FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2022132736> ?p ?o ?g. }

• W2022132736 endingPage "12066" @default.
• W2022132736 startingPage "12054" @default.
• W2022132736 abstract "Upon activation, Toll-like receptor 4 (TLR4) binds adapter proteins, including MyD88 (myeloid differentiation primary response gene 88) and Mal (MyD88 adapter-like) for its signal transduction. TLR4 and the adapter proteins each contain a Toll/Il-1 receptor domain (TIR domain). In this study we used random mutagenesis and the mammalian two-hybrid method MAPPIT (mammalian protein-protein interaction trap) to identify mutations in Mal that disrupt its interaction with TLR4 and/or MyD88. Our study shows that four potential binding sites and the AB-loop in the Mal TIR domain all contribute to formation of the TLR4-Mal-MyD88 complex. Mutations in the symmetrical back-to-back Mal homodimer interface affect Mal homodimerization and interaction with MyD88 and TLR4. Our data suggest that Mal dimerization may lead to formation of potential binding platforms on the top and the side of the Mal dimer that bind MyD88 or TLR4. Mutations that affect the interaction of Mal with MyD88 also affect NF-κB activation induced by Mal overexpression. In MAPPIT, co-expression of the MyD88 TIR domain enhances Mal dimerization and Mal binding to TLR4. Similarly, co-expression of Mal and the MyD88 TIR domain strongly promotes dimerization of the TLR4 intracellular domain in MAPPIT. The different types of TIR-TIR interactions in the TLR4-Mal-MyD88 complex thus show cooperative binding in MAPPIT. We present plausible models for the TIR-TIR interactions in the TLR4-Mal-MyD88 complex. Upon activation, Toll-like receptor 4 (TLR4) binds adapter proteins, including MyD88 (myeloid differentiation primary response gene 88) and Mal (MyD88 adapter-like) for its signal transduction. TLR4 and the adapter proteins each contain a Toll/Il-1 receptor domain (TIR domain). In this study we used random mutagenesis and the mammalian two-hybrid method MAPPIT (mammalian protein-protein interaction trap) to identify mutations in Mal that disrupt its interaction with TLR4 and/or MyD88. Our study shows that four potential binding sites and the AB-loop in the Mal TIR domain all contribute to formation of the TLR4-Mal-MyD88 complex. Mutations in the symmetrical back-to-back Mal homodimer interface affect Mal homodimerization and interaction with MyD88 and TLR4. Our data suggest that Mal dimerization may lead to formation of potential binding platforms on the top and the side of the Mal dimer that bind MyD88 or TLR4. Mutations that affect the interaction of Mal with MyD88 also affect NF-κB activation induced by Mal overexpression. In MAPPIT, co-expression of the MyD88 TIR domain enhances Mal dimerization and Mal binding to TLR4. Similarly, co-expression of Mal and the MyD88 TIR domain strongly promotes dimerization of the TLR4 intracellular domain in MAPPIT. The different types of TIR-TIR interactions in the TLR4-Mal-MyD88 complex thus show cooperative binding in MAPPIT. We present plausible models for the TIR-TIR interactions in the TLR4-Mal-MyD88 complex." @default.
• W2022132736 created "2016-06-24" @default.
• W2022132736 creator A5001764273 @default.
• W2022132736 creator A5021511969 @default.
• W2022132736 creator A5032088939 @default.
• W2022132736 creator A5054960368 @default.
• W2022132736 creator A5054994879 @default.
• W2022132736 creator A5062595440 @default.
• W2022132736 date "2013-04-01" @default.
• W2022132736 modified "2023-10-17" @default.
• W2022132736 title "Identification of Binding Sites for Myeloid Differentiation Primary Response Gene 88 (MyD88) and Toll-like Receptor 4 in MyD88 Adapter-like (Mal)" @default.
• W2022132736 cites W101470933 @default.
• W2022132736 cites W1519843522 @default.
• W2022132736 cites W1543052543 @default.
• W2022132736 cites W1556574075 @default.
• W2022132736 cites W1966772446 @default.
• W2022132736 cites W1967269498 @default.
• W2022132736 cites W1976424894 @default.
• W2022132736 cites W1978901379 @default.
• W2022132736 cites W1982185661 @default.
• W2022132736 cites W1984616248 @default.
• W2022132736 cites W1991931339 @default.
• W2022132736 cites W1993211211 @default.
• W2022132736 cites W1998055077 @default.
• W2022132736 cites W2003385732 @default.
• W2022132736 cites W2005571008 @default.
• W2022132736 cites W2006348886 @default.
• W2022132736 cites W2013469022 @default.
• W2022132736 cites W2013601771 @default.
• W2022132736 cites W2015045770 @default.
• W2022132736 cites W2015263036 @default.
• W2022132736 cites W2015833994 @default.
• W2022132736 cites W2025450536 @default.
• W2022132736 cites W2032972084 @default.
• W2022132736 cites W2039582913 @default.
• W2022132736 cites W2042482956 @default.
• W2022132736 cites W2043823247 @default.
• W2022132736 cites W2046743509 @default.
• W2022132736 cites W2049262799 @default.
• W2022132736 cites W2050962647 @default.
• W2022132736 cites W2054979063 @default.
• W2022132736 cites W2055043387 @default.
• W2022132736 cites W2058658435 @default.
• W2022132736 cites W2061319403 @default.
• W2022132736 cites W2082890018 @default.
• W2022132736 cites W2089217951 @default.
• W2022132736 cites W2091176630 @default.
• W2022132736 cites W2092713838 @default.
• W2022132736 cites W2094148186 @default.
• W2022132736 cites W2102502076 @default.
• W2022132736 cites W2109491705 @default.
• W2022132736 cites W2110061191 @default.
• W2022132736 cites W2111428445 @default.
• W2022132736 cites W2115185894 @default.
• W2022132736 cites W2116455233 @default.
• W2022132736 cites W2119747146 @default.
• W2022132736 cites W2120772351 @default.
• W2022132736 cites W2122242846 @default.
• W2022132736 cites W2127863596 @default.
• W2022132736 cites W2129319296 @default.
• W2022132736 cites W2132629607 @default.
• W2022132736 cites W2147038697 @default.
• W2022132736 cites W2164146079 @default.
• W2022132736 cites W2167593547 @default.
• W2022132736 cites W95014119 @default.
• W2022132736 doi "https://doi.org/10.1074/jbc.m112.415810" @default.
• W2022132736 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3636891" @default.
• W2022132736 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23460645" @default.
• W2022132736 hasPublicationYear "2013" @default.
• W2022132736 type Work @default.
• W2022132736 sameAs 2022132736 @default.
• W2022132736 citedByCount "36" @default.
• W2022132736 countsByYear W20221327362013 @default.
• W2022132736 countsByYear W20221327362014 @default.
• W2022132736 countsByYear W20221327362015 @default.
• W2022132736 countsByYear W20221327362016 @default.
• W2022132736 countsByYear W20221327362017 @default.
• W2022132736 countsByYear W20221327362018 @default.
• W2022132736 countsByYear W20221327362019 @default.
• W2022132736 countsByYear W20221327362020 @default.
• W2022132736 countsByYear W20221327362021 @default.
• W2022132736 countsByYear W20221327362022 @default.
• W2022132736 countsByYear W20221327362023 @default.
• W2022132736 crossrefType "journal-article" @default.
• W2022132736 hasAuthorship W2022132736A5001764273 @default.
• W2022132736 hasAuthorship W2022132736A5021511969 @default.
• W2022132736 hasAuthorship W2022132736A5032088939 @default.
• W2022132736 hasAuthorship W2022132736A5054960368 @default.
• W2022132736 hasAuthorship W2022132736A5054994879 @default.
• W2022132736 hasAuthorship W2022132736A5062595440 @default.
• W2022132736 hasBestOaLocation W20221327361 @default.
• W2022132736 hasConcept C104317684 @default.
• W2022132736 hasConcept C107824862 @default.
• W2022132736 hasConcept C119599485 @default.
• W2022132736 hasConcept C127413603 @default.
• W2022132736 hasConcept C136449434 @default.
• W2022132736 hasConcept C153911025 @default.
• W2022132736 hasConcept C16318435 @default.

• next