Evidence map›Paper›PMID 24598927›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Crystallization and preliminary X-ray diffraction analysis of the interleukin-3 alpha receptor bound to the Fab fragment of antibody CSL362.

Sophie E Broughton, Timothy R Hercus, Tracy L Nero, Urmi Dhagat, Catherine M Owczarek, Matthew P Hardy, Louis J Fabri, Pierre D Scotney, Andrew D Nash, Nicholas J Wilson and 2 more

Open access · greenAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

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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

12 authors at 5 institutions in 1 country.

Sophie E BroughtonAustralian Cancer Research Foundation Rational Drug Discovery Centre and Biota Structural Biology Laboratory, St Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Timothy R HercusDivision of Human Immunology, The Centre for Cancer Biology, SA Pathology, Adelaide, South Australia, Australia.
Tracy L NeroAustralian Cancer Research Foundation Rational Drug Discovery Centre and Biota Structural Biology Laboratory, St Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Urmi DhagatAustralian Cancer Research Foundation Rational Drug Discovery Centre and Biota Structural Biology Laboratory, St Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Catherine M OwczarekCSL Limited, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Matthew P HardyCSL Limited, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Louis J FabriCSL Limited, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Pierre D ScotneyCSL Limited, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Andrew D NashCSL Limited, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Nicholas J WilsonCSL Limited, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Angel F LopezDivision of Human Immunology, The Centre for Cancer Biology, SA Pathology, Adelaide, South Australia, Australia.
Michael W ParkerAustralian Cancer Research Foundation Rational Drug Discovery Centre and Biota Structural Biology Laboratory, St Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
University of Melbourne · AUAustralian Cancer Research Foundation · AUCentre for Cancer Biology · AUSouth Australia Pathology · AUSt Vincents Institute of Medical Research · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interleukin-3 (IL-3) is a member of the beta common family of cytokines that regulate multiple functions of myeloid cells. The IL-3 receptor-specific alpha subunit (IL3Rα) is overexpressed on stem cells/progenitor cells of patients with acute myeloid leukaemia, where elevated receptor expression correlates clinically with a reduced patient survival rate. The monoclonal antibody (MAb) CSL362 is a humanized MAb derived from the murine MAb 7G3, originally identified for its ability to specifically recognize the human IL-3 receptor and for blocking the signalling of IL-3 in myeloid and endothelial cells. In order to elucidate the molecular mechanism of CSL362 antagonism, a preliminary structure of human IL3Rα in complex with the MAb CSL362 has been determined.

Indexed as

Amino Acid SequenceAntibodies, Monoclonal, HumanizedCrystallizationHumansInterleukin-3 Receptor alpha SubunitMolecular Sequence DataProtein BindingX-Ray DiffractionAntibodies, Monoclonal, HumanizedIL3RA protein, humanInterleukin-3 Receptor alpha SubunitcytokinesIL-3 receptor-specific alpha subunitinterleukin-3

Identifiers

PMID24598927
PMCPMC3944702
OpenAlexW1982811150

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.