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Cyclic di-AMP traps proton-coupled K+ transporters of the KUP family in an inward-occluded conformation
PDF) Cyclic di-AMP traps proton-coupled K + transporters of the KUP family in an inward-occluded conformation
Molecular Mechanisms for Bacterial Potassium Homeostasis - ScienceDirect
Structural basis for c-di-AMP–dependent regulation of the bacterial stringent response by receptor protein DarB - ScienceDirect
Membranes, Free Full-Text
c-di-AMP hydrolysis by a novel type of phosphodiesterase promotes differentiation of multicellular bacteria
Cyclic di-AMP: Small molecule with big roles in bacteria - ScienceDirect
Asan Turdiev's research works University of Maryland, College
Fabian COMMICHAU, Professor, Professor
Inhibition of KupA and KupB transport activity by c-di-AMP. E. coli
Structural basis for c-di-AMP–dependent regulation of the bacterial stringent response by receptor protein DarB - ScienceDirect
c-di-AMP assists osmoadaptation by regulating the Listeria monocytogenes potassium transporters KimA and KtrCD - ScienceDirect
Cyclic di-AMP traps proton-coupled K+transporters of the KUP family in an inward-occluded conformation - Abstract - Europe PMC
Fabian COMMICHAU, Professor, Professor