Evidence map›Paper›PMID 23046137›Full record

ReviewImmunological reviews2012

Structural insights into the common γ-chain family of cytokines and receptors from the interleukin-7 pathway.

Scott T R Walsh

Open access · greenAbstract readReview
In one paragraph

Review in Immunological reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Interleukin-7 and Immunosenescence.Journal of immunology research · 2017
    Review
  10. IL-7 Induces an Epitope Masking ofMediators of inflammation · 2017
    Article
  11. Article
  12. The common γ-chain cytokine receptor: tricks-and-treats for T cells.Cellular and molecular life sciences : CMLS · 2016
    Review
  13. Article
  14. Reversal of tumor immune inhibition using a chimeric cytokine receptor.Molecular therapy : the journal of the American Society of Gene Therapy · 2014
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. 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

1 author at 1 institution in 1 country.

Scott T R WalshDepartment of Cell Biology and Molecular Genetics, Institute for Bioscience and Biotechnology Research, W. M. Keck Laboratory for Structural Biology, Rockville, MD, USA. swalsh12@umd.edu
Institute for Bioscience and Biotechnology Research

Funding

Molecular Recognition Studies of the Interleukin-7 PathwayR01AI072142 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI WALSH, SCOTT T · 2008 to 2012
$1.6M
Molecular Recognition Studies of the Interleukin-7 PathwayR56AI072142 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI WALSH, SCOTT T · 2013 to 2013
$357k
NIAID NIH HHS AI72142NIAID NIH HHS R01 AI072142NIAID NIH HHS R56 AI072142
6 · The paper itself

Abstract

Over the past 13 years, numerous crystal structures of complexes of the common γ-chain (γ(c)) cytokine receptors and their cytokines have been solved. Even with the remarkable progress in the structural biology of γ(c) receptors and their cytokines or interleukins, there are valuable lessons to be learned from the structural and biophysical studies of interleukin-7 (IL-7) and its α-receptor (IL-7Rα) and comparisons with other γ(c) family members. The structure of the IL-7/IL-7Rα complex teaches that interfaces between the γ(c) interleukins and their receptors can vary in size, polarity, and specificity, and that significant conformational changes might be necessary for complexes of interleukins and their receptors to bind the shared, activating γ(c) receptor. Binding, kinetic, and thermodynamic studies of IL-7 and IL-7Rα show that glycosylation and electrostatics can be important to interactions between interleukins and their receptor, even where the glycans and charged residues are distant from the interface. The structure of the IL-7Rα homodimer is a reminder that often-ignored non-activating complexes likely perform roles just as important to signaling as activating complexes. And last but not least, the structural and biophysical studies help explain and potentially treat the diseases caused by aberrant IL-7 signaling.

Indexed as

Binding SitesGlycosylationHumansInterleukin-7KineticsModels, MolecularProtein BindingProtein ConformationProtein MultimerizationReceptors, Interleukin-7Signal TransductionStatic ElectricityThermodynamicsT-LymphocytesIL7 protein, humanInterleukin-7Receptors, Interleukin-7

Identifiers

PMID23046137
PMCPMC3471675
OpenAlexW2148710439

What OpenQuestion holds

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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.