ArticleFEBS open bio2017
Increasing the length and hydrophobicity of the C-terminal sequence of transthyretin strengthens its binding affinity to retinol binding protein.
Article in FEBS open bio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 1 citations in OpenAlex.
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Transthyretin (TTR) is a transporter for thyroid hormone (TH) and retinol, the latter via binding with retinol binding protein (RBP). Both the N-terminal and C-terminal regions of the TTR subunit are located in close proximity to the central binding channel for ligands. During the evolution of vertebrates, these regions changed in length and hydropathy. The changes in the N-terminal sequence were demonstrated to affect the binding affinities for THs and RBP. Here, the effects of changes in the C-terminal sequence were determined. Three chimeric TTRs, namely pigC/huTTR (human TTR with the C-terminal sequence changed to that of
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