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A kinase bioscavenger provides antibiotic resistance by extremely tight substrate binding
Author(s) -
Stanislav S. Terekhov,
Yuliana A. Mokrushina,
Anton S. Nazarov,
Alexander Zlobin,
Arthur O. Zalevsky,
Gleb Bourenkov,
Andrey V. Golovin,
Alexey A. Belogurov,
Ilya А. Osterman,
Alexandra A. Kulikova,
Vladimir A. Mitkevich,
Hua Jane Lou,
Benjamin E. Turk,
Matthias Wilmanns,
I. V. Smirnov,
Sidney Altman,
Alexander G. Gabibov
Publication year - 2020
Publication title -
science advances
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 5.928
H-Index - 146
ISSN - 2375-2548
DOI - 10.1126/sciadv.aaz9861
Subject(s) - subfamily , kinase , phosphotransferase , phosphorylation , substrate (aquarium) , antibiotics , biochemistry , biology , kinome , chemistry , microbiology and biotechnology , computational biology , gene , ecology
The substrate-driven closure determines an outstanding efficacy of antibiotic inactivation in a new kinase subfamily.

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