Evidence map›Paper›PMID 26074875›Full record

ReviewFrontiers in endocrinology2015

The Novel Functions of High-Molecular-Mass Complexes Containing Insulin Receptor Substrates in Mediation and Modulation of Insulin-Like Activities: Emerging Concept of Diverse Functions by IRS-Associated Proteins.

Fumihiko Hakuno, Toshiaki Fukushima, Yosuke Yoneyama, Hiroyasu Kamei, Atsufumi Ozoe, Hidehito Yoshihara, Daisuke Yamanaka, Takashi Shibano, Meri Sone-Yonezawa, Bu-Chin Yu and 2 more

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in endocrinology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.1field-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

24 citing papers in PubMed, 45 citations in OpenAlex.

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  17. Etiology of Metabolic Syndrome and Dietary Intervention.International journal of molecular sciences · 2018
    Review
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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

12 authors at 3 institutions in 1 country.

Fumihiko HakunoDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Toshiaki FukushimaLaboratory of Biomedical Chemistry, Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University , Hiroshima , Japan ; Department of Biological Sciences, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology , Kanagawa , Japan.
Yosuke YoneyamaDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Hiroyasu KameiDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Atsufumi OzoeDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Hidehito YoshiharaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science , Tokyo , Japan.
Daisuke YamanakaDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Takashi ShibanoDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Meri Sone-YonezawaDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Bu-Chin YuDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Kazuhiro ChidaDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
Shin-Ichiro TakahashiDepartment of Animal Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan ; Department of Applied Biological Chemistry, Graduate School of Agriculture and Life Sciences, The University of Tokyo , Tokyo , Japan.
The University of Tokyo · JPHiroshima University · JPTokyo Metropolitan Institute of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insulin-like peptides, such as insulin-like growth factors (IGFs) and insulin, induce a variety of bioactivities, such as growth, differentiation, survival, increased anabolism, and decreased catabolism in many cell types and in vivo. In general, IGFs or insulin bind to IGF-I receptor (IGF-IR) or insulin receptor (IR), activating the receptor tyrosine kinase. Insulin receptor substrates (IRSs) are known to be major substrates of receptor kinases, mediating IGF/insulin signals to direct bioactivities. Recently, we discovered that IRSs form high-molecular-mass complexes (referred to here as IRSomes) even without IGF/insulin stimulation. These complexes contain proteins (referred to here as IRSAPs; IRS-associated proteins), which modulate tyrosine phosphorylation of IRSs by receptor kinases, control IRS stability, and determine intracellular localization of IRSs. In addition, in these complexes, we found not only proteins that are involved in RNA metabolism but also RNAs themselves. Thus, IRSAPs possibly contribute to modulation of IGF/insulin bioactivities. Since it is established that disorder of modulation of insulin-like activities causes various age-related diseases including cancer, we could propose that the IRSome is an important target for treatment of these diseases.

Indexed as

cancerinsulininsulin-like growth factorinsulin receptor substrateIRS-associated proteinIRSome

Identifiers

PMID26074875
PMCPMC4443775
OpenAlexW1602996820

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.