Evidence map›Paper›PMID 29899450›Full record

ArticleNature2018

Cryo-EM structure of human rhodopsin bound to an inhibitory G protein.

Yanyong Kang, Oleg Kuybeda, Parker W de Waal, Somnath Mukherjee, Ned Van Eps, Przemyslaw Dutka, X Edward Zhou, Alberto Bartesaghi, Satchal Erramilli, Takefumi Morizumi and 11 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 153 papers.

0numbers the graph read from it
0cells of the map it votes in
153citing papers in PubMed
14.9field-weighted citation impact, top 1% 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

153 citing papers in PubMed, 274 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. The polybasic puzzle: how N-terminal charges modulate GαiCell communication and signaling : CCS · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Non-canonical GScientific reports · 2025
    Article
  12. Article
  13. Article
  14. Structural basis of the cysteinyl leukotriene receptor type 2 activation by LTD4.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

93 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

21 authors at 9 institutions in 4 countries.

Yanyong Kang *Center for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Oleg Kuybeda *Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
Parker W de Waal *Center for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Somnath MukherjeeDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Ned Van EpsDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Przemyslaw DutkaDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
X Edward ZhouCenter for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Alberto BartesaghiCancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
Satchal ErramilliDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Takefumi MorizumiDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Xin GuCenter for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Yanting YinCenter for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Ping LiuUniversity of Chinese Academy of Sciences, Beijing, China.
Yi JiangKey Laboratory of Receptor Research, VARI-SIMM Center, Center for Structure and Function of Drug Targets, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Xing MengDavid Van Andel Advanced Cryo-Electron Microscopy Suite, Van Andel Research Institute, Grand Rapids, MI, USA.
Gongpu ZhaoDavid Van Andel Advanced Cryo-Electron Microscopy Suite, Van Andel Research Institute, Grand Rapids, MI, USA.
Karsten MelcherCenter for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Oliver P ErnstDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Anthony A KossiakoffDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA. koss@bsd.uchicago.edu.
Sriram SubramaniamCancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA. ss1@nih.gov.
H Eric XuCenter for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Grand Rapids, MI, USA. eric.xu@vai.org.
Van Andel Institute · USUniversity of Chicago · USUniversity of Toronto · CAFrederick National Laboratory for Cancer Research · USChinese Academy of Sciences · CNJagiellonian University · PLNational Cancer Institute · USShanghai Institute of Materia Medica · CNUniversity of Chinese Academy of Sciences · CN

Funding

Molecular structures of membrane protein assembliesZIABC010824 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$8.0M
Structural Genomics of Orphan Nuclear ReceptorsR01DK071662 · NIDDK · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2005 to 2017
$5.1M
Chaperone-Assisted Structure Determination of Membrane ProteinsR01GM117372 · NIGMS · UNIVERSITY OF CHICAGO · PI ANTHONY A KOSSIAKOFF · 2016 to 2026
$4.0M
Imaging cellular assemblies with three-dimensional EMZ01BC010278 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 1999 to 2008
$1.1M
CCR NIH HHS HHSN261200800001CIntramural NIH HHS Z01 BC010278NCI NIH HHS HHSN261200800001ENIDDK NIH HHS R01 DK071662NIGMS NIH HHS R01 GM117372NIH HHS DK071662
6 · The paper itself

Abstract

G-protein-coupled receptors comprise the largest family of mammalian transmembrane receptors. They mediate numerous cellular pathways by coupling with downstream signalling transducers, including the hetrotrimeric G proteins G

Indexed as

Cryoelectron MicroscopyArrestinBinding SitesGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, GsHumansModels, MolecularReceptors, Adrenergic, beta-2RhodopsinSignal TransductionSubstrate SpecificityArrestinGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, GsReceptors, Adrenergic, beta-2Rhodopsin

Identifiers

PMID29899450
PMCPMC8054211
OpenAlexW2808524678

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.