Evidence map›Paper›PMID 25647032›Full record

ArticleFEBS letters2015

Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.

Jose Luis Ortega-Roldan, Felipe Ossa, Nader T Amin, Jason R Schnell

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  9. Protein Misfolding and ER Stress in Huntington's Disease.Frontiers in molecular biosciences · 2019
    Review
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  16. Peeking into Sigma-1 Receptor Functions Through the Retina.Advances in experimental medicine and biology · 2017
    Review
  17. Article
  18. 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 1 institution in 1 country.

Jose Luis Ortega-RoldanDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: Jose.Ortega-Roldan@bioch.ox.ac.uk.
Felipe OssaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Nader T AminDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Jason R SchnellDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: Jason.Schnell@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Medical Research Council K018590Medical Research Council MR/K018590/1
6 · The paper itself

Abstract

The sigma-1 receptor (S1R) is a ligand-regulated membrane chaperone protein associated with endoplasmic reticulum stress response, and modulation of ion channel activities at the plasma membrane. We report here a solution NMR study of a S1R construct (S1R(Δ35)) in which only the first transmembrane domain and the eight-residue N-terminus have been removed. The second transmembrane helix is found to be composed of residues 91-107, which corresponds to the first steroid binding domain-like region. The cytosolic domain is found to contain three helices, and the secondary structure and backbone dynamics of the chaperone domain are consistent with that determined previously for the chaperone domain alone. The position of TM2 provides a framework for ongoing studies of S1R ligand binding and oligomerisation.

Indexed as

Circular DichroismHumansMagnetic Resonance SpectroscopyProtein Structure, SecondaryProtein Structure, TertiaryReceptors, sigmaSigma-1 ReceptorReceptors, sigmaSigma-1 ReceptorNMRSigma-1 receptorTransmembrane domain

Identifiers

PMID25647032
PMCPMC4332692
OpenAlexW2025169180

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.