Evidence map›Paper›PMID 12052773›Full record

ReviewEMBO reports2002

Peptidyl-prolyl isomerases: a new twist to transcription.

Peter E Shaw

Open access · greenAbstract readReview
In one paragraph

Review in EMBO reports, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 9% 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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 157 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. A tethering mechanism underlies Pin1-catalyzed prolineProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
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  11. Article
  12. The cellular response to ocean warming inFrontiers in microbiology · 2023
    Article
  13. Article
  14. Review
  15. Review
  16. Unravelling theMolecules (Basel, Switzerland) · 2022
    Article
  17. Article
  18. Inhibitors of theCells · 2021
    Review
  19. Review
  20. Article

1 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Peter E ShawSchool of Biomedical Sciences and Institute of Cell Signalling, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK. peter.shaw@nottingham.ac.uk
Queen's Medical Centre · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Peptidyl-prolyl isomerases (PPIs) catalyse the cis-trans isomerisation of peptide bonds N-terminal to proline residues in polypeptide chains. They have roles in the folding of newly synthesised proteins and in the function of the immune system. In addition, members of the parvulin-like family of PPIs have been implicated in cell cycle control. Their activity is directed by the prior phosphorylation of target proteins in both yeast and mammalian cells. More recent data have illustrated that they may also influence other nuclear events. This review examines PPI activity in the context of eukaryotic transcriptional regulation. The findings are consistent with a two-step model of conformational control, in which the outcome depends on the transcription factor involved.

Indexed as

Transcription, GeneticAnimalsGene SilencingHumansNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomeraseRNA Polymerase IITranscription FactorsNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePIN1 protein, humanRNA Polymerase IITranscription Factors

Identifiers

PMID12052773
PMCPMC1084152
OpenAlexW1987774012

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.