ArticleBiophysical journal1997
The structure of divalent cation-induced aggregates of PIP2 and their alteration by gelsolin and tau.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 86 citations in OpenAlex.
- Phosphoinositide signaling at the cytoskeleton in the regulation of cell dynamics.Cell death & disease · 2025Review
- The Interplay between GSK3β and Tau Ser262 Phosphorylation during the Progression of Tau Pathology.International journal of molecular sciences · 2022Article
- Heparan Sulfate Proteoglycans (HSPGs) Serve as the Mediator Between Monomeric Tau and Its Subsequent Intracellular ERK1/2 Pathway Activation.Journal of molecular neuroscience : MN · 2022Article
- Methods to study phosphoinositide regulation of ion channels.Methods in enzymology · 2021Article
- Divalent cations bind to phosphoinositides to induce ion and isomer specific propensities for nano-cluster initiation in bilayer membranes.Royal Society open science · 2020Article
- ATP competes with PIP2 for binding to gelsolin.PloS one · 2018Article
- Roles of tau protein in health and disease.Acta neuropathologica · 2017Review
- Cholesterol-Dependent Phase-Demixing in Lipid Bilayers as a Switch for the Activity of the Phosphoinositide-Binding Cytoskeletal Protein Gelsolin.Biochemistry · 2016Article
- Tau Protein Hyperphosphorylation and Aggregation in Alzheimer's Disease and Other Tauopathies, and Possible Neuroprotective Strategies.Biomolecules · 2016Review
- Physical chemistry and membrane properties of two phosphatidylinositol bisphosphate isomers.Physical chemistry chemical physics : PCCP · 2015Article
- Identification of Novel Tau Interactions with Endoplasmic Reticulum Proteins in Alzheimer's Disease Brain.Journal of Alzheimer's disease : JAD · 2015Article
- 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
- Structural basis for PI(4)P-specific membrane recruitment of the Legionella pneumophila effector DrrA/SidM.Structure (London, England : 1993) · 2014Article
- Decrease in phosphatidylinositol 4,5-bisphosphate levels mediates desensitization of the cold sensor TRPM8 channels.The Journal of physiology · 2011Article
- Electrostatic field effects on membrane domain segregation and on lateral diffusion.Biophysical reviews · 2011Review
- Divalent cation-dependent formation of electrostatic PIP2 clusters in lipid monolayers.Biophysical journal · 2011Article
- The many faces of tau.Neuron · 2011Review
- Calcium-dependent lateral organization in phosphatidylinositol 4,5-bisphosphate (PIP2)- and cholesterol-containing monolayers.Biochemistry · 2009Article
- Combined electrostatics and hydrogen bonding determine intermolecular interactions between polyphosphoinositides.Journal of the American Chemical Society · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Phosphatidylinositol bisphosphate (PIP2) serves as a precursor for diacylglycerol and inositol trisphosphate in signal transduction cascades and regulates the activities of several actin binding proteins that influence the organization of the actin cytoskeleton. Molecules of PIP2 form 6-nm diameter micelles in water, but aggregate into larger, multilamellar structures in physiological concentrations of divalent cations. Electron microscopic analysis of these aggregates reveals that they are clusters of striated filaments, suggesting that PIP2 aggregates form stacks of discoid micelles rather than multilamellar vesicles or inverted hexagonal arrays as previously inferred from indirect observations. The distance between striations within the filaments varies from 4.2 to 5.4 nm and the diameter of the filaments depends on the dehydrated ionic radius of the divalent cation, with average diameters of 19, 12, and 10 nm for filaments formed by Mg2+, Ca2+, and Ba2+, respectively. The structure of the divalent cation-induced aggregates can be altered by PIP2 binding proteins. Gelsolin and the microtubule associated protein tau both affect the formation of aggregates, indicating that tau acts as a PIP2 binding protein in a manner similar to gelsolin. In contrast, another PIP2 binding protein, profilin, does not modify the aggregates.
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.