GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004149 describes the catalytic activity that transfers a succinyl group from succinyl-CoA onto a dihydrolipoyllysine residue within the 2-oxoglutarate dehydrogenase complex (OGDHC).
• The reaction is the committed step that regenerates the lipoyl arm of the E2 subunit (DLST) and produces the CoA and succinyl-dihydrolipoamide intermediates needed for mitochondrial oxidative decarboxylation of 2-oxoglutarate.
• DLST (dihydrolipoamide S-succinyltransferase) is the canonical enzyme carrying this activity, and its dysfunction is linked to mitochondrial ATP deficits when complex I is impaired.
• The activity is part of a larger multienzyme assembly that includes OGDH (E1), DLST (E2), and DLD (E3), and it is functionally coupled to the TCA cycle and to mitochondrial energy homeostasis.
• Because the reaction depends on lipoylation and CoA chemistry, it is sensitive to metabolic stress, nutritional state, and post-translational regulation of the complex.
• GO:0004149 is a molecular_function term, so it should be distinguished from the biological process of oxidative decarboxylation and from the cellular component of the OGDHC assembly.
Description
GO:0004149, dihydrolipoyllysine-residue succinyltransferase activity, is a molecular_function term that captures a single, chemically precise step in mitochondrial metabolism: the transfer of a succinyl group from succinyl-CoA to the dihydrolipoyllysine arm of the 2-oxoglutarate dehydrogenase complex component E2. This activity is essential for the catalytic cycle of the 2-oxoglutarate dehydrogenase complex (OGDHC), which links the tricarboxylic acid (TCA) cycle to oxidative phosphorylation and to the production of reducing equivalents. Researchers study this term because it defines the enzymatic identity of DLST and because defects in the OGDHC can produce measurable mitochondrial ATP deficits, especially when respiratory chain complex I is already compromised. The reaction is also a useful anchor for interpreting proteomic and metabolomic changes in tissues undergoing metabolic remodeling, such as wheat leaves exposed to phenanthrene, post-ripening Torreya grandis nuts, and human chorionic villi in recurrent pregnancy loss. In each case, the enzyme activity is part of a broader signature of mitochondrial and TCA-cycle function rather than an isolated event [1,2,3,4]. Because the term is defined by a specific donor (succinyl-CoA) and a specific acceptor (dihydrolipoyllysine), it is not interchangeable with other lipoate-dependent acyltransferases, and this specificity matters for annotation, for inhibitor design, and for interpreting disease-associated variants.
dihydrolipoyllysine-residue succinyltransferase activity At A Glance
| GO ID | GO:0004149 |
|---|---|
| GO term | dihydrolipoyllysine-residue succinyltransferase activity |
| Ontology | molecular_function |
| Synonym | dihydrolipoamide S-succinyltransferase activity; dihydrolipoamide succinyltransferase activity; dihydrolipoyl transsuccinylase activity; succinyl-CoA:dihydrolipoamide S-succinyltransferase activity |
| Major function | Transfers a succinyl group from succinyl-CoA to a dihydrolipoyllysine residue on the E2 component of the 2-oxoglutarate dehydrogenase complex |
| Reaction direction | Succinyl-CoA + dihydrolipoyllysine-E2 = CoA + succinyl-dihydrolipoyllysine-E2 |
| Cofactor / co-substrate | Lipoamide/lipoate-dependent chemistry and CoA thioester chemistry |
| Representative enzyme | DLST (dihydrolipoamide S-succinyltransferase), the E2 subunit of OGDHC |
| Pathway context | 2-oxoglutarate dehydrogenase complex and TCA-cycle flux |
What Is GO:0004149?
In plain terms, GO:0004149 is the activity that takes a succinyl group from succinyl-CoA and attaches it to a dihydrolipoyllysine residue on the E2 subunit of the 2-oxoglutarate dehydrogenase complex, releasing CoA and forming a succinyl-dihydrolipoamide intermediate. The QuickGO definition specifies the reaction as N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA. This is a molecular_function annotation: it describes what the enzyme does at the level of substrates and products, not the full pathway or the assembly state of the complex.
Why Is dihydrolipoyllysine-residue succinyltransferase activity Important in Cell Biology?
GO:0004149 matters because it defines the catalytic heart of the E2 subunit of the 2-oxoglutarate dehydrogenase complex, a mitochondrial machine that converts 2-oxoglutarate into succinyl-CoA and feeds reducing equivalents into the respiratory chain. When this activity is compromised, the downstream consequences can include reduced mitochondrial ATP production, especially in settings where complex I is already deficient. Because the reaction is chemically specific and depends on lipoylation, it is also a sensitive readout of mitochondrial metabolic state in proteomic and metabolomic studies of plant, animal, and human tissues [2,3,4]. In translational research, the same activity appears in autoimmune contexts where mitochondrial autoantigens are targeted, such as primary biliary cirrhosis, where autoreactive responses to the pyruvate dehydrogenase complex and related 2-oxo acid dehydrogenase complexes are well documented [6,8]. The term therefore connects enzymology, mitochondrial physiology, autoimmunity, and metabolic disease, making it a useful entity for annotation, biomarker interpretation, and experimental modeling [1,6,8].
• Defines the E2 catalytic step of the 2-oxoglutarate dehydrogenase complex, a key TCA-cycle and mitochondrial energy node.
• Provides a mechanistic explanation for mitochondrial ATP deficits when complex I is impaired.
• Serves as a proteomic/metabolomic marker of TCA-cycle remodeling in plants and human tissues [2,3,4].
• Connects to autoimmune disease biology through mitochondrial autoantigen responses in primary biliary cirrhosis [6,8].
• Helps distinguish lipoate-dependent succinyltransferases from other acyltransferases in annotation pipelines.
• Supports interpretation of metabolic enzyme expression changes in cardiomyocytes and other stress models.
• Is relevant to nutrition conversion and post-ripening metabolism in crop species such as Torreya grandis.
• Can be studied with CRISPR knockout, point-mutation, knock-in, and overexpression models of DLST and OGDHC components.
What Happens During dihydrolipoyllysine-residue succinyltransferase activity?
Substrate recognition and succinyl transfer
In simple terms: The enzyme picks up a succinyl group from succinyl-CoA and hands it to a swinging lipoyl arm.
The reaction begins when succinyl-CoA binds the E2 active site and the succinyl group is transferred to the dihydrolipoyllysine residue of the 2-oxoglutarate dehydrogenase complex component E2, releasing CoA. This is the defining chemistry of GO:0004149 and is the step that regenerates the acylated lipoyl arm needed for the overall OGDHC catalytic cycle. Because the acceptor is a specific dihydrolipoyllysine, the activity is distinct from other CoA-dependent acyltransferases.
Coupling to the OGDHC catalytic cycle
In simple terms: This step is one link in a chain that lets the complex convert 2-oxoglutarate into succinyl-CoA.
Within the 2-oxoglutarate dehydrogenase complex, the E1 component (OGDH) decarboxylates 2-oxoglutarate, the E2 component (DLST) carries the lipoyl arm and performs the succinyl transfer described by GO:0004149, and the E3 component (DLD) reoxidizes the lipoamide. The succinyltransferase activity is therefore not a standalone event but a coordinated part of a multienzyme assembly that produces succinyl-CoA and NADH. Defective function of this complex has been linked to exacerbated mitochondrial ATP deficits during complex I deficiency.
Lipoate dependence and redox chemistry
In simple terms: The reaction needs a lipoate cofactor that swings between reduced and acylated states.
GO:0004149 depends on the lipoyl moiety being in its dihydrolipoamide (reduced) form so that it can accept the succinyl group. After succinyl transfer, the lipoyl arm is reoxidized by the E3 component, allowing the cycle to continue. This redox-coupled chemistry explains why the activity is sensitive to the mitochondrial redox environment and to the availability of lipoate and CoA.
Integration with TCA-cycle flux and energy homeostasis
In simple terms: The activity helps keep the TCA cycle and mitochondrial energy production running.
By generating succinyl-CoA and supporting OGDHC turnover, GO:0004149 contributes to TCA-cycle flux and to mitochondrial ATP production. Proteomic studies in wheat leaves exposed to phenanthrene show TCA-cycle responses that include enzymes of this pathway, and proteomic analysis of human chorionic villi in recurrent pregnancy loss reveals dysregulated metabolic pathways that can involve mitochondrial enzymes. In cardiomyocytes, inhibition of MMP-2 expression alters metabolic enzyme expression levels, illustrating how this activity can be indirectly remodeled by cellular stress.
Nutritional and post-ripening metabolic context
In simple terms: In crops and seeds, this activity is part of the metabolic shifts that occur as tissues mature.
In Torreya grandis nuts, key genes and enzymes contributing to nutrition conversion during post-ripening include TCA-cycle and mitochondrial metabolic components. This places GO:0004149 within a broader metabolic remodeling program rather than an isolated enzymatic event. Such studies help researchers interpret how succinyltransferase activity may change with developmental and nutritional state.
Key Genes Involved in GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity
The genes and proteins most directly associated with GO:0004149 are the components of the 2-oxoglutarate dehydrogenase complex and related lipoate-dependent mitochondrial enzymes.
| Gene | Major Role | Research Relevance |
|---|---|---|
| DLST | E2 subunit of OGDHC carrying the dihydrolipoyllysine succinyltransferase activity | Core enzyme for GO:0004149; knockout and point-mutation models test catalytic and assembly functions |
| OGDH | E1 subunit that decarboxylates 2-oxoglutarate and feeds the E2 lipoyl arm | Upstream partner; its dysfunction can alter demand on GO:0004149 |
| DLD | E3 subunit that reoxidizes the lipoamide arm | Redox partner; needed for continuous turnover of the succinyltransferase reaction |
| DLAT | E2 subunit of pyruvate dehydrogenase complex, a related lipoate-dependent acyltransferase [6,8] | Autoantigen in primary biliary cirrhosis; useful comparator for lipoate-dependent autoimmunity [6,8] |
| PDHA1 | E1 subunit of pyruvate dehydrogenase complex [6,8] | Autoantigen context; helps distinguish OGDHC from PDC autoimmunity [6,8] |
| PDHB | E1 beta subunit of pyruvate dehydrogenase complex [6,8] | Related mitochondrial autoantigen; comparative disease biology [6,8] |
| MMP2 | Matrix metalloproteinase-2; its inhibition alters metabolic enzyme expression | Indirect regulator of metabolic enzyme levels in cardiomyocytes |
| NDUFS1 | Complex I subunit; complex I deficiency interacts with OGDHC dysfunction | Model context for ATP deficit studies involving GO:0004149 |
| NDUFV1 | Complex I subunit; relevant to mitochondrial ATP deficit models | Genetic background for testing OGDHC-dependent energy failure |
| SDHA | TCA-cycle enzyme adjacent to OGDHC flux | Pathway context for interpreting succinyltransferase activity |
| SDHB | TCA-cycle enzyme adjacent to OGDHC flux | Pathway context for metabolic flux studies |
| IDH2 | Mitochondrial isocitrate dehydrogenase feeding 2-oxoglutarate | Upstream metabolic node that supplies substrate for OGDHC |
| GOT2 | Mitochondrial aspartate aminotransferase linked to TCA-cycle intermediates | Metabolic context for 2-oxoglutarate and succinyl-CoA pools |
| ACO2 | Mitochondrial aconitase in the TCA cycle | Pathway marker for TCA-cycle remodeling |
| CS | Citrate synthase, TCA-cycle entry enzyme | Reference enzyme for mitochondrial metabolic studies |
| FH | Fumarate hydratase, TCA-cycle enzyme | Pathway context for succinyl-CoA and energy metabolism |
| MDH2 | Malate dehydrogenase, TCA-cycle enzyme | Pathway context for mitochondrial redox and energy state |
How Is dihydrolipoyllysine-residue succinyltransferase activity Regulated?
GO:0004149 is regulated indirectly through the assembly and post-translational control of the 2-oxoglutarate dehydrogenase complex rather than by a single dedicated transcription factor. Because the reaction depends on lipoylation of the E2 subunit and on the redox state of the lipoyl arm, changes in mitochondrial lipoate availability, CoA pools, and NAD+/NADH balance can modulate flux through this step. In complex I deficiency, defective OGDHC function can exacerbate mitochondrial ATP deficits, indicating that the activity is sensitive to the broader respiratory chain context. Metabolic stress and nutritional state also remodel TCA-cycle enzyme expression, as seen in wheat leaves exposed to phenanthrene and in post-ripening Torreya grandis nuts. In cardiomyocytes, inhibition of MMP-2 expression affects metabolic enzyme expression levels, showing that extracellular matrix signaling can indirectly influence mitochondrial metabolic enzymes. Autoimmune responses to mitochondrial 2-oxo acid dehydrogenase complexes in primary biliary cirrhosis further illustrate that immune recognition can target these enzymes, although this is a disease-associated phenomenon rather than a canonical regulatory mechanism [6,8].
dihydrolipoyllysine-residue succinyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| DLST | Mitochondrial energy failure and OGDHC dysfunction | DLST knockout or point-mutation cell models with mitochondrial ATP readouts |
| OGDH | Complex I deficiency-associated ATP deficits | OGDH knockout combined with complex I inhibition |
| DLD | Redox imbalance in 2-oxo acid dehydrogenase complexes | DLD knockout or rescue with lipoate supplementation |
| DLAT | Primary biliary cirrhosis autoimmunity [6,8] | Autoantigen expression and autoantibody profiling models [6,8] |
| PDHA1 | Primary biliary cirrhosis autoimmunity [6,8] | PDC component knockout and autoantibody response studies [6,8] |
Mitochondrial energy failure and complex I deficiency
Defective function of the 2-oxoglutarate dehydrogenase complex, which houses GO:0004149, exacerbates mitochondrial ATP deficits during complex I deficiency. This links the succinyltransferase activity to mitochondrial disease biology and to conditions where respiratory chain impairment limits energy production. Experimental models that combine complex I lesions with OGDHC perturbations can test whether the succinyltransferase step is rate-limiting for ATP maintenance.
Primary biliary cirrhosis and mitochondrial autoimmunity
Primary biliary cirrhosis is characterized by peculiar autoimmunity directed against mitochondrial 2-oxo acid dehydrogenase complexes, including the pyruvate dehydrogenase complex and related lipoate-dependent enzymes. Autoreactive responses to the pyruvate dehydrogenase complex are well documented in the pathogenesis of this disease. Although GO:0004149 is specific to the 2-oxoglutarate dehydrogenase complex E2, the shared lipoate-dependent chemistry and structural similarity of these complexes make this disease context relevant for understanding how mitochondrial autoantigens are recognized [6,8].
Reproductive and developmental metabolic stress
Proteomics analysis of human chorionic villi reveals dysregulated pathways that contribute to recurrent pregnancy loss, including metabolic pathways that can involve mitochondrial enzymes. This suggests that mitochondrial metabolic activity, including TCA-cycle and OGDHC-related steps, may be relevant to pregnancy maintenance. The finding is descriptive, and direct causal links to GO:0004149 require further experimental validation.
Neurodevelopmental and immune-metabolic contexts
A mouse strain with autistic-like behavior shows immunity and autoantibody features that can include mitochondrial antigens. This places mitochondrial metabolic enzymes within a broader immune-metabolic landscape, although the specific relationship to GO:0004149 is not established by that study alone. Such models are useful for hypothesis generation about how mitochondrial autoimmunity and metabolism intersect.
From dihydrolipoyllysine-residue succinyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is DLST catalytic activity required for OGDHC flux? | DLST knockout cell line with succinyltransferase activity assay |
| Does a patient variant alter succinyl transfer? | DLST point-mutation knock-in cell line |
| Can a tagged DLST report complex assembly? | Tagged knock-in of DLST with affinity purification |
| Does DLST overexpression change mitochondrial ATP? | DLST overexpression cell line with ATP measurements |
| Does complex I deficiency sensitize cells to OGDHC loss? | DLST knockout in a complex I-deficient background |
| Can metabolic enzyme expression be remodeled by MMP-2 inhibition? | Cardiomyocyte model with MMP-2 knockdown and proteomics |
How to Study the dihydrolipoyllysine-residue succinyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Succinyltransferase activity assay | Enzymatic transfer of succinyl groups from succinyl-CoA | Testing DLST variants and knockouts |
| Proteomics | Abundance of DLST and OGDHC components [3,4,7] | Metabolic remodeling in tissues and cells [3,4,7] |
| Metabolomics | TCA-cycle intermediates including succinyl-CoA | Pathway flux interpretation |
| Respirometry | Mitochondrial oxygen consumption | Energy metabolism in OGDHC models |
| ATP luminescence | Cellular ATP levels | Complex I deficiency and OGDHC dysfunction |
| Autoantibody profiling | Immune recognition of mitochondrial antigens [6,8] | Primary biliary cirrhosis research [6,8] |
| Western blot | Protein expression of DLST, OGDH, DLD | Validation of CRISPR models |
| Immunoprecipitation | Complex assembly and interactions | Tagged knock-in studies |
Enzymatic activity assays
Direct measurement of dihydrolipoyllysine-residue succinyltransferase activity uses succinyl-CoA and a dihydrolipoamide substrate, often coupled to NADH production through the OGDHC reaction. These assays are the most direct way to test whether a variant or knockout affects GO:0004149 specifically. They are typically performed on mitochondrial lysates or purified complex preparations.
Proteomics and metabolomics
Proteomic studies can quantify DLST and other OGDHC components across conditions, as shown in wheat leaves exposed to phenanthrene, human chorionic villi in recurrent pregnancy loss, and cardiomyocytes with MMP-2 inhibition. Metabolomic profiling of TCA-cycle intermediates complements these data by showing whether succinyl-CoA and related metabolites change. Together, these methods place GO:0004149 within a broader metabolic network [1,3,4,7].
Mitochondrial function and ATP measurements
Because OGDHC dysfunction can exacerbate mitochondrial ATP deficits during complex I deficiency, ATP measurements and respirometry are useful readouts for models targeting GO:0004149. These assays connect the enzymatic activity to cellular energy homeostasis. They are especially informative when combined with genetic perturbations of complex I subunits.
Autoantibody and immune profiling
In primary biliary cirrhosis, autoantibody profiling against mitochondrial 2-oxo acid dehydrogenase complexes is a key research method [6,8]. These approaches can reveal whether lipoate-dependent enzymes are recognized by the immune system [6,8]. They are relevant for understanding the disease context of mitochondrial autoantigens, even when the primary target is a related complex [6,8].
How CRISPR Can Be Used to Study GO:0004149 dihydrolipoyllysine-residue succinyltransferase activity
Knockout
CRISPR knockout of DLST removes the E2 subunit that carries GO:0004149, allowing researchers to test whether the succinyltransferase activity is required for OGDHC flux and mitochondrial ATP production. Knockout models are also useful for distinguishing the catalytic function of DLST from its structural role in complex assembly. In complex I-deficient backgrounds, DLST knockout can reveal synthetic effects on energy homeostasis.
Point Mutation
Point-mutation models can target the catalytic residues or lipoyl-lysine acceptor site of DLST to dissect the mechanism of succinyl transfer without eliminating the protein. These models help determine whether a specific residue is required for GO:0004149 activity versus for complex stability. They are also useful for testing patient-derived variants of uncertain significance.
Knock-in
Knock-in of epitope-tagged DLST enables affinity purification and localization studies of the OGDHC E2 subunit. Tagged knock-in can also be used to monitor complex assembly and turnover in live cells. This approach preserves endogenous regulation better than overexpression.
Overexpression
Overexpression of DLST or other OGDHC components can test whether increasing succinyltransferase activity changes TCA-cycle flux or mitochondrial ATP levels. Overexpression models are useful for gain-of-function studies and for testing whether the activity is limiting under stress. They should be interpreted alongside knockout data to avoid artifacts from supraphysiological expression.
How EDITGENE Supports dihydrolipoyllysine-residue succinyltransferase activity Research
Researchers studying dihydrolipoyllysine-residue succinyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in OGDHC function, mitochondrial energy homeostasis, or disease-associated metabolic remodeling. EDITGENE provides CRISPR-based cell model services that allow precise interrogation of DLST and related genes at the knockout, point-mutation, knock-in, and overexpression levels.
Contact EDITGENE today to design your custom CRISPR model for dihydrolipoyllysine-residue succinyltransferase activity research.
Frequently Asked Questions About dihydrolipoyllysine-residue succinyltransferase activity
What is GO:0004149?
GO:0004149 is the molecular_function term for dihydrolipoyllysine-residue succinyltransferase activity, which transfers a succinyl group from succinyl-CoA to a dihydrolipoyllysine residue on the E2 subunit of the 2-oxoglutarate dehydrogenase complex.
What does dihydrolipoyllysine-residue succinyltransferase activity do?
It catalyzes the succinyl transfer step that regenerates the acylated lipoyl arm of the OGDHC E2 subunit, releasing CoA and forming a succinyl-dihydrolipoamide intermediate.
Which gene encodes the enzyme for GO:0004149?
DLST encodes the E2 subunit of the 2-oxoglutarate dehydrogenase complex, which carries the dihydrolipoyllysine-residue succinyltransferase activity.
What genes are involved in dihydrolipoyllysine-residue succinyltransferase activity?
The main genes are DLST (E2), OGDH (E1), and DLD (E3), which together form the 2-oxoglutarate dehydrogenase complex.
Why is GO:0004149 important for mitochondria?
It supports TCA-cycle flux and mitochondrial ATP production, and its dysfunction can exacerbate ATP deficits during complex I deficiency.
Is GO:0004149 a molecular function or a biological process?
GO:0004149 is a molecular_function term; it describes a specific catalytic activity rather than a whole pathway or process.
How is dihydrolipoyllysine-residue succinyltransferase activity measured?
It is measured using succinyl-CoA and a dihydrolipoamide substrate, often coupled to NADH production through the OGDHC reaction.
What diseases are linked to OGDHC and GO:0004149?
Mitochondrial energy failure and complex I deficiency are linked to OGDHC dysfunction, and related lipoate-dependent complexes are targeted in primary biliary cirrhosis autoimmunity [1,6,8].
Can CRISPR be used to study GO:0004149?
Yes, CRISPR knockout, point-mutation, knock-in, and overexpression models of DLST and OGDHC components can be used to study this activity.
What is the difference between GO:0004149 and pyruvate dehydrogenase complex activity?
GO:0004149 is specific to the 2-oxoglutarate dehydrogenase complex E2 subunit, whereas pyruvate dehydrogenase complex enzymes use pyruvate and have distinct subunit identities, although both are lipoate-dependent [1,6,8].
Conclusion
GO:0004149 defines a chemically precise and biologically central step in mitochondrial metabolism: the succinyl transfer reaction carried out by the E2 subunit of the 2-oxoglutarate dehydrogenase complex. Its importance extends from TCA-cycle flux and ATP production to disease contexts such as complex I deficiency and mitochondrial autoimmunity [1,6,8]. Because the activity is lipoate-dependent and tightly integrated with the OGDHC assembly, it is best studied with a combination of enzymatic assays, proteomics, metabolomics, and CRISPR-based genetic models [1,3,4,7]. Researchers can use these approaches to determine whether DLST and related genes are causally involved in metabolic and disease phenotypes.
References
- 1. Piroli GG et al.. 2023. Defective function of α-ketoglutarate dehydrogenase exacerbates mitochondrial ATP deficits during complex I deficiency.. Redox Biol 67:102932 PMID: 37883842
- 2. Song L et al.. 2022. Identification of key genes and enzymes contributing to nutrition conversion of Torreya grandis nuts during post-ripening process.. Food Chem 384:132454 PMID: 35228003
- 3. Shen Y et al.. 2019. Phenanthrene-triggered tricarboxylic acid cycle response in wheat leaf.. Sci Total Environ 665:107-112 PMID: 30772538
- 4. Davalieva K et al.. 2024. Proteomics Analysis of Human Chorionic Villi Reveals Dysregulated Pathways That Contribute to Recurrent Pregnancy Loss.. Proteomics Clin Appl 18(6):e202400020 PMID: 39182192
- 5. Uddin MN et al.. 2020. Immunity and autoantibodies of a mouse strain with autistic-like behavior.. Brain Behav Immun Health 4:100069 PMID: 34589851
- 6. Mackay IR et al.. 2000. The peculiar autoimmunity of primary biliary cirrhosis.. Immunol Rev 174:226-37 PMID: 10807519
- 7. Lin HB et al.. 2014. Inhibition of MMP-2 expression affects metabolic enzyme expression levels: proteomic analysis of rat cardiomyocytes.. J Proteomics 106:74-85 PMID: 24769238
- 8. Yeaman SJ et al.. 2000. Autoreactive responses to pyruvate dehydrogenase complex in the pathogenesis of primary biliary cirrhosis.. Immunol Rev 174:238-49 PMID: 10807520
