The DOI matches its Crossref record; 246 of the 251 references it cites were found in a registry or an index; none of the 132 sources its claims cite is checked for support yet.
Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications
Open accessAbstract
Mitochondria are critically important in providing cellular energy ATP as well as their involvement in anti-oxidant defense, fat oxidation, intermediary metabolism and cell death processes. It is well-established that mitochondrial functions are suppressed when living cells or organisms are exposed to potentially toxic agents including alcohol, high fat diets, smoking and certain drugs or in many pathophysiological states through increased levels of oxidative/nitrative stress. Under elevated nitroxidative stress, cellular macromolecules proteins, DNA, and lipids can undergo different oxidative modifications, leading to disruption of their normal, sometimes critical, physiological functions. Recent reports also indicated that many mitochondrial proteins are modified via various post-translation modifications (PTMs) and primarily inactivated. Because of the recently-emerging information, in this review, we specifically focus on the mechanisms and roles of five major PTMs (namely oxidation, nitration, phosphorylation, acetylation, and adduct formation with lipid-peroxides, reactive metabolites, or advanced glycation end products) in experimental models of alcoholic and nonalcoholic fatty liver disease as well as acute hepatic injury caused by toxic compounds. We also highlight the role of the ethanol-inducible cytochrome P450-2E1 (CYP2E1) in some of these PTM changes. Finally, we discuss translational research opportunities with natural and/or synthetic anti-oxidants, which can prevent or delay the onset of mitochondrial dysfunction, fat accumulation and tissue injury.
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
This review argues that five major post-translational modifications (oxidation, nitration, phosphorylation, acetylation, and electrophilic adduct formation) of mitochondrial proteins drive mitochondrial dysfunction, fat accumulation, inflammation, and tissue injury in alcoholic and nonalcoholic fatty liver disease and acute drug-induced liver injury. It highlights the ethanol-inducible CYP2E1 as a recurring contributor and discusses mitochondria-targeted antioxidants as translational opportunities.
Key findings
- Mass-spectral analyses cited in the review identified more than 87 mitochondrial and 60 cytosolic proteins oxidatively modified in alcohol-exposed rodents, and more than 70 mitochondrial and 30 cytosolic proteins nitrated in acetaminophen (APAP)-exposed mice; the authors note these may represent a small fraction of the estimated 1100–1400 total mitochondrial proteins.
- Oxidative/S-nitrosylation modification of active-site Cys residues inactivates key enzymes including ALDH2, thiolase, Prx1, and NADP+-ICDH; ALDH2 activity suppressed in ethanol-exposed rats was fully restored by DTT treatment.
- In APAP-treated mice, N-acetyl-cysteine completely protected the liver from necrotic injury and prevented Tyr nitration and inactivation of five selected enzymes (SOD2, Gpx, ATP synthase, ALDH2, thiolase).
- Acetylation studies identified 91 acetylated mitochondrial proteins in alcohol-exposed mice (including ALDH2, ATP synthase, Gpx, thiolase); approximately 20% of mitochondrial proteins and 44% of NAD+-dependent mitochondrial dehydrogenases are acetylated under physiological conditions.
- In 50 alcoholic cirrhosis patients, average MDA- and HNE-protein adduct levels were significantly higher than in nonalcoholic cirrhosis or healthy individuals, while ACR- and MGO-adducts did not differ; MDA/HNE adducts were also higher in 51 alcoholic patients with advanced fibrosis/cirrhosis than in 23 fatty liver or 30 healthy controls.
Methods
- Narrative review of the literature on five major PTMs of mitochondrial proteins in experimental models of alcoholic fatty liver disease (AFLD), nonalcoholic fatty liver disease (NAFLD), and acute liver injury, with emphasis on CYP2E1.
- Synthesizes cited experimental evidence including rodent and cell-culture models (e.g., binge/chronic alcohol, high-fat diets, APAP, MDMA, ischemia-reperfusion, LPS), mass-spectrometry-based proteomic identification of modified proteins, and human patient adduct measurements.
- Concludes with a discussion of natural and synthetic antioxidants and mitochondria-targeted compounds (SS-peptides, MitoQ, Mito-CP).
Limitations
- Stated by the paper: it is difficult to clearly demonstrate the deleterious effect of each single PTM or which PTM plays a critical role, since many proteins may be modified by multiple PTMs simultaneously; identifying modified amino acids and their roles in activity changes is challenging; it remains unknown which low-abundance proteins are modified; other PTM types (methylation, glycosylation, sumoylation, ubiquitination) and extra-hepatic tissues (brain, heart, pancreas, adipose, intestine) need further study.
- Stated by the paper: technical limitations in identification and purification of oxidized proteins and detection methods, especially for low-abundance proteins, mean the actual number of oxidized proteins could be significantly higher than reported.
- Evident from the text: as a review, it presents no new primary data, and several cited mechanistic conclusions (e.g., that HNE-modified proteins are functionally suppressed) are described as assumptions rather than measured outcomes.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
0 of 132 cited sources checked · 0 supported · 0 flagged
None of the sources cited for this claim have been checked yet.
In the paper
“Similar numbers of oxidatively-modified mitochondrial proteins were also identified by mass-spectral analysis in mice with I/R injury [38] and rats exposed to 3,4-methylenedioxymethamphetamine (MDMA) [39].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Oxidation of mitochondrial proteins
What the sources say
- Not checked yetcites [38] Moon, 2008, Oxidative inactivation of key mitochondrial proteins leads to dysfunction and injury in hepatic ischemia reperfusion, Gastroenterology source
- Not checked yetcites [39] Moon, 2008, Mechanism of 3,4-methylenedioxymethamphetamine (MDMA, ecstasy)-mediated mitochondrial dysfunction in rat liver, Proteomics source
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIn the paper
“The rates of protein oxidation in CYP2E1-containing E47-HepG2 hepatoma cells [36] exhibited a dose- and time- dependent pattern in response to alcohol as well as the presence of CYP2E1 [37].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Oxidation of mitochondrial proteins
What the sources say
- Not checked yetcites [37] Suh, 2004, Identification of oxidized mitochondrial proteins in alcohol-exposed human hepatoma cells and mouse liver, Proteomics source
Strength:plain· not yet calibratedCausal:correlational· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesNone of the sources cited for this claim have been checked yet.
In the paper
“In fact, mass-spectral analysis revealed that more than 87 mitochondrial and 60 cytosolic proteins were oxidatively-modified in alcohol-exposed rodents [34], [35].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Oxidation of mitochondrial proteins
What the sources say
- Not checked yetcites [34] Moon, 2006, Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats, Hepatology (Baltimore, Md.) source
- Not checked yetcites [35] Kim, 2006, Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells, Proteomics source
Strength:plain· not yet calibratedCausal:correlational· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIn the paper
“Treatment with NAC completely protected the liver from the APAP-induced necrotic injury measured by increased serum transaminase activities and liver histology.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [94] Abdelmegeed, 2013, Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury, Free Radical Biology and Medicine source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“Furthermore, NAC ameliorated the inactivation of the five critical enzymes via preventing Tyr nitration, as evidenced by immunoprecipitation with a specific antibody to each protein followed by immunoblot with anti-3-NT antibody.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [94] Abdelmegeed, 2013, Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury, Free Radical Biology and Medicine source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“Furthermore, oxidative modification of the active site Cys residue of peroxiredoxin 1 (Prx1) and inactivation was observed in alcohol-exposed mice [47].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Oxidation of mitochondrial proteins
What the sources say
- Not checked yetcites [47] Bae, 2011, Concerted action of sulfiredoxin and peroxiredoxin I protects against alcohol-induced oxidative injury in mouse liver, Hepatology (Baltimore, Md.) source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“In fact, after immunoaffinity purification followed by mass-spectral analysis, we demonstrated that more than 70 mitochondrial proteins and 30 cytosolic proteins were nitrated in APAP-exposed mice [94].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [94] Abdelmegeed, 2013, Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury, Free Radical Biology and Medicine source
Load-bearingStrength:boosted· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“Our results showed that pro-apoptotic Bax in the cytosol can be phosphorylated (activated) by p-JNK and/or p-p38K, resulting in its conformational change with exposure of the C-terminal membrane domain.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Phosphorylation of mitochondrial proteins
What the sources say
- Not checked yetcites [129] Kim, 2006, JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells, Journal of Biological Chemistry source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“Our results revealed that Thr167 of Bax was phosphorylated before it was translocated to mitochondria to stimulate mitochondria-dependent apoptosis [129].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Phosphorylation of mitochondrial proteins
What the sources say
- Not checked yetcites [129] Kim, 2006, JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells, Journal of Biological Chemistry source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“By using immunoprecipitation with anti-Ac-Lys antibody followed by mass spectral analysis, 91 acetylated mitochondrial proteins were recently identified in alcohol exposed mice [152].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Acetylation of mitochondrial proteins
What the sources say
- Not checked yetcites [152] Fritz, 2012, Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice, Journal of Proteome Research source
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passes
- It may state two separate claims as one. 24
- Probably not a substantial claim. 3
None of the sources cited for this claim have been checked yet.
In the paper
“Oxidative modification and inactivation of ALDH2 were also observed after exposure to MDMA [39] or I/R injury [38], resulting in the accumulation of lipid peroxidation products, which are metabolized by ALDH2 [46].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Oxidation of mitochondrial proteins
What the sources say
- Not checked yetcites [39] Moon, 2008, Mechanism of 3,4-methylenedioxymethamphetamine (MDMA, ecstasy)-mediated mitochondrial dysfunction in rat liver, Proteomics source
- Not checked yetcites [38] Moon, 2008, Oxidative inactivation of key mitochondrial proteins leads to dysfunction and injury in hepatic ischemia reperfusion, Gastroenterology source
- Not checked yetcites [46] Hartley, 1995, The hepatocellular metabolism of 4-hydroxynonenal by alcohol dehydrogenase, aldehyde dehydrogenase, and glutathione S-transferase, Archives of Biochemistry and Biophysics source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“Mass-spectral analysis confirmed that Cys305 and Cys387 of NADP+-ICDH were S-nitrosylated, resulting in its inactivation in alcohol-exposed animals [53].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Oxidation of mitochondrial proteins
What the sources say
- Not checked yetcites [53] Lee, 2003, Inactivation of NADP+-dependent isocitrate dehydrogenase by peroxynitrite. Implications for cytotoxicity and alcohol-induced liver injury, Journal of Biological Chemistry source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“The identified nitrated proteins are involved in cellular energy production, fat metabolism, intermediary metabolism, urea cycle, chaperone activity, and anti-oxidant defense.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [94] Abdelmegeed, 2013, Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury, Free Radical Biology and Medicine source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“Furthermore, AA-AGE but not N-ethyllysine (NEL) caused apoptosis of rat hepatocytes, suggesting an important role of AA-AGE in alcohol-induced hepatotoxicity and fatty liver injury [193].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Electrophilic adduct formation of mitochondrial proteins
What the sources say
- Not checked yetcites [193] Hayashi, 2013, Acetaldehyde-derived advanced glycation end-products promote alcoholic liver disease, PloS One source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
The paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“It is well-established that mitochondrial functions are suppressed when living cells or organisms are exposed to potentially toxic agents including alcohol, high fat diets, smoking and certain drugs or in many pathophysiological states through increased levels of oxidative/nitrative stress.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✗ Based: failsProbably not a substantial claim. The paper may give no reason why it holds.
None of the sources cited for this claim have been checked yet.
In the paper
“Although increased nitroxidative stress can oxidatively damage mitochondrial DNA and lipids, the majority of insults can also take place at the protein levels through different forms of post-translational modification (PTM) [26], [27].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Introduction
What the sources say
- Not checked yetcites [26] Song, 2013, Increased nitroxidative stress promotes mitochondrial dysfunction in alcoholic and nonalcoholic fatty liver disease, Oxidative Medicine and Cellular Longevity source
- Not checked yetcites [27] Abdelmegeed, 2014, Functional roles of protein nitration in acute and chronic liver diseases, Oxidative Medicine and Cellular Longevity source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“Recent reports also indicated that many mitochondrial proteins are modified via various post-translation modifications (PTMs) and primarily inactivated.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes? Based: unclearIt may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“Continued mitochondrial dysfunction with increased oxidative stress also sensitizes the hepatocytes to subsequent necrosis and/or apoptosis of hepatocytes, which likely lead to activation of resident liver macrophage (i.e., Kupffer cells) and recruitment of infiltrating immune cells into the liver with elevated levels of hepatic inflammation (steatohepatitis) and pro-inflammatory cytokines/chemok”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Introduction
What the sources say
- Not checked yetcites [13] Purohit, 2009, Molecular mechanisms of alcoholic fatty liver, Alcoholism, Clinical and Experimental Research source
- Not checked yetcites [14] Gao, 2011, Alcoholic liver disease: pathogenesis and new therapeutic targets, Gastroenterology source
- Not checked yetcites [15] Barnes, 2014, Innate immunity and cell death in alcoholic liver disease: role of cytochrome P4502E1, Redox Biology source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
The paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“Under elevated nitroxidative stress, cellular macromolecules proteins, DNA, and lipids can undergo different oxidative modifications, leading to disruption of their normal, sometimes critical, physiological functions.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesProbably not a substantial claim.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Consequently, hepatic stellate cells can be activated and transformed into myofibroblast-like cells, producing pro-fibrotic cytokines such as transforming growth factor-beta and platelet derived growth factor, leading to hepatic fibrosis/cirrhosis and cancer.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Introduction
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“However, many toxic agents such as alcohol, APAP and LPS can induce iNOS, which produces greater amounts of NO, likely leading to nitrosative/nitrative stress [27], [75], [76], [77].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [27] Abdelmegeed, 2014, Functional roles of protein nitration in acute and chronic liver diseases, Oxidative Medicine and Cellular Longevity source
- Not checked yetcites [75] Calcerrada, 2011, Nitric oxide-derived oxidants with a focus on peroxynitrite: molecular targets, cellular responses and therapeutic implications, Current Pharmaceutical Design source
- Not checked yetcites [76] Brenner, 2013, Decoding cell death signals in liver inflammation, Journal of Hepatology source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“APAP was first shown to induce and promote mitochondrial protein nitration and that peroxynitrite can cause mitochondrial DNA damage by Cover et al. [18].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [18] Cover, 2005, Peroxynitrite-induced mitochondrial and endonuclease-mediated nuclear DNA damage in acetaminophen hepatotoxicity, Journal of Pharmacology and Experimental Therapeutics source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“In this case, NO can interact with ROS to produce a potently toxic peroxynitrite, which can nitrate Tyr residues to generate 3-nitroTyr (3-NT) or S-nitrosylate Cys residues of many proteins [77].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [77] Radi, 1991, Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide, Journal of Biological Chemistry source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“Regulatory mechanism of AMP-dependent protein kinase (AMPK) by alcohol and other non-alcoholic substances, including high fat diet has become an important research topic, since AMPK serves as a key sensor and/regulator of metabolic syndrome and many cellular processes [136].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Phosphorylation of mitochondrial proteins
What the sources say
- Not checked yetcites [136] Hardie, 2014, AMP-activated protein kinase: maintaining energy homeostasis at the cellular and whole-body levels, Annual Review of Nutrition source
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“Pretreatment with a specific inhibitor of CYP2E1 blocked metabolic activation of some hepatotoxic agents, which are CYP2E1 substrates [110], [111], [112], [113], [114], [115], [116], [117], [118], and prevented JNK activation.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Phosphorylation of mitochondrial proteins
What the sources say
- Not checked yetcites [110] Lee, 2005, Pro- and anti-apoptotic roles of c-Jun N-terminal kinase (JNK) in ethanol and acetaldehyde exposed rat hepatocytes, European Journal of Pharmacology source
- Not checked yetcites [111] Yang, 2012, Cytochrome P4502E1, oxidative stress, JNK, and autophagy in acute alcohol-induced fatty liver, Free Radical Biology and Medicine source
- Not checked yetcites [112] Bae, 2001, Acetaminophen induces apoptosis of C6 glioma cells by activating the c-Jun NH(2)-terminal protein kinase-related cell death pathway, Molecular Pharmacology source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Suppressed ATP synthase activity would lead to decreased ATP production, interfering with vital cell functions and ultimately causing necrosis.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes? Based: unclearIt may state two separate claims as one.
In the paper
“However, it would be prudent to double-check the function of each nitrated protein, since nitration can also increase the activity of some proteins such as glutathions S-transferase (GST), heat shock protein 90 (HSP90), and protein phosphatase type 2 [PP2], or exert no effects at all as reported with transferrin [27].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [27] Abdelmegeed, 2014, Functional roles of protein nitration in acute and chronic liver diseases, Oxidative Medicine and Cellular Longevity source
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
In the paper
“Furthermore, suppressed ALDH2 would lead to the accumulation of toxic, reactive aldehydes and lipid peroxidation, as previously mentioned in the oxidation section [42].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Nitration of many mitochondrial proteins
What the sources say
- Not checked yetcites [42] Song, 2011, Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications, Journal of Proteomics source
Strength:hedged· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
In the paper
“For instance, AMPK can be activated by hydrogen peroxide and mitochondria-derived ROS since its activation can be prevented by pretreatment with antioxidants such as NAC or GSH-ethyl ester [101].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Phosphorylation of mitochondrial proteins
What the sources say
- Not checked yetcites [101] Sid, 2013, Role of AMPK activation in oxidative cell damage: Implications for alcohol-induced liver disease, Biochemical Pharmacology source
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
In the paper
“A recent study also showed that sustained JNK activation led to phosphorylation at Ser-46 of sirtuin 1, NAD+-dependent deacetylase in cytosol (described later), followed by ubiquitin-dependent degradation, contributing to fat accumulation in obese mice [124].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Phosphorylation of mitochondrial proteins
What the sources say
- Not checked yetcites [124] Gao, 2011, Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity, Journal of Biological Chemistry source
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“It is well-established that excessive alcohol intake and many potentially toxic compounds can suppress low Km mitochondrial ALDH2 activity in rodents and humans through various PTMs of the active site Cys residue and other redox-sensitive amino acids, as reviewed [26], [27], [42], resulting in the accumulation of toxic acetaldehyde and other lipid aldehydes.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Electrophilic adduct formation of mitochondrial proteins
What the sources say
- Not checked yetcites [26] Song, 2013, Increased nitroxidative stress promotes mitochondrial dysfunction in alcoholic and nonalcoholic fatty liver disease, Oxidative Medicine and Cellular Longevity source
- Not checked yetcites [27] Abdelmegeed, 2014, Functional roles of protein nitration in acute and chronic liver diseases, Oxidative Medicine and Cellular Longevity source
- Not checked yetcites [42] Song, 2011, Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications, Journal of Proteomics source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“The number of acetylated proteins can be significantly increased in experimental models of pathological conditions or following exposure to hepatotoxic agents, possibly resulting from redox-mediated suppression of deacetylases, as shown in alcohol-exposed [142], [143], [144], [145] or high-fat exposed rodents [146], [147], [148].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Acetylation of mitochondrial proteins
What the sources say
- Not checked yetcites [142] You, 2008, Involvement of mammalian sirtuin 1 in the action of ethanol in the liver, American Journal of Physiology: Gastrointestinal and Liver Physiology
- Not checked yetcites [143] Lieber, 2008, Effect of chronic alcohol consumption on hepatic SIRT1 and PGC-1alpha in rats, Biochemical and Biophysical Research Communications source
- Not checked yetcites [144] Picklo, 2008, Ethanol intoxication increases hepatic N-lysyl protein acetylation, Biochemical and Biophysical Research Communications source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“In addition, Cyp2e1-null mice were resistant to alcohol-mediated gut leakiness, which was clearly observed in the corresponding wild-type mice [238].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Conclusion and future research opportunities
What the sources say
- Not checked yetcites [238] Abdelmegeed, 2013, CYP2E1 potentiates binge alcohol-induced gut leakiness, steatohepatitis, and apoptosis, Free Radical Biology and Medicine source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“A large scale proteomics study revealed that approximately 20% of mitochondrial proteins and 44% of NAD+-dependent mitochondrial dehydrogenases are acetylated under physiological conditions [141].”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Acetylation of mitochondrial proteins
What the sources say
- Not checked yetcites [141] Kim, 2006, Substrate and functional diversity of lysine acetylation revealed by a proteomics survey, Molecular Cell source
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“Elevated levels of cross-linked AGEs in many tissues can up-regulate the expression of the receptor for AGEs (RAGE), which activates NADPH oxidase, leading to increased oxidative stress, insulin resistance, and inflammation with disruption of normal cell signaling pathways.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Electrophilic adduct formation of mitochondrial proteins
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Although several PTMs in many mitochondrial proteins were identified in different disease states or under increased nitroxidative stress, it is quite possible that many proteins can be modified by multiple PTMs simultaneously.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Conclusion and future research opportunities
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✗ Based: failsProbably not a substantial claim. The paper may give no reason why it holds.
None of the sources cited for this claim have been checked yet.
In the paper
“In contrast, activation of sirtuins by small molecule polyphenols including resveratrol [156] and green tea extracts [157] can reduce the number of acetylated proteins, including PGC-1α, which contributes to increased fat oxidation and insulin sensitivity with improved outcome against metabolic syndrome.”
§ Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications > Post-translational modifications of mitochondrial proteins > Acetylation of mitochondrial proteins
What the sources say
- Not checked yetcites [156] Yang, 2014, Resveratrol ameliorates hepatic metaflammation and inhibits NLRP3 inflammasome activation, Metabolism: Clinical and Experimental source
- Not checked yetcites [157] Wang, 2014, Novel insights of dietary polyphenols and obesity, Journal of Nutritional Biochemistry source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
The paper relies on this without support.
The experimental models used in the cited and own studies are adequate to infer mechanisms of human alcoholic/nonalcoholic fatty liver disease and acute liver injury.
“We used APAP as a well-established model agent for acute drug-induced liver injury (DILI) to study the functional role of nitrated mitochondrial proteins and the mechanisms of mitochondrial dysfunction and hepatotoxicity.”
The authors state this as an assumption.
The functional activities of some of the HNE-modified mitochondrial proteins could be suppressed.
“Although the activities of each HNE-modified protein were not determined in this study, it is reasonable to assume that the functional activities of some of the modified proteins could be suppressed.”
The paper relies on this without support.
Treatment with the antioxidant NAC or the CYP2E1 inhibitor chlormethiazole significantly prevents gut leakiness and liver injury in binge alcohol-induced gut leakiness.
“since treatment with an antioxidant NAC or a CYP2E1 inhibitor chlormethiazole significantly prevented gut leakiness and liver injury.”
The paper relies on this without support.
The functional roles of redox-regulated PTMs on many intestinal proteins are still poorly understood.
“Despite numerous reports on gut leakiness caused by alcohol and fructose [232], [233], [234], [235], [236], [237], [238], [239], [240], [241], [242], the functional roles of redox-regulated PTMs on many intestinal proteins are still poorly understood.”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“AGEs also stimulate mitochondrial ROS production and c-Jun N-terminal protein kinase (JNK) and NADPH oxidase activity to induce mitochondrial dysfunction and oxidative stress51–53.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [53]
In the citing paper
“Dietary AGEs have been found to disrupt and downregulate sirtuin1 (SIRT1) expression, resulting in the acetylation and inactivation of peroxisome proliferator-activated receptor γ coactivator-1α (PGC1α), a master regulator of mitochondrial metabolism.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [53]
In the citing paper
“The presence of acetaldehyde in the brain also alters DNA integrity and neuronal viability.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [53]
In the citing paper
“Excessive alcohol exposure increases oxidative stress and the levels of reactive acetaldehyde and lipid aldehydes with a simultaneous decrease in defensive molecules and detoxification enzymes, including GSH and ALDH253,172,177.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [53]
In the citing paper
“can prevent alcohol-induced oxidative stress and the formation of various adducts, including AA adducts137 and AA-MAA adducts53,285”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [53]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
ALDH2 restoration is attributed to DDT instead of DTT
MinorThe treatment group is described as receiving dithiothreitol (DTT), but the subsequent sentence attributes restoration of ALDH2 activity to DDT treatment. These name different treatments.
“Furthermore, the significantly decreased ALDH2 activity in ethanol-exposed rats was fully restored by DDT treatment [34].”
“dithiothreitol (DTT)-treated mitochondria from alcohol-exposed rats”
Citations
Cites
2 retracted
Doser, T. A., Turdi, S., Thomas, D. P., Epstein, P. N., Li, S., & Ren, J. T. (2009) · Circulation · doi:10.1161/circulationaha.108.823799 · Cited by 196
RetractedShulga, N., & Pastorino, J. G. (2010) · Journal of Cell Science · doi:10.1242/jcs.073502 · Cited by 76 · cited 2×
“As mentioned earlier, key mitochondrial proteins in regulating the fatty acid metabolism are acetylated and that the number of acetylated proteins can be significantly increased through suppression of the mitochondrial deacetylase sirtuin 3 and other sirtuin isoforms by alcohol [142–145,149,150–153], high fat [148], a…”
BackgroundRetractedWallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185
Peroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,492
H 2 O 2 , a Necessary Evil for Cell Signaling
Rhee, S. G. (2006) · Science · doi:10.1126/science.1130481 · Cited by 2,160
Nonalcoholic steatohepatitis: association of insulin resistance and mitochondrial abnormalities
Sanyal, A. J., Campbell–Sargent, C., Mirshahi, F., Rizzo, W. B., Contos, M. J., Sterling, R. K., Luketic, V. A., Shiffman, M. L., & Clore, J. N. (2001) · Gastroenterology · doi:10.1053/gast.2001.23256 · Cited by 2,078 · cited 2×
“Parkinson's disease [4–12], although etiological causes of each disease are different.”
BackgroundThe thioredoxin antioxidant system
Lu, J., & Holmgren, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.036 · Cited by 2,055 · cited 1×
“It is known that Cys-glutathionylation of mixed disulfide groups can create a functional cycle consisting of the forward reaction (glutathione S-transferase P) and the reverse reaction (glutaredoxin system) [67,73,74].”
BackgroundA Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994 · cited 1×
“The number of oxidatively-modified mitochondrial proteins we characterized may represent a small fraction of the estimated number of 1100– 1400 total mitochondrial proteins [40,41].”
BackgroundAlcoholic Liver Disease: Pathogenesis and New Therapeutic Targets
Gao, B., & Bataller, R. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.09.002 · Cited by 1,963 · cited 2×
“and pro-inflammatory cytokines/chemokines [13–15].”
BackgroundKamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792
Flagged first, then by citations
5 of the 251 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Mitochondrial Dysfunction and Signaling in Chronic Liver Diseases
Mansouri, A., Gattolliat, C., & Asselah, T. (2018) · Gastroenterology · doi:10.1053/j.gastro.2018.06.083 · Cited by 839
Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411
Self-citationByun, K., Yoo, Y., Son, M., Lee, J., Jeong, G.-B., Park, Y. M., Salekdeh, G. H., & Lee, B. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.030 · Cited by 357
“, 2010), alcoholic fatty liver disease (AFLD) (Song et al., 2014), diabetes (Rolo & Palmeira, 2006), and chondrocyte degeneration (Blanco et al.”
Self-citationRepairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337
Cho, Y., Kim, D., Seo, W., Gao, B., Yoo, S., & Song, B. (2019) · Hepatology · doi:10.1002/hep.30652 · Cited by 266
“Increased hepatic CYP2E1 is known to directly cause fatty liver disease by elevating oxidative/nitrative stress and various forms of posttranslational modification of cellular proteins, contributing to endoplasmic reticulum stress, mitochondrial dysfunction, and apoptosis of hepatocytes.(32) Furthermore, intestinal CY…”
BackgroundSelf-citationMetaPro-IQ: a universal metaproteomic approach to studying human and mouse gut microbiota
Zhang, X., Ning, Z., Mayne, J., Moore, J. I., Li, J. S. Y., Butcher, J., Deeke, S. A., Chen, R., Chiang, C., Wen, M., et al. (2016) · Microbiome · doi:10.1186/s40168-016-0176-z · Cited by 200
LeFort, K. R., Rungratanawanich, W., & Song, B.-J. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05061-7 · Cited by 202
“…is well documented that CYP2E1 contributes to oxidative stress pathways in ALD and DILI, many reports have also demonstrated the critical role of CYP2E1 in MASLD through the production of ROS and LPOs; this may represent the second hit in the progression of steatosis to MASH [26, 41, 68, 178, 244].”
BackgroundInfluentialSelf-citationMitochondrial dysfunction and cell death in neurodegenerative diseases through nitroxidative stress
Akbar, M. D., Essa, M. M., Daradkeh, G., Abdelmegeed, M. A., Choi, Y., Mahmood, L., & Song, B. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.016 · Cited by 182
“glycosylation, carbonylation, palmitoylation, myristoylation and other modifications including protein adduct formation (Song et al., 2014).”
InfluentialSelf-citationMitochondrial 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 190
“Mitochondrial DNA mutations caused by oxidative modifications are damaging to cellular integrity and are linked to higher ROS leakage from organelles and cells [156].”
BackgroundFrom Mitochondrial Function to Neuroprotection—an Emerging Role for Methylene Blue
Tucker, D., Lu, Y., & Zhang, Q. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0712-2 · Cited by 162
“Modifications to proteins by ROS/RNS include, but are not limited to: oxidation, nitrosylation, acetylation, and phosphorylation [36].”
Role of Endogenous Lipopolysaccharides in Neurological Disorders
Kalyan, M., Hediyal, T. A., Sonali, S., Vichitra, C., Sunanda, T., Praveenraj, S. S., Ray, B., Gorantla, V. R., Rungratanawanich, W., Mahalakshmi, A. M., et al. (2022) · Cells · doi:10.3390/cells11244038 · Cited by 172
“nitration of Tyr and S-nitrosylation of Cys residues of many proteins in the mitochondria and endoplasmic reticulum (ER), leading to mitochondrial dysfunction, ER stress, and cell death, as reviewed [80,81].”
BackgroundSelf-citationPost-translational modifications in mitochondria: protein signaling in the powerhouse
Stram, A. R., & Payne, R. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2280-4 · Cited by 149
Oxidative stress, antioxidants and intestinal calcium absorption
de Barboza, G. D., Guizzardi, S., Moine, L., & de Talamoni, N. T. (2017) · World Journal of Gastroenterology · doi:10.3748/wjg.v23.i16.2841 · Cited by 149
Mitochondrial dysfunction induced by Bisphenol A is a factor of its hepatotoxicity in rats
Khan, S., Beigh, S., Chaudhari, B. P., Sharma, S., Abdi, S. A. H., Ahmad, S., Ahmad, F., Parvez, S., & Raisuddin, S. (2015) · Environmental Toxicology · doi:10.1002/tox.22193 · Cited by 105
“It is also reported that the mitochondrial respiratory chain dysfunction significantly contributes to tissue injury (Ten and Starkov, 2012; Song et al., 2014).”
BackgroundCho, Y.-E., Yu, L.-R., Abdelmegeed, M. A., Yoo, S.-H., & Song, B.-J. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.02.005 · Cited by 99
“Immunoblots showed markedly elevated levels of apoptosis-related marker proteins [15] activated p-JNK, cleaved-caspase-3 and cleaved-caspase-9 in alcohol-exposed rats (Fig.”
BackgroundInfluentialSelf-citationMetabolic Plasticity of Tumor Cell Mitochondria
Cannino, G., Ciscato, F., Masgras, I., Sànchez‐Martìn, C., & Rasola, A. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00333 · Cited by 97
Nunes, P. T., Kipp, B. T., Reitz, N. L., & Savage, L. M. (2019) · International review of neurobiology · doi:10.1016/bs.irn.2019.09.002 · Cited by 103
“These data suggest that although CET did not alter expression of the IκB-α gene, the acute withdrawal period from alcohol triggered the activation of the NF-κB pathway.”
BackgroundInfluentialHenriques, J. F., Portugal, C. C., Canedo, T., Relvas, J. B., Summavielle, T., & Socodato, R. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2017.11.002 · Cited by 89
Mitochondrial oxidative injury: a key player in nonalcoholic fatty liver disease
Dornas, W., & Schuppan, D. (2020) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00121.2020 · Cited by 89
“The deletion and/or mutation of mitochondrial DNA and protein through nitroxidative modifications is deleterious to cells and is linked to increased ROS leakage out of organelles and cells (102).”
BackgroundEpigenetic Modifications in the Biology of Nonalcoholic Fatty Liver Disease
Pirola, C. J., Scian, R., Gianotti, T. F., Dopazo, H., Rohr, C., Martino, J. S., Castaño, G. O., & Sookoian, S. C. (2015) · Medicine · doi:10.1097/md.0000000000001480 · Cited by 88
Lai, W., Zhang, J., Sun, J., Min, T., Bai, Y., He, J., Cao, H., Che, Q., Guo, J., & Su, Z. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134809 · Cited by 89
Rungratanawanich, W., Lin, Y., Wang, X., Kawamoto, T., Chidambaram, S. B., & Song, B. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102577 · Cited by 88
“Although the protein nitration was performed with 534 a few selected TJ/AJ proteins, the current results are in agreement with previous reports [9, 10, 535 43], where the other gut TJ/AJ proteins tended to undergo similar types of nitration or other PTMs 536 like phosphorylation and acetylation, contributing to the de…”
ResultSelf-citationCho, Y.-E., & Song, B.-J. (2018) · Redox Biology · doi:10.1016/j.redox.2018.07.012 · Cited by 78
Self-citationHao, L., Sun, Q., Zhong, W. H., Zhang, W., Sun, X., & Zhou, Z. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.005 · Cited by 76
Alcohol-Mediated Organ Damages: Heart and Brain
Obad, A. S., Peeran, A. A., Little, J. I., Haddad, G. E., & Tarzami, S. T. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00081 · Cited by 81
“Generally speaking, mechanisms of alcohol-related organ injury were attributed to increases in oxidative stress, impairments in methylation, unusual posttranslational modifications of proteins, dysregulation in lipid metabolism and signal transduction pathways, all of which ultimately affect cell survival and function…”
BackgroundCho, Y., Song, B., Akbar, M. D., & Baek, M. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.03.009 · Cited by 70
“…stimulation of the cell death associated stressactivated protein kinases such as c-Jun N-terminal protein kinase (JNK), p38K and mitochondrial dysfunction through various posttranslational modifications of mitochondrial proteins (Abdelmegeed & Song, 2014; Jang et al., 2015; Song et al., 2014).”
BackgroundSelf-citationBallway, J. W., & Song, B.-J. (2021) · Antioxidants · doi:10.3390/antiox10030384 · Cited by 72
“Thus, the CYP2E1 enzyme, constitutively expressed under normal physiological states and then induced by ethanol, at least via protein stabilization [57,58], becomes functionally important in ethanol metabolism, as well as in alcohol-mediated oxidative liver damage, particularly because CYP2E1-mediated alcohol metaboli…”
BackgroundInfluentialSelf-citationElectrophilic Aldehyde 4-Hydroxy-2-Nonenal Mediated Signaling and Mitochondrial Dysfunction
Sharma, S., Sharma, P., Bailey, T., Bhattarai, S., Subedi, U., Miller, C., Ara, H., Kidambi, S., Sun, H., Panchatcharam, M., et al. (2022) · Biomolecules · doi:10.3390/biom12111555 · Cited by 66
“The primary therapeutics targeting 4-HNE are antioxidants such as N-acetylcysteine and α-lipoic acid, which enhance ALDH activity and expression [39,40].”
BackgroundMusso, G., Saba, F., Cassader, M., & Gambino, R. (2023) · Progress in Lipid Research · doi:10.1016/j.plipres.2023.101238 · Cited by 71
Abdelmegeed, M. A., Choi, Y., Ha, S.-K., & Song, B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.016 · Cited by 57
“Oxidative stress-mediated cell damage is related to the balance between the production of oxidants and the defense capacity of the anti-oxidant system [32, 34, 64].”
Self-citationCho, Y.-E., Lee, M., & Song, B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169945 · Cited by 59
Self-citationAlcohol Metabolism in the Progression of Human Nonalcoholic Steatohepatitis
Li, H., Toth, E. L., & Cherrington, N. J. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy106 · Cited by 57
Cho, Y., Seo, W., Kim, D., Moon, P., Kim, S., Lee, B.-H., Song, B., & Baek, M. (2018) · Scientific Reports · doi:10.1038/s41598-018-34309-7 · Cited by 55
Self-citationFang, L., Zhang, Y., Wang, Q., et al. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.07.219 · Cited by 55
Kim, D.-H., Sim, Y., Hwang, J.-H., Kwun, I., Lim, J., Kim, J., Kim, J., Baek, M., Akbar, M. D., Seo, W., et al. (2021) · Antioxidants · doi:10.3390/antiox10091386 · Cited by 51
“Finally, EA treatment attenuated apoptosis marker proteins in binge alcohol-exposed mice possibly neutralizing the p-JNK mediated cell death signaling pathway, which is stimulated under increased oxidative stress [33,66].”
BackgroundSelf-citationJang, S., Yu, L., Abdelmegeed, M. A., Gao, Y., Banerjee, A., & Song, B. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.040 · Cited by 51
Self-citationSong, B., Akbar, M. D., Jo, I., Hardwick, J. P., & Abdelmegeed, M. A. (2015) · Advances in pharmacology · doi:10.1016/bs.apha.2015.04.002 · Cited by 51
Self-citationCellular Bioenergetics: Experimental Evidence for Alcohol-induced Adaptations
Simon, L., & Molina, P. E. (2022) · Function · doi:10.1093/function/zqac039 · Cited by 45
Roles of Oxidative Stress and Autophagy in Alcohol-Mediated Brain Damage
Ruiter-Lopez, L., Khan, M. A. S., Wang, X., & Song, B. (2025) · Antioxidants · doi:10.3390/antiox14030302 · Cited by 49
Self-citationNewer Therapeutic Approaches in Treating Alzheimer’s Disease: A Comprehensive Review
Sree, R. R., Kalyan, M., Anand, N., Mani, S., Gorantla, V. R., Sakharkar, M. K., Song, B., & Chidambaram, S. B. (2025) · ACS Omega · doi:10.1021/acsomega.4c05527 · Cited by 45
Self-citationGut Microbiota and Metabolic Dysfunction-Associated Steatotic Liver Disease
Scarpellini, E., Scarcella, M., Tack, J. F., Scarlata, G. G. M., Zanetti, M., & Abenavoli, L. (2024) · Antioxidants · doi:10.3390/antiox13111386 · Cited by 48
Kuo, C., Wu, L., Chen, H., Yu, J. Q., & Wu, C. (2024) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.16539 · Cited by 45
Effects of quercetin on bisphenol A-induced mitochondrial toxicity in rat liver.
Mahdavinia, M., Alizadeh, S., Vanani, A. R., Dehghani, M. A., Shirani, M., Alipour, M., Shahmohammadi, H. A., & Asl, S. R. (2019) · PubMed Central · doi:10.22038/ijbms.2019.32486.7952 · Cited by 37
Chronic mild stress augments MPTP induced neurotoxicity in a murine model of Parkinson's disease
Janakiraman, U., Manivasagam, T., Justin Thenmozhi, A., Dhanalakshmi, C., Essa, M. M., Song, B.-J., & Guillemin, G. J. (2017) · Physiology & Behavior · doi:10.1016/j.physbeh.2017.01.046 · Cited by 36
Self-citationMitochondrial dysfunction in psychiatric morbidity: current evidence and therapeutic prospects
Agam, G., & Toker, L. (2015) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s70346 · Cited by 36
“61 These findings are highly important in view of the high incidence of comorbidity between psychiatric disorders and substance abuse; 60,62–64 yet it is unclear whether there is a causative relationship between the two.”
Choi, Y., Abdelmegeed, M. A., & Song, B. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.08.013 · Cited by 35
Self-citationHu, X., Jogasuria, A. P., Wang, J., Kim, C., Han, Y., Shen, H., Wu, J., & You, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.737015 · Cited by 34
“Considerable evidence indicates that hepatic ethanol metabolism is associated with alterations in hepatic mitochondria function, and consequently, promotes liver injury (29, 30).”
BackgroundToxicological implications of mitochondrial localization of CYP2E1
Hartman, J. H., Miller, G. P., & Meyer, J. N. (2017) · Toxicology Research · doi:10.1039/c7tx00020k · Cited by 32
Ogedengbe, O. O., Naidu, E. C., Akang, E. N., Offor, U., Onanuga, I. O., Peter, A. I., Jegede, A. I., & Azu, O. O. (2018) · Andrology · doi:10.1111/andr.12490 · Cited by 34
“It is well established that mitochondrial energy metabolism is critical to the efficient functioning of sperm cells which can be compromised when exposed to toxicants (Piomboni et al., 2012; Song et al., 2014).”
BackgroundSong, B., Abdelmegeed, M. A., Cho, Y., Akbar, M. D., Rhim, J. S., Song, M., & Hardwick, J. P. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-22254-3_6 · Cited by 35
Self-citationNature and Implications of Oxidative and Nitrosative Stresses in Autoimmune Hepatitis
Czaja, A. J. (2016) · Digestive Diseases and Sciences · doi:10.1007/s10620-016-4247-6 · Cited by 32
Targeting Hepatic Fibrosis in Autoimmune Hepatitis
Montaño‐Loza, A. J., Thandassery, R. B., & Czaja, A. J. (2016) · Digestive Diseases and Sciences · doi:10.1007/s10620-016-4254-7 · Cited by 30
“their ability to provoke changes in protein structure and function (post-translational modifications) [91, 92].”
Background3-ketodihydrosphingosine reductase mutation induces steatosis and hepatic injury in zebrafish
Park, K.-H., Ye, Z., Zhang, J., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-37946-0 · Cited by 31
Cranberry antioxidant power on oxidative stress, inflammation and mitochondrial damage
Caldas, A. P. S., Coelho, O. G. L., & Bressan, J. (2018) · International Journal of Food Properties · doi:10.1080/10942912.2017.1409758 · Cited by 30
“Under conditions of high oxidative stress, the cellular macromolecules may undergo different oxidative modifications, leading to their rupture and impairment of physiological functions.([71]) As they are the chief producers of ROS in the mammalian cells, the mitochondria naturally become predisposed to oxidative damag…”
BackgroundMekala, N. K., Trivedi, J., Bhoj, P. S., Togre, N. S., Rom, S., Sriram, U., & Persidsky, Y. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-023-01461-1 · Cited by 30
“In the liver, chronic alcohol consumption and cigarette smoke accelerate reactive oxygen and nitrogen species (ROS/RNS) accumulation through NADPH oxidase (NOX) and cytochrome P450-2E1 (CYP2E1) enzyme activation [45].”
BackgroundRasineni, K., Penrice, D. D., Natarajan, S. K., McNiven, M. A., McVicker, B. L., Kharbanda, K. K., Casey, C. A., & Harris, E. N. (2016) · BMC Gastroenterology · doi:10.1186/s12876-016-0433-4 · Cited by 28
Kim, J., Kim, D.-H., Gil, M.-C., Kwon, H., Seo, W., Kim, D., & Cho, Y. (2023) · Journal of Medicinal Food · doi:10.1089/jmf.2023.k.0060 · Cited by 28
The role of lysine acetylation in metabolic sensing and proteostasis
Eftekhari, A., Sabir, U., & Kasumov, T. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108908 · Cited by 30
High-Fat Diet Augments the Effect of Alcohol on Skeletal Muscle Mitochondrial Dysfunction in Mice
Ismaeel, A., Laudato, J. A., Fletcher, E., Papoutsi, E., Tice, A. L., Hwa, L. S., Miserlis, D., Jamurtas, A. Z., Steiner, J. L., & Koutakis, P. (2022) · Nutrients · doi:10.3390/nu14051016 · Cited by 27
“In addition to mitochondrial dynamics, toxic agents including alcohol and HF can also induce oxidative stress which promotes post-translational modification and subsequent inactivation of mitochondrial proteins [47].”
BackgroundMekala, N. K., Gheewala, N., Rom, S., Sriram, U., & Persidsky, Y. (2022) · Antioxidants · doi:10.3390/antiox11071328 · Cited by 24
“Earlier studies have shown various pathw ys by which drugs of abuse impair the mitochondrial function due to mitochondrial DNA damage [45], electrons escaping throu h a broken electro transp rt system [46], hrough expression of pro-i flammatory cytokines like TNF-α or IL-1β [47], and phosphorylation of stress-activat…”
BackgroundRungratanawanich, W., Ballway, J. W., Wang, X., Won, K., Hardwick, J. P., & Song, B. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108547 · Cited by 22
Self-citationLeFort, K. R., Rungratanawanich, W., & Song, B. (2023) · Antioxidants · doi:10.3390/antiox13010043 · Cited by 21
“…as oxidation, S-nitrosylation, nitration, MAPK-mediated phosphorylation, acetylation, and adduct formations in mitochondria and endoplasmic reticuli, leading to mitochondrial dysfunction, endoplasmic reticulum (ER) stress, and apoptosis of hepatocytes and other cells like gut enterocytes [24,62].”
BackgroundSelf-citationWang, P., Zheng, X., Du, R., Xu, J., Li, J., Zhang, H., Liang, X., & Liang, H. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c05529 · Cited by 20
Xia, Y., Gong, Y., Lin, X., Yang, Y., Song, X., Wang, G., Xiong, Z., Qian, Y., Liao, Z., Zhang, H., et al. (2023) · Food Science and Human Wellness · doi:10.26599/fshw.2022.9250076 · Cited by 19
Abdelmegeed, M. A., Choi, Y., Ha, S.-K., & Song, B. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.08.022 · Cited by 19
“The superoxide anion can become a potent oxidative radical that can cause severe tissue damage through interaction with other free radicals such as nitric oxide (NO) to produce a more potently toxic peroxynitrite and may also produce toxic hydroxyl radical in the presence of metals (Abdelmegeed et al., 2015; Abdelmege…”
BackgroundInfluentialSelf-citationYang, Q., Luo, C., Zhang, X., Liu, Y., Wang, Z., Cacciamani, P., Shi, J., Cui, Y., Wang, C., Sinha, B., et al. (2020) · PubMed Central · Cited by 19
Self-citationClustering Patients With Gout Based on Comorbidities and Biomarkers: A Cross-Sectional Study
Alduraibi, F. K., Saleem, M., Ricart, K. C., Patel, R. P., Szalai, A. J., & Singh, J. A. (2022) · The Journal of Rheumatology · doi:10.3899/jrheum.220635 · Cited by 17
“Patients, N = 88 24 (27) 25 (28) 39 (44) Demographics Male sex 24 (100) 23 (92) 18 (46) White race 19 (79) 15 (60) 9 (23) BMIa, mean (SD) 29.”
Cortés, A., Sotillo, J., Muñoz-Antolí, C., Fried, B. N., Esteban, J. G., & Toledo, R. (2015) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0004082 · Cited by 17
Ethanol Metabolism and Melanoma
Zhai, Z., Yamauchi, T., Shangraw, S., Hou, V., Matsumoto, A., & Fujita, M. (2023) · Cancers · doi:10.3390/cancers15041258 · Cited by 15
“The mechanistic basis behind ALDH2 downregulation without ALDH2 polymorphisms is complex and multi-factorial: (1) ALDH2 expression can be epigenetically regulated through gene methylation and hyperacetylation [108–111]; (2) ALDH2 expression is regulated by several transcriptional factors [112–114] and can be negativel…”
BackgroundAuger, C., Sivayoganathan, T., Abdullahi, A., Parousis, A., & Jeschke, M. G. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.07.006 · Cited by 16
“Although no significant increase in apoptosis was noted at the time points reported here, prolonged mitochondrial abnormalities may be associated with increased nitro-oxidative stress and sensitize hepatocytes to apoptosis/necrosis as well as the subsequent recruitment of infiltrating immune cells and consequently, in…”
BackgroundZaslavsky, K., & Margolin, E. (2021) · Journal of Neuro-Ophthalmology · doi:10.1097/wno.0000000000001333 · Cited by 16
“Both smoking and alcohol increase oxidative stress by interfering with mitochondrial function (14,16).”
BackgroundWang, X., Liang, G., Zhou, Y., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-55043-3 · Cited by 15
Hymavathi, R. V., Govatati, S., Matha, S. K., et al. (2017) · Journal of Advanced Research · doi:10.1016/j.jare.2017.02.002 · Cited by 15
“In addition, mitochondria involved in antioxidant defense system, fat oxidation, intermediary metabolic processes which includes alcohol metabolism and bioenergetics of the hepatocytes [7].”
BackgroundShen, W., Wan, X., Hou, J., Liu, Z., Mao, G., Xu, X., Yu, C., Zhu, X., & Ju, Z. (2022) · Life Medicine · doi:10.1093/lifemedi/lnac031 · Cited by 14
He, Q., Yin, Z., Chen, Y., Wu, Y., Pan, D., Cui, Y., Zhang, Z., Ma, H., Li, X., Shen, C., et al. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167259 · Cited by 16
Astaxanthin Is Able to Prevent Alcohol-Induced Dysfunction of Liver Mitochondria
Krestinina, O. V., Odinokova, I. V., Sotnikova, L. D., Krestinin, R. R., Zvyagina, A. I., & Baburina, Y. L. (2022) · Antioxidants · doi:10.3390/antiox11102019 · Cited by 13
“Under the influence of pathological factors (including alcohol), there are violations of the structure and functioning of these complexes, as well as the OXPHOS system as a whole [7,8].”
BackgroundSex-specific susceptibility to type 2 diabetes mellitus and preventive effect of linalyl acetate
Shin, Y. K., Hsieh, Y.-S., Han, A. Y., Kwon, S., Kang, P., & Seol, G. H. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118432 · Cited by 13
Rungratanawanich, W., LeFort, K. R., Cho, Y., Li, X., & Song, B. (2024) · Journal of Pineal Research · doi:10.1111/jpi.13007 · Cited by 14
Self-citationTherapeutic strategies of small molecules in the microbiota–gut–brain axis for alcohol use disorder
Xie, L., Rungratanawanich, W., Yang, Q., Tong, G., Fu, E., Lu, S., Liu, Y., Akbar, M. D., Song, B., & Wang, X. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103552 · Cited by 11
Self-citationPich, E. M., Tarnanas, I., Brigidi, P., & Collo, G. (2025) · Neurobiology of Stress · doi:10.1016/j.ynstr.2025.100713 · Cited by 16
“…circuits and produced by the concurrent effects of alcohol, cytokines, hormones, metabolic products, and bacterial endo-toxins (Haorah et al., 2008; Song et al., 2014); (c) Increased inflammation markers in liver and gut tissue (Bishehsari et al., 2017; Osna et al., 2017); (d) Reduce liver…”
Methylene blue post-treatment improves hypoxia-ischemic recovery in a neonatal rat model
Zhang, G., Lu, Y., Yang, L., Dong, Y., Wen, J., Xu, J., & Zhang, Q. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104782 · Cited by 9
Wang, Z., Luo, C.-L., Zhou, E. W., Sandhu, A. F., Yuan, X.-J., Williams, G. E., Cheng, J., Sinha, B., Akbar, M., Bhattacharya, P., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108805 · Cited by 11
Self-citationEvaluation of intoxicating effects of liquor products on drunken mice.
Wu, Z.-Q., Tian, X.-F., He, S.-G., Quan, L., Wei, Y.-L., & Wu, Z. (2017) · MedChemComm · doi:10.1039/c6md00491a · Cited by 9
Kozaeva, R., Klymenko, M. O., & Kostenko, V. О. (2021) · Fìzìologìčnij žurnal · doi:10.15407/fz67.06.060 · Cited by 10
Zhang, S., Liu, L., Li, X., Zhou, T., Shi, Q., Li, D., & Ju, X. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-04101-8 · Cited by 8
Hua, S., Li, M., Zhao, Q., et al. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.09.001 · Cited by 8
Anastasiou, I. A., Tentolouris, K. N., Lambadiari, V., Eleftheriadou, I., Tektonidou, M. G., & Tentolouris, N. (2023) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557523666230510123038 · Cited by 8
Yin, X., Hongbo, Z., Wei, Z., Wang, Y., Han, S., Zhou, M., Xu, W., & Han, W. (2023) · Cancer Management and Research · doi:10.2147/cmar.s424422 · Cited by 9
Pan, E., Sun, H., Zhang, S., Wang, J., Liu, Y., Wang, F., Xia, J., Qian, Y., Xu, X., & Dong, J. (2025) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2025139 · Cited by 7
Kelly, J., & Murphy, J. E. (2016) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2016.11.005 · Cited by 6
Moltó, E., Pintado, C., Louzada, R. A. N., Bernal‐Mizrachi, E., Andrés, A., Gallardo, N., & Bonzón‐Kulichenko, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216172 · Cited by 6
Salimi, A., Khezri, S., Amani, M., Badrinezhad, N., Hosseiny, S., & Saadati, R. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05180-0 · Cited by 7
Immunopathogenesis of Autoimmune Liver Damage
Czaja, A. J. (2017) · Technical report · doi:10.1016/b978-0-444-63707-9.00002-7 · Cited by 5
Cederbaum, A. I. (2015) · Current Pathobiology Reports · doi:10.1007/s40139-015-0092-0 · Cited by 5
Popova, T. A., Khusainova, G. K., Prokofiev, I. I., et al. (2020) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-020-04854-1 · Cited by 5
Pavlova, O., Bilous, V. L., Корса, В. В., Stepanenko, S. P., IuM, P., & Tykhomyrov, A. A. (2022) · Neurophysiology · doi:10.1007/s11062-023-09932-4 · Cited by 4
Role of ghrelin hormone in the development of alcohol-associated liver disease
Mahalingam, S., Bellamkonda, R., Kharbanda, K. K., Arumugam, M. K., Kumar, V. S., Casey, C. A., Leggio, L., & Rasineni, K. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116595 · Cited by 4
Oral supplementation of fucoxanthin regulates gene expression in the brain of middle-aged rats
Park, H., Amjad, E. C., Burnett, G., Ferdous, K. A., Scott, M., Jansen, J., Bannerman, S., Scott, M., Correll, R. N., Ciesla, L. M., et al. (2025) · British Journal Of Nutrition · doi:10.1017/s0007114525104996 · Cited by 3
“…the burden of these age-related neurodegenerative diseases will intensify (5) , especially as widely consumed dietary factors such as fructose, alcohol and high-fat diets have been implicated in promoting oxidative stress, lipid peroxidation, mitochondrial dysfunction and possibly ageing (6 – 8) .”
Pascual‐Morena, C., Lucerón‐Lucas‐Torres, M., Martínez‐García, I., Rodríguez‐Gutiérrez, E., Reynolds-Cortez, V., & Patiño‐Cardona, S. (2025) · Clinical Research in Cardiology · doi:10.1007/s00392-025-02818-x · Cited by 4
Converging mechanisms in ethanol neurotoxicity
Virgolini, M. B., & Pautassi, R. M. (2022) · Advances in neurotoxicology · doi:10.1016/bs.ant.2022.06.002 · Cited by 6
Metadata
- Authors
- Song, B.-J., Akbar, M., Abdelmegeed, M. A., Byun, K., Lee, B., Yoon, S. K., & Hardwick, J. P.
- Affiliations
- National Institutes of Health (US)
- Gachon University (KR)
- Catholic University of Korea (KR)
- Northeast Ohio Medical University (US)
- Corresponding author
- Song, Byoung-Joon
- ORCID
- Venue
- Redox Biology
- Publisher
- Elsevier BV
- Published
- 2014
- Volume
- 3
- Pages
- 109-123
- ISSN
- 2213-2317 (ISSN-L)
- PMC
- PMC4297931
- OpenAlex
- W2044394582
- Semantic Scholar
- 9ac8ad35c9150429a0fcab4a6ea86e3c3e4f9b88
- Cited by
- 123
- References
- 251
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 14 · 2023: 13 · 2022: 13 · 2021: 6 · 2020: 6 · 2019: 9 · 2018: 13 · 2017: 14 · 2016: 11 · 2015: 8
- FWCI
- 4.51
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Redox Biology (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute on Alcohol Abuse and Alcoholism
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Drug-Induced Hepatotoxicity and Protection
- Keywords
- mitochondrial dysfunction, post-translational modification, oxidative stress, nitrosative stress, alcohol-induced liver injury, non-alcoholic fatty liver disease, high-fat diet, CYP2E1, protein oxidation, protein nitration, protein phosphorylation, protein acetylation, advanced glycation end products, antioxidants, tissue damage
- MeSH terms
- Ethanol, Animals, Antioxidants, Humans, Liver Diseases, Mitochondria, Oxidation-Reduction, Protein Processing, Post-Translational, Oxidative Stress, Translational Research, Biomedical, Diet, High-Fat
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
A language model drew the claims from the paper on 2026-10-10, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-10-10 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
