The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested protein is unambiguously human SIRT5/SIR2L5, UniProt Q9NXA8. The accession is explicitly assigned to SIRT5 in a 2024 biochemical study, and the literature consistently identifies the protein as a class-III, NAD⁺-dependent sirtuin deacylase concentrated in the mitochondrial matrix. Its domain architecture—a Rossmann-like NAD-binding domain, small zinc-binding sirtuin domain, and catalytic cleft—is concordant with the supplied UniProt/InterPro annotations. No conflicting gene or organism identity was encountered. (fiorentino2022therapeuticpotentialand pages 3-5, bohl2024inhibitionofsirtuin pages 1-3, shen2024mitochondrialsirtuinsin pages 3-5)
SIRT5’s primary biochemical function is not conventional lysine deacetylation. It preferentially hydrolyzes negatively charged lysine acyl modifications—especially glutaryl-, succinyl-, and malonyl-lysine—using NAD⁺ and producing deacylated protein, nicotinamide, and 2′-O-acyl-ADP-ribose. Its best-established physiological role is therefore to control mitochondrial protein acylation generated by reactive acyl-CoA metabolites, thereby tuning nitrogen disposal, central-carbon and lipid metabolism, respiration, and oxidative-stress defenses. (fiorentino2022therapeuticpotentialand pages 2-3, fiorentino2022therapeuticpotentialand pages 3-5, fiorentino2022therapeuticpotentialand pages 1-2)
Four human isoforms have been reported. The canonical form is imported into mitochondria through an N-terminal targeting sequence and is concentrated in the mitochondrial matrix. Isoform 2 lacks 11 C-terminal residues, isoform 3 lacks an internal 18-residue segment, and isoform 4 lacks 108 N-terminal residues—including the mitochondrial targeting sequence—and is consequently associated with the cytosol. Isoforms 2–4 appear much less abundant than the canonical form in surveyed human cells. Smaller pools have also been detected in the cytosol, nucleus, and peroxisomes. (fiorentino2022therapeuticpotentialand pages 2-3, fiorentino2022therapeuticpotentialand pages 3-5)
Localization is condition dependent rather than absolute. A November 26, 2024 mouse study found strong recruitment of SIRT5 to hepatic peroxisomes during dodecanedioic-acid metabolism, while earlier work detected peroxisomal SIRT5 in human HepG2 and Huh7 cells. Thus, the correct annotation is predominantly mitochondrial, with isoform- and metabolic-state-dependent extramitochondrial localization, not “mitochondria only.” (zhang2024sirtuin5isrecruited pages 1-2)
For an acylated lysine in a protein substrate, the overall reaction is:
protein–Lys–acyl + NAD⁺ + H₂O → protein–Lys + nicotinamide + 2′-O-acyl-ADP-ribose.
The mechanism begins with NAD⁺ glycosidic-bond cleavage and formation of an acyl-imidate intermediate. Attack by the ADP-ribose 2′-hydroxyl generates a bicyclic intermediate, whose collapse releases deacylated lysine and acyl-ADP-ribose. Human SIRT5 crystal structures captured a succinyl-peptide complex and the bicyclic intermediate, providing direct structural support for this chemistry. Nicotinamide can drive the reverse “base-exchange” step and consequently inhibit sirtuins. (rajabi2017mechanismbasedinhibitorsof pages 6-10, fiorentino2022therapeuticpotentialand pages 1-2, sharma2023multifunctionalactivitybasedchemical pages 1-2)
Reported catalytic efficiencies are approximately 18,699 M⁻¹s⁻¹ for deglutarylation, 13,995 for desuccinylation, 3,758 for demalonylation, and only 16 for deacetylation. On these assays, deglutarylation is about 1,169-fold and desuccinylation about 875-fold more efficient than deacetylation. Thus, annotations that describe SIRT5 chiefly as a histone or protein “deacetylase” are chemically misleading. (fiorentino2022therapeuticpotentialand pages 2-3, fiorentino2022therapeuticpotentialand pages 1-2)
Specificity is encoded by Tyr102 and Arg105, which form hydrogen-bonding and electrostatic interactions with the terminal carboxylate of negatively charged acyl groups. Ala86 helps provide space for bulky glutaryl/succinyl substrates. Mutating Tyr102 and Arg105 shifts SIRT5 toward deacetylation, experimentally demonstrating that these residues determine acyl preference rather than merely accompanying it structurally. (fiorentino2022therapeuticpotentialand pages 3-5, yu2016roleofthe pages 24-25)
The relevant substrate is an acylated lysine within a protein or peptide, not free succinate, malonate, or glutarate. Many mitochondrial acylations can arise nonenzymatically because reactive succinyl-CoA and related acyl-CoAs encounter exposed lysines in the alkaline mitochondrial matrix. SIRT5 acts as an acyl-damage-control and regulatory enzyme, although not every acylation site altered after SIRT5 loss is necessarily its direct substrate. (zhao2024upregulatedsuccinylationmodifications pages 1-3, zhang2024sirtuin5isrecruited pages 1-2)
Carbamoyl-phosphate synthetase 1 (CPS1) is the canonical physiological target. SIRT5-dependent deacylation increases CPS1 activity, supporting mitochondrial conversion of ammonia into carbamoyl phosphate and hepatic urea-cycle flux, especially under conditions demanding increased nitrogen disposal. Foundational work initially framed this as deacetylation; subsequent discovery of SIRT5’s strong desuccinylase activity and mitochondrial succinylome established negatively charged deacylation as its dominant chemistry. The CPS1 evidence is strong mechanistically but derives mainly from purified proteins and mouse liver rather than human intervention studies. (zhou2012structurefunctionstudieson pages 66-71, yu2016roleofthe pages 24-25, shen2024mitochondrialsirtuinsin pages 3-5)
SIRT5-regulated substrates occur throughout glycolysis/gluconeogenesis, the TCA cycle, electron-transport chain, glutamine and amino-acid metabolism, ketogenesis, and oxidative phosphorylation. Demalonylation is particularly enriched on glycolytic enzymes, and SIRT5-null mouse hepatocytes exhibit reduced glycolytic flux. SIRT5 can also support antioxidant capacity through substrates including IDH2 and G6PD, coupling mitochondrial or pentose-phosphate metabolism to NADPH production and ROS control. (shen2024mitochondrialsirtuinsin pages 20-21, fiorentino2022therapeuticpotentialand pages 3-5)
Recent mechanistic examples sharpen this broad annotation. In a 2023 disc-degeneration study, reduced SIRT5 increased AIFM1 succinylation, disrupted AIFM1–CHCHD4 binding, lowered electron-transport-chain subunits, and impaired mitochondrial protein import and respiration. SIRT5 overexpression or methylene blue improved disease measures in rat models, but this remains preclinical. (mao2023sirt5relateddesuccinylationmodification pages 1-2)
SIRT5 regulates mitochondrial fatty-acid oxidation through direct deacylation of enzymes such as VLCAD and contributes to ketone-body production through HMGCS2-related regulation. In recombinant human VLCAD, SIRT5 desuccinylates K299 near the FAD-binding site and K482/K492/K507 in a cardiolipin-binding region; deacylation restores mitochondrial-membrane association, illustrating that SIRT5 can regulate both catalytic activity and protein localization. (fiorentino2022therapeuticpotentialand pages 2-3, fiorentino2022therapeuticpotentialand pages 23-24)
Its peroxisomal effect is more nuanced. In dodecanedioic-acid-fed mice, SIRT5 knockout impaired peroxisomal β-oxidation, yet proteomics found no coherent global pattern of direct peroxisomal SIRT5 sites. Recombinant SIRT5 partially desuccinylated ACOX1 and EHHADH; this did not alter ACOX1a or EHHADH activity and reduced ACOX1b activity by about 15%. Consequently, peroxisomal SIRT5 is experimentally supported, but a simple model in which it globally activates peroxisomal β-oxidation is not. (zhang2024sirtuin5isrecruited pages 8-10, zhang2024sirtuin5isrecruited pages 1-2)
By maintaining IDH2/G6PD-related reducing capacity and deacylating antioxidant or detoxification enzymes, SIRT5 generally limits ROS under metabolic stress. A 2024 acetaminophen-overdose study identified ALDH2 K385 as a causal substrate: APAP reduced SIRT5 in mouse liver and AML12 hepatocytes; SIRT5 deficiency worsened oxidative stress, inflammation, and injury, whereas AAV-mediated overexpression was protective. K385 desuccinylation preserved ALDH2 activity, and K385 succinylation abolished the protection. Most mouse comparisons used six animals per group. (yu2024sirtuin5‐mediateddesuccinylation pages 1-4)
SIRT5 itself is redox regulated. Bohl et al., published October 1, 2024, verified Q9NXA8 and showed that peroxynitrite delivered through SIN-1 nitrates human SIRT5, including sites in its catalytic core, and inhibits desuccinylase activity. No detectable SIRT5 cysteine sulfenylation was found under those conditions. This offers a mechanistic explanation for loss of SIRT5 function during nitroxidative stress, although the experiment used purified proteins and requires in-vivo validation. DOI: https://doi.org/10.1021/acs.biochem.4c00257. (bohl2024inhibitionofsirtuin pages 1-3)
SIRT5 also acts beyond intermediary metabolism. A PNAS study published April 18, 2024 showed that SIRT5 desuccinylates mitochondrial-antiviral-signaling protein MAVS at K7, reducing MAVS aggregation and functioning as a brake on RIG-I-like-receptor/type-I-interferon signaling. SIRT3-mediated deacetylation at the same lysine has the opposite effect. Sirt3/Sirt5 double-deficient mice had viral susceptibility comparable with wild type, counteracting the susceptibility produced by Sirt3 loss. This demonstrates that competing acyl states at one lysine can tune pathway output. (liu2024dualmodifyingof pages 1-2)
The following table distinguishes human evidence from animal and cell models and summarizes the strongest recent quantitative findings.
| Aspect or target | Compartment or pathway | Molecular action or site | Experimental evidence or model | Key quantitative result | Interpretation or limitation | Source date and DOI URL |
|---|---|---|---|---|---|---|
| Core catalytic specificity | Mainly mitochondrial matrix; class III sirtuin catalytic core | NAD⁺-dependent removal of glutaryl-, succinyl-, and malonyl-lysine; weak deacetylation. Products are deacylated lysine, nicotinamide, and 2′-O-acyl-ADP-ribose. Tyr102 and Arg105 recognize the anionic acyl group; Ala86 accommodates bulky substrates. | Recombinant human SIRT5, enzyme kinetics, crystallography, and mutagenesis | Catalytic efficiencies: deglutarylation 18,699, desuccinylation 13,995, demalonylation 3,758, and deacetylation 16 M⁻¹ s⁻¹; approximately 1,000-fold preference over deacetylation | Establishes negatively charged lysine deacylation, rather than conventional deacetylation, as the primary biochemical function. Peptide kinetics may not fully reproduce full-length-protein selectivity. | July 2022; 10.1021/acs.jmedchem.2c00687 (fiorentino2022therapeuticpotentialand pages 2-3, fiorentino2022therapeuticpotentialand pages 3-5, fiorentino2022therapeuticpotentialand pages 1-2) |
| CPS1 | Mitochondrial matrix; hepatic urea cycle and ammonia detoxification | SIRT5-dependent deacylation increases carbamoyl-phosphate synthetase 1 activity | Purified enzyme, liver CPS1, and Sirt5-knockout mouse studies; principally nonhuman and preclinical | SIRT5 loss altered CPS1 acylation and compromised the adaptive urea-cycle response; no human intervention data | Canonical physiological substrate linking SIRT5 to nitrogen disposal. Early work described deacetylation, whereas later evidence established desuccinylation as SIRT5’s dominant chemistry. | 2009–2013 foundational studies; 10.1016/j.cell.2009.02.026 and 10.1016/j.molcel.2013.06.001 (zhou2012structurefunctionstudieson pages 66-71, yu2016roleofthe pages 24-25, shen2024mitochondrialsirtuinsin pages 3-5) |
| ALDH2 K385 | Mitochondria; aldehyde detoxification and oxidative-stress control in acetaminophen liver injury | Desuccinylates ALDH2 at K385, preserving ALDH2 activity | Mouse liver, AML12 mouse hepatocytes, knockout and AAV overexpression, quantitative succinylomics, site mutants, and puerarin virtual screening; preclinical | Most animal comparisons used n = 6 per group. APAP lowered SIRT5; loss worsened injury, whereas overexpression reduced injury, inflammation, and oxidative stress. | Strong site-specific causal chain, but puerarin is not established as a selective SIRT5 activator and efficacy has not been demonstrated clinically. | August 2024; 10.1002/advs.202402710 (yu2024sirtuin5‐mediateddesuccinylation pages 1-4) |
| AIFM1 | Mitochondrial intermembrane-space protein import, ETC maintenance, and disc-cell homeostasis | Desuccinylates AIFM1, preserving its interaction with CHCHD4 and the abundance of ETC complex subunits | Human degenerative-disc observations supplemented by rat nucleus-pulposus cells, a rat compression model, Sirt5-knockout mice, IP-MS, and co-IP; preclinical | Rat treatment groups used n = 5. Lentiviral Sirt5 or methylene blue improved compression-induced degeneration. | Supports mitochondrial protein import as a downstream mechanism, but the precise causal lysine site and clinical efficacy remain unresolved. | January 18, 2023; 10.1038/s12276-023-00928-y (mao2023sirt5relateddesuccinylationmodification pages 1-2) |
| MAVS K7 | Mitochondrial outer membrane; RIG-I-like receptor and type-I-interferon signaling | Desuccinylates MAVS at K7, reducing MAVS aggregation and acting as a brake on antiviral signaling; opposes SIRT3-mediated K7 deacetylation | Human H1299 cells plus mouse and zebrafish genetic infection models; preclinical | Sirt3 and Sirt5 double-knockout mice showed viral susceptibility comparable with wild type, counteracting the susceptibility associated with Sirt3 loss alone. | Demonstrates a signaling role beyond intermediary metabolism. The outcome depends on competing acyl modifications and infection context. | April 18, 2024; 10.1073/pnas.2314201121 (liu2024dualmodifyingof pages 1-2) |
| c-MYC K369 | Nuclear or cytosolic oncogenic signaling in chordoma | Interacts with c-MYC and lowers its succinylation at K369 | Human chordoma tissues and U-CH1 or U-CH2 cells, HEK293T site assays, and mouse xenografts; preclinical | Cohort included 26 patients, divided into 13 high- and 13 low-SIRT5 cases. SIRT5 silencing reduced proliferation, migration, invasion, and xenograft growth. | Suggests a tumor-promoting SIRT5–c-MYC axis, but the cohort was small and site-specific biochemistry relied partly on overexpression systems. | March 2024; 10.1186/s12885-024-12140-w (jiang2024sirt5promotemalignant pages 1-2) |
| ACOX1 and EHHADH | Hepatic peroxisomes; dicarboxylic-fatty-acid beta-oxidation | Stress-dependent peroxisomal recruitment; partially desuccinylates ACOX1 isoforms and EHHADH | Sirt5-knockout and wild-type mice fed dodecanedioic acid; purified peroxisomes, flux assays, co-IP, and recombinant proteins; preclinical | n = 5 per group; 253 succinylated peptides from 45 proteins quantified; SIRT5 co-immunoprecipitated with 15 proteins; ACOX1b activity fell by approximately 15% after in-vitro desuccinylation. | Confirms conditional peroxisomal localization and impaired beta-oxidation after knockout, but found no coherent SIRT5-dependent peroxisomal succinylome. ACOX1a and EHHADH activity were unchanged. | November 26, 2024; 10.3390/biom14121508 (zhang2024sirtuin5isrecruited pages 8-10, zhang2024sirtuin5isrecruited pages 1-2) |
| Rheumatoid-arthritis succinylome | Human fibroblast-like synoviocytes; amino-acid and fatty-acid metabolism | siRNA depletion of SIRT5 changes protein abundance and lysine succinylation | Primary human RA synovial fibroblasts, anti-succinyllysine enrichment, and LC–MS/MS; ex-vivo and preclinical | 679 proteins and 2,471 sites detected; 436 proteins and 1,548 sites differed; 48 sites increased in 38 proteins and 144 sites decreased in 82 proteins. | Broad association with RA metabolism and candidate biomarkers, but bidirectional changes show that not every site is a direct SIRT5 substrate. Clinical validation was limited. | May 2024; 10.5582/irdr.2023.01114 (shi2024lysinesuccinylationanalysis pages 1-2) |
| Microglial senescence | Mitochondrial energy metabolism, succinate dehydrogenase, fatty-acid oxidation, ROS, and neuroinflammation | Sirt5 knockdown raises succinylation and alters SDH and ECHA function, shifting cells from adaptable oxidative metabolism toward glycolysis | Mouse BV2 microglial cells, LPS activation, site mutants, enzyme assays, and rodent in-vivo succinyl-phosphonate experiments; preclinical | Knockdown significantly increased senescence genes, ROS, lipid droplets, and lipid peroxidation; numerical effect sizes were not reported in the abstract. | Supports metabolic consequences of impaired desuccinylation, but uses a mouse cell line and a nonspecific succinylation-lowering intervention rather than human microglia or a selective SIRT5 drug. | November 2024; 10.1186/s12974-024-03284-4 (zhao2024upregulatedsuccinylationmodifications pages 1-3) |
| Histone-desuccinylation caveat | Nucleus and chromatin | Class-I HDAC1, HDAC2, and HDAC3, rather than SIRT5, remove most bulk and promoter histone succinylation | CRISPR SIRT5-knockout human HeLa cells, HDAC depletion or inhibition, purified complexes, and genomic profiling | SIRT5 loss broadly increased cellular protein succinylation but did not increase histone succinylation. Treatment with 1 μM TSA for 3 hours substantially elevated histone succinylation. | Restricts functional annotation: SIRT5 is a major metabolic-protein deacylase, not the principal cellular histone desuccinylase. Isolated histone-peptide activity should not be interpreted as a dominant nuclear role. | August 2023; 10.1038/s41421-023-00573-9 (li2023hdac123aremajor pages 1-2) |
Table: Evidence linking verified human SIRT5/Q9NXA8 chemistry to major substrates, pathways, and recent disease models. Human observations are separated from animal or cell-model findings, with translational limitations stated explicitly.
Additional notable findings include the following:
SIRT5’s anionic substrate pocket permits selective mechanism-based inhibitor design. Thiourea/thioacyl-lysine analogues exploit formation of a long-lived ADP-ribose thioimidate intermediate, and human SIRT5 inhibitor complexes have been structurally solved. Activity-based probes use thiosuccinylated or related peptide warheads plus photo-crosslinkers and click handles to label active SIRT5, enrich it from biological samples, and conduct competition-based inhibitor screening. A 2023 RSC Advances study demonstrated this general probe platform with recombinant SIRT5(34–302) and human sirtuin systems. (rajabi2017mechanismbasedinhibitorsof pages 6-10, sharma2023multifunctionalactivitybasedchemical pages 1-2)
The therapeutic strategy is necessarily context dependent:
The field remains preclinical. The 2022 medicinal-chemistry assessment concluded that only a few cellularly active peptide inhibitors existed and that potent, selective, drug-like small molecules remained a major unmet need. Later reviews describe additional inhibitor chemotypes and candidate activators, but the retrieved clinical-trial search found no relevant interventional SIRT5 trial. Puerarin, succinyl phosphonate, methylene blue, and genetic overexpression should therefore be regarded as experimental pathway interventions, not clinically validated SIRT5 therapies. (shen2024mitochondrialsirtuinsin pages 20-21, fiorentino2022therapeuticpotentialand pages 1-2, yu2024sirtuin5‐mediateddesuccinylation pages 1-4, mao2023sirt5relateddesuccinylationmodification pages 1-2)
The most defensible functional annotation is:
SIRT5 is a predominantly mitochondrial NAD⁺-dependent protein lysine deacylase specialized for negatively charged glutaryl, succinyl, and malonyl modifications. It maintains metabolic-enzyme function and mitochondrial homeostasis by coupling the cellular NAD⁺ state to removal of reactive acyl-CoA-derived protein modifications.
Three qualifications are important.
First, proteome-wide hypersuccinylation after knockout establishes SIRT5 as a major regulator but does not prove direct enzymatic targeting at every altered site. Changes in substrate flux, acyl-CoA abundance, protein expression, or organelle physiology can produce indirect and even counter-directional effects, as illustrated by the peroxisomal and RA datasets. (shi2024lysinesuccinylationanalysis pages 1-2, zhang2024sirtuin5isrecruited pages 8-10)
Second, the biological consequence of desuccinylation is substrate specific. It can activate CPS1 or ALDH2, restore VLCAD membrane binding, reduce ACOX1b activity, or restrain MAVS signaling. “Desuccinylation activates proteins” is therefore not a valid general rule. (shen2024mitochondrialsirtuinsin pages 3-5, zhang2024sirtuin5isrecruited pages 1-2, yu2024sirtuin5‐mediateddesuccinylation pages 1-4, liu2024dualmodifyingof pages 1-2)
Third, disease directionality is tissue dependent. Authoritative 2022–2024 reviews describe SIRT5 as protective in many cardiac, neuronal, and oxidative-stress settings but either tumor-promoting or tumor-suppressive according to cancer genotype and metabolic state. This Janus behavior argues for compartment-, substrate-, and disease-selective modulation rather than systemic activation or inhibition. (shen2024mitochondrialsirtuinsin pages 20-21, fiorentino2022therapeuticpotentialand pages 1-2)
References
(fiorentino2022therapeuticpotentialand pages 3-5): Francesco Fiorentino, Carola Castiello, Antonello Mai, and Dante Rotili. Therapeutic potential and activity modulation of the protein lysine deacylase sirtuin 5. Journal of Medicinal Chemistry, 65:9580-9606, Jul 2022. URL: https://doi.org/10.1021/acs.jmedchem.2c00687, doi:10.1021/acs.jmedchem.2c00687. This article has 65 citations and is from a highest quality peer-reviewed journal.
(bohl2024inhibitionofsirtuin pages 1-3): Kelsey S. Bohl, Sarah L. Wynia-Smith, Rachel A. Jones Lipinski, and Brian C. Smith. Inhibition of sirtuin deacylase activity by peroxynitrite. Biochemistry, 63:2463-2476, Sep 2024. URL: https://doi.org/10.1021/acs.biochem.4c00257, doi:10.1021/acs.biochem.4c00257. This article has 7 citations and is from a peer-reviewed journal.
(shen2024mitochondrialsirtuinsin pages 3-5): Hui Shen, Wei Ma, Yue Hu, Yuan Liu, Yaowen Song, Leilei Fu, and Zheng Qin. Mitochondrial sirtuins in cancer: a revisited review from molecular mechanisms to therapeutic strategies. Theranostics, 14:2993-3013, May 2024. URL: https://doi.org/10.7150/thno.97320, doi:10.7150/thno.97320. This article has 33 citations and is from a domain leading peer-reviewed journal.
(fiorentino2022therapeuticpotentialand pages 2-3): Francesco Fiorentino, Carola Castiello, Antonello Mai, and Dante Rotili. Therapeutic potential and activity modulation of the protein lysine deacylase sirtuin 5. Journal of Medicinal Chemistry, 65:9580-9606, Jul 2022. URL: https://doi.org/10.1021/acs.jmedchem.2c00687, doi:10.1021/acs.jmedchem.2c00687. This article has 65 citations and is from a highest quality peer-reviewed journal.
(fiorentino2022therapeuticpotentialand pages 1-2): Francesco Fiorentino, Carola Castiello, Antonello Mai, and Dante Rotili. Therapeutic potential and activity modulation of the protein lysine deacylase sirtuin 5. Journal of Medicinal Chemistry, 65:9580-9606, Jul 2022. URL: https://doi.org/10.1021/acs.jmedchem.2c00687, doi:10.1021/acs.jmedchem.2c00687. This article has 65 citations and is from a highest quality peer-reviewed journal.
(zhang2024sirtuin5isrecruited pages 1-2): Yuxun Zhang, Bob B. Zhang, Sivakama S. Bharathi, Joanna Bons, Jacob P. Rose, Samah Shah, Steven F. Dobrowolski, Sunder Sims-Lucas, Birgit Schilling, and Eric S. Goetzman. Sirtuin-5 is recruited to hepatic peroxisomes in mice fed dodecanedioic acid but has little impact on the peroxisomal succinylome. Biomolecules, 14:1508, Nov 2024. URL: https://doi.org/10.3390/biom14121508, doi:10.3390/biom14121508. This article has 4 citations.
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(mao2023sirt5relateddesuccinylationmodification pages 1-2): Jianxin Mao, Di Wang, Dong Wang, Qi Wu, Qiliang Shang, Chu Gao, Huanbo Wang, Han Wang, Mu Du, Pandi Peng, Haoruo Jia, Xiaolong Xu, Jie Wang, Liu Yang, and Zhuojing Luo. Sirt5-related desuccinylation modification of aifm1 protects against compression-induced intervertebral disc degeneration by regulating mitochondrial homeostasis. Jan 2023. URL: https://doi.org/10.1038/s12276-023-00928-y, doi:10.1038/s12276-023-00928-y. This article has 76 citations and is from a peer-reviewed journal.
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(yu2024sirtuin5‐mediateddesuccinylation pages 1-4): Qiwen Yu, Jiakai Zhang, Jiye Li, Yaodong Song, Jie Pan, Chaopeng Mei, Mengwei Cui, Qianqian He, Haifeng Wang, Huihui Li, Bo Cheng, Yan Zhang, Wenzhi Guo, Changju Zhu, and Sanyang Chen. Sirtuin 5‐mediated desuccinylation of aldh2 alleviates mitochondrial oxidative stress following acetaminophen‐induced acute liver injury. Advanced Science, Aug 2024. URL: https://doi.org/10.1002/advs.202402710, doi:10.1002/advs.202402710. This article has 61 citations and is from a peer-reviewed journal.
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