Evidence map›Paper›PMID 10823900›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

A potent dimeric peptide antagonist of interleukin-5 that binds two interleukin-5 receptor alpha chains.

B P England, P Balasubramanian, I Uings, S Bethell, M J Chen, P J Schatz, Q Yin, Y F Chen, E A Whitehorn, A Tsavaler and 3 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Identification of cyclic peptides able to mimic the functional epitope of IgG1-Fc for human Fc gammaRI.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009
    Article
  3. Article
  4. Synthetic multivalent ligands as probes of signal transduction.Angewandte Chemie (International ed. in English) · 2006
    Review
  5. Article
  6. Stable "zeta" peptides that act as potent antagonists of the high-affinity IgE receptor.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  7. Review
  8. Understanding cytokine and growth factor receptor activation mechanisms.Critical reviews in biochemistry and molecular biology
    Review
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

13 authors.

B P EnglandAffymax Research Institute, 4001 Miranda Avenue, Palo Alto, CA 94304, USA. bruce_england@affymax.com
P Balasubramanian
I Uings
S Bethell
M J Chen
P J Schatz
Q Yin
Y F Chen
E A Whitehorn
A Tsavaler
C L Martens
R W Barrett
M McKinnon

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two series of peptides that specifically bind to the extracellular domain of the alpha chain of the human interleukin-5 receptor (IL-5Ralpha), but share no primary sequence homology to IL-5, were identified from libraries of random recombinant peptides. Affinity maturation procedures generated a 19-aa peptide that binds to the IL-5 receptor alpha/beta heterodimer complex with an affinity equal to that of IL-5 and is a potent and specific antagonist of IL-5 activity in a human eosinophil adhesion assay. The active form of the peptide is a disulfide-crosslinked dimer that forms spontaneously in solution. Gel filtration analysis, receptor-binding studies, and analytical ultracentrifugation reveal that the dimeric peptide binds simultaneously to two receptor alpha chains in solution. Furthermore, the dimer peptide, but not IL-5, can activate a chimeric receptor consisting of the IL-5Ralpha extracellular domain fused to the intracellular domain of the epidermal growth factor receptor, thus demonstrating that the peptide also promotes receptor dimerization in a cellular context. The functional antagonism produced by the bivalent interaction of the dimeric peptide with two IL-5R alpha chains represents a distinctive mechanism for the antagonism of cytokines that use heteromeric receptors.

Indexed as

Amino Acid SequenceDimerizationEosinophilsHumansInterleukin-5Molecular Sequence DataPeptide LibraryPeptidesReceptors, InterleukinReceptors, Interleukin-5Interleukin-5Peptide LibraryPeptidesReceptors, InterleukinReceptors, Interleukin-5

Identifiers

PMID10823900
PMCPMC18766

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.