Evidence map›Paper›PMID 21307234›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011

Heparan sulfate sugar modifications mediate the functions of slits and other factors needed for mouse forebrain commissure development.

Christopher D Conway, Kathy M Howe, Nicole K Nettleton, David J Price, John O Mason, Thomas Pratt

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

42 citing papers in PubMed, 66 citations in OpenAlex.

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  14. Deciphering functional glycosaminoglycan motifs in development.Current opinion in structural biology · 2018
    Review
  15. Review
  16. Diverse roles for glycosaminoglycans in neural patterning.Developmental dynamics : an official publication of the American Association of Anatomists · 2018
    Review
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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

6 authors at 1 institution in 1 country.

Christopher D ConwayGenes and Development Group, Centre for Integrative Physiology, University of Edinburgh, Edinburgh EH8 9XD, United Kingdom.
Kathy M Howe
Nicole K Nettleton
David J Price
John O Mason
Thomas Pratt
University of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0701460Medical Research Council G0800429Wellcome Trust
6 · The paper itself

Abstract

Heparan sulfate proteoglycans are cell surface and secretory proteins that modulate intercellular signaling pathways including Slit/Robo and FGF/FGFR. The heparan sulfate sugar moieties on HSPGs are subject to extensive postsynthetic modification, generating enormous molecular complexity that has been postulated to provide increased diversity in the ability of individual cells to respond to specific signaling molecules. This diversity could help explain how a relatively small number of axon guidance molecules are able to instruct the extremely complex connectivity of the mammalian brain. Consistent with this hypothesis, we previously showed that mutant mice lacking the heparan sulfotransferases (Hsts) Hs2st or Hs6st1 display major axon guidance defects at the developing optic chiasm. Here we further explore the role of these Hsts at the optic chiasm and investigate their function in corpus callosum development. Each Hst is expressed in a distinct pattern and each mutant displays a specific spectrum of axon guidance defects. Particular Hs2st(-/-) and Hs6st1(-/-) phenotypes closely match those of Slit1(-/-) and Slit2(-/-) embryos respectively, suggesting possible functional relationships. To test functional interactions between Hs2st or Hs6st1 and Slits we examined optic chiasm and corpus callosum phenotypes in a panel of genotypes where Hs2st or Hs6st1 and Slit1 or Slit2 function were simultaneously reduced or absent. We find examples of Hs2st and Hs6st1 having epistatic, synergistic, and antagonistic genetic relationships with Slit1 and/or Slit2 depending on the context. At the corpus callosum we find that Hs6st1 has Slit-independent functions and our data indicate additional roles in FGF signaling.

Indexed as

Amino AcidsAnimalsBody PatterningCell DifferentiationCorpus CallosumEmbryo, MammalianGene Expression Regulation, DevelopmentalIntercellular Signaling Peptides and ProteinsMiceMice, KnockoutMutationNerve Tissue ProteinsNeuronsOptic ChiasmProsencephalonRetinaAmino Acidsdolaisoleucineheparan-sulfate 2-sulfotransferaseHs6st1 protein, mouseIntercellular Signaling Peptides and ProteinsNerve Tissue ProteinsSlit1 protein, mouseSlit Homolog 2 ProteinSulfotransferases

Identifiers

PMID21307234
PMCPMC6633041
OpenAlexW2006032860

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.