Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
about
Membrane manipulations by the ESCRT machineryVfa1 Binds to the N-terminal Microtubule-interacting and Trafficking (MIT) Domain of Vps4 and Stimulates Its ATPase ActivityThe high-resolution crystal structure of phosphatidylinositol 4-kinase IIβ and the crystal structure of phosphatidylinositol 4-kinase IIα containing a nucleoside analogue provide a structural basis for isoform-specific inhibitor designA novel minimal in vitro system for analyzing HIV-1 Gag-mediated buddingPre-transition effects mediate forces of assembly between transmembrane proteins.Reverse-topology membrane scission by the ESCRT proteins.Molecular mechanisms of the membrane sculpting ESCRT pathway.Ubiquitin-dependent sorting in endocytosis.Nature's lessons in design: nanomachines to scaffold, remodel and shape membrane compartments.Design principles for robust vesiculation in clathrin-mediated endocytosis.Bud-neck scaffolding as a possible driving force in ESCRT-induced membrane budding.Scaffolding the cup-shaped double membrane in autophagy.CURVATURE-DRIVEN MOLECULAR FLOW ON MEMBRANE SURFACE.Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol.Biophysics of membrane curvature remodeling at molecular and mesoscopic lengthscalesDomes and cones: Adhesion-induced fission of membranes by ESCRT proteins
P2860
Q26784625-F81058B4-69A8-4452-8CA9-82F7601A2326Q27681885-6A992CA7-AD49-46BF-B4DB-55BF63034062Q27701469-F5FA2247-96A1-45A4-A563-C09213F569D5Q35196756-FCF35CBF-0C79-4E58-936B-26207488B2ABQ36827589-525CDBD2-5730-4173-BA59-F75872754E16Q37543507-489731FB-2C75-454C-A2FC-888C258E28A6Q38134065-5E9C6DFD-E357-43C4-8C2E-8FD385071346Q38175272-F6566BDF-D09F-44BE-8543-E93C36F238AAQ38389680-5F08B5F8-0525-4931-AA98-58F73ADE3706Q42320409-DA70BA8B-043F-44C5-A8FE-76966AF8A1E0Q43157483-D40CEF38-4F00-4D70-9EBB-461D5AB8CAB4Q46102755-2F32BDFF-4737-4082-AB4B-9AFC3CD4B4C3Q46278089-2FA5C14B-5F0E-4020-9921-067C25E4193DQ47104814-E4B5AF1C-C952-4E05-A3E7-99B3A888244AQ57176468-FBD29E75-D5B9-442F-A4F1-170EABEC6B57Q58727790-280181CD-21E1-48D5-879A-AC0D7EE7BD1B
P2860
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@ast
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@en
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@nl
type
label
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@ast
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@en
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@nl
prefLabel
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@ast
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@en
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@nl
P2860
P1476
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
@en
P2093
Evzen Boura
James H Hurley
P2860
P304
P356
10.1371/JOURNAL.PCBI.1002736
P577
2012-10-18T00:00:00Z