ReviewBiochemical Society transactions2024
Structure, function, and lipid sensing activity in the thioesterase superfamily.
Review in Biochemical Society transactions, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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.
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.
Who cites it
5 citing papers in PubMed.
- Ahcy Acts as an Effector of Hnf4a-Driven Super-Enhancer Activation to Alleviate MASLD During Intermittent Fasting.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- EchoVisuALL: From Echocardiography to Gene Discovery.bioRxiv : the preprint server for biology · 2026Article
- The Crystal Structure of Human Transport and Golgi Organization 2 Homolog (TANGO2) Protein Reveals an αββα-Fold Arrangement.Proteins · 2026Article
- Acyl-CoA thioesterases and their derived lipid mediators: linking Acyl-CoA metabolic reprogramming to the tumor microenvironment.Frontiers in immunology · 2026Review
- An origin for a eukaryotic lipid transfer protein fold in Asgard archaea.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Lipid synthesis and transport are essential for energy, production of cell membrane, and cell signaling. Acyl-CoA thioesterases (ACOTs) function to regulate intracellular levels of fatty acyl-CoAs through hydrolysis. Two members of this family, ACOT11 and ACOT12, contain steroidogenic acute regulatory related lipid transfer domains, which typically function as lipid transport or regulatory domains. This work reviews ACOT11 and ACOT12 structures and functions, and the potential role of the START domains in lipid transfer activity and the allosteric regulation of catalytic activity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.