Evidence map›Paper›PMID 11733546›Full record

ArticleThe Journal of cell biology2001

Microtubule-associated protein 1B: a neuronal binding partner for myelin-associated glycoprotein.

R Franzen, S L Tanner, S M Dashiell, C A Rottkamp, J A Hammer, R H Quarles

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Neuroprotection and repair in multiple sclerosis.Nature reviews. Neurology · 2012
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. The Nogo-66 receptor homolog NgR2 is a sialic acid-dependent receptor selective for myelin-associated glycoprotein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005
    Article
  12. 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

6 authors at 2 institutions in 1 country.

R FranzenLaboratory of Molecular and Cellular Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892-4440, USA.
S L Tanner
S M Dashiell
C A Rottkamp
J A Hammer
R H Quarles
National Institutes of Health · USNational Institute of Neurological Disorders and Stroke · US

Funding

Structure And Function Of Unconventional Myosins and CARMIL ProteinsZIAHL000514 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI HAMMER, JOHN A · 2009 to 2018
$9.6M
THE STRUCTURE AND SEQUENCE OF NON-MUSCLE MYOSIN GENESZ01HL000514 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI HAMMER, JOHN A · 1985 to 2008
$4.7M
GLYCOPROTEINS OF MYELIN IN DEVELOPMENT AND DISEASEZ01NS001808 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI QUARLES, RICHARD · 1985 to 2007
$614k
6 · The paper itself

Abstract

Myelin-associated glycoprotein (MAG) is expressed in periaxonal membranes of myelinating glia where it is believed to function in glia-axon interactions by binding to a component of the axolemma. Experiments involving Western blot overlay and coimmunoprecipitation demonstrated that MAG binds to a phosphorylated neuronal isoform of microtubule-associated protein 1B (MAP1B) expressed in dorsal root ganglion neurons (DRGNs) and axolemma-enriched fractions from myelinated axons of brain, but not to the isoform of MAP1B expressed by glial cells. The expression of some MAP1B as a neuronal plasma membrane glycoprotein (Tanner, S.L., R. Franzen, H. Jaffe, and R.H. Quarles. 2000. J. Neurochem. 75:553-562.), further documented here by its immunostaining without cell permeabilization, is consistent with it being a binding partner for MAG on the axonal surface. Binding sites for a MAG-Fc chimera on DRGNs colocalized with MAP1B on neuronal varicosities, and MAG and MAP1B also colocalized in the periaxonal region of myelinated axons. In addition, expression of the phosphorylated isoform of MAP1B was increased significantly when DRGNs were cocultured with MAG-transfected COS cells. The interaction of MAG with MAP1B is relevant to the known role of MAG in affecting the cytoskeletal structure and stability of myelinated axons.

Indexed as

AnimalsAxonsCoculture TechniquesCOS CellsGanglia, SpinalMicrotubule-Associated ProteinsMyelin-Associated GlycoproteinNeurogliaNeuronsPhosphorylationProtein BindingRatsTransfectionmicrotubule-associated protein 1BMicrotubule-Associated ProteinsMyelin-Associated Glycoprotein

Identifiers

PMID11733546
PMCPMC2150906
OpenAlexW2165277581

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.