Evidence map›Paper›PMID 29097144›Full record

ReviewSteroids2018

Paxillin actions in the nucleus.

Xiaoting Ma, Stephen R Hammes

Abstract readReview
In one paragraph

Review in Steroids, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Working a second job: Cell adhesion proteins that moonlight in the nucleus.Frontiers in cell and developmental biology · 2023
    Review
  13. Physiological and pathological roles of Hic‑5 in several organs (Review).International journal of molecular medicine · 2022
    Review
  14. Review
  15. Review
  16. DNA methylation and gene expression alterations in zebrafish embryos exposed to cadmium.Environmental science and pollution research international · 2021
    Article
  17. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Xiaoting MaDepartment of Medicine, Division of Endocrinology and Metabolism, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, United States; Department of Pathology and Laboratory Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, United States. Electronic address: Xiaoting_Ma@urmc.rochester.edu.
Stephen R HammesDepartment of Medicine, Division of Endocrinology and Metabolism, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, United States; Department of Pathology and Laboratory Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, United States. Electronic address: Stephen_Hammes@urmc.rochester.edu.
University of Rochester · US

Funding

Estrogen Signaling in a Mouse Model for LymphangioleiomyomatosisR01CA193583 · NCI · UNIVERSITY OF ROCHESTER · PI HAMMES, STEPHEN R. · 2016 to 2020
$1.7M
Paxillin as a Liaison between Extranuclear and Intranuclear Steroid SignalingR01GM101709 · NIGMS · UNIVERSITY OF ROCHESTER · PI HAMMES, STEPHEN R. · 2013 to 2016
$1.2M
NCI NIH HHS R01 CA193583NIGMS NIH HHS R01 GM101709
6 · The paper itself

Abstract

Paxillin is a group III LIM domain protein that is best characterized as a cytoplasmic scaffold/adaptor protein that functions primarily as a mediator of focal adhesion. However, emerging studies indicate that paxillin's functions are far broader. Not only does paxillin appear to regulate cytoplasmic kinase signaling, but it also cycles between the cytoplasm and nucleus, and may serve as an important regulator of mRNA trafficking and subsequent translation. Herein, we provide some insights suggesting that paxillin, like its relative Hic-5, has nuclear binding partners and mediates critical processes within the nucleus, at least in part functioning as coregulator of nuclear receptors and nuclear kinases to mediate genomic signaling.

Indexed as

Amino Acid MotifsAnimalsCell NucleusHumansMolecular Targeted TherapyNuclear Export SignalsPaxillinNuclear Export SignalsPaxillinAndrogenCancerCoregulatorNuclearPaxillin

Identifiers

PMID29097144
PMCPMC5902031
OpenAlexW2766206099

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.