PPARGC1A can enhance medium-chain fatty-acyl-CoA metabolism and test whether increased flux is protective in disease models [3,2]. Overexpression studies complement knockout approaches to establish causality.
How EDITGENE Supports medium-chain fatty-acyl-CoA metabolic process Research
Researchers studying medium-chain fatty-acyl-CoA metabolic process-related genes often need to determine whether a candidate gene is causally involved in the pathway or merely correlated with metabolic changes. EDITGENE provides a comprehensive suite of CRISPR-based services to generate precisely engineered cell and animal models, enabling rigorous functional validation of genes within GO:0036112.
Contact EDITGENE today to design your custom CRISPR model for medium-chain fatty-acyl-CoA metabolic process research.
Frequently Asked Questions About medium-chain fatty-acyl-CoA metabolic process
What is medium-chain fatty-acyl-CoA metabolic process?
It is the set of chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, which are coenzyme A derivatives with 6 to 12 carbon fatty-acyl chains, as defined by GO:0036112.
What genes are involved in medium-chain fatty-acyl-CoA metabolic process?
Key genes include ACSM3, ACADM, ACADVL, HADHA, HADHB, CPT1A, CPT2, SLC25A20 and ACOT family members, among others [2,3,8].
What is the GO ID for medium-chain fatty-acyl-CoA metabolic process?
The GO ID is GO:0036112.
How is medium-chain fatty-acyl-CoA metabolic process linked to kidney disease?
ACSM3 deficiency impairs medium-chain fatty acid metabolism and aggravates kidney fibrosis, linking this process to renal pathology.
What diseases are associated with defects in medium-chain fatty-acyl-CoA metabolism?
VLCAD deficiency, MCAD deficiency and mitochondrial trifunctional protein deficiency are associated with impaired fatty acid oxidation [4,5,8].
Can medium-chain fatty acids be used therapeutically?
Medium-chain triglycerides and triheptanoin have been studied in VLCAD-deficient mice and may modulate cardiac energy metabolism [6,7].
What methods are used to study medium-chain fatty-acyl-CoA metabolism?
Acylcarnitine profiling, stable isotope flux analysis, CRISPR screens, RNA sequencing and proteomics are commonly used [1,2,3].
What is the role of ACADM in medium-chain fatty-acyl-CoA metabolism?
ACADM encodes medium-chain acyl-CoA dehydrogenase, which catalyzes the first step of medium-chain fatty acid beta-oxidation.
How can CRISPR be used to study GO:0036112?
CRISPR knockout, point mutation, knock-in and overexpression models allow functional testing of genes involved in medium-chain fatty-acyl-CoA metabolism [3,8].
Why is medium-chain fatty-acyl-CoA metabolism important for energy production?
Medium-chain fatty acids are efficiently oxidized in mitochondria to produce acetyl-CoA and reducing equivalents for the citric acid cycle and oxidative phosphorylation [1,2].
Conclusion
GO:0036112 medium-chain fatty-acyl-CoA metabolic process is a fundamental biological process that connects medium-chain fatty acid handling to energy production, biosynthesis and tissue-specific disease pathology. The QuickGO definition and published literature highlight its roles in mitochondrial beta-oxidation, kidney fibrosis, cardiac metabolism and fatty acid oxidation disorders [1,2,3,4,5,6,7,8]. Continued research using CRISPR-engineered models and metabolic profiling will clarify how this pathway can be targeted for therapeutic benefit.
References
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- 2. Adeva-Andany MM et al.. 2019. Mitochondrial β-oxidation of saturated fatty acids in humans.. Mitochondrion 46:73-90 PMID: 29551309
- 3. Li J et al.. 2025. Tubular ACSM3 deficiency impairs medium-chain fatty acid metabolism and aggravates kidney fibrosis.. Proc Natl Acad Sci U S A 122(38):e2505752122 PMID: 40953271
- 4. Sharma S et al.. 2025. The Pathogenesis of Very Long-Chain Acyl-CoA Dehydrogenase Deficiency.. Biomolecules 15(3) PMID: 40149952
- 5. Scalais E et al.. 2015. Familial very long chain acyl-CoA dehydrogenase deficiency as a cause of neonatal sudden infant death: improved survival by prompt diagnosis.. Am J Med Genet A 167A(1):211-4 PMID: 25338548
- 6. Tucci S et al.. 2015. De novo fatty acid biosynthesis and elongation in very long-chain acyl-CoA dehydrogenase-deficient mice supplemented with odd or even medium-chain fatty acids.. FEBS J 282(21):4242-53 PMID: 26284828
- 7. Gaston G et al.. 2020. Cardiac tissue citric acid cycle intermediates in exercised very long-chain acyl-CoA dehydrogenase-deficient mice fed triheptanoin or medium-chain triglyceride.. J Inherit Metab Dis 43(6):1232-1242 PMID: 33448436
- 8. Odendaal C et al.. 2023. Personalised modelling of clinical heterogeneity between medium-chain acyl-CoA dehydrogenase patients.. BMC Biol 21(1):184 PMID: 37667308
