Evidence map›Paper›PMID 39587078›Full record

ArticleCell discovery2024

Structural mechanisms of human sodium-coupled high-affinity choline transporter CHT1.

Jing Xue, Hongwen Chen, Yong Wang, Youxing Jiang

Abstract read
In one paragraph

Article in Cell discovery, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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.

Jing XueInstitute of Aging & Tissue Regeneration, Renji Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. jxue@shsmu.edu.cn.ORCID http://orcid.org/0000-0002-7331-1382
Hongwen ChenDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Yong WangCollege of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0001-9156-0377
Youxing JiangHoward Hughes Medical Institute and Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID http://orcid.org/0000-0002-1874-0504

Funding

Cancer Prevention and Research Institute of Texas (Cancer Prevention Research Institute of Texas) RP170644National Natural Science Foundation of China (National Science Foundation of China) 32371300Welch Foundation I-1578
6 · The paper itself

Abstract

Mammalian sodium-coupled high-affinity choline transporter CHT1 uptakes choline in cholinergic neurons for acetylcholine synthesis and plays a critical role in cholinergic neurotransmission. Here, we present the high-resolution cryo-EM structures of human CHT1 in apo, substrate- and ion-bound, hemicholinium-3-inhibited, and ML352-inhibited states. These structures represent three distinct conformational states, elucidating the structural basis of the CHT1-mediated choline uptake mechanism. Three ion-binding sites, two for Na

Identifiers

PMID39587078
PMCPMC11589582

What OpenQuestion holds

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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.