Evidence map›Paper›PMID 38062020›Full record

ArticleNature communications2023

Understanding the molecular mechanisms of odorant binding and activation of the human OR52 family.

Chulwon Choi, Jungnam Bae, Seonghan Kim, Seho Lee, Hyunook Kang, Jinuk Kim, Injin Bang, Kiheon Kim, Won-Ki Huh, Chaok Seok and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
9.6field-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

32 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
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  15. The science of minerality.RSC advances · 2025
    Review
  16. Article
  17. CHARMM-GUIJournal of chemical information and modeling · 2025
    Article
  18. Review
  19. Olfactory receptors and human diseases.Cell and tissue research · 2025
    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

13 authors at 3 institutions in 3 countries.

Chulwon Choi *Department of Biological Sciences, Seoul National University, Seoul, 08826, Republic of Korea.
Jungnam Bae *Department of Biological Sciences, Seoul National University, Seoul, 08826, Republic of Korea.
Seonghan KimDepartment of Bioengineering, Lehigh University, Bethlehem, PA, 18015, USA.ORCID 0000-0002-1890-0061
Seho LeeDepartment of Chemistry, Seoul National University, Seoul, 08826, Republic of Korea.ORCID 0000-0001-7415-8191
Hyunook KangDepartment of Biological Sciences, Seoul National University, Seoul, 08826, Republic of Korea.ORCID 0000-0002-7017-4597
Jinuk KimDepartment of Biological Sciences, Seoul National University, Seoul, 08826, Republic of Korea.
Injin BangDepartment of Biological Sciences, Seoul National University, Seoul, 08826, Republic of Korea.
Kiheon KimDepartment of Biological Sciences, Seoul National University, Seoul, 08826, Republic of Korea.
Won-Ki HuhDepartment of Biological Sciences, Seoul National University, Seoul, 08826, Republic of Korea.ORCID 0000-0002-9091-6594
Chaok SeokDepartment of Chemistry, Seoul National University, Seoul, 08826, Republic of Korea.ORCID 0000-0002-1419-9888
Hahnbeom ParkBrain Science Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Wonpil ImDepartment of Bioengineering, Lehigh University, Bethlehem, PA, 18015, USA.ORCID 0000-0001-5642-6041
Hee-Jung ChoiDepartment of Biological Sciences, Seoul National University, Seoul, 08826, Republic of Korea. choihj@snu.ac.kr.ORCID 0000-0002-1167-1526
Seoul National University · KRLehigh University · USKorea Institute of Brain Science · KR

Funding

Breakthrough Molecular Dynamics Research via an Anton2 SupercomputerR01GM116961 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BLOOD, PHILIP D. · 2016 to 2023
$3.0M
NIGMS NIH HHS R01 GM116961
6 · The paper itself

Abstract

Structural and mechanistic studies on human odorant receptors (ORs), key in olfactory signaling, are challenging because of their low surface expression in heterologous cells. The recent structure of OR51E2 bound to propionate provided molecular insight into odorant recognition, but the lack of an inactive OR structure limited understanding of the activation mechanism of ORs upon odorant binding. Here, we determined the cryo-electron microscopy structures of consensus OR52 (OR52

Indexed as

OdorantsReceptors, OdorantCryoelectron MicroscopyHumansMolecular Dynamics SimulationNeoplasm ProteinsSmellNeoplasm ProteinsOR51E2 protein, humanReceptors, Odorant

Identifiers

PMID38062020
PMCPMC10703812
OpenAlexW4389429309

What OpenQuestion holds

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Registered trials

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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.