Evidence map›Paper›PMID 27519525›Full record

ArticleActa neuropathologica communications2016

Isoaspartic acid is present at specific sites in myelin basic protein from multiple sclerosis patients: could this represent a trigger for disease onset?

Michael G Friedrich, Sarah E Hancock, Mark J Raftery, Roger J W Truscott

Open access · goldAbstract read
In one paragraph

Article in Acta neuropathologica communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Mammalian Tolerance to Amino Acid Heterochirality.Chembiochem : a European journal of chemical biology · 2025
    Review
  4. Repair of Isoaspartyl Residues by PCMT1 and Kidney Fibrosis.Journal of the American Society of Nephrology : JASN · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Molecular Processes Implicated in Human Age-Related Nuclear Cataract.Investigative ophthalmology & visual science · 2019
    Review
  14. Article
  15. Cleavage C-terminal to Asp leads to covalent crosslinking of long-lived human proteins.Biochimica et biophysica acta. Proteins and proteomics · 2019
    Article
  16. Article
  17. 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

4 authors at 3 institutions in 1 country.

Michael G FriedrichIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia.
Sarah E HancockIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia.
Mark J RafteryBioanalytical Mass Spectrometry Facility, University of New South Wales, Sydney, NSW, 2052, Australia.
Roger J W TruscottIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, 2522, Australia. rjwt@uow.edu.au.
University of Wollongong · AUIllawarra Health and Medical Research Institute · AUUNSW Sydney · AU

Funding

BRAIN TISSUE RESOURCE CENTER FOR ALCOHOL RESEARCHR24AA012725 · NIAAA · UNIVERSITY OF SYDNEY · PI KRIL, JILLIAN JUNE · 2000 to 2011
$2.2M
NIAAA NIH HHS R24 AA012725
6 · The paper itself

Abstract

Multiple sclerosis (MS) is associated with breakdown of the myelin sheath that coats neurons in the central nervous system. The cause of MS is not known, although the pathogenesis involves destruction of myelin by the immune system. It was the aim of this study to examine the abundant myelin protein, myelin basic protein (MBP), to determine if there are sites of modification that may be characteristic for MS. MBP from the cerebellum was examined from controls and MS patients across the age range using mass spectrometry and amino acid analysis. Amino acid racemization data indicated that myelin basic protein is long-lived and proteomic analysis of MBP showed it to be highly modified. A common modification of MBP was racemization of Asp and this was significantly greater in MS patients. In long-lived proteins, L-Asp and L-Asn can racemize to three other isomers, D-isoAsp, L-isoAsp and D-Asp and this is significant because isoAsp formation in peptides renders them immunogenic.Proteomic analysis revealed widespread modifications of MBP with two surface regions that are altered in MS. In particular, isoAsp was significantly elevated at these sites in MS patients. The generation of isoAsp could be responsible for eliciting an immune response to modified MBP and therefore be implicated in the etiology of MS.

Indexed as

Protein Processing, Post-TranslationalAdultAgedAgingArginineAspartic AcidCerebellumGlutamineHumansIsoaspartic AcidMass SpectrometryMiddle AgedModels, MolecularMultiple Sclerosis, Chronic ProgressiveMultiple Sclerosis, Relapsing-RemittingMyelin Basic ProteinArginineAspartic AcidGlutamineIsoaspartic AcidMBP protein, humanMyelin Basic Protein

Identifiers

PMID27519525
PMCPMC4983062
OpenAlexW2512829199

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.