Evidence map›Paper›PMID 17142269›Full record

ArticleBiophysical journal2007

Cytoplasmic domain of human myelin protein zero likely folded as beta-structure in compact myelin.

Xiaoyang Luo, Deepak Sharma, Hideyo Inouye, Daniel Lee, Robin L Avila, Mario Salmona, Daniel A Kirschner

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

19 citing papers in PubMed, 38 citations in OpenAlex.

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  10. Pathological transitions in myelin membranes driven by environmental and multiple sclerosis conditions.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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  17. Cholesterol regulates the endoplasmic reticulum exit of the major membrane protein P0 required for peripheral myelin compaction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    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

7 authors at 2 institutions in 2 countries.

Xiaoyang LuoDepartment of Biology, Boston College, Chestnut Hill, Massachusetts, USA.
Deepak Sharma
Hideyo Inouye
Daniel Lee
Robin L Avila
Mario Salmona
Daniel A Kirschner
Boston College · USMario Negri Institute for Pharmacological Research · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myelin protein zero (P0 or P0 glycoprotein), the major integral membrane protein in peripheral nervous system myelin, plays a key role in myelin membrane compaction and stability. While the structure of P0 extracellular domain was determined by crystallography, the paucity of any structural data on the highly positive-charged P0 cytoplasmic domain (P0-cyt) has greatly limited our understanding of the mechanism of P0 function. Here, using circular dichroism and intrinsic fluorescence spectroscopy, we attempted to elucidate the structure of human P0-cyt (hP0-cyt) in membrane mimetic environments composed of detergents or lipid vesicles. We found that the secondary structure of P0-cyt was polymorphic-at the lipid/protein ratio corresponding to that of mature peripheral myelin ( approximately 50:1), hP0-cyt mainly adopted a beta-conformation, whereas when the proportion of lipid increased, the structure underwent a beta-->alpha transition. By contrast, the secondary structure of the major isoform of myelin basic protein, another myelin protein with a very large positive charge, remained unchanged across a wide range of lipid/protein ratios. We propose that when hP0-cyt is bound at sufficient concentration to lamellar lipid bilayers such as myelin, it folds into a beta-conformation; before this threshold lipid/protein ratio is reached, the domain is alpha-helical. We suggest that the cytoplasmic apposition (major dense line) in compact myelin may be stabilized via the hydrogen-bonding of beta-strands formed as a result of local P0-P0 aggregation.

Indexed as

Protein FoldingAmino Acid SequenceDimerizationHumansHydrogen BondingLipidsMembranes, ArtificialMolecular Sequence DataMyelin Basic ProteinMyelin P0 ProteinMyelin SheathProtein Structure, SecondaryLipidsMembranes, ArtificialMyelin Basic ProteinMyelin P0 Protein

Identifiers

PMID17142269
PMCPMC1796833
OpenAlexW2019455082

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.