Evidence map›Paper›PMID 21647440›Full record

ArticlePloS one2011

Charge isomers of myelin basic protein: structure and interactions with membranes, nucleotide analogues, and calmodulin.

Chaozhan Wang, Ute Neugebauer, Jochen Bürck, Matti Myllykoski, Peter Baumgärtel, Jürgen Popp, Petri Kursula

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-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

22 citing papers in PubMed, 46 citations in OpenAlex.

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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

7 authors at 5 institutions in 2 countries.

Chaozhan WangDepartment of Biochemistry, University of Oulu, Oulu, Finland.
Ute Neugebauer
Jochen Bürck
Matti Myllykoski
Peter Baumgärtel
Jürgen Popp
Petri Kursula
University of Oulu · FIFriedrich Schiller University Jena · DEHelmholtz-Zentrum Berlin für Materialien und Energie · DEKarlsruhe Institute of Technology · DELeibniz Institute of Photonic Technology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As an essential structural protein required for tight compaction of the central nervous system myelin sheath, myelin basic protein (MBP) is one of the candidate autoantigens of the human inflammatory demyelinating disease multiple sclerosis, which is characterized by the active degradation of the myelin sheath. In this work, recombinant murine analogues of the natural C1 and C8 charge components (rmC1 and rmC8), two isoforms of the classic 18.5-kDa MBP, were used as model proteins to get insights into the structure and function of the charge isomers. Various biochemical and biophysical methods such as size exclusion chromatography, calorimetry, surface plasmon resonance, small angle X-ray and neutron scattering, Raman and fluorescence spectroscopy, and conventional as well as synchrotron radiation circular dichroism were used to investigate differences between these two isoforms, both from the structural point of view, and regarding interactions with ligands, including calmodulin (CaM), various detergents, nucleotide analogues, and lipids. Overall, our results provide further proof that rmC8 is deficient both in structure and especially in function, when compared to rmC1. While the CaM binding properties of the two forms are very similar, their interactions with membrane mimics are different. CaM can be used to remove MBP from immobilized lipid monolayers made of synthetic lipids--a phenomenon, which may be of relevance for MBP function and its regulation. Furthermore, using fluorescently labelled nucleotides, we observed binding of ATP and GTP, but not AMP, by MBP; the binding of nucleoside triphosphates was inhibited by the presence of CaM. Together, our results provide important further data on the interactions between MBP and its ligands, and on the differences in the structure and function between MBP charge isomers.

Indexed as

AnimalsCalmodulinCalorimetryCell MembraneChromatography, GelLigandsLipid MetabolismMiceModels, MolecularMyelin Basic ProteinNucleotidesProtein BindingProtein IsoformsProtein Structure, SecondarySpectrum Analysis, RamanSurface Plasmon ResonanceCalmodulinLigandsMyelin Basic ProteinNucleotidesProtein IsoformsXenotropic and Polytropic Retrovirus ReceptorXpr1 protein, mouse

Identifiers

PMID21647440
PMCPMC3102069
OpenAlexW2080583464

What OpenQuestion holds

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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.