Evidence map›Paper›PMID 35640380›Full record

ArticleRedox biology2022

Quantitative analysis of redox proteome reveals oxidation-sensitive protein thiols acting in fundamental processes of developmental hematopoiesis.

K Pimkova, M Jassinskaja, R Munita, M Ciesla, N Guzzi, P Cao Thi Ngoc, M Vajrychova, E Johansson, C Bellodi, J Hansson

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
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

13 citing papers in PubMed, 20 citations in OpenAlex.

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  9. Redox organization of living systems.Free radical biology & medicine · 2024
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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

10 authors at 2 institutions in 2 countries.

K PimkovaLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden; BIOCEV, 1st Medical Faculty, Charles University, Vestec, Czech Republic. Electronic address: kristyna.pimkova@lf1.cuni.cz.
M JassinskajaLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden.
R MunitaLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden.
M CieslaLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden.
N GuzziLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden.
P Cao Thi NgocLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden.
M VajrychovaBiomedical Research Center, University Hospital Hradec Kralove, Hradec Kralove, Czech Republic.
E JohanssonLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden.
C BellodiLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden.
J HanssonLund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden. Electronic address: jenny.hansson@med.lu.se.
Lund University · SEUniversity Hospital Hradec Králové · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fetal and adult hematopoietic stem and progenitor cells (HSPCs) are characterized by distinct redox homeostasis that may influence their differential cellular behavior in normal and malignant hematopoiesis. In this work, we have applied a quantitative mass spectrometry-based redox proteomic approach to comprehensively describe reversible cysteine modifications in primary mouse fetal and adult HSPCs. We defined the redox state of 4,438 cysteines in fetal and adult HSPCs and demonstrated a higher susceptibility to oxidation of protein thiols in fetal HSPCs. Our data identified ontogenic changes to oxidation state of thiols in proteins with a pronounced role in metabolism and protein homeostasis. Additional redox proteomic analysis identified oxidation changes to thiols acting in mitochondrial respiration as well as protein homeostasis to be triggered during onset of MLL-ENL leukemogenesis in fetal HSPCs. Our data has demonstrated that redox signaling contributes to the regulation of fundamental processes of developmental hematopoiesis and has pinpointed potential targetable redox-sensitive proteins in in utero-initiated MLL-rearranged leukemia.

Indexed as

ProteomeProteomicsAnimalsCysteineHematopoiesisMiceOxidation-ReductionSulfhydryl CompoundsCysteineProteomeSulfhydryl CompoundsCysteine oxidative modificationsDevelopmental biologyHematopoiesisLeukemiaProtein translationRedox proteomics

Identifiers

PMID35640380
PMCPMC9157258
OpenAlexW4281388702

What OpenQuestion holds

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LicenceCC BY
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.