Results 51 to 60 of about 641,315 (246)

New Insights into BAR Domain-Induced Membrane Remodeling [PDF]

open access: yesBiophysical Journal, 2009
Mesoscopic simulations and electron microscopy of N-BAR domain-induced liposome remodeling are used to characterize the process of liposome tubulation and vesiculation. The overall process of membrane remodeling is found to involve complex couplings among the N-BAR protein density, the degree of N-BAR oligomerization, and the membrane density.
Ayton, Gary S.   +6 more
openaire   +2 more sources

Membrane Curvature: How BAR Domains Bend Bilayers [PDF]

open access: yesCurrent Biology, 2004
An important new structure suggests the BAR domain is a membrane-binding module that can both produce and sense membrane curvature. BAR resembles a banana that binds membranes electrostatically through its positively charged, concave surface.
Zimmerberg, Joshua, McLaughlin, Stuart
openaire   +2 more sources

Tailoring magnetization reversal of a single-domain bar nanomagnet via its end geometry

open access: yesAIP Advances, 2021
Nanoscale single-domain bar magnets are building blocks for a variety of fundamental and applied mesoscopic magnetic systems, such as artificial spin ices, magnetic shape-morphing microbots, and magnetic majority logic gates.
Jianhua Li   +14 more
doaj   +1 more source

Membrane-Bending Mechanism of Amphiphysin N-BAR Domains [PDF]

open access: yesBiophysical Journal, 2009
BAR domains are highly conserved protein domains participating in a diversity of cellular processes that involve membrane remodeling. The mechanisms underlying such remodeling are debated. For the relatively well-studied case of amphiphysin N-BAR domain, one suggested mechanism involves scaffolding, i.e., binding of a negatively charged membrane to the
Arkhipov, Anton   +2 more
openaire   +2 more sources

Membrane sculpting by curved DNA origami scaffolds

open access: yesNature Communications, 2018
BAR domain proteins feature a “banana-like” shape which is thought to aid membrane scaffolding and membrane tubulation. Here authors use DNA origami mimicking BAR domains, giant unilamellar vesicles and fluorescence imaging to study how different BAR ...
Henri G. Franquelim   +4 more
doaj   +1 more source

Revisiting I-BAR Proteins at Central Synapses

open access: yesFrontiers in Neural Circuits, 2021
Dendritic spines, the distinctive postsynaptic feature of central nervous system (CNS) excitatory synapses, have been studied extensively as electrical and chemical compartments, as well as scaffolds for receptor cycling and positioning of signaling ...
Christina Chatzi, Gary L. Westbrook
doaj   +1 more source

The eisosome core is composed of BAR domain proteins

open access: yesMolecular Biology of the Cell, 2011
Eisosomes define sites of plasma membrane organization. In Saccharomyces cerevisiae, eisosomes delimit furrow-like plasma membrane invaginations that concentrate sterols, transporters, and signaling molecules. Eisosomes are static macromolecular assemblies composed of cytoplasmic proteins, most of which have no known function.
Olivera-Couto, Agustina   +3 more
openaire   +2 more sources

BAR Domain Scaffolds in Dynamin-Mediated Membrane Fission [PDF]

open access: yesCell, 2014
Biological membranes undergo constant remodeling by membrane fission and fusion to change their shape and to exchange material between subcellular compartments. During clathrin-mediated endocytosis, the dynamic assembly and disassembly of protein scaffolds comprising members of the bin-amphiphysin-rvs (BAR) domain protein superfamily constrain the ...
Daumke, Oliver   +2 more
openaire   +3 more sources

The cryo-EM structure of the SNX–BAR Mvp1 tetramer

open access: yesNature Communications, 2020
SNX-BAR proteins are a family of PX and BAR domain-containing proteins with pivotal roles in trafficking processes. Here authors present the cryo-EM structure of the full-length fungal SNX-BAR Mvp1, which is an autoinhibited tetramer and provides ...
Dapeng Sun   +5 more
doaj   +1 more source

A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling

open access: yeseLife, 2021
Membrane protein recycling systems are essential for maintenance of the endosome-lysosome system. In yeast, retromer and Snx4 coat complexes are recruited to the endosomal surface, where they recognize cargos. They sort cargo and deform the membrane into
Sho W Suzuki   +5 more
doaj   +1 more source

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