Evidence map›Paper›PMID 26315937›Full record

ArticleExperimental neurology2015

Sugar-dependent modulation of neuronal development, regeneration, and plasticity by chondroitin sulfate proteoglycans.

Gregory M Miller, Linda C Hsieh-Wilson

Open access · greenAbstract read
In one paragraph

Article in Experimental neurology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

48 citing papers in PubMed, 100 citations in OpenAlex.

  1. Trial
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  8. Article
  9. Article
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  14. Chondroitin 4-Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Extracellular Matrix in Neural Plasticity and Regeneration.Cellular and molecular neurobiology · 2022
    Review
  20. 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

2 authors at 1 institution in 1 country.

Gregory M MillerDivision of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.
Linda C Hsieh-WilsonDivision of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA. Electronic address: lhw@caltech.edu.
California Institute of Technology · US

Funding

PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
A chemical approach to elucidating the structure-function relationships of chondronitin sulfate glycosaminoglycansR01GM093627 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HSIEH-WILSON, LINDA C · 2010 to 2018
$3.6M
NIGMS NIH HHS R01 GM093627NIGMS NIH HHS T32 GM007616NIGMS NIH HHS T32GM07616
6 · The paper itself

Abstract

Chondroitin sulfate proteoglycans (CSPGs) play important roles in the developing and mature nervous system, where they guide axons, maintain stable connections, restrict synaptic plasticity, and prevent axon regeneration following CNS injury. The chondroitin sulfate glycosaminoglycan (CS GAG) chains that decorate CSPGs are essential for their functions. Through these sugar chains, CSPGs are able to bind and regulate the activity of a diverse range of proteins. CSPGs have been found both to promote and inhibit neuronal growth. They can promote neurite outgrowth by binding to various growth factors such as midkine (MK), pleiotrophin (PTN), brain-derived neurotrophic factor (BDNF) and other neurotrophin family members. CSPGs can also inhibit neuronal growth and limit plasticity by interacting with transmembrane receptors such as protein tyrosine phosphatase σ (PTPσ), leukocyte common antigen-related (LAR) receptor protein tyrosine phosphatase, and the Nogo receptors 1 and 3 (NgR1 and NgR3). These CS-protein interactions depend on specific sulfation patterns within the CS GAG chains, and accordingly, particular CS sulfation motifs are upregulated during development, in the mature nervous system, and in response to CNS injury. Thus, spatiotemporal regulation of CS GAG biosynthesis may provide an important mechanism to control the functions of CSPGs and to modulate intracellular signaling pathways. Here, we will discuss these sulfation-dependent processes and highlight how the CS sugars on CSPGs contribute to neuronal growth, axon guidance, and plasticity in the nervous system.

Indexed as

Central Nervous SystemAnimalsChondroitin Sulfate ProteoglycansHumansNerve RegenerationNeuronal PlasticityChondroitin Sulfate ProteoglycansAxon guidanceAxon regenerationChondroitin sulfate (CS)CSPGCSPG receptorGlycosaminoglycansNeuronal growthNeuronal injuryPlasticityProteoglycan

Identifiers

PMID26315937
PMCPMC4679498
OpenAlexW2140570830

What OpenQuestion holds

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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.