ArticleBiochemical Society transactions2014
Sec14-like phosphatidylinositol-transfer proteins and diversification of phosphoinositide signalling outcomes.
Article in Biochemical Society transactions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics.Frontiers in plant science · 2023Review
- A Sec14 domain protein is required for photoautotrophic growth and chloroplast vesicle formation inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Invading, Leading and Navigating Cells inGenetics · 2018Review
- NuA4 Lysine Acetyltransferase Complex Contributes to Phospholipid Homeostasis inG3 (Bethesda, Md.) · 2017Article
- Molecular Docking: From Lock and Key to Combination Lock.Journal of molecular medicine and clinical applications · 2017Article
- Article
- Article
- Role of flippases, scramblases and transfer proteins in phosphatidylserine subcellular distribution.Traffic (Copenhagen, Denmark) · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The physiological functions of phosphatidylinositol (PtdIns)-transfer proteins (PITPs)/phosphatidylcholine (PtdCho)-transfer proteins are poorly characterized, even though these proteins are conserved throughout the eukaryotic kingdom. Much of the progress in elucidating PITP functions has come from exploitation of genetically tractable model organisms, but the mechanisms for how PITPs execute their biological activities remain unclear. Structural and molecular dynamics approaches are filling in the details for how these proteins actually work as molecules. In the present paper, we discuss our recent work with Sec14-like PITPs and describe how PITPs integrate diverse territories of the lipid metabolome with phosphoinositide signalling.
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.