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- W3202594848 abstract "The search for tumor-specific targets among membrane proteins is important for the development for new effective anticancer drugs because membrane proteins represent 60% of drug targets. Transmembrane proteins in cancer cells exhibit an altered pattern of post-translational modifications and generally contain a large extracellular domains with multiple glycosylation and sulfhydryl sites with unknown function. We analyze the features of membrane protein which are required for recognition by monoclonal antibodies using the sodium-dependent phosphate transporter NaPi2b, containing a large extracellular domain 4 (EMD4, 250-360 a.a.) with 4 cysteines and 6 potential asparagine-linked glycosylation sites which can potentially contribute to foldability of conformationally exposed epitope corresponding to this domain." @default.
- W3202594848 created "2021-10-11" @default.
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- W3202594848 date "2021-09-01" @default.
- W3202594848 modified "2023-10-14" @default.
- W3202594848 title "26P Structurally constrained tumor-specific epitope within the largest extracellular domain of sodium-dependent phosphate transporter NaPi2b" @default.
- W3202594848 doi "https://doi.org/10.1016/j.annonc.2021.08.304" @default.
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