Modifying the Vicinity of the Isopeptide Bond To Reveal Differential Behavior of Ubiquitin Chains with Interacting Proteins: Organic Chemistry Applied to Synthetic Proteins | Zendy

HajYahya Najat | Zendy; HajYahya Mahmood | Zendy; Castañeda Carlos A. | Zendy; Spasser Liat | Zendy; Hemantha Hosahalli P. | Zendy; Jbara Muhammad | Zendy; Penner Marlin | Zendy; Ciechanover Aaron | Zendy; Fushman David | Zendy; Brik Ashraf | Zendy

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Modifying the Vicinity of the Isopeptide Bond To Reveal Differential Behavior of Ubiquitin Chains with Interacting Proteins: Organic Chemistry Applied to Synthetic Proteins

Author(s) -

HajYahya Najat,

HajYahya Mahmood,

Castañeda Carlos A.,

Spasser Liat,

Hemantha Hosahalli P.,

Jbara Muhammad,

Penner Marlin,

Ciechanover Aaron,

Fushman David,

Brik Ashraf

Publication year - 2013

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201306118

Subject(s) - ubiquitin , chemistry , ubiquitins , ubiquitin ligase , biophysics , biochemistry , biology , gene

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.

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