ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2010
Phosphoinositide-binding interface proteins involved in shaping cell membranes.
Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- The LOK C-terminus is an IBAR-like domain that facilitates membrane binding and ezrin colocalization.Biophysical journal · 2026Article
- Characterization of the malaria parasiteMicrobiology spectrum · 2025Article
- Inhibitory Effect and Mechanism of Hexanal on the Maturation of Peach-ShapedJournal of fungi (Basel, Switzerland) · 2025Article
- Phosphoinositides in plant-pathogen interaction: trends and perspectives.Stress biology · 2023Review
- Profilin: many facets of a small protein.Biophysical reviews · 2020Review
- VIPP1 rods engulf membranes containing phosphatidylinositol phosphates.Scientific reports · 2019Article
- Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells.International journal of molecular sciences · 2017Review
- Male functions and malfunctions: the impact of phosphoinositides on pollen development and pollen tube growth.Plant reproduction · 2016Review
- F-BAR family proteins, emerging regulators for cell membrane dynamic changes-from structure to human diseases.Journal of hematology & oncology · 2015Review
- Phosphoinositides: tiny lipids with giant impact on cell regulation.Physiological reviews · 2013Review
- HIV entry and envelope glycoprotein-mediated fusion.The Journal of biological chemistry · 2012Review
- Possible role of IRTKS in Tks5-driven osteoclast fusion.Communicative & integrative biology · 2012Article
- Proline-serine-threonine phosphatase-interacting protein 2 (PSTPIP2), a host membrane-deforming protein, is critical for membranous web formation in hepatitis C virus replication.Journal of virology · 2012Article
- The plasma membrane potential and the organization of the actin cytoskeleton of epithelial cells.International journal of cell biology · 2012Article
- Intracellular curvature-generating proteins in cell-to-cell fusion.The Biochemical 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
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanism by which cell and cell membrane shapes are created has long been a subject of great interest. Among the phosphoinositide-binding proteins, a group of proteins that can change the shape of membranes, in addition to the phosphoinositide-binding ability, has been found. These proteins, which contain membrane-deforming domains such as the BAR, EFC/F-BAR, and the IMD/I-BAR domains, led to inward-invaginated tubes or outward protrusions of the membrane, resulting in a variety of membrane shapes. Furthermore, these proteins not only bind to phosphoinositide, but also to the N-WASP/WAVE complex and the actin polymerization machinery, which generates a driving force to shape the membranes.
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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.