Evidence map›Paper›PMID 19737434›Full record

ArticleNeuron glia biology2008

Myelin sheaths are formed with proteins that originated in vertebrate lineages.

Robert M Gould, Todd Oakley, Jared V Goldstone, Jason C Dugas, Scott T Brady, Alexander Gow

Abstract read
In one paragraph

Article in Neuron glia biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

19 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Myelin development in the peripheral nervous system ofFrontiers in cell and developmental biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Effects of Insulin on Immortalized Rat Schwann Cells, IFRS1.International journal of molecular sciences · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Symbiotic organs shaped by distinct modes of genome evolution in cephalopods.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Review
  17. Article
  18. Article
  19. Schwann cell myelination.Cold Spring Harbor perspectives in biology · 2015
    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

6 authors at 5 institutions in 1 country.

Robert M GouldDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, 60612, USA. rmgould@uic.edu
Todd Oakley
Jared V Goldstone
Jason C Dugas
Scott T Brady
Alexander Gow
University of Illinois Chicago · USStanford University · USUniversity of California, Santa Barbara · USWayne State University · USWoods Hole Oceanographic Institution · US

Funding

Molecular Mechanisms of NeurodegenerationR01NS043783 · NINDS · WAYNE STATE UNIVERSITY · PI GOW, ALEXANDER · 2002 to 2010
$2.6M
Hearing loss in claudin 11-null miceR01DC006262 · NIDCD · WAYNE STATE UNIVERSITY · PI GOW, ALEXANDER · 2003 to 2007
$1.2M
NIDCD NIH HHS R01 DC006262NINDS NIH HHS NS043783NINDS NIH HHS R01 NS043783
6 · The paper itself

Abstract

All vertebrate nervous systems, except those of agnathans, make extensive use of the myelinated fiber, a structure formed by coordinated interplay between neuronal axons and glial cells. Myelinated fibers, by enhancing the speed and efficiency of nerve cell communication allowed gnathostomes to evolve extensively, forming a broad range of diverse lifestyles in most habitable environments. The axon-covering myelin sheaths are structurally and biochemically novel as they contain high portions of lipid and a few prominent low molecular weight proteins often considered unique to myelin. Here we searched genome and EST databases to identify orthologs and paralogs of the following myelin-related proteins: (1) myelin basic protein (MBP), (2) myelin protein zero (MPZ, formerly P0), (3) proteolipid protein (PLP1, formerly PLP), (4) peripheral myelin protein-2 (PMP2, formerly P2), (5) peripheral myelin protein-22 (PMP22) and (6) stathmin-1 (STMN1). Although widely distributed in gnathostome/vertebrate genomes, neither MBP nor MPZ are present in any of nine invertebrate genomes examined. PLP1, which replaced MPZ in tetrapod CNS myelin sheaths, includes a novel 'tetrapod-specific' exon (see also Möbius et al., 2009). Like PLP1, PMP2 first appears in tetrapods and like PLP1 its origins can be traced to invertebrate paralogs. PMP22, with origins in agnathans, and STMN1 with origins in protostomes, existed well before the evolution of gnathostomes. The coordinated appearance of MBP and MPZ with myelin sheaths and of PLP1 with tetrapod CNS myelin suggests interdependence - new proteins giving rise to novel vertebrate structures.

Indexed as

Evolution, MolecularAnimalsCentral Nervous SystemDatabases, FactualGenomicsHumansMyelin ProteinsMyelin SheathPeripheral Nervous SystemVertebratesMyelin Proteins

Identifiers

PMID19737434
PMCPMC3781599
OpenAlexW1974961366

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.