Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase 1

The 436-amino acid protein enolase 1 from yeast was degraded in vitro by purified wild-type and mutant yeast 20S proteasome particles. Analysis of the cleavage products at different times revealed a processive degradation mechanism and a length distribution of fragments ranging from 3 to 25 amino ac...

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Hlavní autoři: Nussbaum, Alexander K., Dick, Tobias P., Keilholz, Wieland, Schirle, Markus, Stevanović, Stefan, Dietz, Klaus, Heinemeyer, Wolfgang, Groll, Michael, Wolf, Dieter H., Huber, Robert, Rammensee, Hans-Georg, Schild, Hansjörg
Médium: Artigo
Jazyk:Inglês
Vydáno: The National Academy of Sciences 1998
Témata:
Biological Sciences
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC22860/
https://ncbi.nlm.nih.gov/pubmed/9770515
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