Matches in SemOpenAlex for { <https://semopenalex.org/work/W2890835610> ?p ?o ?g. }
- W2890835610 endingPage "61" @default.
- W2890835610 startingPage "47" @default.
- W2890835610 abstract "Arrestins were discovered as proteins that bind active phosphorylated G protein-coupled receptors (GPCRs) and block their interactions with G proteins, i.e., for their role in homologous desensitization of GPCRs. Mammals express only four arrestin subtypes, two of which are largely restricted to the retina. Two nonvisual arrestins are ubiquitous and interact with hundreds of different GPCRs and dozens of other binding partners. Changes of just a few residues on the receptor-binding surface were shown to dramatically affect GPCR preference of inherently promiscuous nonvisual arrestins. Mutations on the cytosol-facing side of arrestins modulate their interactions with individual downstream signaling molecules. Thus, it appears feasible to construct arrestin mutants specifically linking particular GPCRs with signaling pathways of choice or mutants that sever the links between selected GPCRs and unwanted pathways. Signaling-biased “designer arrestins” have the potential to become valuable molecular tools for research and therapy." @default.
- W2890835610 created "2018-09-27" @default.
- W2890835610 creator A5049089914 @default.
- W2890835610 creator A5055148764 @default.
- W2890835610 creator A5078326314 @default.
- W2890835610 date "2018-01-01" @default.
- W2890835610 modified "2023-09-26" @default.
- W2890835610 title "Arrestins: Introducing Signaling Bias Into Multifunctional Proteins" @default.
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