Evidence map›Paper›PMID 42875468›Full record

ArticleNature communications2026

Regulation of PDH via cysteine oxidation on DLAT.

Fabiola Garcia-Cortizo, Tobias Weber, Hana Nůsková, Daniel Pfaff, Michael Büttner, Angela Wirth, Elisabeth Kliemank, Gernot Poschet, Marc Freichel, Thomas Fleming and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Fabiola Garcia-CortizoGerman Cancer Research Center (DKFZ) Heidelberg, Division B140, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-5244-5376
Tobias WeberGerman Cancer Research Center (DKFZ) Heidelberg, Division B140, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-0134-170X
Hana NůskováGerman Cancer Research Center (DKFZ) Heidelberg, Division B140, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-5562-9207
Daniel PfaffGerman Cancer Research Center (DKFZ) Heidelberg, Division B140, Heidelberg, Germany.
Michael BüttnerCentre for Organismal Studies (COS), Metabolomics Core Technology Platform, Heidelberg University, Im Neuenheimer Feld 360, Heidelberg, Germany.
Angela WirthInstitute of Pharmacology, Heidelberg University, Heidelberg, Germany.
Elisabeth KliemankDepartment for Endocrinology, Diabetology, Metabolic diseases and Clinical Chemistry, University Hospital Heidelberg, Im Neuenheimer Feld 410, Heidelberg, Germany.
Gernot PoschetCentre for Organismal Studies (COS), Metabolomics Core Technology Platform, Heidelberg University, Im Neuenheimer Feld 360, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-5344-0865
Marc FreichelInstitute of Pharmacology, Heidelberg University, Heidelberg, Germany.ORCID http://orcid.org/0000-0003-1387-2636
Thomas FlemingDepartment for Endocrinology, Diabetology, Metabolic diseases and Clinical Chemistry, University Hospital Heidelberg, Im Neuenheimer Feld 410, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-3232-4515
Alba SulajDepartment for Endocrinology, Diabetology, Metabolic diseases and Clinical Chemistry, University Hospital Heidelberg, Im Neuenheimer Feld 410, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-6051-6696
Peter Paul NawrothDepartment of Internal Medicine I and Clinical Chemistry, University Hospital, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-6134-7804
Julia SzendroediDepartment for Endocrinology, Diabetology, Metabolic diseases and Clinical Chemistry, University Hospital Heidelberg, Im Neuenheimer Feld 410, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-7296-7152
Aurelio A TelemanGerman Cancer Research Center (DKFZ) Heidelberg, Division B140, Heidelberg, Germany. a.teleman@dkfz.de.ORCID http://orcid.org/0000-0002-4237-9368

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) SFB1118
6 · The paper itself

Abstract

Pyruvate dehydrogenase (PDH) complex is a key regulator of metabolism, controlling flux from glycolysis into the tricarboxylic acid (TCA) cycle. PDH is often dysregulated in metabolic diseases and cancer. We discover here that in addition to its well characterized regulation by phosphorylation, PDH activity is also regulated via inhibitory oxidation of three cysteines of the DLAT subunit - Cys488, Cys586 and Cys618. Oxidation of these cysteines increases under oxidative stress, and is highly prevalent in mouse and human tissues. This mechanism enables cells to efficiently fight oxidative stress. Under oxidative stress, cells execute a metabolic shift, blocking glycolytic flux into the TCA cycle to shunt glycolytic carbons toward the pentose phosphate pathway. This generates NADPH which cells use to detoxify H

Indexed as

CysteinePyruvate Dehydrogenase ComplexAnimalsCitric Acid CycleGlucoseGlycolysisHumansHydrogen PeroxideMetabolic ReprogrammingMiceNADPOxidation-ReductionOxidative StressCysteineGlucoseHydrogen PeroxideNADPPyruvate Dehydrogenase Complex

Identifiers

PMID42875468
PMCPMC13669365

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.