Evidence map›Paper›PMID 32900959›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

CydDC functions as a cytoplasmic cystine reductase to sensitize

Alexander Mironov, Tatyana Seregina, Konstantin Shatalin, Maxim Nagornykh, Rustem Shakulov, Evgeny Nudler

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Envelope destabilization by AcrABCommunications biology · 2026
    Article
  3. Article
  4. Disruptions ofCells · 2024
    Article
  5. Article
  6. Activation of Purine Biosynthesis Suppresses the Sensitivity ofInternational journal of molecular sciences · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Frontiers in microbiology · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Article
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

6 authors at 2 institutions in 2 countries.

Alexander MironovDepartment of Molecular Biology, Engelhardt Institute of Molecular Biology, Russian Academy of Science, 119991 Moscow, Russia.ORCID 0000-0003-3914-1380
Tatyana SereginaDepartment of Molecular Biology, Engelhardt Institute of Molecular Biology, Russian Academy of Science, 119991 Moscow, Russia.
Konstantin ShatalinDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016.ORCID 0000-0001-8653-2355
Maxim NagornykhDepartment of Molecular Biology, Engelhardt Institute of Molecular Biology, Russian Academy of Science, 119991 Moscow, Russia.
Rustem ShakulovDepartment of Molecular Biology, Engelhardt Institute of Molecular Biology, Russian Academy of Science, 119991 Moscow, Russia.
Evgeny NudlerDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016; evgeny.nudler@nyulangone.org.
Engelhardt Institute of Molecular Biology · RUNew York University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

l-cysteine is the source of all bacterial sulfurous biomolecules. However, the cytoplasmic level of l-cysteine must be tightly regulated due to its propensity to reduce iron and drive damaging Fenton chemistry. It has been proposed that in

Indexed as

AminoglycosidesAnti-Bacterial AgentsATP-Binding Cassette TransportersCysteineCytochrome b GroupCytoplasmElectron Transport Chain Complex ProteinsEscherichia coli ProteinsHydrogen PeroxideNADH, NADPH OxidoreductasesOxidative StressOxidoreductasesPeriplasmAminoglycosidesAnti-Bacterial AgentsATP-Binding Cassette TransportersCysteineCystine reductasecytochrome bd terminal oxidase complex, E coliCytochrome b GroupElectron Transport Chain Complex ProteinsEscherichia coli ProteinsHydrogen PeroxideNADH, NADPH OxidoreductasesOxidoreductasesaminoglycosidesbacteriacytochromel-cysteineoxidative stress

Identifiers

PMID32900959
PMCPMC7519257
OpenAlexW3083816072

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.