Evidence map›Paper›PMID 29158260›Full record

ArticleThe Journal of biological chemistry2018

The actin-organizing formin protein Fhod3 is required for postnatal development and functional maintenance of the adult heart in mice.

Tomoki Ushijima, Noriko Fujimoto, Sho Matsuyama, Meikun Kan-O, Hiroshi Kiyonari, Go Shioi, Yohko Kage, Sho Yamasaki, Ryu Takeya, Hideki Sumimoto

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.

  1. Pooled it
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  7. Article
  8. Review
  9. Article
  10. Article
  11. FHODs: Nuclear tethered formins for nuclear mechanotransduction.Frontiers in cell and developmental biology · 2023
    Review
  12. Review
  13. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
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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

10 authors at 3 institutions in 2 countries.

Tomoki UshijimaDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582.
Noriko FujimotoDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582.
Sho MatsuyamaDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582; Department of Pharmacology, Faculty of Medicine, University of Miyazaki, Miyazaki 889-1692.
Meikun Kan-ODepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582.
Hiroshi KiyonariAnimal Resource Development Unit, Kobe 650-0047; Genetic Engineering Team, RIKEN Center for Life Science Technologies, Kobe 650-0047.
Go ShioiGenetic Engineering Team, RIKEN Center for Life Science Technologies, Kobe 650-0047.
Yohko KageDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582; Department of Pharmacology, Faculty of Medicine, University of Miyazaki, Miyazaki 889-1692.
Sho YamasakiDivision of Molecular Immunology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.
Ryu TakeyaDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582; Department of Pharmacology, Faculty of Medicine, University of Miyazaki, Miyazaki 889-1692. Electronic address: takeya@med.miyazaki-u.ac.jp.
Hideki SumimotoDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582. Electronic address: hsumi@med.kyushu-u.ac.jp.
Kyushu University · JPUniversity of Miyazaki · JPCLS Technology (Norway) · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cardiac development and function require actin-myosin interactions in the sarcomere, a highly organized contractile structure. Sarcomere assembly mediated by formin homology 2 domain-containing 3 (Fhod3), a member of formins that directs formation of straight actin filaments, is essential for embryonic cardiogenesis. However, the role of Fhod3 in the neonatal and adult stages has remained unknown. Here, we generated floxed

Indexed as

Actin CytoskeletonActinsAnimalsForminsGene Knockout TechniquesHeartHeart Function TestsMiceMice, Inbred C57BLMice, KnockoutMice, TransgenicMicrofilament ProteinsMuscle ProteinsMyocytes, CardiacMyofibrilsSarcomeresActinsFhod3 protein, mouseForminsMicrofilament ProteinsMuscle Proteinsactincardiac developmentcardiac hypertrophyforminheartmyofibrilsarcomere

Identifiers

PMID29158260
PMCPMC5766910
OpenAlexW2770070927

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.