The DOI matches its Crossref record; 134 of the 136 references it cites were found in a registry or an index, and 1 are not checked yet; none of the 142 sources its claims cite is checked for support yet.
Influence of Metabolism on Epigenetics and Disease
Open accessAbstract
Chemical modifications of histones and DNA, such as histone methylation, histone acetylation, and DNA methylation, play critical roles in epigenetic gene regulation. Many of the enzymes that add or remove such chemical modifications are known, or might be suspected, to be sensitive to changes in intracellular metabolism. This knowledge provides a conceptual foundation for understanding how mutations in the metabolic enzymes SDH, FH, and IDH can result in cancer and, more broadly, for how alterations in metabolism and nutrition might contribute to disease. Here, we review literature pertinent to hypothetical connections between metabolic and epigenetic states in eukaryotic cells.
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In the paper
“When undifferentiated ESCs are exposed to a specific chemical inhibitor of the TDH enzyme, intracellular levels of acetyl-CoA drop precipitously”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA Fluctuation
What the sources say
- Not checked yetcites Alexander et al., 2011 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesNone of the sources cited for this claim have been checked yet.
In the paper
“numerous acetylation marks on the K9, K14, K23, and K27 residues of histone H3 and the K5, K8, and K12 residues on histone H4 only appear over a 30–45 min window corresponding exactly with the Ox/RB boundary that is coincident with the peak abundance of intracellular acetyl-CoA.”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Control of Gene Expression by Acetyl-CoA
What the sources say
- Not checked yetcites Cai et al., 2011
- Not checked yetcites Cai and Tu, 2011
- Not checked yetcites Cai and Tu, 2012 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesNone of the sources cited for this claim have been checked yet.
In the paper
“Undifferentiated ESCs contain significantly higher levels of acetyl-CoA than the embryoid body (EB) cells induced to differentiate by the combined withdrawal of leukemia-inhibitory factor (LIF) and application of retinoic acid (RA)”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA Fluctuation
What the sources say
- Not checked yetcites Wang et al., 2009a
- Not checked yetcites Wang et al., 2011 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesNone of the sources cited for this claim have been checked yet.
In the paper
“Studies of two different eukaryotic cells have indeed given evidence of significant fluctuation in acetyl-CoA.”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA Fluctuation
What the sources say
- Not checked yetcites Klevecz et al., 2004 source
- Not checked yetcites Tu et al., 2005
- Not checked yetcites Tu and McKnight, 2006
Load-bearingStrength:boosted· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“the off-rate of acetyl-CoA binding to the yeast GCN5 enzyme is more than an order of magnitude more rapid than that of human p300/CBP HAT enzyme, human GCN5, or Tetrahymena GCN5”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA and Histone Acetyltransferase Enzymes
What the sources say
- Not checked yetcites Langer et al., 2002 source
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesNone of the sources cited for this claim have been checked yet.
In the paper
“Acetyl-CoA levels peak at a 6-fold-higher level at the transition of the oxidative (Ox) phase to the reductive building (RB) phase relative to the metabolically quiescent, reductive charging (RC) phase of the YMC”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA Fluctuation
What the sources say
- Not checked yetcites Cai et al., 2011
- Not checked yetcites Tu et al., 2007
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“The GCN5 histone acetylase enzyme of the SAGA complex has been identified as the critical enzyme responsible for transient acetylation of growth genes at the Ox/RB boundary”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA and Histone Acetyltransferase Enzymes
What the sources say
- Not checked yetcites Cai et al., 2011
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesNone of the sources cited for this claim have been checked yet.
In the paper
“Further DNA microarray and ChIP-seq experiments led to the identification of roughly 1,000 growth genes selectively acetylated and activated only when intracellular levels of acetyl-CoA peak”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Control of Gene Expression by Acetyl-CoA
What the sources say
- Not checked yetcites Cai et al., 2011
- Not checked yetcites Tu et al., 2005
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“catalytically active GCN5 is critically required for YMC oscillation”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA and Histone Acetyltransferase Enzymes
What the sources say
- Not checked yetcites Cai et al., 2011
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“when NAD+ levels were measured as a function of the YMC, which is far more robust in amplitude than metabolic fluctuation taking place as a function of the circadian cycle, no changes in NAD+ levels were observed”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ and Sirtuin Deacetylases
What the sources say
- Not checked yetcites Tu et al., 2007
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes
- It may state two separate claims as one. 28
- Probably not a substantial claim. 9
- The quote only partly states this claim. 1
None of the sources cited for this claim have been checked yet.
In the paper
“Undifferentiated mouse ESCs express levels of TDH upward of 1,000-fold higher relative to any other source of mouse cells or tissues, and the gene encoding TDH is stringently repressed immediately upon induction of ESC differentiation”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA Fluctuation
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“When NAD+ levels were measured in liver tissue of wild-type mice, two ultradian sets of peaks and troughs of NAD+ abundance were observed per 24 hr cycle (Ramsey et al., 2009). The peak-to-trough fluctuation in NAD+ abundance varied by 20%–30%, as reported in the latter study.”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ and Sirtuin Deacetylases
What the sources say
- Not checked yetcites Ramsey et al., 2009 source
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
In the paper
“By administering β-hydroxybutyrate to laboratory mice via an intraperitoneal pump, Shimazu and colleagues were able to demonstrate enhancement of H3K9 and H3K14 acetylation, induced expression of FOXO3A–regulated genes, and resistance to oxidative stress.”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ Independent Histone Deacetylases
What the sources say
- Not checked yetcites Shimazu et al., 2013 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
“Acetyl-CoA can also be produced catabolically from threonine via a mitochondrial threonine dehydrogenase enzyme uniquely expressed in mouse embryonic stem cells”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA Generation
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✗ Based: failsProbably not a substantial claim. The paper’s conclusions may not depend on it. The paper may give no reason why it holds.
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
“Acetyl-CoA can be produced through a variety of metabolic pathways, both catabolic and anabolic”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA Generation
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“This yeast growth gene battery matches closely with the genes induced by the c-Myc oncoprotein in mammalian cells”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Cancer Connection
What the sources say
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
“metazoan cells have evolved the malate-citrate antiporter system to move mitochondrial citrate to the cytoplasm, where it can combine with ATP and CoA to be converted to acetyl-CoA and oxaloacetate via the ATP citrate lyase enzyme, thereby affording a cytoplasmic pool of acetyl-CoA for lipid biosynthesis.”
§ Influence of Metabolism on Epigenetics and Disease > Acetyl-CoA: “Activated Acetate” and Histone Acetylation > Acetyl-CoA Generation
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
“the genes encoding SIRT3 and SIRT6 are tumor suppressors”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ and Sirtuin Deacetylases
What the sources say
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.
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
“S-adenosylmethionine (SAM) contains the active methyl donor group utilized by most methyltransferase enzymes”
§ Influence of Metabolism on Epigenetics and Disease > Methylation of DNA and Histones: SAM and the “Activated Methyl Cycle“
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“NAD+ levels fluctuate as a function of the circadian cycle, thereby instructing nuclear sirtuin enzymes to control the epigenetic state of chromatin in an NAD+-regulated manner.”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ and Sirtuin Deacetylases
What the sources say
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
“sirtuin enzymes sit in diametric opposition to protein acetylating and that protein acetylation can be influenced by intracellular levels of acetyl-CoA.”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ and Sirtuin Deacetylases
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
- Rests on an assumption: Histone and DNA chemical modifications are central to epigenetic control of gene expression.
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
“The activated methyl cycle can then be looped back via the transfer of a methyl group from N5-MTHF to homocysteine, regenerating methionine.”
§ Influence of Metabolism on Epigenetics and Disease > Methylation of DNA and Histones: SAM and the “Activated Methyl Cycle“
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“those that are NAD+-dependent, yielding O-acetyl-ADP-ribose, the deacetylated substrate, and nicotinamide as products”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation
What the sources say
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
“These data provide evidence that a distinct metabolite, β-hydroxybutyrate, is able not only to fuel metabolic adaptation to starvation but also to help sustain a protective epigenetic state by inhibiting the activities of NAD+-independent histone deacetylase enzymes.”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ Independent Histone Deacetylases
What the sources say
- Not checked yetcites Shimazu et al., 2013 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
- Rests on an assumption: Histone and DNA chemical modifications are central to epigenetic control of gene expression.
None of the sources cited for this claim have been checked yet.
In the paper
“AceCS2 is acetylated on a specific lysine residue that inhibits the ability of the enzyme to convert acetate into acetyl-CoA, a regulatory scheme conserved from Salmonella to mammals”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ and Sirtuin Deacetylases
What the sources say
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.
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
“SAM is produced by the condensation of methionine and ATP during the first of nine steps required for the conversion of methionine to succinyl-CoA.”
§ Influence of Metabolism on Epigenetics and Disease > Methylation of DNA and Histones: SAM and the “Activated Methyl Cycle“
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
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
“access to ample nutrients can simplistically be understood to inhibit the activities of the two proteins via acetyl-CoA-mediated acetylation. This inhibition, in turn, can be respectively counterbalanced by the mitochondrial SIRT3 and nuclear SIRT1 enzymes.”
§ Influence of Metabolism on Epigenetics and Disease > NAD+ and Deacetylation > NAD+ and Sirtuin Deacetylases
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
“Enzyme-catalyzed donation of the methyl group of SAM to an acceptor macromolecule yields S-adenosylhomocysteine (SAH), which, in turn, is hydrolyzed to homocysteine and adenosine.”
§ Influence of Metabolism on Epigenetics and Disease > Methylation of DNA and Histones: SAM and the “Activated Methyl Cycle“
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
In the paper
“Simultaneous increases in the intracellular abundance of threonine and 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) were observed upon TDH inhibition in ESCs.”
§ Influence of Metabolism on Epigenetics and Disease > Methylation of DNA and Histones: SAM and the “Activated Methyl Cycle“ > Threonine Dehydrogenase and SAM
What the sources say
- Not checked yetcites Alexander et al., 2011 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“These impediments were selective; threonine deprivation had no effect on the deposition of H3K4me1, H3K9me3, H3K27me3, H3K36me3, or H3K79me3 marks on histone tails.”
§ Influence of Metabolism on Epigenetics and Disease > Methylation of DNA and Histones: SAM and the “Activated Methyl Cycle“ > Threonine Dehydrogenase and SAM
What the sources say
- Not checked yetcites Shyh-Chang et al., 2013 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one. The quote only partly states this claim.
In the paper
“In a landmark paper, Yang Shi and coworkers showed that LSD1 (also called KDM1A or AOF2) is a nuclear FAD-dependent enzyme capable of demethylating methylated H3K4 both in vitro and in vivo, thereby establishing that histone methylation is a dynamic, reversible process (Shi et al., 2004).”
§ Influence of Metabolism on Epigenetics and Disease > FAD and Histone Demethylation
What the sources say
- Not checked yetcites Shi et al., 2004 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
- Rests on an assumption: FAD is derived from riboflavin and functions as a prosthetic group for certain oxidation-reduction enzymes.
None of the sources cited for this claim have been checked yet.
In the paper
“The latter protein is a small bZip transcription factor that, depending upon its heterodimeric partner, can either repress or activate gene expression (Hintze et al., 2007; Igarashi and Sun, 2006; Muto et al., 1998; Ochiai et al., 2006; Zhang et al., 2006).”
§ Influence of Metabolism on Epigenetics and Disease > Methylation of DNA and Histones: SAM and the “Activated Methyl Cycle“ > SAM and Histone/DNA Methylation
What the sources say
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
In the paper
“LSD1, in turn, regulates mitochondrial respiration and energy expenditure.”
§ Influence of Metabolism on Epigenetics and Disease > FAD and Histone Demethylation
What the sources say
- Not checked yetcites Hino et al., 2012 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“In this regard, intracellular fumarate and succinate concentrations are estimated to be in the high micromolar and low millimolar range, respectively (Johnson et al., 2008).”
§ Influence of Metabolism on Epigenetics and Disease > 2-Oxoglutarate-Dependent Dioxygenases > 2-Oxoglutarate
What the sources say
- Not checked yetcites Johnson et al., 2008 source
Load-bearingStrength:hedged· not yet calibratedTests✓ 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
“This presumably allows such enzymes to respond to changes in the concentrations of available agonists and antagonists.”
§ Influence of Metabolism on Epigenetics and Disease > 2-Oxoglutarate-Dependent Dioxygenases > 2-Oxoglutarate
Strength:hedged· not yet calibratedCausal:conditional· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
In the paper
“By contrast, the collagen prolyl hydroxylases have very low O2 Km, presumably so that they can function in environments such as poorly vascularized wounds (Hirsilä et al., 2003).”
§ Influence of Metabolism on Epigenetics and Disease > 2-Oxoglutarate-Dependent Dioxygenases > Iron and Oxygen
What the sources say
- Not checked yetcites Hirsilä et al., 2003 source
Strength:hedged· not yet calibratedCausal:conditional· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
In the paper
“5hmC in the nervous system is associated with actively transcribed genes and is recognized by the histone-reader protein MeCP2, which is mutationally inactivated in the neurological disorder of Rett syndrome (Mellén et al., 2012).”
§ Influence of Metabolism on Epigenetics and Disease > 2-Oxoglutarate-Dependent Dioxygenases > JmjC and TET Demethylases
What the sources say
- Not checked yetcites Mellén et al., 2012 source
Strength:plain· not yet calibratedCausal:correlational· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ 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
“This suggests either that these phenotypes are not due to epigenetic targets of R-2HG or that R-2HG-induced epigenetic changes are surprisingly dynamic.”
§ Influence of Metabolism on Epigenetics and Disease > SDH, FH, and IDH Mutations and Cancer
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
“These metabolites appear to cause cancer by affecting the behavior of various 2-oxoglutarate-dependent dioxygenases, including dioxygenases linked to DNA and histone methylation, and therefore have the potential to alter the epigenome.”
§ Influence of Metabolism on Epigenetics and Disease > SDH, FH, and IDH Mutations and Cancer
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
“In addition, TET2 inactivation is sufficient to promote hematopoietic stem cell self-renewal and to block differentiation (Figueroa et al., 2010; Li et al., 2011; Moran-Crusio et al., 2011; Noushmehr et al., 2010; Turcan et al., 2012; Losman et al., 2013).”
§ Influence of Metabolism on Epigenetics and Disease > SDH, FH, and IDH Mutations and Cancer
What the sources say
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
“In summary, SDH, FH, and IDH mutations cause the accumulation of succinate, fumarate, and R-2HG, respectively.”
§ Influence of Metabolism on Epigenetics and Disease > SDH, FH, and IDH Mutations and Cancer
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“Deletion of HIF1α, however, worsened the pathological changes observed in mice engineered to lack FH, suggesting that it normally constrains, rather than promotes, the emergence of FH-defective tumors (Adam et al., 2011).”
§ Influence of Metabolism on Epigenetics and Disease > SDH, FH, and IDH Mutations and Cancer
What the sources say
- Not checked yetcites Adam et al., 2011 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
In the paper
“In this regard, TET2 and IDH mutations are both found in acute myelogenous leukemia and are mutually exclusive, consistent with the idea that R-2HG produced by mutant IDH provides an alterative means of inactivating TET2 (Figueroa et al., 2010).”
§ Influence of Metabolism on Epigenetics and Disease > SDH, FH, and IDH Mutations and Cancer
What the sources say
- Not checked yetcites Figueroa et al., 2010 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
“This might suggest that folate deficiency correlates with, but does not cause, cancer or that folate is important during an early time window, perhaps occurring at an early age and prior to or during tumor initiation, but not thereafter.”
§ Influence of Metabolism on Epigenetics and Disease > Nutrition, Epigenetics, and Disease
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
“There is increasing evidence that early exposures, including intrauterine exposures, can lead to lasting epigenetic changes and that epigenetic differences can influence many phenotypes, including the risk of disease.”
§ Influence of Metabolism on Epigenetics and Disease > Conclusions and Future Questions
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
“Interestingly, R-2HG is sufficient to promote cytokine independence and block differentiation of hematopoietic cells in vitro and these effects are fairly rapidly reversed upon R-2HG withdrawal (Losman et al., 2013; K. Yen, personal communication).”
§ Influence of Metabolism on Epigenetics and Disease > SDH, FH, and IDH Mutations and Cancer
What the sources say
- Not checked yetcites Losman et al., 2013 source
- Not checked yetcites K. Yen, personal communication
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
The paper relies on this without support.
Histone and DNA chemical modifications are central to epigenetic control of gene expression.
“Chemical modifications of histones and DNA, such as histone methylation, histone acetylation, and DNA methylation, play critical roles in epigenetic gene regulation.”
The paper relies on this without support.
Cancer can arise from mutations in the metabolic enzymes SDH, FH, and IDH.
“This knowledge provides a conceptual foundation for understanding how mutations in the metabolic enzymes SDH, FH, and IDH can result in cancer”
The paper relies on this without support.
Both histone and DNA methylation require SAM as the high-energy methyl donor.
“Both histone and DNA methylation require SAM as the high-energy methyl donor (Figure 3).”
The paper relies on this without support.
FAD is derived from riboflavin and functions as a prosthetic group for certain oxidation-reduction enzymes.
“Flavin adenine dinucleotide (FAD) is derived from the vitamin riboflavin (vitamin B2) and functions as the prosthetic group for certain oxidation-reduction enzymes.”
The paper relies on this without support.
Riboflavin is phosphorylated by riboflavin kinase to FMN, which is converted to FAD by FAD synthetase.
“Riboflavin is phosphorylated by riboflavin kinase to generate riboflavin 5′-phosphate (sometimes called flavin monucleotide or FMN), which is then converted to FAD by FAD synthetase (also called FMN adenyl-transferase).”
The paper relies on this without support.
Riboflavin kinase appears rate limiting for FAD production.
“The former enzyme appears to be rate limiting for FAD production.”
The paper relies on this without support.
FAD is produced in mitochondria.
“FAD is produced in mitochondria.”
The paper relies on this without support.
2-oxoglutarate-dependent dioxygenases require oxygen and Fe(II) in addition to 2-oxoglutarate.
“2-oxoglutarate-dependent dioxygenases require oxygen and Fe (II) in addition to 2-oxoglutarate (also called α-ketoglutarate).”
The paper relies on this without support.
2-oxoglutarate is decarboxylated to succinate during the oxidation reaction.
“The latter metabolite is decarboxylated to succinate during the oxidation reaction (Figure 5).”
The paper relies on this without support.
These enzymes are sensitive to reactive oxygen species and their activity is enhanced by ascorbic acid.
“These enzymes are also sensitive to reactive oxygen species and their activity is enhanced in the presence of ascorbic acid.”
The paper relies on this without support.
HIF synthesis is influenced by the PI3K-AKT-mTOR pathway sensing nutrients, while its degradation is controlled by EglN prolyl hydroxylases responding to oxygen and Krebs cycle intermediates.
“HIF synthesis is influenced by the PI3K-AKT-mTOR pathway, which senses nutrients such as glucose and amino acids, while its degradation is under the control of the EglN prolyl hydroxylases, which respond to changes in oxygen and different Krebs cycle intermediates (Figure 6A).”
The paper relies on this without support.
2-oxoglutarate is produced from isocitrate in mitochondria by IDH2 and IDH3 in the TCA cycle and can also be generated from several amino acids including arginine, proline, histidine, and glutamine.
“2-oxoglutarate is produced from isocitrate in the mitochondria by the action of isocitrate dehydrogenases 2 and 3 (IDH2 and IDH3) in the TCA cycle and can also be generated from several amino acids including arginine, proline, histidine, and glutamine, which can be converted to glutamic acid and transaminated to produce 2-oxoglutarate.”
The paper relies on this without support.
2-oxoglutarate generated in the TCA cycle is converted to succinyl CoA by the 2-oxoglutarate dehydrogenase complex and is consumed during conversion of cysteine and lysine to pyruvate and acetyl-CoA.
“2-oxoglutarate generated in the course of the TCA cycle is converted to succinyl CoA by the action of the 2-oxoglutarate dehydrogenase complex and is also consumed during the conversion of cysteine and lysine to pyruvate and acetyl-CoA, respectively.”
The paper relies on this without support.
2-oxoglutarate generated in mitochondria can enter the cytosol via specific transporters such as the malate-2-oxoglutarate antiporter.
“2-oxoglutarate generated in the mitochondria can enter the cytosol, either as 2-oxoglutarate or after transamination to produce glutamic acid, via specific transporter proteins such as the malate-2-oxoglutarate antiporter, which participates in the malate-aspartate shuttle.”
The paper relies on this without support.
IDH1 resides in the cytosol and peroxisomes and provides an alternative source for nonmitochondrial 2-oxoglutarate.
“A third IDH paralog, IDH1, resides in the cytosol and peroxisomes and provides an alternative source for nonmitochondrial 2-oxoglutarate.”
The paper relies on this without support.
Altered epigenetics is believed to play a part in diseases including diabetes, obesity, dyslipidemia, hypertension, and neurodegeneration.
“Altered epigenetics is believed to play a part in a variety of diseases in addition to cancer, including diabetes, obesity, dyslipidemia, hypertension, and neurodegeneration.”
The paper relies on this without support.
Diet influences one-carbon metabolism, which plays an important role in DNA and histone methylation and in disease risk.
“In this regard, particular attention has been paid to the influence of diet on one-carbon metabolism, which plays an important role in DNA and histone methylation and in risk of disease.”
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“metabolic intermediates of the TCA cycle affect epigenetic-mediated control of gene expression through regulating the modification of histones and DNA 137,138”
From Inside and out: the activities of senescence in cancer (2014) · cites this paper as [137]
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Threonine-sensitive histone mark changes from H3K4me3 to H3K3me3
MinorOne passage identifies H3K4me3 as a mark whose deposition is impaired by threonine restriction, but the next identifies H3K3me3 as the mark that disappears alongside H3K4me2. The two passages give different identities for the affected mark.
“The H3K4me2 and H3K3me3 marks that disappear when mouse ESCs are deprived of threonine”
“Intriguingly, threonine restriction was observed to dramatically impede deposition of the H3K4me2 and H3K4me3 marks on chromatin.”
Citations
Cites
DNA methylation patterns and epigenetic memory
Bird, A. (2002) · Genes & Development · doi:10.1101/gad.947102 · Cited by 7,124
Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836
A bivalent chromatin structure marks key developmental genes in embryonic stem cells
Bernstein, B. E., Mikkelsen, T. S., Xie, X., Kamal, M., Huebert, D. J., Cuff, J., Fry, B., Meissner, A., Wernig, M., Plath, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.02.041 · Cited by 5,361
Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051
Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
Ito, S., Shen, L., Dai, Q., Wu, S. C., Collins, L. B., Swenberg, J. A., He, C., & Zhang, Y. (2011) · Science · doi:10.1126/science.1210597 · Cited by 3,451
Cancer epigenetics: from mechanism to therapy
Dawson, M. A., & Kouzarides, T. (2012) · Cell · doi:10.1016/j.cell.2012.06.013 · Cited by 3,203
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
Xu, W., Yang, H., Liu, Y., Yang, Y., Wang, P., Kim, S.-H., Ito, S., Yang, C., Wang, P., Xiao, M.-T., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.12.014 · Cited by 2,875
Tet-Mediated Formation of 5-Carboxylcytosine and Its Excision by TDG in Mammalian DNA
He, Y., Li, B.-Z., Li, Z., Liu, P., Wang, Y., Tang, Q., Ding, J., Jia, Y., Chen, Z., Li, L., et al. (2011) · Science · doi:10.1126/science.1210944 · Cited by 2,776
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Items 401–500 of 925
Yang, D., Peng, M., Hou, Y., Qin, Y., Wan, X., Zhu, P., Liu, S., Yang, L., Zeng, H., Jin, T., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2714-7 · Cited by 36
The metabolic-epigenetic nexus in type 2 diabetes mellitus
Davison, G. W., Irwin, R. E., & Walsh, C. P. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.12.025 · Cited by 35
The Basally Expressed p53-Mediated Homeostatic Function
Nagpal, I., & Yuan, Z.-M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.775312 · Cited by 35
Cardiac Metabolism in Perspective
Taegtmeyer, H., Lam, T., & Davogustto, G. (2016) · Comprehensive physiology · doi:10.1002/cphy.c150056 · Cited by 40
Threonine metabolism and embryonic stem cell self-renewal
Chen, G., & Wang, J. (2013) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000007 · Cited by 34
Circles of Life: linking metabolic and epigenetic cycles to immunity
Lio, C. J., & Huang, S. C. (2020) · Immunology · doi:10.1111/imm.13207 · Cited by 36
Monitoring Metabolites Using an NAD(P)H‐sensitive Polymer Dot and a Metabolite‐Specific Enzyme
Chen, H., Yu, J., Zhang, J., Sun, K., Ding, Z., Jiang, Y., Hu, Q., Wu, C., & Chiu, D. T. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202106156 · Cited by 34
Mito-Nuclear Communication in Hepatocellular Carcinoma Metabolic Rewiring
Mello, T., Simeone, I., & Galli, A. (2019) · Cells · doi:10.3390/cells8050417 · Cited by 34
Nalbantoğlu, S., & Karadağ, A. (2021) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2021.114031 · Cited by 34
Molecular or Metabolic Reprograming: What Triggers Tumor Subtypes?
Eason, K., & Sadanandam, A. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0141 · Cited by 33
The Regulatory Role of NAD in Human and Animal Cells
Kulikova, V., Gromyko, D. V., & Nikiforov, A. A. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918070040 · Cited by 34
Metabolism Is a Key Regulator of Induced Pluripotent Stem Cell Reprogramming
Spyrou, J., Gardner, D. K., & Harvey, A. J. (2019) · Stem Cells International · doi:10.1155/2019/7360121 · Cited by 33
Mitochondrial DNA and Neurodegeneration: Any Role for Dietary Antioxidants?
Bordoni, L., & Gabbianelli, R. (2020) · Antioxidants · doi:10.3390/antiox9080764 · Cited by 32
Lysine-Specific Demethylase 2 Suppresses Lipid Influx and Metabolism in Hepatic Cells
Nagaoka, K., Hino, S., Sakamoto, A., Anan, K., Takase, R., Umehara, T., Yokoyama, S., Sasaki, Y., & Nakao, M. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01404-14 · Cited by 33
Evaluating the therapeutic potential of one-carbon donors in nonalcoholic fatty liver disease
Bakir, M. B., Salama, M. A., Refaat, R., Ali, M. A., Khalifa, E. A., & Kamel, M. A. E.-N. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.01.039 · Cited by 33
Li, A. M., & Ye, J. (2023) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-062822-120857 · Cited by 31
Mechanisms by Which Different Functional States of Mitochondria Define Yeast Longevity
Beach, A., Leonov, A., Arlia‐Ciommo, A., Svistkova, V., Lutchman, V., & Titorenko, V. I. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16035528 · Cited by 32
Understanding the Complexity of Epigenetic Target Space
Pande, V. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01507 · Cited by 35
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Patro, C. P. K., Biswas, N., Pingle, S. C., Feng, L., Anekoji, M., Jones, L., Kesari, S., Wang, F., & Ashili, S. (2022) · Journal of Translational Medicine · doi:10.1186/s12967-022-03823-8 · Cited by 35
Orlandi, I., Pellegrino-Coppola, D., Vai, M., & Dipartimento di Biotecnologie e Bioscienze, U. D. M.-B. (2014) · Microbial Cell · doi:10.15698/mic2014.12.178 · Cited by 32
From the (Epi)Genome to Metabolism and Vice Versa; Examples from Hematologic Malignancy
Karagianni, P., Giannouli, S., & Voulgarelis, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126321 · Cited by 35
Chen, P., Shi, G.-X., Liu, T., Li, B., Jiang, S., Zheng, X., & Jiang, L. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4036274 · Cited by 31
mTORC2 and Metabolic Reprogramming in GBM: at the Interface of Genetics and Environment
Masui, K., Cavenee, W. K., & Mischel, P. S. (2015) · Brain Pathology · doi:10.1111/bpa.12307 · Cited by 31
Developmental roles of protein N‐terminal acetylation
Silva, R. D., & Martinho, R. G. (2015) · PROTEOMICS · doi:10.1002/pmic.201400631 · Cited by 31
Pavlova, O., Fraitag, S., & Hohl, D. (2016) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2016.07.015 · Cited by 30
Li, Y., Lei, X., Guo, W., Wu, S., Duan, Y., Yang, X., & Yang, X. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.01.095 · Cited by 30
Tanaka, Y., Konishi, A., Obinata, H., & Tsuneoka, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-55075-0 · Cited by 31
HIF-1α Mediates Osteoclast-Induced Mandibular Condyle Growth via AMPK Signaling
Tang, Y., Hong, C., Cai, Y., Zhu, J., Hu, X., Tian, Y., Song, X., Song, Z., Jiang, R., & Kang, F. (2020) · Journal of Dental Research · doi:10.1177/0022034520935788 · Cited by 30
Shteinfer‐Kuzmine, A., Verma, A., Arif, T., Aizenberg, O., Paul, A., & Shoshan‐Barmatz, V. (2020) · IUBMB Life · doi:10.1002/iub.2407 · Cited by 31
Loss of ciliated cells and altered airway epithelial integrity in cystic fibrosis
Collin, A. M., Lecocq, M., Detry, B. R., Carlier, F. M., Bouzin, C., de Sany, P., Hoton, D., Verleden, S. E., Froidure, A., Pilette, C., et al. (2021) · Journal of Cystic Fibrosis · doi:10.1016/j.jcf.2021.09.019 · Cited by 30
Targeting the methionine addiction of cancer.
Sedillo, J. C., & Cryns, V. L. (2022) · PubMed Central · Cited by 30
Takaya, J., Iharada, A., Okihana, H., & Kaneko, K. (2013) · Nutrition Research · doi:10.1016/j.nutres.2013.07.015 · Cited by 33
Stunff, H. L., Véret, J., Kassis, N., Denom, J., Meneyrol, K., Paul, J., Cruciani‐Guglielmacci, C., Magnan, C., & Janel, N. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00807 · Cited by 31
Subramanian, C., Frank, M. W., Tangallapally, R. P., Yun, M., White, S. W., Lee, R. E., Jr., Rock, C. O., & Jackowski, S. (2022) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12570 · Cited by 29
Kim, Y. H., Yoon, S. J., Kim, M., Kim, H. H., Song, Y. S., Jung, J. W., Han, D., Cho, S. W., Kwon, S. W., & Park, Y. J. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-2025 · Cited by 29
The role of mitophagy in metabolic diseases and its exercise intervention
Tang, S., Geng, Y., & Lin, Q. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1339128 · Cited by 34
Adam, A., Lie, K. K., Whatmore, P., Jakt, L. M., Moren, M., & Skjærven, K. H. (2019) · PLoS ONE · doi:10.1371/journal.pone.0220934 · Cited by 31
Oxygen in the neonatal period: Oxidative stress, oxygen load and epigenetic changes
Lorente-Pozo, S., Llorca, A. P., Lara‐Cantón, I., Soláz-García, Á., García‐Giménez, J. L., Pallardó, F. V., & Vento, M. (2020) · Seminars in Fetal and Neonatal Medicine · doi:10.1016/j.siny.2020.101090 · Cited by 29
The Mitochondrial Protein VDAC1 at the Crossroads of Cancer Cell Metabolism: The Epigenetic Link
Amsalem, Z., Arif, T., Shteinfer‐Kuzmine, A., Caspi, V. C., & Shoshan‐Barmatz, V. (2020) · Cancers · doi:10.3390/cancers12041031 · Cited by 30
Oncometabolites and the response to radiotherapy
Xiang, K., Jendrossek, V., & Matschke, J. (2020) · Radiation Oncology · doi:10.1186/s13014-020-01638-9 · Cited by 30
Protein Acetylation at the Interface of Genetics, Epigenetics and Environment in Cancer
Harachi, M., Masui, K., Cavenee, W. K., Mischel, P. S., & Shibata, N. (2021) · Metabolites · doi:10.3390/metabo11040216 · Cited by 29
Zaiou, M., Amrani, R., Rihn, B. H., & Hajri, T. (2021) · Biomedicines · doi:10.3390/biomedicines9091256 · Cited by 30
Epithelial-mesenchymal transition promotes metabolic reprogramming to suppress ferroptosis
Guo, W., Duan, Z., Wu, J., & Zhou, B. P. (2025) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2025.02.013 · Cited by 33
Epigenetic modulation of metabolic decisions
Öst, A., & Pospisilik, J. A. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.12.005 · Cited by 28
Touch, act and go: landing and operating on nucleosomes
Speranzini, V., Pilotto, S., Sixma, T. K., & Mattevi, A. (2016) · The EMBO Journal · doi:10.15252/embj.201593377 · Cited by 32
Epigenetics and Reproductive Medicine
Huntriss, J., Balen, A., Sinclair, K., Brison, D. R., & Picton, H. (2018) · BJOG An International Journal of Obstetrics & Gynaecology · doi:10.1111/1471-0528.15240 · Cited by 28
Polyunsaturated fatty acids and DNA methylation in colorectal cancer
Sarabi, M. M., Khorramabadi, R. M., Zare, Z., & Eftekhar, E. (2019) · World Journal of Clinical Cases · doi:10.12998/wjcc.v7.i24.4172 · Cited by 28
Xu, X., Zhang, C., Xu, X., Cai, R., Guan, Q., Chen, X., Chen, Y., Zhang, Z., XuHan, X., Lin, Y., et al. (2023) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiad139 · Cited by 28
Etiology of super-enhancer reprogramming and activation in cancer
Zhou, R. W., & Parsons, R. E. (2023) · Epigenetics & Chromatin · doi:10.1186/s13072-023-00502-w · Cited by 31
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Lomberk, G. A., & Urrutia, R. A. (2015) · Surgical Clinics of North America · doi:10.1016/j.suc.2015.05.011 · Cited by 28
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Nagashima, F., Nishiyama, R., Iwao, B., Kawai, Y., Ishii, C., Yamanaka, T., Uchino, H., & Inazu, M. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2017.113 · Cited by 27
Pereira, S., Crisóstomo, L., Sousa, M., Oliveira, P. F., & Alves, M. G. (2020) · Current Zoology · doi:10.1093/eep/dvaa019 · Cited by 29
Fernandez-Fuente, G., Rigby, M. J., & Puglielli, L. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101653 · Cited by 30
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Sureshchandra, S., Stull, C., Ligh, B. J. K., Nguyen, S. B., Grant, K. A., & Messaoudi, I. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.04.027 · Cited by 26
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Masui, K., Harachi, M., Cavenee, W. K., Mischel, P. S., & Shibata, N. (2020) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.20002 · Cited by 24
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Ferreira, L. M. R., Li, A. M., Serafim, T. L., Sobral, M. C. M., Alpoim, M. C., & Urbano, A. M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165887 · Cited by 27
Critical roles and clinical perspectives of RNA methylation in cancer
Li, G., Yao, Q., Liu, P., Zhang, H., Liu, Y., Li, S., Shi, Y., Li, Z., & Zhu, W. (2024) · MedComm · doi:10.1002/mco2.559 · Cited by 29
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Rapizzi, E., Fucci, R., Giannoni, E., Canu, L., Richter, S., Cirri, P., & Mannelli, M. (2015) · Endocrine Related Cancer · doi:10.1530/erc-14-0479 · Cited by 26
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Lee, S., Lee, J., Chae, S., Moon, Y., Lee, H., Park, B., Yang, E. G., Hwang, D., & Park, H. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx747 · Cited by 26
Sano, A., Kakazu, E., Morosawa, T., Inoue, J., Kogure, T., Ninomiya, M., Iwata, T., Umetsu, T., Nakamura, T., Takai, S., et al. (2018) · Journal of Gastroenterology · doi:10.1007/s00535-018-1435-5 · Cited by 26
Xiao, J., Liu, Y., Wu, F., Liu, R., Xie, Y., Yang, Q., Li, Y., Liu, M., Li, S., & Tang, H. (2019) · Molecular Therapy · doi:10.1016/j.ymthe.2019.11.021 · Cited by 26
RetractedDecoding mitochondria's role in immunity and cancer therapy
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Wang, Y., Wu, J., Zhang, G., Shi, Y., Meng, Y., Lv, P., Huang, W., Su, Y., Zhou, Z., Wang, B., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62951-z · Cited by 28
Kakazu, E., Sano, A., Morosawa, T., Inoue, J., Ninomiya, M., Iwata, T., Nakamura, T., Takai, S., Sawada, S., Katagiri, H., et al. (2019) · Hepatology Research · doi:10.1111/hepr.13346 · Cited by 26
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Rabhi, N., Hannou, S. A., Froguel, P., & Annicotte, J. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00304 · Cited by 27
Tsai, T., & John, J. C. S. (2016) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2016.03.005 · Cited by 25
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Zhang, X., Liu, J., & Cao, X. (2017) · Cellular and Molecular Immunology · doi:10.1038/cmi.2017.115 · Cited by 24
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Liu, S., Lai, W., Shi, Y., Liu, N., Ouyang, L., Zhang, Z., Chen, L., Wang, X., Qian, B., Xiao, D., et al. (2020) · npj Precision Oncology · doi:10.1038/s41698-020-0110-5 · Cited by 23
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Lim, H. J., & Kim, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228617 · Cited by 24
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Burg, T., & Van Den Bosch, L. (2023) · Current Opinion in Neurology · doi:10.1097/wco.0000000000001164 · Cited by 24
Demethylation of the Human Eotaxin-3 Gene Promoter Leads to the Elevated Expression of Eotaxin-3
Lim, E. J., & Rothenberg, M. E. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1302454 · Cited by 24
Ortbauer, M., Ripper, D., Fuhrmann, T., Lassi, M., Auernigg‐Haselmaier, S., Stiegler, C., & König, J. S. (2015) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500819 · Cited by 24
Li, Y., Lei, X., Yin, Z., Guo, W., Wu, S., & Yang, X. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.04.009 · Cited by 24
Bernardini, C., Algieri, C., Mantia, D. L., Zannoni, A., Salaroli, R., Trombetti, F., Forni, M., Pagliarani, A., & Nesci, S. (2021) · Histochemistry and Cell Biology · doi:10.1007/s00418-021-01981-2 · Cited by 24
Simmons, R. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-323-40139-5.00006-1 · Cited by 24
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Fernandez-Fuente, G., Overmyer, K. A., Lawton, A. J., Kasza, I., Shapiro, S. L., Gallego‐Muñoz, P., Coon, J. J., Denu, J. M., Alexander, C. M., & Puglielli, L. (2023) · Communications Biology · doi:10.1038/s42003-023-05311-1 · Cited by 23
Qin, Y., Yang, P. C., He, W., Li, D., Zeng, L., Li, J., Zhou, T., Peng, J., Cao, L., & Huang, W. G. (2024) · Clinical Epigenetics · doi:10.1186/s13148-024-01650-w · Cited by 26
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Spannl, S., Buhl, T., Nellas, I., Zeidan, S. A., Iyer, K. V., Khaliullina, H., Schultz, C., Nadler, A., Dye, N. A., & Eaton, S. (2020) · The EMBO Journal · doi:10.15252/embj.2019101767 · Cited by 23
Abnormal early folliculogenesis due to impeded pyruvate metabolism in mouse oocytes
Tanaka, K., Hayashi, Y., Takehara, A., Ito‐Matsuoka, Y., Tachibana, M., Yaegashi, N., & Matsui, Y. (2021) · Biology of Reproduction · doi:10.1093/biolre/ioab064 · Cited by 23
Ghirardini, E., Calugi, F., Sagona, G., Vetta, F. D., Palma, M., Battini, R., Cioni, G., Pizzorusso, T., & Baroncelli, L. (2021) · Genes · doi:10.3390/genes12081123 · Cited by 24
Yu, Z., Peng, Y., Gao, J., Zhou, M., Shi, L., Zhao, F. H., Wang, C., Tian, X., Feng, L., Huo, X., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade0387 · Cited by 24
Functional genomics in the study of mind-body therapies.
Niles, H. F., Mehta, D. H., Corrigan, A. A., Bhasin, M., & Denninger, J. W. (2014) · PubMed Central · Cited by 23
Epigenetic regulation by endogenous metabolite pharmacology
Kulkarni, R. A., Montgomery, D. C., & Meier, J. L. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.02.002 · Cited by 24
Hartwig, F. P., Smith, G. D., Simpkin, A. J., Victora, C. G., Relton, C. L., & Caramaschi, D. (2020) · Nutrients · doi:10.3390/nu12113309 · Cited by 24
GnRH antagonist alters the migration of endometrial epithelial cells by reducing CKB
Chen, Q., Fan, Y., Zhou, X., Yan, Z., Kuang, Y., Zhang, A., & Xu, C. (2020) · Reproduction · doi:10.1530/rep-19-0578 · Cited by 22
HO-1 and Heme: G-Quadruplex Interaction Choreograph DNA Damage Responses and Cancer Growth
Canesin, G., Muralidharan, A. M., Swanson, K. D., & Wegiel, B. (2021) · Cells · doi:10.3390/cells10071801 · Cited by 22
Park, E., Jeong, J., Won, S., Sharma, S. P., Gebru, Y. A., Ganesan, R., Gupta, H., Suk, K. T., & Kim, D. J. (2021) · Cells · doi:10.3390/cells10102634 · Cited by 22
Targeted metabolic profiling of wounds in diabetic and nondiabetic mice
Sood, R. F., Gu, H., Djukovic, D., Deng, L., Ga, M., Muffley, L. A., Raftery, D., & Hocking, A. M. (2015) · Wound Repair and Regeneration · doi:10.1111/wrr.12299 · Cited by 22
Arif, T., Stern, O., Pittala, S., Caspi, V. C., & Shoshan‐Barmatz, V. (2019) · Cells · doi:10.3390/cells8111330 · Cited by 22
Specific regulation of epigenome landscape by metabolic enzymes and metabolites
Yu, X., & Li, S. (2024) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.13049 · Cited by 24
Endocrine Disruptors and Metabolic Changes: Impact on Puberty Control
Peralta, M., & Lizcano, F. (2024) · Endocrine Practice · doi:10.1016/j.eprac.2024.01.006 · Cited by 25
Epigenome–metabolism nexus in the retina: implications for aging and disease
Mondal, A. K., Gaur, M., Advani, J., & Swaroop, A. (2024) · Trends in Genetics · doi:10.1016/j.tig.2024.04.012 · Cited by 20
MicroRNA 195-5p Targets Foxo3 Promoter Region to Regulate Its Expression in Granulosa Cells
Bai, Y., Pan, B., Zhan, X., Silver, H., & Li, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136721 · Cited by 21
Salman, M. S. K., Kamel, M. A. E.-N., El‐Nabi, S. H., Ismail, A. H. A., Ullah, S., Al-Ghamdi, A. K., Hathout, H. M. R., & El‐Garawani, I. M. (2022) · PLoS ONE · doi:10.1371/journal.pone.0265455 · Cited by 21
RetractedCassiano, L. M. G., Oliveira, M. D. S., Pioline, J., Salim, A. C. M., & Coimbra, R. S. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02624-6 · Cited by 21
Aprile, M., Cataldi, S., Perfetto, C., Federico, A., Ciccodicola, A., & Costa, V. (2023) · British Journal of Cancer · doi:10.1038/s41416-023-02282-2 · Cited by 21
Metabolic-epigenetic coupling in osteoclast differentiation
Ivashkiv, L. B. (2015) · Nature Medicine · doi:10.1038/nm.3815 · Cited by 21
Metadata
- Authors
- Kaelin, W. G., & McKnight, S. L.
- Affiliations
- Brigham and Women's Hospital (US)
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Kaelin, William G.
- McKnight, Steven L.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2013-03
- Volume
- 153
- Issue
- 1
- Pages
- 56-69
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3775362
- OpenAlex
- W2035010201
- Semantic Scholar
- 732b8265382027a841509c4b7ef3185231cba71c
- Cited by
- 920
- References
- 136
- Citations by year
- 2026: 89 · 2025: 41 · 2024: 52 · 2023: 49 · 2022: 57 · 2021: 85 · 2020: 74 · 2019: 84 · 2018: 58 · 2017: 70 · 2016: 73 · 2015: 82 · 2014: 71 · 2013: 32
- FWCI
- 8.09
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (R01CA068490, R01CA076120)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- metabolism, epigenetics, histone methylation, histone acetylation, DNA methylation, epigenetic regulation, succinate dehydrogenase, fumarase, isocitrate dehydrogenase, cancer, nutrition and disease
- MeSH terms
- Acetylation, Animals, Disease, Histones, Humans, Metabolism, Methylation, DNA Methylation, Epigenesis, Genetic
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 2026-10-06, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-10-06 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
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