Evidence map›Paper›PMID 31909437›Full record

ArticleProtoplasma2020

Functional properties and the oligomeric state of alkyl hydroperoxide reductase subunit F (AhpF) in Pseudomonas aeruginosa.

Sung Hyun Hong, Sudhir Singh, Bhumi Nath Tripathi, Suvendu Mondal, Sangmin Lee, Hyun Suk Jung, Chuloh Cho, Shubhpreet Kaur, Jin-Hong Kim, Sungbeom Lee and 5 more

Abstract read
PubMed Publisher
In one paragraph

Article in Protoplasma, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Inhibition of ascorbic acid on Pseudomonas bubulae under super-chilled storage.World journal of microbiology & biotechnology · 2026
    Article
  2. Article
  3. Oxidative Stress Response inPathogens (Basel, Switzerland) · 2021
    Review
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

15 authors.

Sung Hyun HongAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Sudhir SinghAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Bhumi Nath TripathiAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Suvendu MondalAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Sangmin LeeDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, 24341, South Korea.
Hyun Suk JungDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, 24341, South Korea.
Chuloh ChoAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Shubhpreet KaurAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Jin-Hong KimAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Sungbeom LeeAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Hyoung-Woo BaiAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea.
Hyeun-Jong BaeDepartment of Bioenergy Science and Technology, Chonnam National University, Gwangju, 61186, South Korea.
Sang Yeol LeeDivision of Applied Life Science (BK21Plus), Gyeongsang National University, Jinju, 52828, South Korea.
Seung Sik LeeAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea. sslee@kaeri.re.kr.ORCID http://orcid.org/0000-0003-3900-9312
Byung Yeoup ChungAdvanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup, 56212, South Korea. bychung@kaeri.re.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alkyl hydroperoxide reductase subunit F (AhpF) is a well-known flavoprotein that transfers electrons from pyridine nucleotides to the peroxidase protein AhpC via redox-active disulfide centers to detoxify hydrogen peroxide. However, study of AhpF has historically been limited to particular eubacteria, and the connection between the functional and structural properties of AhpF remains unknown. The present study demonstrates the dual function of Pseudomonas aeruginosa AhpF (PaAhpF) as a reductase and a molecular chaperone. It was observed that the functions of PaAhpF are closely linked with its structural status. The reductase and foldase chaperone function of PaAhpF predominated for its low-molecular-weight (LMW) form, whereas the holdase chaperone function of PaAhpF was found associated with its high-molecular-weight (HMW) complex. Further, the present study also demonstrates the multiple function of PaAhpF in controlling oxidative and heat stresses in P. aeruginosa resistance to oxidative and heat stress.

Indexed as

Amino Acid SequenceBacterial ProteinsMolecular ChaperonesOxidation-ReductionPeroxiredoxinsPseudomonas aeruginosaBacterial ProteinsMolecular ChaperonesPeroxiredoxinsAlkyl hydroperoxide reductase subunit FChaperoneHeatHydrogen peroxidePseudomonas aeruginosa

Identifiers

PMID31909437

What OpenQuestion holds

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Registered trials

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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.