ArticleFEBS open bio2019
The hydrophobic C-terminal sequence of transthyretin affects its catalytic kinetics towards amidated neuropeptide Y.
Article in FEBS open bio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Extracellular Vesicles Contribute to the Metabolism of Transthyretin Amyloid in Hereditary Transthyretin Amyloidosis.Frontiers in molecular biosciences · 2022Article
- Faecal proteome in clinically healthy dogs and cats: Findings in pooled faeces from 10 cats and 10 dogs.Veterinary record open · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transthyretin (TTR) is a transporter for thyroid hormone and retinol binding protein that has recently been reported to have proteolytic activity against certain substrates, including amidated neuropeptide Y (NPY). However, the proteolytic activity of TTR towards NPY is not fully understood. Here, we used fluorescence-based assays to determine the catalytic kinetics of human TTR towards human amidated NPY. The Michaelis constant (
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Registered trials
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