Evidence map›Paper›PMID 30121871›Full record

ReviewJournal of biomolecular NMR2018

On the use of Pichia pastoris for isotopic labeling of human GPCRs for NMR studies.

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

Open access · greenAbstract readReview
In one paragraph

Review in Journal of biomolecular NMR, 2018. 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
1.8field-weighted citation impact, top 15% 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, 40 citations in OpenAlex.

  1. A random fractionalMagnetic resonance letters · 2026
    Article
  2. Article
  3. Article
  4. Membrane mimetic-dependence of GPCR energy landscapes.Structure (London, England : 1993) · 2024
    Article
  5. Article
  6. Uniform [Journal of biomolecular NMR · 2024
    Article
  7. Membrane Mimetic-Dependence of GPCR Energy Landscapes.bioRxiv : the preprint server for biology · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Applications of In-Cell NMR in Structural Biology and Drug Discovery.International journal of molecular sciences · 2019
    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.

Lindsay ClarkDepartment of Biophysics, The University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX, 75390-8816, USA.
Igor DikiyStructural Biology Initiative, CUNY Advanced Science Research Center, 85 St. Nicholas Terrace, New York, NY, 10031, USA.ORCID http://orcid.org/0000-0002-8155-7788
Daniel M RosenbaumDepartment of Biophysics, The University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX, 75390-8816, USA. Daniel.Rosenbaum@utsouthwestern.edu.
Kevin H GardnerStructural Biology Initiative, CUNY Advanced Science Research Center, 85 St. Nicholas Terrace, New York, NY, 10031, USA. Kevin.Gardner@asrc.cuny.edu.ORCID http://orcid.org/0000-0002-8671-2556
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
American Heart Association 16PRE27200004National Institute of General Medical Sciences F32 GM119311National Institute of General Medical Sciences R01 GM106239National Institute of General Medical Sciences R01 GM113050National Science Foundation 1000136529NIGMS NIH HHS F32 GM119311NIGMS NIH HHS R01 GM106239NIGMS NIH HHS R01 GM113050Welch Foundation I-1770
6 · The paper itself

Abstract

NMR studies of human integral membrane proteins provide unique opportunities to probe structure and dynamics at specific locations and on multiple timescales, often with significant implications for disease mechanism and drug development. Since membrane proteins such as G protein-coupled receptors (GPCRs) are highly dynamic and regulated by ligands or other perturbations, NMR methods are potentially well suited to answer basic functional questions (such as addressing the biophysical basis of ligand efficacy) as well as guiding applications (such as novel ligand design). However, such studies on eukaryotic membrane proteins have often been limited by the inability to incorporate optimal isotopic labels for NMR methods developed for large protein/lipid complexes, including methyl TROSY. We review the different expression systems for production of isotopically labeled membrane proteins and highlight the use of the yeast Pichia pastoris to achieve perdeuteration and

Indexed as

AnimalsCarbon IsotopesDeuteriumHumansIsotope LabelingMembrane ProteinsNuclear Magnetic Resonance, BiomolecularPichiaReceptors, G-Protein-CoupledCarbon IsotopesDeuteriumMembrane ProteinsReceptors, G-Protein-CoupledDeuterationGPCRIntegral membrane proteinsPichia pastorisSolution NMRStable isotope labeling

Identifiers

PMID30121871
PMCPMC7282444
OpenAlexW2887519488

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.