Evidence map›Paper›PMID 30611431›Full record

ArticleMethods in enzymology2019

Isotopic Labeling of Eukaryotic Membrane Proteins for NMR Studies of Interactions and Dynamics.

Igor Dikiy, Lindsay D Clark, Kevin H Gardner, Daniel M Rosenbaum

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
2.0field-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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Expression ofEPJ web of conferences · 2023
    Article
  2. Article
  3. Review
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 3 institutions in 1 country.

Igor DikiyStructural Biology Initiative, CUNY Advanced Science Research Center, New York, NY, United States.
Lindsay D ClarkDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, United States; Molecular Biophysics Graduate Program, The University of Texas Southwestern Medical Center, Dallas, TX, United States.
Kevin H GardnerStructural Biology Initiative, CUNY Advanced Science Research Center, New York, NY, United States; Department of Chemistry and Biochemistry, City College of New York, New York, NY, United States; Biochemistry, Chemistry and Biology Ph.D. Programs, Graduate Center, City University of New York, New York, NY, United States. Electronic address: kevin.gardner@asrc.cuny.edu.
Daniel M RosenbaumDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, United States; Molecular Biophysics Graduate Program, The University of Texas Southwestern Medical Center, Dallas, TX, United States. Electronic address: daniel.rosenbaum@utsouthwestern.edu.
The Graduate Center, CUNY · USSouthwestern Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

Summer Undergraduate Research Support - Ms. Anastasiia FisiukR01GM106239 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GARDNER, KEVIN H · 2013 to 2024
$4.5M
Molecular mechanism of a master regulator of sterol homeostasisR01GM113050 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ROSENBAUM, DANIEL · 2015 to 2019
$1.5M
Characterizing the molecular mechanism of signal transduction from sensor to catalytic domain in sensor histidine kinasesF32GM119311 · NIGMS · ADVANCED SCIENCE RESEARCH CENTER · PI DIKIY, IGOR · 2017 to 2018
$118k
NIGMS NIH HHS F32 GM119311NIGMS NIH HHS R01 GM106239NIGMS NIH HHS R01 GM113050
6 · The paper itself

Abstract

Membrane proteins, and especially G-protein coupled receptors (GPCRs), are increasingly important targets of structural biology studies due to their involvement in many biomedically critical pathways in humans. These proteins are often highly dynamic and thus benefit from studies by NMR spectroscopy in parallel with complementary crystallographic and cryo-EM analyses. However, such studies are often complicated by a range of practical concerns, including challenges in preparing suitably isotopically labeled membrane protein samples, large sizes of protein/detergent or protein/lipid complexes, and limitations on sample concentrations and stabilities. Here we describe our approach to addressing these challenges via the use of simple eukaryotic expression systems and modified NMR experiments, using the human adenosine A

Indexed as

DeuteriumGene ExpressionGlycerolHumansIsotope LabelingMagnetic Resonance SpectroscopyPichiaPlasmidsReceptor, Adenosine A2ARecombinant ProteinsSaccharomyces cerevisiaeStaining and LabelingTransfectionADORA2A protein, humanDeuteriumGlycerolReceptor, Adenosine A2ARecombinant ProteinsDynamicsGPCRsIsotopic labelingMembrane proteinsNMR spectroscopyPichia pastorisRelaxation

Identifiers

PMID30611431
PMCPMC7309954
OpenAlexW2904695402

What OpenQuestion holds

Textmetadata
LicenceTDM
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.