Evidence map›Paper›PMID 23457259›Full record

ReviewCold Spring Harbor perspectives in biology2013

The insulin receptor: both a prototypical and atypical receptor tyrosine kinase.

Stevan R Hubbard

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

80 citing papers in PubMed, 1 synthesis or guideline pooled it, 147 citations in OpenAlex.

  1. Pooled it
  2. Insulin-like growth factor receptor signaling in physiology and disease.Signal transduction and targeted therapy · 2026
    Review
  3. Article
  4. Article
  5. The role of PYY in improving insulin resistance.Frontiers in endocrinology · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Insulin receptor responsiveness governs TGFβ-induced hepatic stellate cell activation: Insulin resistance instigates liver fibrosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. IRTKS contributes to the malignant progression of cervical cancer cells.Medical oncology (Northwood, London, England) · 2024
    Article
  18. Article
  19. Positive Effects of Physical Activity on Insulin Signaling.Current issues in molecular biology · 2024
    Review
  20. Article

20 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

1 author at 1 institution in 1 country.

Stevan R HubbardKimmel Center for Biology and Medicine of the Skirball Institute and Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, New York 10016, USA. stevan.hubbard@med.nyu.edu
New York University · US

Funding

STRUCTURAL STUDY OF THE INSULIN RECEPTOR TYROSINE KINASER01DK052916 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUBBARD, STEVAN R. · 1997 to 2010
$3.8M
NIDDK NIH HHS DK052916NIDDK NIH HHS R01 DK052916
6 · The paper itself

Abstract

Unlike prototypical receptor tyrosine kinases (RTKs), which are single-chain polypeptides, the insulin receptor (InsR) is a preformed, covalently linked tetramer with two extracellular α subunits and two membrane-spanning, tyrosine kinase-containing β subunits. A single molecule of insulin binds asymmetrically to the ectodomain, triggering a conformational change that is transmitted to the cytoplasmic kinase domains, which facilitates their trans-phosphorylation. As in prototypical RTKs, tyrosine phosphorylation in the juxtamembrane region of InsR creates recruitment sites for downstream signaling proteins (IRS [InsR substrate] proteins, Shc) containing a phosphotyrosine-binding (PTB) domain, and tyrosine phosphorylation in the kinase activation loop stimulates InsR's catalytic activity. For InsR, phosphorylation of the activation loop, which contains three tyrosine residues, also creates docking sites for adaptor proteins (Grb10/14, SH2B2) that possess specialized Src homology-2 (SH2) domains, which are dimeric and engage two phosphotyrosines in the activation loop.

Indexed as

Models, MolecularAdaptor Proteins, Signal TransducingEnzyme ActivationHumansInsulinPhosphorylationProtein Structure, TertiaryReceptor, InsulinSignal TransductionAdaptor Proteins, Signal TransducingInsulinReceptor, Insulin

Identifiers

PMID23457259
PMCPMC3578362
OpenAlexW2153554962

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.