Evidence map›Paper›PMID 21854986›Full record

ArticleCell2011

Structural linkage between ligand discrimination and receptor activation by type I interferons.

Christoph Thomas, Ignacio Moraga, Doron Levin, Peter O Krutzik, Yulia Podoplelova, Angelica Trejo, Choongho Lee, Ganit Yarden, Susan E Vleck, Jeffrey S Glenn and 4 more

Abstract read
In one paragraph

Article in Cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 206 papers.

0numbers the graph read from it
0cells of the map it votes in
206citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

206 citing papers in PubMed, 353 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. A modular platform for Sterically Masked Activated Cytokines (SMACks).Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Interferon-Based Therapeutics in Cancer Therapy: Past, Present, and Future.International journal of molecular sciences · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

146 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 5 institutions in 3 countries.

Christoph ThomasHoward Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Ignacio Moraga
Doron Levin
Peter O Krutzik
Yulia Podoplelova
Angelica Trejo
Choongho Lee
Ganit Yarden
Susan E Vleck
Jeffrey S Glenn
Garry P Nolan
Jacob Piehler
Gideon Schreiber
K Christopher Garcia
Stanford University · USBaxter (United States) · USWeizmann Institute of Science · ILHoward Hughes Medical Institute · USOsnabrück University · DE

Funding

Structure-based engineering of immune cytokine signalingR01AI051321 · NIAID · STANFORD UNIVERSITY · PI Kenan Christopher GARCIA · 2002 to 2026
$5.6M
Structure, function and engineering of immune cytokine receptor signalingR37AI051321 · NIAID · STANFORD UNIVERSITY · PI GARCIA, KENAN CHRISTOPHER · 2013 to 2022
$4.2M
HCV NS4B: Translating molecular virology into novel antiviral therapiesR01AI087917 · NIAID · STANFORD UNIVERSITY · PI GLENN, JEFFREY S · 2010 to 2014
$2.0M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI051321NIAID NIH HHS R01 AI087917NIAID NIH HHS R01-AI087917NIAID NIH HHS R01-AI51321NIAID NIH HHS R37 AI051321
6 · The paper itself

Abstract

Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer. Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects. The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs. Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity. Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.

Indexed as

Amino Acid SequenceCell Line, TumorCrystallography, X-RayHumansInterferon-alphaInterferon Type ILigandsModels, MolecularMolecular Sequence DataReceptors, InterferonSequence AlignmentInterferon-alphainterferon omega 1Interferon Type ILigandsReceptors, Interferon

Identifiers

PMID21854986
PMCPMC3166218
OpenAlexW2073526502

What OpenQuestion holds

Textmetadata
LicenceTDM
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.