Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
about
Dynamics and instabilities of lipid bilayer membrane shapesCurvature-undulation coupling as a basis for curvature sensing and generation in bilayer membranesMembrane remodeling and mechanics: Experiments and simulations of α-SynucleinMutations in BIN1 associated with centronuclear myopathy disrupt membrane remodeling by affecting protein density and oligomerizationMembrane tension and peripheral protein density mediate membrane shape transitionsStructural insights into the cooperative remodeling of membranes by amphiphysin/BIN1.Membrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Coarse-Grained Models for Protein-Cell Membrane Interactions.Linear aggregation of proteins on the membrane as a prelude to membrane remodelingEndophilin A1 induces different membrane shapes using a conformational switch that is regulated by phosphorylation.α-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry.Mechanisms shaping cell membranesSolvent-Free, Highly Coarse-Grained Models for Charged Lipid Systems.Multiscale computational models in physical systems biology of intracellular trafficking.Defining the free-energy landscape of curvature-inducing proteins on membrane bilayersEndophilin-A1 BAR domain interaction with arachidonyl CoA.Tubulation by amphiphysin requires concentration-dependent switching from wedging to scaffolding.Application of a free-energy-landscape approach to study tension-dependent bilayer tubulation mediated by curvature-inducing proteins.Phenomenology based multiscale models as tools to understand cell membrane and organelle morphologies.Kinetics of endophilin N-BAR domain dimerization and membrane interactions.A time course of orchestrated endophilin action in sensing, bending, and stabilizing curved membranes.Protein-mediated transformation of lipid vesicles into tubular networks.How curvature-generating proteins build scaffolds on membrane nanotubes.Suppressing membrane height fluctuations leads to a membrane-mediated interaction among proteins.Engineering lipid bilayer membranes for protein studies.Nature's lessons in design: nanomachines to scaffold, remodel and shape membrane compartments.Multiscale simulations of protein-facilitated membrane remodelingThe Role of BAR Domain Proteins in the Regulation of Membrane DynamicsSalt Bridge Formation between the I-BAR Domain and Lipids Increases Lipid Density and Membrane Curvature.Membrane Remodeling by a Bacterial Phospholipid-Methylating Enzyme.The N-Terminal Amphipathic Helix of Endophilin Does Not Contribute to Its Molecular Curvature Generation Capacity.Long-Range Organization of Membrane-Curving Proteins.Fluorescent quantification of size and lamellarity of membrane nanotubes.Generation of wavy structure on lipid membrane by peripheral proteins: a linear elastic analysis.Anisotropic spontaneous curvatures in lipid membranes.Directed Supramolecular Organization of N-BAR Proteins through Regulation of H0 Membrane Immersion Depth
P2860
Q26824845-90F5ED2D-4553-46D3-A83C-0C65FCBF2E4AQ27315156-D816FE89-4B93-44E8-8740-04E430351862Q28066666-3EFD9F84-D003-4498-A00E-ABBF00EDFBE2Q28538108-4B9436B7-730B-44D5-BB9A-DB2FC51AD7B5Q28652627-075A47AC-57F4-4E78-B78F-8A144DA74E40Q30009082-7F611292-6F32-4CD4-ADF8-B9FD4F13DEC3Q30378040-F5C8BF8D-AFD9-4A9D-8C02-0C9B5FA09C72Q30398145-8A9BE44E-7168-4145-9A88-E7C884C040E2Q30560383-EA6CD159-8FEB-45DB-931C-367FA278DA44Q33627399-ADC22CD1-C487-4794-91A4-9D4E5B9C6378Q33926400-E66133F7-CA84-4B5B-B03D-661007A83C17Q34269214-8018164B-5E1B-4BB7-B1B4-12D501C37F19Q34337372-C3BB3673-FD3B-45D6-A264-E5D78397E660Q35106771-6DDFCD81-9332-46A2-9661-3F2C47BB84CBQ35106834-10A60903-A4CB-45AD-8C24-D75948247222Q35596442-C343AABE-8BF6-49EE-8F94-6A809E790C4CQ35623993-D055F3D9-5A65-486C-A1AA-1BBA2440A5F7Q36692985-45885190-ED66-4C99-B191-404F05EB126FQ36793933-1783744F-6363-48CC-B217-5F698DF1A607Q36812328-364112D9-A85C-46B8-976F-490D6430F22FQ37052748-034EF286-3C2B-4567-A2AD-AFA4C596239AQ37078355-1633071B-930B-4A4E-A5B4-CA2FE4BAC9F2Q37323085-4DE989A6-7D9C-4EAC-A727-22954C5C2DB3Q37733385-E5AFD694-EE71-444E-97C1-85D95BB7C292Q38159483-F63EC7EF-A0EC-4DAE-9F80-AD7FCB6B5E54Q38389680-4111AAFA-FC6D-472E-8F49-285566B01821Q38871983-86732C85-BEA2-472D-8DC6-B14EC326818AQ39066567-06899843-7E28-47C7-8882-88402B6D96BBQ42120252-B0CFD922-F240-439B-9179-88D6811670EFQ42321186-B29B8522-D093-442F-A09F-20238A629435Q43131566-D2C872E1-62E0-40CB-9CF0-136BF99CE01CQ47135815-52504BD1-51DF-4FF9-BE47-15C57139894BQ47434281-D2799D9A-9F2D-4872-9BE3-81260A7C5444Q47872931-EF01904D-9DC3-4DF3-9A4C-92D6BC21B3BAQ51067691-626371F2-5E77-4E2A-B39E-7D74404BD816Q58608835-809A4B90-64C0-4E43-8E37-A9318D89D8D0
P2860
Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
@ast
Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
@en
type
label
Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
@ast
Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
@en
prefLabel
Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
@ast
Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
@en
P2093
P2860
P1433
P1476
Understanding the role of amphipathic helices in N-BAR domain driven membrane remodeling
@en
P2093
Carsten Mim
Edward Lyman
Francisco X Vázquez
Haosheng Cui
Vinzenz M Unger
P2860
P304
P356
10.1016/J.BPJ.2012.12.006
P407
P577
2013-01-01T00:00:00Z