Matches in SemOpenAlex for { <https://semopenalex.org/work/W4214511119> ?p ?o ?g. }
Showing items 1 to 70 of
70
with 100 items per page.
- W4214511119 abstract "The oligomerization of membrane proteins is an important biological process that plays a critical role in the initialization of membrane protein receptor signaling. Unveiling how transmembrane segments oligomerize is critical for understanding the mechanism of membrane receptor signaling activation. Owing to the complicated membrane environment and the extraordinary dynamic properties of the ionizable residues in the transmembrane segment, it is extremely challenging to thoroughly understand the oligomerization process of the transmembrane domain. In this study, transmembrane domain 5 (TMD5) of latent membrane protein-1 from Epstein-Barr virus was used as a prototype model to investigate the trimerization process of the transmembrane segment with ionizable residues. The trimerization process of TMD5 was rebuilt and investigated via conventional molecular dynamics simulations and constant-pH molecular dynamics simulations. When TMD5s approached each other, the tilting angles of the TMD5 monomer decreased. TMD5s formed stable trimers until two interacting sites (D150s and Q139s) along each transmembrane helix were created to lock the TMD5s. The pKa values of D150 shifted toward neutral states in the membrane environment. When TMD5s were monomers, the pKa shift of D150 was mainly influenced by its microenvironment in the lipid bilayer. When TMD5s were moving close to each other, protein-protein interactions became the main contributing factor for the pKa shift of D150s. Overall, this work elucidates the behavior of the TMD5 helix and the pKa shift of ionizable residue D150 in the process of TMD5 oligomerization. This study may provide insight into the development of agents for targeting the oligomerization of membrane proteins." @default.
- W4214511119 created "2022-03-02" @default.
- W4214511119 creator A5011877804 @default.
- W4214511119 creator A5022930741 @default.
- W4214511119 creator A5029286871 @default.
- W4214511119 creator A5057490932 @default.
- W4214511119 date "2022-01-01" @default.
- W4214511119 modified "2023-10-16" @default.
- W4214511119 title "Exploring the Trimerization Process of Transmembrane Helix with Ionizable Residue by Molecular Dynamics Simulations: A Case Study of Transmembrane Domain 5 of LMP-1" @default.
- W4214511119 doi "https://doi.org/10.1039/d2cp00102k" @default.
- W4214511119 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35262149" @default.
- W4214511119 hasPublicationYear "2022" @default.
- W4214511119 type Work @default.
- W4214511119 citedByCount "0" @default.
- W4214511119 crossrefType "journal-article" @default.
- W4214511119 hasAuthorship W4214511119A5011877804 @default.
- W4214511119 hasAuthorship W4214511119A5022930741 @default.
- W4214511119 hasAuthorship W4214511119A5029286871 @default.
- W4214511119 hasAuthorship W4214511119A5057490932 @default.
- W4214511119 hasConcept C118892022 @default.
- W4214511119 hasConcept C12554922 @default.
- W4214511119 hasConcept C144647389 @default.
- W4214511119 hasConcept C147597530 @default.
- W4214511119 hasConcept C170493617 @default.
- W4214511119 hasConcept C185592680 @default.
- W4214511119 hasConcept C18903297 @default.
- W4214511119 hasConcept C24530287 @default.
- W4214511119 hasConcept C2777339483 @default.
- W4214511119 hasConcept C2778530040 @default.
- W4214511119 hasConcept C2779965526 @default.
- W4214511119 hasConcept C39944091 @default.
- W4214511119 hasConcept C41625074 @default.
- W4214511119 hasConcept C55493867 @default.
- W4214511119 hasConcept C59593255 @default.
- W4214511119 hasConcept C71240020 @default.
- W4214511119 hasConcept C86803240 @default.
- W4214511119 hasConceptScore W4214511119C118892022 @default.
- W4214511119 hasConceptScore W4214511119C12554922 @default.
- W4214511119 hasConceptScore W4214511119C144647389 @default.
- W4214511119 hasConceptScore W4214511119C147597530 @default.
- W4214511119 hasConceptScore W4214511119C170493617 @default.
- W4214511119 hasConceptScore W4214511119C185592680 @default.
- W4214511119 hasConceptScore W4214511119C18903297 @default.
- W4214511119 hasConceptScore W4214511119C24530287 @default.
- W4214511119 hasConceptScore W4214511119C2777339483 @default.
- W4214511119 hasConceptScore W4214511119C2778530040 @default.
- W4214511119 hasConceptScore W4214511119C2779965526 @default.
- W4214511119 hasConceptScore W4214511119C39944091 @default.
- W4214511119 hasConceptScore W4214511119C41625074 @default.
- W4214511119 hasConceptScore W4214511119C55493867 @default.
- W4214511119 hasConceptScore W4214511119C59593255 @default.
- W4214511119 hasConceptScore W4214511119C71240020 @default.
- W4214511119 hasConceptScore W4214511119C86803240 @default.
- W4214511119 hasLocation W42145111191 @default.
- W4214511119 hasLocation W42145111192 @default.
- W4214511119 hasOpenAccess W4214511119 @default.
- W4214511119 hasPrimaryLocation W42145111191 @default.
- W4214511119 hasRelatedWork W2030388655 @default.
- W4214511119 hasRelatedWork W2073947642 @default.
- W4214511119 hasRelatedWork W2142656017 @default.
- W4214511119 hasRelatedWork W2156897191 @default.
- W4214511119 hasRelatedWork W2229141637 @default.
- W4214511119 hasRelatedWork W2337172652 @default.
- W4214511119 hasRelatedWork W2790579675 @default.
- W4214511119 hasRelatedWork W3004806557 @default.
- W4214511119 hasRelatedWork W4214511119 @default.
- W4214511119 hasRelatedWork W2185486812 @default.
- W4214511119 isParatext "false" @default.
- W4214511119 isRetracted "false" @default.
- W4214511119 workType "article" @default.