Evidence map›Paper›PMID 10631974›Full record

ArticleProtein science : a publication of the Protein Society1999

The structures of the neurotrophin 4 homodimer and the brain-derived neurotrophic factor/neurotrophin 4 heterodimer reveal a common Trk-binding site.

R C Robinson, C Radziejewski, G Spraggon, J Greenwald, M R Kostura, L D Burtnick, D I Stuart, S Choe, E Y Jones

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

36 citing papers in PubMed, 99 citations in OpenAlex.

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  20. Nanoparticles-induced apoptosis of human airway epithelium is mediated by proNGF/p75Journal of toxicology and environmental health. Part A · 2017
    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

9 authors at 5 institutions in 3 countries.

R C RobinsonStructural Biology Laboratory, The Salk Institute, La Jolla, California 92037, USA. bob@sbl.salk.edu
C Radziejewski
G Spraggon
J Greenwald
M R Kostura
L D Burtnick
D I Stuart
S Choe
E Y Jones
Salk Institute for Biological Studies · USUniversity of Oxford · GBRegeneron (United States) · USUniversity of British Columbia · CAUniversity of California San Diego · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neurotrophins are growth factors that are involved in the development and survival of neurons. Neurotrophin release by a target tissue results in neuron growth along the neurotrophin concentration gradient, culminating in the eventual innervation of the target tissue. These activities are mediated through trk cell surface receptors. We have determined the structures of the heterodimer formed between brain-derived neurotrophic factor (BDNF) and neurotrophin 4 (NT4), as well as the structure of homodimer of NT4. We also present the structure of the Neurotrophin 3 homodimer, which is refined to higher resolution than previously published. These structures provide the first views of the architecture of the NT4 protomer. Comparison of the surface of a model of the BDNF homodimer with the structures of the neurotrophin homodimers reveals common features that may be important in the binding between the neurotrophins and their receptors. In particular, there exists an analogous region on the surface of each neurotrophin that is likely to be involved in trk receptor binding. Variations in sequence on the periphery of this common region serve to confer trk receptor specificity.

Indexed as

Binding SitesBrain-Derived Neurotrophic FactorCrystallizationCrystallography, X-RayHumansMolecular Sequence DataNerve Growth FactorsProtein Structure, QuaternaryReceptor, Nerve Growth FactorReceptor Protein-Tyrosine KinasesBrain-Derived Neurotrophic FactorNerve Growth Factorsneurotrophin 4Receptor, Nerve Growth FactorReceptor Protein-Tyrosine Kinases

Identifiers

PMID10631974
PMCPMC2144242
OpenAlexW2117219210

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.