Matches in SemOpenAlex for { <https://semopenalex.org/work/W2584279036> ?p ?o ?g. }
Showing items 1 to 80 of
80
with 100 items per page.
- W2584279036 endingPage "138a" @default.
- W2584279036 startingPage "137a" @default.
- W2584279036 abstract "Phosphoinositide, a phosphorylated form of phosphatidylinositol (PI), plays an important role in, e.g., cell signaling and membrane trafficking. Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) found in, for instance, the plasma membrane and the Golgi apparatus is known to bind to a number of proteins. How the PI(4,5)P2-binding proteins recognize their substrate and how the binding is regulated and fine-tuned remains unclear. In this work, we hypothesize that the increasing cholesterol concentration along a path from the nucleus towards the plasma membrane may be one of the key regulators in this process.To consider this hypothesis, we employed both atomistic and coarse-grained (CG) molecular dynamics simulations to study the binding of PI(4,5)P2 with phospholipase C delta 1 (PLC) that is an important signaling enzyme known to bind PI(4,5)P2. Unbiased CG MARTINI simulations in POPC/PI(4,5)P2 and POPC/PI(4,5)P2/cholesterol mixtures were complemented by umbrella sampling simulations to measure the free energy of PI(4,5)P2 binding to PLC. The final structures of the PLC-PI(4,5)P2 complexes were fine-grained to atomistic detail and simulated over microseconds to explore the details of the binding process.In essence, we observed deeper free energy minima for the binding of PI(4,5)P2 to PLC in the cholesterol-rich membrane system, compared to cholesterol-free membranes, thus supporting the underlying hypothesis that PI(4,5)P2 binding to PLC and possibly also other PI(4,5)P2-binding proteins is strengthened by increasing cholesterol concentration. The atom-scale features such as hydrogen bonding patterns and lipid-specific interactions that dictate the binding preference are discussed in detail in the presented work." @default.
- W2584279036 created "2017-02-10" @default.
- W2584279036 creator A5029212835 @default.
- W2584279036 creator A5031182653 @default.
- W2584279036 creator A5065920817 @default.
- W2584279036 creator A5082983574 @default.
- W2584279036 date "2017-02-01" @default.
- W2584279036 modified "2023-09-26" @default.
- W2584279036 title "PI(4,5)P 2 Binds to Phospholipase C Delta 1 in a Cholesterol Concentration Dependent Manner: Perspective on Implications to PI(4,5)P 2 -Binding Proteins" @default.
- W2584279036 doi "https://doi.org/10.1016/j.bpj.2016.11.762" @default.
- W2584279036 hasPublicationYear "2017" @default.
- W2584279036 type Work @default.
- W2584279036 sameAs 2584279036 @default.
- W2584279036 citedByCount "1" @default.
- W2584279036 countsByYear W25842790362018 @default.
- W2584279036 crossrefType "journal-article" @default.
- W2584279036 hasAuthorship W2584279036A5029212835 @default.
- W2584279036 hasAuthorship W2584279036A5031182653 @default.
- W2584279036 hasAuthorship W2584279036A5065920817 @default.
- W2584279036 hasAuthorship W2584279036A5082983574 @default.
- W2584279036 hasBestOaLocation W25842790361 @default.
- W2584279036 hasConcept C12554922 @default.
- W2584279036 hasConcept C128747166 @default.
- W2584279036 hasConcept C147597530 @default.
- W2584279036 hasConcept C185592680 @default.
- W2584279036 hasConcept C2778597717 @default.
- W2584279036 hasConcept C2780610907 @default.
- W2584279036 hasConcept C2780943371 @default.
- W2584279036 hasConcept C39944091 @default.
- W2584279036 hasConcept C41625074 @default.
- W2584279036 hasConcept C53009064 @default.
- W2584279036 hasConcept C55493867 @default.
- W2584279036 hasConcept C59593255 @default.
- W2584279036 hasConcept C62478195 @default.
- W2584279036 hasConcept C86803240 @default.
- W2584279036 hasConceptScore W2584279036C12554922 @default.
- W2584279036 hasConceptScore W2584279036C128747166 @default.
- W2584279036 hasConceptScore W2584279036C147597530 @default.
- W2584279036 hasConceptScore W2584279036C185592680 @default.
- W2584279036 hasConceptScore W2584279036C2778597717 @default.
- W2584279036 hasConceptScore W2584279036C2780610907 @default.
- W2584279036 hasConceptScore W2584279036C2780943371 @default.
- W2584279036 hasConceptScore W2584279036C39944091 @default.
- W2584279036 hasConceptScore W2584279036C41625074 @default.
- W2584279036 hasConceptScore W2584279036C53009064 @default.
- W2584279036 hasConceptScore W2584279036C55493867 @default.
- W2584279036 hasConceptScore W2584279036C59593255 @default.
- W2584279036 hasConceptScore W2584279036C62478195 @default.
- W2584279036 hasConceptScore W2584279036C86803240 @default.
- W2584279036 hasIssue "3" @default.
- W2584279036 hasLocation W25842790361 @default.
- W2584279036 hasOpenAccess W2584279036 @default.
- W2584279036 hasPrimaryLocation W25842790361 @default.
- W2584279036 hasRelatedWork W104307719 @default.
- W2584279036 hasRelatedWork W2009614301 @default.
- W2584279036 hasRelatedWork W2061511089 @default.
- W2584279036 hasRelatedWork W2096478565 @default.
- W2584279036 hasRelatedWork W2114470810 @default.
- W2584279036 hasRelatedWork W2120930184 @default.
- W2584279036 hasRelatedWork W2128846365 @default.
- W2584279036 hasRelatedWork W2134419616 @default.
- W2584279036 hasRelatedWork W2200356026 @default.
- W2584279036 hasRelatedWork W2270742048 @default.
- W2584279036 hasRelatedWork W236817708 @default.
- W2584279036 hasRelatedWork W2584627424 @default.
- W2584279036 hasRelatedWork W2584712739 @default.
- W2584279036 hasRelatedWork W2765315469 @default.
- W2584279036 hasRelatedWork W2791268153 @default.
- W2584279036 hasRelatedWork W2793618585 @default.
- W2584279036 hasRelatedWork W2919576184 @default.
- W2584279036 hasRelatedWork W3022866527 @default.
- W2584279036 hasRelatedWork W3126807732 @default.
- W2584279036 hasRelatedWork W3194385762 @default.
- W2584279036 hasVolume "112" @default.
- W2584279036 isParatext "false" @default.
- W2584279036 isRetracted "false" @default.
- W2584279036 magId "2584279036" @default.
- W2584279036 workType "article" @default.