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  Decelerated degradation of short peptides by the 20s proteasome

Dolenc, I., Seemüller, E., & Baumeister, W. (1998). Decelerated degradation of short peptides by the 20s proteasome. FEBS Letters, 434(3), 357-361.

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Dolenc, I., Author
Seemüller, E.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Proteasome; Molecular ruler; Protein degradation; Thermoplasma acidophilum.; Thermoplasma-acidophilum; Complex; Proteins; Generation; Chain.; Biochemistry & biophysics.
 Abstract: Based on a twelve residue master peptide comprising all five specific cleavage sites defined for the proteasome, a set of variant peptides was generated in order to probe specificity and to elucidate the mechanism which determines product size. It is shown that the rate of degradation by the 20S proteasome from Thermoplasma acidophilum depends critically on the length of the peptide substrate. Peptides of 14 residues and longer are degraded much faster than shorter peptides although the sites of cleavage remain unchanged. The decelerated degradation of peptides shorter than 14 residues explains the accumulation of products with an average length of seven to nine residues, (C) 1998 Federation of European Biochemical Societies. [References: 17]

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 Dates: 1998-09-04
 Publication Status: Published in print
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 Identifiers: eDoc: 318402
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 434 (3) Sequence Number: - Start / End Page: 357 - 361 Identifier: -