Evidence map›Paper›PMID 28547763›Full record

ReviewProtein science : a publication of the Protein Society2017

New approaches towards the understanding of integral membrane proteins: A structural perspective on G protein-coupled receptors.

Reinhard Grisshammer

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2017. 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
2.9field-weighted citation impact, top 8% 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, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Side-chain dynamics of the αProtein science : a publication of the Protein Society · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. A high-resolution description of βNature communications · 2020
    Article
  15. Receptor selectivity between the G proteins GαFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. 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

1 author at 1 institution in 1 country.

Reinhard GrisshammerDepartment of Health and Human Services, Membrane Protein Structure Function Unit, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Rockville, Maryland, 20852.
National Institute of Neurological Disorders and Stroke · US

Funding

Structure of integral membrane proteinsZIANS003016 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI GRISSHAMMER, REINHARD · 2009 to 2017
$8.5M
6 · The paper itself

Abstract

Three-dimensional structure determination of integral membrane proteins has advanced in unprecedented detail our understanding of mechanistic events of how ion channels, transporters, receptors, and enzymes function. This exciting progress required a tremendous amount of methods development, as exemplified here with G protein-coupled receptors (GPCRs): Optimizing the production of GPCRs in recombinant hosts; increasing the probability of crystal formation using high-affinity ligands, nanobodies, and minimal G proteins for co-crystallization, thus stabilizing receptors into one conformation; using the T4 lysozyme technology and other fusion partners to promote crystal contacts; advancing crystallization methods including the development of novel detergents, and miniaturization and automation of the lipidic cubic phase crystallization method; the concept of conformational thermostabilization of GPCRs; and developing microfocus X-ray synchrotron technologies to analyze small GPCR crystals. However, despite immense progress to explain how GPCRs function, many receptors pose intractable hurdles to structure determination at this time. Three emerging methods, serial femtosecond crystallography, micro electron diffraction, and single particle electron cryo-microscopy, hold promise to overcome current limitations in structural membrane biology.

Indexed as

ArchaeaBacteriaCryoelectron MicroscopyCrystallizationCrystallographyDetergentsEukaryotaLipidsMicroscopy, Electron, TransmissionMolecular ConformationMuramidaseNuclear Magnetic Resonance, BiomolecularReceptors, G-Protein-CoupledSingle-Domain AntibodiesDetergentsLipidsMuramidaseReceptors, G-Protein-CoupledSingle-Domain AntibodiesG protein-coupled receptorintegral membrane proteinlipidic cubic phase (LCP)micro electron diffraction (MicroED)serial femtosecond crystallography (SFX)single particle electron cryo-microscopy (cryo-EM)three-dimensional structure determination

Identifiers

PMID28547763
PMCPMC5521582
OpenAlexW2617324567

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.