Evidence map›Paper›PMID 30311978›Full record

ReviewProtein science : a publication of the Protein Society2019

Structural biology of G protein-coupled receptor signaling complexes.

X Edward Zhou, Karsten Melcher, H Eric Xu

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
2.4field-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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Receptor Pharmacogenomics: Deciphering Genetic Influence on Drug Response.International journal of molecular sciences · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 2 countries.

X Edward ZhouCenter for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, Michigan.
Karsten MelcherCenter for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, Michigan.
H Eric XuCenter for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, Michigan.
Van Andel Institute · USChinese Academy of Sciences · CN

Funding

Structural Genomics of Orphan Nuclear ReceptorsR01DK071662 · NIDDK · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2005 to 2017
$5.1M
Structural and functional analysis of a dynamic ABA signaling complexR01GM102545 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2012 to 2014
$1.1M
Structural Mechanisms of AMPK RegulationR01GM129436 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2018 to 2019
$767k
NIDDK NIH HHS DK071662NIDDK NIH HHS R01 DK071662NIGMS NIH HHS R01 GM102545NIGMS NIH HHS R01 GM129436NIH HHS GM102545NIH HHS GM129436
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) constitute the largest family of cell surface receptors that mediate numerous cell signaling pathways, and are targets of more than one-third of clinical drugs. Thanks to the advancement of novel structural biology technologies, high-resolution structures of GPCRs in complex with their signaling transducers, including G-protein and arrestin, have been determined. These 3D complex structures have significantly improved our understanding of the molecular mechanism of GPCR signaling and provided a structural basis for signaling-biased drug discovery targeting GPCRs. Here we summarize structural studies of GPCR signaling complexes with G protein and arrestin using rhodopsin as a model system, and highlight the key features of GPCR conformational states in biased signaling including the sequence motifs of receptor TM6 that determine selective coupling of G proteins, and the phosphorylation codes of GPCRs for arrestin recruitment. We envision the future of GPCR structural biology not only to solve more high-resolution complex structures but also to show stepwise GPCR signaling complex assembly and disassembly and dynamic process of GPCR signal transduction.

Indexed as

Signal TransductionAmino Acid SequenceAnimalsHumansModels, MolecularProtein ConformationProtein Interaction MapsReceptors, G-Protein-CoupledSequence AlignmentReceptors, G-Protein-CoupledarrestinGPCRG proteinG protein-coupled receptorssignalingStructural biology

Identifiers

PMID30311978
PMCPMC6371222
OpenAlexW2897622241

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.