ArticleJournal of the American Chemical Society2008
Combined electrostatics and hydrogen bonding determine intermolecular interactions between polyphosphoinositides.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
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.
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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
- The degree and position of phosphorylation determine the impact of toxic and trace metals on phosphoinositide containing model membranes.BBA advances · 2021Article
- A multiscale biophysical model for the recruitment of actin nucleating proteins at the membrane interface.Soft matter · 2020Article
- Plasma membranes are asymmetric in lipid unsaturation, packing and protein shape.Nature chemical biology · 2020Article
- Divalent cations bind to phosphoinositides to induce ion and isomer specific propensities for nano-cluster initiation in bilayer membranes.Royal Society open science · 2020Article
- Characterization of Specific Ion Effects on PI(4,5)PThe journal of physical chemistry. B · 2020Article
- GαBiochemistry · 2019Article
- Structural mechanism for Bruton's tyrosine kinase activation at the cell membrane.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Regulation of actin assembly by PI(4,5)P2 and other inositol phospholipids: An update on possible mechanisms.Biochemical and biophysical research communications · 2018Review
- Article
- Multivalent Cation-Bridged PI(4,5)PBiophysical journal · 2018Article
- Cations induce shape remodeling of negatively charged phospholipid membranes.Physical chemistry chemical physics : PCCP · 2017Article
- Calcium Directly Regulates Phosphatidylinositol 4,5-Bisphosphate Headgroup Conformation and Recognition.Journal of the American Chemical Society · 2017Article
- The Ebola virus protein VP40 hexamer enhances the clustering of PI(4,5)PPhysical chemistry chemical physics : PCCP · 2016Article
- Cellular and molecular interactions of phosphoinositides and peripheral proteins.Chemistry and physics of lipids · 2014Review
- Counterion-mediated cluster formation by polyphosphoinositides.Chemistry and physics of lipids · 2014Review
- Counterion-mediated pattern formation in membranes containing anionic lipids.Advances in colloid and interface science · 2014Review
- Quantum and all-atom molecular dynamics simulations of protonation and divalent ion binding to phosphatidylinositol 4,5-bisphosphate (PIP2).The journal of physical chemistry. B · 2013Article
- Divalent cation-induced cluster formation by polyphosphoinositides in model membranes.Journal of the American Chemical Society · 2012Article
- The physical chemistry of the enigmatic phospholipid diacylglycerol pyrophosphate.Frontiers in plant science · 2012Article
- Divalent cation-dependent formation of electrostatic PIP2 clusters in lipid monolayers.Biophysical journal · 2011Article
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 at 2 institutions in 2 countries.
Funding
Abstract
Membrane lipids are active contributors to cell function as key mediators in signaling pathways controlling cell functions including inflammation, apoptosis, migration, and proliferation. Recent work on multimolecular lipid structures suggests a critical role for lipid organization in regulating the function of both lipids and proteins. Of particular interest in this context are the polyphosphoinositides (PPI's), especially phosphatidylinositol (4,5) bisphosphate (PIP 2). The cellular functions of PIP 2 are numerous but the organization of PIP 2 in the inner leaflet of the plasma membrane, as well as the factors controlling targeting of PIP 2 to specific proteins, remains poorly understood. To analyze the organization of PIP 2 in a simplified planar system, we used Langmuir monolayers to study the effects of subphase conditions on monolayers of purified naturally derived PIP 2 and other anionic or zwitterionic phospholipids. We report a significant molecular area expanding effect of subphase monovalent salts on PIP 2 at biologically relevant surface densities. This effect is shown to be specific to PIP 2 and independent of subphase pH. Chaotropic agents (e.g., salts, trehalose, urea, temperature) that disrupt water structure and the ability of water to mediate intermolecular hydrogen bonding also specifically expanded PIP 2 monolayers. These results suggest a combination of water-mediated hydrogen bonding and headgroup repulsion in determining the organization of PIP 2, and may contribute to an explanation for the unique functionality of PIP 2 compared to other anionic phospholipids.
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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.