Evidence map›Paper›PMID 25347290›Full record

ArticlePloS one2014

Solution NMR of MPS-1 reveals a random coil cytosolic domain structure.

Pan Li, Pan Shi, Chaohua Lai, Juan Li, Yuanyuan Zheng, Ying Xiong, Longhua Zhang, Changlin Tian

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 91% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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.

Pan LiHefei National Laboratory of Microscale Physical Sciences, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, P. R. China.
Pan ShiHigh Magnetic Field Laboratory, Hefei institutes of Physical Science, Chinese Academy of Sciences, Hefei, Anhui, P. R. China.
Chaohua LaiHefei National Laboratory of Microscale Physical Sciences, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, P. R. China.
Juan LiHefei National Laboratory of Microscale Physical Sciences, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, P. R. China.
Yuanyuan ZhengHefei National Laboratory of Microscale Physical Sciences, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, P. R. China.
Ying XiongHefei National Laboratory of Microscale Physical Sciences, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, P. R. China.
Longhua ZhangHefei National Laboratory of Microscale Physical Sciences, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, P. R. China.
Changlin TianHefei National Laboratory of Microscale Physical Sciences, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, P. R. China; High Magnetic Field Laboratory, Hefei institutes of Physical Science, Chinese Academy of Sciences, Hefei, Anhui, P. R. China.
University of Science and Technology of China · CNHigh Magnetic Field Laboratory · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Caenorhabditis elegans MPS1 is a single transmembrane helical auxiliary subunit that co-localizes with the voltage-gated potassium channel KVS1 in the nematode nervous system. MPS-1 shares high homology with KCNE (potassium voltage-gated channel subfamily E member) auxiliary subunits, and its cytosolic domain was reported to have a serine/threonine kinase activity that modulates KVS1 channel function via phosphorylation. In this study, NMR spectroscopy indicated that the full length and truncated MPS-1 cytosolic domain (134-256) in the presence or absence of n-dodecylphosphocholine detergent micelles adopted a highly flexible random coil secondary structure. In contrast, protein kinases usually adopt a stable folded conformation in order to implement substrate recognition and phosphoryl transfer. The highly flexible random coil secondary structure suggests that MPS-1 in the free state is unstructured but may require a substrate or binding partner to adopt stable structure required for serine/threonine kinase activity.

Indexed as

Nuclear Magnetic Resonance, BiomolecularProtein Interaction Domains and MotifsAnimalsCaenorhabditis elegans ProteinsMagnetic Resonance SpectroscopyMicellesPeptidesPhosphorylcholinePotassium ChannelsProtein ConformationRecombinant ProteinsSolutionsCaenorhabditis elegans ProteinsdodecylphosphocholineMicellesMPS-1 protein, C elegansPeptidesPhosphorylcholinePotassium ChannelsRecombinant ProteinsSolutions

Identifiers

PMID25347290
PMCPMC4210162
OpenAlexW2067521125

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Registered trials

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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.