Evidence map›Paper›PMID 16406810›Full record

ArticleJournal of the American Society for Mass Spectrometry2006

Proteomics of bovine myelin sheath: characterization of a truncated form of P0 by MALDI-TOF/TOF mass spectrometry.

Antonio Qualtieri, Elena Urso, Maria Le Pera, Massimo Scornaienchi, Aldo Quattrone, Leonardo Di Donna, Anna Napoli, Giovanni Sindona

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
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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

8 authors at 2 institutions in 1 country.

Antonio QualtieriInstitute of Neurological Sciences, Mangone (CS), Italy.
Elena Urso
Maria Le Pera
Massimo Scornaienchi
Aldo Quattrone
Leonardo Di Donna
Anna Napoli
Giovanni Sindona
Institute of Neurological Sciences · ITUniversity of Calabria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glycoprotein P0, the major structural protein of the peripheral nerve myelin, plays a critical role in holding myelin lamellae together via interaction of both extracellular and cytoplasmic domains. Mutations in the human P0 gene give rise to severe and progressive forms of dominantly inherited peripheral neuropathies like CMT1B. Here we report on the characterization of a bovine P0-derived protein of nearly 26 kD that corresponds to the P0 protein truncated in its cytoplasmic domain. Matrix assisted laser desorption ionization (MALDI)-time-of-flight/time-of-flight (TOF/TOF) mass spectrometry (MS) analysis on its tryptic digest has provided a peptide mapping, the main difference of which from the normal P0 analog was represented by the absence of the cluster of peaks at m/z 1513.7501, 1530.7701, and 1546.7651. The latter corresponds to the P0 fragment QTPVLYAMLDHSR and to its pyroglutamic and methionine-oxidized derivatives. The species at 1530.7701 covering the sequence 186-198 of P0 is not an artifact and might have a functional role in the myelin architecture.

Indexed as

ProteomicsAmino Acid SequenceAnimalsCattleElectrophoresisHydrolysisMolecular Sequence DataMyelin P0 ProteinMyelin SheathProtein ConformationSciatic NerveSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTrypsinMyelin P0 ProteinTrypsin

Identifiers

PMID16406810
OpenAlexW2062867565

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.