Evidence map›Paper›PMID 25662955›Full record

ReviewExperimental biology and medicine (Maywood, N.J.)2015

Landscape of Pin1 in the cell cycle.

Cheng-Han Lin, Hao-Yi Li, Yu-Cheng Lee, Marcus J Calkins, Kuen-Haur Lee, Chia-Ning Yang, Pei-Jung Lu

Open access · greenAbstract readReview
In one paragraph

Review in Experimental biology and medicine (Maywood, N.J.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. Expression and significance of pin1 in the wound healing.Archives of dermatological research · 2024
    Article
  4. Protein Oxidation in Aging and Alzheimer's Disease Brain.Antioxidants (Basel, Switzerland) · 2024
    Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Post-translational Modifications of the Peptidyl-Prolyl Isomerase Pin1.Frontiers in cell and developmental biology · 2020
    Review
  19. Review
  20. Activity and Affinity of Pin1 Variants.Molecules (Basel, Switzerland) · 2019
    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

7 authors at 3 institutions in 1 country.

Cheng-Han LinInstitute of Clinical Medicine, Medical College, National Cheng Kung University, Tainan 704, Taiwan.
Hao-Yi LiInstitute of Clinical Medicine, Medical College, National Cheng Kung University, Tainan 704, Taiwan.
Yu-Cheng LeeInstitute of Clinical Medicine, Medical College, National Cheng Kung University, Tainan 704, Taiwan.
Marcus J CalkinsInstitute of Clinical Medicine, Medical College, National Cheng Kung University, Tainan 704, Taiwan.
Kuen-Haur LeeGraduate Institute of Cancer Biology and Drug Discovery, College of Medical Science and Technology, Taipei Medical University, Taipei 115, Taiwan.
Chia-Ning YangInstitute of Biotechnology, National University of Kaohsiung, 811, Kaohsiung, Taiwan pjlu2190@mail.ncku.edu.tw.
Pei-Jung LuInstitute of Clinical Medicine, Medical College, National Cheng Kung University, Tainan 704, Taiwan pjlu2190@mail.ncku.edu.tw.
National Cheng Kung University · TWNational University of Kaohsiung · TWTaipei Medical University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pin1 is a peptidyl-prolyl isomerase which plays a critical role in many diseases including cancer and Alzheimer's disease. The essential role of Pin1 is to affect stability, localization or function of phosphoproteins by catalyzing structural changes. Among the collection of Pin1 substrates, many have been shown to be involved in regulating cell cycle progression. The cell cycle disorder caused by dysregulation of these substrates is believed to be a common phenomenon in cancer. A number of recent studies have revealed possible functions of several important Pin1-binding cell cycle regulators. Investigating the involvement of Pin1 in the cell cycle may assist in the development of future cancer therapeutics. In this review, we summarize current knowledge regarding the network of Pin1 substrates and Pin1 regulators in cell cycle progression. In G1/S progression, cyclin D1, RB, p53, p27, and cyclin E are all well-known cell cycle regulators that are modulated by Pin1. During G2/M transition, our lab has shown that Aurora A suppresses Pin1 activity through phosphorylation at Ser16 and cooperates with hBora to modulate G2/M transition. We conclude that Pin1 may be thought of as a molecular timer which modulates cell cycle progression networks.

Indexed as

Cell CycleHumansNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphoproteinsSignal TransductionNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphoproteinsPIN1 protein, humanAurora Acell cyclehBoraPin1

Identifiers

PMID25662955
PMCPMC4935233
OpenAlexW1998983060

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.