ArticleNature communications2015
Structural basis for phosphatidylinositol-phosphate biosynthesis.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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Who cites it
25 citing papers in PubMed, 52 citations in OpenAlex.
- Dynamic Lipidomic Responses to Inflammation and Physical Insult: A Comparative Review Across Blunt Force Trauma, Thermal Burn Injury, and Viral Infection.Expert reviews in molecular medicine · 2026Review
- Expression and Purification of Integral Membrane Enzymes for Functional and Structural Studies.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structural basis for catalysis and selectivity of phospholipid synthesis by eukaryotic choline-phosphotransferase.Nature communications · 2025Article
- The small molecule CBR-5884 inhibits themBio · 2024Article
- Innovations in Antifungal Drug Discovery among Cell Envelope Synthesis Enzymes through Structural Insights.Journal of fungi (Basel, Switzerland) · 2024Review
- Architects of the membrane: structures of eukaryotic choline phosphotransferase 1 and choline/ethanolamine phosphotransferase 1.Nature structural & molecular biology · 2023Article
- Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis.Nature communications · 2023Article
- Structural basis for catalysis of human choline/ethanolamine phosphotransferase 1.Nature communications · 2023Article
- Access and utilization of long chain fatty acyl-CoA by zDHHC protein acyltransferases.Current opinion in structural biology · 2022Review
- Article
- Characterization of inositol lipid metabolism in gut-associated Bacteroidetes.Nature microbiology · 2022Article
- Phospholipid Membrane Transport and Associated Diseases.Biomedicines · 2022Review
- Crystal structures of phosphatidyl serine synthase PSS reveal the catalytic mechanism of CDP-DAG alcohol O-phosphatidyl transferases.Nature communications · 2021Article
- Elucidating the Antimycobacterial Mechanism of Action of Decoquinate Derivative RMB041 Using Metabolomics.Antibiotics (Basel, Switzerland) · 2021Article
- Elucidating the Antimycobacterial Mechanism of Action of Ciprofloxacin Using Metabolomics.Microorganisms · 2021Article
- Mapping the Substrate-Binding Sites in the Phosphatidylserine Synthase inFrontiers in cellular and infection microbiology · 2021Article
- The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interface.Current research in structural biology · 2021Article
- Lipoarabinomannan as a Point-of-Care Assay for Diagnosis of Tuberculosis: How Far Are We to Use It?Frontiers in microbiology · 2021Review
- Structural and Functional Characterization of Phosphatidylinositol-Phosphate Biosynthesis in Mycobacteria.Journal of molecular biology · 2020Article
- Structure ofCommunications biology · 2019Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Phosphatidylinositol is critical for intracellular signalling and anchoring of carbohydrates and proteins to outer cellular membranes. The defining step in phosphatidylinositol biosynthesis is catalysed by CDP-alcohol phosphotransferases, transmembrane enzymes that use CDP-diacylglycerol as donor substrate for this reaction, and either inositol in eukaryotes or inositol phosphate in prokaryotes as the acceptor alcohol. Here we report the structures of a related enzyme, the phosphatidylinositol-phosphate synthase from Renibacterium salmoninarum, with and without bound CDP-diacylglycerol to 3.6 and 2.5 Å resolution, respectively. These structures reveal the location of the acceptor site, and the molecular determinants of substrate specificity and catalysis. Functional characterization of the 40%-identical ortholog from Mycobacterium tuberculosis, a potential target for the development of novel anti-tuberculosis drugs, supports the proposed mechanism of substrate binding and catalysis. This work therefore provides a structural and functional framework to understand the mechanism of phosphatidylinositol-phosphate biosynthesis.
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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.