Evidence map›Paper›PMID 21852138›Full record

ReviewTrends in biochemical sciences2011

Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins.

Yih-Cherng Liou, Xiao Zhen Zhou, Kun Ping Lu

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 182 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
182citing papers in PubMed, 2 pooled it
12.2field-weighted citation impact, top 1% 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

182 citing papers in PubMed, 2 syntheses or guidelines pooled it, 325 citations in OpenAlex.

  1. Pooled it
  2. Association of rs2233678 and rs2233679 polymorphisms in the PIN1 gene with cancer risk: a meta-analysis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Pooled it
  3. Trial
  4. Trial
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Proline/sidechain C-H/O interactions stabilizePhysical chemistry chemical physics : PCCP · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Pin1 promotes human CaCell communication and signaling : CCS · 2024
    Article
  18. Expression and significance of pin1 in the wound healing.Archives of dermatological research · 2024
    Article
  19. Protein Oxidation in Aging and Alzheimer's Disease Brain.Antioxidants (Basel, Switzerland) · 2024
    Review
  20. Article

122 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

3 authors at 3 institutions in 2 countries.

Yih-Cherng LiouDepartment of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543. dbslyc@nus.edu.sg
Xiao Zhen Zhou
Kun Ping Lu
Beth Israel Deaconess Medical Center · USHarvard University · USNational University of Singapore · SG

Funding

Function and Regulation of the Prolyl Isomerase Pin1R01GM058556 · NIGMS · BETH ISRAEL DEACONESS MEDICAL CENTER · PI LU, KUN PING · 1999 to 2010
$3.9M
Role of the Prolyl lsomerase Pin1 in Alzheimer's DiseaseR01AG017870 · NIA · BETH ISRAEL DEACONESS MEDICAL CENTER · PI LU, KUN PING · 2001 to 2011
$2.7M
Role of the Putative Tumor Suppressor PinX1 in the Etiology of Liver CancerR01CA122434 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI ZHOU, XIAO ZHEN · 2006 to 2010
$1.5M
PinX1, a Putative Tumor Suppressor for Prostate CancerR21CA100301 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI ZHOU, XIAO ZHEN · 2003 to 2004
$340k
NCI NIH HHS R01 CA122434NCI NIH HHS R01CA122434NCI NIH HHS R21 CA100301NIA NIH HHS AG017870NIA NIH HHS R01 AG017870NIGMS NIH HHS R01 GM058556NIGMS NIH HHS R01GM058556
6 · The paper itself

Abstract

Pin1 is a highly conserved enzyme that only isomerizes specific phosphorylated Ser/Thr-Pro bonds in certain proteins, thereby inducing conformational changes. Such conformational changes represent a novel and tightly controlled signaling mechanism regulating a spectrum of protein activities in physiology and disease; often through phosphorylation-dependent, ubiquitin-mediated proteasomal degradation. In this review, we summarize recent advances in elucidating the role and regulation of Pin1 in controlling protein stability. We also propose a mechanism by which Pin1 functions as a molecular switch to control the fates of phosphoproteins. We finally stress the need to develop tools to visualize directly Pin1-catalyzed protein conformational changes as a way to determine their roles in the development and treatment of human diseases.

Indexed as

AgingGene ExpressionHumansNeoplasmsNeurodegenerative DiseasesNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphoproteinsProtein ConformationProtein StabilityProteolysisTelomereNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphoproteinsPIN1 protein, human

Identifiers

PMID21852138
PMCPMC3185210
OpenAlexW2059977521

What OpenQuestion holds

Textmetadata
LicenceTDM
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.