Evidence map›Paper›PMID 20874719›Full record

ReviewJournal of cellular and molecular medicine2010

Genes, proteins and complexes: the multifaceted nature of FHL family proteins in diverse tissues.

Thiruchelvi Shathasivam, Thomas Kislinger, Anthony O Gramolini

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of cellular and molecular medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed, 1 pooled it
4.4field-weighted citation impact, top 5% 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

65 citing papers in PubMed, 1 synthesis or guideline pooled it, 110 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. FHL2 in arterial medial calcification in chronic kidney disease.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2024
    Article
  10. Article
  11. Article
  12. The roles of FHL2 in cancer.Clinical and experimental medicine · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022
    Review
  19. Article
  20. The Roles of FHL3 in Cancer.Frontiers in oncology · 2022
    Review

5 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 2 institutions in 1 country.

Thiruchelvi ShathasivamDepartment of Physiology, University of Toronto, Toronto, Canada.
Thomas Kislinger
Anthony O Gramolini
University of Toronto · CAUniversity Health Network · CA

Funding

Canadian Institutes of Health Research MOP-84267
6 · The paper itself

Abstract

Four and a half LIM domain protein 1 (FHL1) is the founding member of the FHL family of proteins characterized by the presence of four and a half highly conserved LIM domains. The LIM domain is a protein-interaction motif and is involved in linking proteins with both the actin cytoskeleton and transcriptional machinery. To date, more than 25 different protein interactions have been identified for full length FHL1 and its spliced variants, and these interactions can be mapped to a variety of functional classes. Because FHL1 is expressed predominantly in skeletal muscle, all of these proteins interactions translate into a multifunctional and integral role for FHL1 in muscle development, structural maintenance, and signalling. Importantly, 27 FHL1 genetic mutations have been identified that result in at least six different X-linked myopathies, with patients often presenting with cardiovascular disease. FHL1 expression is also significantly up-regulated in a variety of cardiac disorders, even at the earliest stages of disease onset. Alternatively, FHL1 expression is suppressed in a variety of cancers, and ectopic FHL1 expression offers potential for some phenotype rescue. This review focuses on recent studies of FHL1 in muscular dystrophies and cardiovascular disease, and provides a comprehensive review of FHL1s multifunctional roles in skeletal muscle.

Indexed as

Intracellular Signaling Peptides and ProteinsMuscle ProteinsAmino Acid SequenceAnimalsCardiovascular DiseasesHumansLIM Domain ProteinsMuscle, SkeletalMuscular DiseasesMuscular DystrophiesMutationNeoplasmsProtein Interaction Domains and MotifsReceptors, NotchSignal TransductionFHL1 protein, humanIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMuscle ProteinsReceptors, Notch

Identifiers

PMID20874719
PMCPMC3822721
OpenAlexW2086333084

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.