Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase
Singled out for special treatment: Naturally occurring glutathione S-transferase (GST) was used to catalyze an efficient “click” ligation between polypeptides with an N-terminal glutathione sequence and biomolecules or chemical probes containing perfluorinated aromatic groups (see scheme). The site-...
Κύριοι συγγραφείς: | Zhang, Chi, Spokoyny, Alexander M., Zou, Yekui, Pentelute, Bradley L., Simon, Mark |
---|---|
Άλλοι συγγραφείς: | Massachusetts Institute of Technology. Department of Chemistry |
Μορφή: | Άρθρο |
Γλώσσα: | en_US |
Έκδοση: |
Wiley Blackwell
2015
|
Διαθέσιμο Online: | http://hdl.handle.net/1721.1/95629 https://orcid.org/0000-0001-9519-7456 https://orcid.org/0000-0003-1632-5195 |
Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
-
Convergent diversity-oriented side-chain macrocyclization scan for unprotected polypeptides
ανά: Zou, Yekui, κ.ά.
Έκδοση: (2015) -
A Perfluoroaryl-Cysteine S[subscript N]Ar Chemistry Approach to Unprotected Peptide Stapling
ανά: Spokoyny, Alexander M., κ.ά.
Έκδοση: (2015) -
Glutathione S-transferase variants and hypertension.
ανά: Delles, C, κ.ά.
Έκδοση: (2008) -
Glutathione S-transferase gene deletions in myelodysplasia.
ανά: Atoyebi, W, κ.ά.
Έκδοση: (1997) -
Organometallic palladium reagents for cysteine bioconjugation
ανά: Vinogradova, Ekaterina V., κ.ά.
Έκδοση: (2017)