Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: organic chemistry applied to synthetic proteins.
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ABSTRACT:
SUBMITTER: Haj-Yahya N
PROVIDER: S-EPMC3904769 | biostudies-literature | 2013 Oct
REPOSITORIES: biostudies-literature
Publications
Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: organic chemistry applied to synthetic proteins.
Haj-Yahya Najat N Haj-Yahya Mahmood M Castañeda Carlos A CA Spasser Liat L Hemantha Hosahalli P HP Jbara Muhammad M Penner Marlin M Ciechanover Aaron A Fushman David D Brik Ashraf A
Angewandte Chemie (International ed. in English) 20130904 42
In every direction: Chemical protein synthesis allows the construction of 14 di-ubiquitin analogues modified in the vicinity of the isopeptide bond to examine their behavior with deubiquitinases and ubiquitin binding domains. The results set the ground for the generation of unique probes for studying the interactions of these chains with various ubiquitin-interacting proteins. ...[more]
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