Evidence map›Paper›PMID 37179328›Full record

ArticleNature communications2023

Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis.

Lie Wang, Ming Zhou

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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

13 citing papers in PubMed, 39 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Lie WangVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA. liew@bcm.edu.ORCID http://orcid.org/0000-0002-9406-5168
Ming ZhouVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA. mzhou@bcm.edu.ORCID http://orcid.org/0000-0001-7198-165X
Baylor College of Medicine · US

Funding

Understanding the role of lipids in structure and function of membrane proteinsRM1GM145416 · NIGMS · TEXAS A&M UNIVERSITY · PI Erin S Baker, Arthur D Laganowsky · 2022 to 2026
$7.4M
Structure and mechanism of mammalian stearoyl-CoA desaturasesR01DK122784 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI TSAI, AH-LIM, ZHOU, MING · 2019 to 2023
$3.2M
NIDDK NIH HHS R01 DK122784NIGMS NIH HHS RM1 GM145416
6 · The paper itself

Abstract

Phosphatidylcholine (PC) is the most abundant phospholipid in eukaryotic cell membranes. In eukaryotes, two highly homologous enzymes, cholinephosphotransferase-1 (CHPT1) and choline/ethanolamine phosphotransferase-1 (CEPT1) catalyze the final step of de novo PC synthesis. CHPT1/CEPT1 joins two substrates, cytidine diphosphate-choline (CDP-choline) and diacylglycerol (DAG), to produce PC, and Mg

Indexed as

Diacylglycerol CholinephosphotransferaseEukaryotic CellsCatalysisCryoelectron MicroscopyCytidine Diphosphate CholinePhosphatidylcholinesPhosphotransferasesSaccharomyces cerevisiaeCytidine Diphosphate CholineDiacylglycerol CholinephosphotransferasePhosphatidylcholinesPhosphotransferases

Identifiers

PMID37179328
PMCPMC10182977
OpenAlexW4376504497

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.