Evidence map›Paper›PMID 24876346›Full record

ArticleScience (New York, N.Y.)2014

Neural migration. Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism.

Kai Xu, Zhuhao Wu, Nicolas Renier, Alexander Antipenko, Dorothea Tzvetkova-Robev, Yan Xu, Maria Minchenko, Vincenzo Nardi-Dei, Kanagalaghatta R Rajashankar, Juha Himanen and 2 more

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

112 citing papers in PubMed, 161 citations in OpenAlex.

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

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 2 institutions in 1 country.

Kai XuStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Zhuhao WuLaboratory of Brain Development and Repair, Rockefeller University, New York, NY 10065, USA.
Nicolas RenierLaboratory of Brain Development and Repair, Rockefeller University, New York, NY 10065, USA.
Alexander AntipenkoStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Dorothea Tzvetkova-RobevStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Yan XuStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Maria MinchenkoStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Vincenzo Nardi-DeiStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Kanagalaghatta R RajashankarDepartment of Chemistry and Chemical Biology, Cornell University and Northeastern Collaborative Access Team, Advanced Photon Source, Argonne, IL 60439, USA.
Juha HimanenStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Marc Tessier-LavigneLaboratory of Brain Development and Repair, Rockefeller University, New York, NY 10065, USA. nikolovd@mskcc.org marctl@mail.rockefeller.edu.
Dimitar B NikolovStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA. nikolovd@mskcc.org marctl@mail.rockefeller.edu.
Memorial Sloan Kettering Cancer Center · USRockefeller University · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Netrins are secreted proteins that regulate axon guidance and neuronal migration. Deleted in colorectal cancer (DCC) is a well-established netrin-1 receptor mediating attractive responses. We provide evidence that its close relative neogenin is also a functional netrin-1 receptor that acts with DCC to mediate guidance in vivo. We determined the structures of a functional netrin-1 region, alone and in complexes with neogenin or DCC. Netrin-1 has a rigid elongated structure containing two receptor-binding sites at opposite ends through which it brings together receptor molecules. The ligand/receptor complexes reveal two distinct architectures: a 2:2 heterotetramer and a continuous ligand/receptor assembly. The differences result from different lengths of the linker connecting receptor domains fibronectin type III domain 4 (FN4) and FN5, which differs among DCC and neogenin splice variants, providing a basis for diverse signaling outcomes.

Indexed as

AnimalsAxonsCell MovementDCC ReceptorFibronectinsLigandsMembrane ProteinsMiceMice, Inbred C57BLMice, Mutant StrainsNerve Growth FactorsNetrin-1Netrin ReceptorsNeuronsProtein MultimerizationProtein Structure, TertiaryDcc protein, mouseDCC ReceptorFibronectinsLigandsMembrane ProteinsneogeninNerve Growth FactorsNetrin-1Netrin ReceptorsNtn1 protein, mouseReceptors, Cell SurfaceTumor Suppressor Proteins

Identifiers

PMID24876346
PMCPMC4369087
OpenAlexW1987423602

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.