Evidence map›Paper›PMID 16754968›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006

An improved resolution structure of the human beta common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope.

P D Carr, F Conlan, S Ford, D L Ollis, I G Young

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–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

11 citing papers in PubMed.

  1. The JAK-STAT pathway: from structural biology to cytokine engineering.Signal transduction and targeted therapy · 2024
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Role of the β Common (βc) Family of Cytokines in Health and Disease.Cold Spring Harbor perspectives in biology · 2018
    Review
  8. Article
  9. Review
  10. Review
  11. 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

5 authors.

P D CarrResearch School of Chemistry, Australian National University, Canberra, Australia. pdc@rsc.anu.edu.au
F Conlan
S Ford
D L Ollis
I G Young

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

X-ray diffraction has been used to produce and refine a model of the extracellular domains of the beta common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule.

Indexed as

Amino AcidsBinding SitesCytokine Receptor Common beta SubunitEpitopesHumansMolecular StructureProtein ConformationReceptors, Cell SurfaceX-Ray DiffractionAmino AcidsCSF2RB protein, humanCytokine Receptor Common beta SubunitEpitopesReceptors, Cell Surface

Identifiers

PMID16754968
PMCPMC2243076

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.