Evidence map›Paper›PMID 23421996›Full record

ArticleCell cycle (Georgetown, Tex.)2013

Regulation of PRDX1 peroxidase activity by Pin1.

Kai Ling Chu, Qiao Jing Lew, Vikneswari Rajasegaran, Jing Ting Kung, Lu Zheng, Qiaoyun Yang, Rachel Shaw, Nge Cheong, Yih-Cherng Liou, Sheng-Hao Chao

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2013. 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
0.9field-weighted citation impact, top 27% 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, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Membrane Bound Peroxiredoxin-1 Serves as a Biomarker forAntioxidants & redox signaling · 2022
    Article
  6. Article
  7. Review
  8. Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. 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

10 authors at 5 institutions in 2 countries.

Kai Ling ChuExpression Engineering Group, Bioprocessing Technology Institute, A*STAR (Agency for Science, Technology and Research), Singapore.
Qiao Jing Lew
Vikneswari Rajasegaran
Jing Ting Kung
Lu Zheng
Qiaoyun Yang
Rachel Shaw
Nge Cheong
Yih-Cherng Liou
Sheng-Hao Chao
Bioprocessing Technology Institute · SGAgency for Science, Technology and Research · SGNational University of Singapore · SGDigital Proteomics (United States) · USProtein Express (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pin1 isomerizes the phosphorylated Ser/Thr-Pro peptide bonds and regulates the functions of its binding proteins by inducing conformational changes. Involvement of Pin1 in the aging process has been suggested based on the phenotype of Pin1-knockout mice and its interaction with lifespan regulator protein, p66 (Shc) . In this study, we utilize a proteomic approach and identify peroxiredoxin 1 (PRDX1), another regulator of aging, as a novel Pin1 binding protein. Pin1 binds to PRDX1 through interacting with the phospho-Thr ( 90) -Pro ( 91) motif of PRDX1, and this interaction is abolished when the Thr ( 90) of PRDX1 is mutated. The Pin1 binding motif, Thr-Pro, is conserved in the 2-Cys PRDXs, PRDX1-4 and the interactions between Pin1 and PRDX2-4 are also demonstrated. An increase in hydrogen peroxide buildup and a decrease in the peroxidase activity of 2-Cys PRDXs were observed in Pin1 (-/-) mouse embryonic fibroblasts (MEFs), with the activity of PRDXs restored when Pin1 was re-introduced into the cells. Phosphorylation of PRDX1 at Thr ( 90) has been shown to inhibit its peroxidase activity; however, how exactly the activity of PRDX1 is regulated by phosphorylation still remains unknown. Here, we demonstrate that Pin1 facilitates the protein phosphatase 2A-mediated dephosphorylation of PRDX1, which helps to explain the accumulation of the inactive phosphorylated form of PRDX1 in Pin1 (-/-) MEFs. Collectively, we identify Pin1 as a novel PRDX1 binding protein and propose a mechanism for Pin1 in regulating the metabolism of reactive oxygen species in cells.

Indexed as

AgingAnimalsHEK293 CellsHeLa CellsHumansHydrogen PeroxideMiceNIMA-Interacting Peptidylprolyl IsomeraseOxidation-ReductionPeptidylprolyl IsomerasePeroxiredoxinsPhosphorylationProtein BindingProtein Phosphatase 2Reactive Oxygen SpeciesTranscription FactorsHydrogen PeroxideNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePeroxiredoxinsPIN1 protein, humanPin1 protein, mousePRDX1 protein, humanProtein Phosphatase 2Reactive Oxygen SpeciesTranscription Factorsaging and reactive oxygen speciesp66ShcphosphorylationPin1PP2APRDX1

Identifiers

PMID23421996
PMCPMC3637353
OpenAlexW1980620031

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.