Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins

Najat Haj-Yahya, Mahmood Haj-Yahya, Carlos A. Castañeda, Liat Spasser, Hosahalli P. Hemantha, Muhammad Jbara, Marlin Penner, Aaron Ciechanover, David Fushman, Ashraf Brik

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)11149-11153
Number of pages5
JournalAngewandte Chemie - International Edition
Volume52
Issue number42
DOIs
StatePublished - 11 Oct 2013
Externally publishedYes

Funding

FundersFunder number
National Institutes of HealthGM065334
National Institute of General Medical SciencesR01GM065334
National Institute of General Medical Sciences

    Keywords

    • deubiquitinases
    • peptide ligation
    • protein synthesis
    • ubiquitin chains
    • ubiquitination

    Fingerprint

    Dive into the research topics of 'Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins'. Together they form a unique fingerprint.

    Cite this