Matches in SemOpenAlex for { <https://semopenalex.org/work/W2153145497> ?p ?o ?g. }
Showing items 1 to 74 of
74
with 100 items per page.
- W2153145497 endingPage "570a" @default.
- W2153145497 startingPage "570a" @default.
- W2153145497 abstract "Internalization of extracellular cargo by eukaryotic cells via the clathrin-dependent endocytosis (CDE) is an important regulatory process prominent in several cellular functions. Subsequent to receptor activation, a sequence of molecular events in CDE is responsible for the recruitment of various accessory proteins such as AP-2, epsin, AP180, eps15, dynamin, amphiphysin, endophilin, and clathrin to the plasma membrane to orchestrate membrane vesiculation. While the involvement of these proteins have been established and their roles in membrane deformation, cargo recognition, and vesicle scission have been identified, current conceptual understanding falls short of a mechanistic description of the cooperativity and the bioenergetics of the underlying vesicle nucleation event which we address here using theoretical models based on an elastic continuum representation for the membrane and atomistic to coarse-grained representations for the proteins. We employ the surface evolution approach to describe membrane geometries by minimizing the Helfrich Hamiltonian in a curvilinear coordinate system and address how the energetics of vesicle formation in a membrane is impacted by the presence of a growing clathrin coat. We consider two limiting scenarios: (1) the clathrin assembly model in which the clathrin coat induces membrane curvature by forming a curvilinear scaffold; (2) the accessory curvature-inducing protein assembly model, in which the clathrin lattice merely serves as a template to spatially pattern curvature inducing proteins such as epsin which collectively induce membrane curvature. Analyzing the energy required for vesicle formation from a planar bilayer, we demonstrate the role of the CDE protein assembly in driving membrane vesiculation. Furthermore, using a time-dependent Ginzburg-Landau formalism along with the thermodynamic method of free energy perturbation, we calculate the free energy the nucleated vesicle and quantify the finite-temperature corrections to the energy landscape of vesicle nucleation in CDE." @default.
- W2153145497 created "2016-06-24" @default.
- W2153145497 creator A5037007496 @default.
- W2153145497 creator A5041625801 @default.
- W2153145497 date "2009-02-01" @default.
- W2153145497 modified "2023-09-26" @default.
- W2153145497 title "Computational Delineation of the Bioenergetics of Protein-Mediated Orchestration of Membrane Vesiculation in Clathrin-Dependent Endocytosis" @default.
- W2153145497 doi "https://doi.org/10.1016/j.bpj.2008.12.3736" @default.
- W2153145497 hasPublicationYear "2009" @default.
- W2153145497 type Work @default.
- W2153145497 sameAs 2153145497 @default.
- W2153145497 citedByCount "0" @default.
- W2153145497 crossrefType "journal-article" @default.
- W2153145497 hasAuthorship W2153145497A5037007496 @default.
- W2153145497 hasAuthorship W2153145497A5041625801 @default.
- W2153145497 hasBestOaLocation W21531454971 @default.
- W2153145497 hasConcept C12554922 @default.
- W2153145497 hasConcept C130316041 @default.
- W2153145497 hasConcept C156407911 @default.
- W2153145497 hasConcept C170493617 @default.
- W2153145497 hasConcept C185592680 @default.
- W2153145497 hasConcept C2777278457 @default.
- W2153145497 hasConcept C2780976139 @default.
- W2153145497 hasConcept C28005876 @default.
- W2153145497 hasConcept C39944091 @default.
- W2153145497 hasConcept C41625074 @default.
- W2153145497 hasConcept C55493867 @default.
- W2153145497 hasConcept C63162447 @default.
- W2153145497 hasConcept C86803240 @default.
- W2153145497 hasConcept C95444343 @default.
- W2153145497 hasConceptScore W2153145497C12554922 @default.
- W2153145497 hasConceptScore W2153145497C130316041 @default.
- W2153145497 hasConceptScore W2153145497C156407911 @default.
- W2153145497 hasConceptScore W2153145497C170493617 @default.
- W2153145497 hasConceptScore W2153145497C185592680 @default.
- W2153145497 hasConceptScore W2153145497C2777278457 @default.
- W2153145497 hasConceptScore W2153145497C2780976139 @default.
- W2153145497 hasConceptScore W2153145497C28005876 @default.
- W2153145497 hasConceptScore W2153145497C39944091 @default.
- W2153145497 hasConceptScore W2153145497C41625074 @default.
- W2153145497 hasConceptScore W2153145497C55493867 @default.
- W2153145497 hasConceptScore W2153145497C63162447 @default.
- W2153145497 hasConceptScore W2153145497C86803240 @default.
- W2153145497 hasConceptScore W2153145497C95444343 @default.
- W2153145497 hasIssue "3" @default.
- W2153145497 hasLocation W21531454971 @default.
- W2153145497 hasOpenAccess W2153145497 @default.
- W2153145497 hasPrimaryLocation W21531454971 @default.
- W2153145497 hasRelatedWork W15592860 @default.
- W2153145497 hasRelatedWork W1948844441 @default.
- W2153145497 hasRelatedWork W1964969305 @default.
- W2153145497 hasRelatedWork W1979080454 @default.
- W2153145497 hasRelatedWork W1987611593 @default.
- W2153145497 hasRelatedWork W2049341203 @default.
- W2153145497 hasRelatedWork W2053031822 @default.
- W2153145497 hasRelatedWork W2055395908 @default.
- W2153145497 hasRelatedWork W2101644849 @default.
- W2153145497 hasRelatedWork W2121117432 @default.
- W2153145497 hasRelatedWork W2134197141 @default.
- W2153145497 hasRelatedWork W2149184242 @default.
- W2153145497 hasRelatedWork W2316490677 @default.
- W2153145497 hasRelatedWork W2584812523 @default.
- W2153145497 hasRelatedWork W2751160857 @default.
- W2153145497 hasRelatedWork W2953822521 @default.
- W2153145497 hasRelatedWork W2954744935 @default.
- W2153145497 hasRelatedWork W3014071257 @default.
- W2153145497 hasRelatedWork W3184042015 @default.
- W2153145497 hasVolume "96" @default.
- W2153145497 isParatext "false" @default.
- W2153145497 isRetracted "false" @default.
- W2153145497 magId "2153145497" @default.
- W2153145497 workType "article" @default.