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- W1978608959 abstract "Myostatin, a negative regulator of muscle mass is a promising target for the treatment of muscle atrophic diseases. The novel myostatin inhibitory peptide, DF-3 is derived from the N-terminal α-helical domain of follistatin, which is an endogenous inhibitor of myostatin and other TGF-β family members. It has been suggested that the optimization of hydrophobic residues is important to enhance the myostatin inhibition. This study describes a structure–activity relationship study focused on hydrophobic residues of DF-3 and designed to obtain a more potent peptide. A methionine residue in DF-3, which is susceptible to oxidation, was successfully converted to homophenylalanine in DF-100, and a new derivative DF-100, with four amino acid substitutions in DF-3 shows twice the potent inhibitory ability as DF-3. This report provides a new platform of a 14-mer peptide muscle enhancer." @default.
- W1978608959 created "2016-06-24" @default.
- W1978608959 creator A5032076592 @default.
- W1978608959 creator A5063965497 @default.
- W1978608959 creator A5088213224 @default.
- W1978608959 date "1993-02-01" @default.
- W1978608959 modified "2023-09-29" @default.
- W1978608959 title "Follistatins: More than follicle-stimulating hormone suppressing proteins" @default.
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- W1978608959 doi "https://doi.org/10.1016/0303-7207(93)90248-i" @default.
- W1978608959 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8472841" @default.
- W1978608959 hasPublicationYear "1993" @default.
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