Evidence map›Paper›PMID 8734447›Full record

ReviewNeurochemical research1996

Phosphorylation of myelin protein: recent advances.

J Eichberg, S Iyer

Abstract readReview
PubMed Publisher
In one paragraph

Review in Neurochemical research, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Myelin P0: new knowledge and new roles.Neurochemical research · 2002
    Review
  14. Article
  15. Article
  16. Glycoproteins of myelin sheaths.Journal of molecular neuroscience : MN · 1997
    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.

J EichbergDepartment of Biochemical and Biophysical Sciences, University of Houston, TX 77204-5934, USA.
S Iyer

Funding

PHOSPHOLIPID METABOLISM IN DIABETIC NEUROPATHYR01DK030577 · NIDDK · UNIVERSITY OF HOUSTON · PI EICHBERG, JOSEPH · 1986 to 2001
$411k
NIDDK NIH HHS DK30577
6 · The paper itself

Abstract

Since it was first described 25 years ago, phosphorylation has come to be recognized as a widespread and dynamic post-translation modification of myelin proteins. In this review, the phosphorylation characteristics of myelin basic protein, protein zero (P0), myelin-associated glycoprotein and 2'3' cyclic nucleotide 3'-phosphodiesterase are summarized. Emphasis is placed on recent advances in our knowledge concerning the protein kinases involved and the sites of phosphorylation in the amino acid sequences, where known. The possible roles of myelin protein phosphorylation in modulating myelin structure, the process of myelin assembly and mediation of signal transduction events are discussed.

Indexed as

2',3'-Cyclic-Nucleotide PhosphodiesterasesAnimalsBinding SitesGlycoproteinsMyelin Basic ProteinMyelin ProteinsPhosphorylationProtein KinasesSignal Transduction2',3'-Cyclic-Nucleotide PhosphodiesterasesGlycoproteinsMyelin Basic ProteinMyelin ProteinsProtein Kinases

Identifiers

PMID8734447

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.