Khaled A. Selim

This study investigates how metabolic signals regulate glutamine synthetase AMPylation in Herbaspirillum seropedicae and reveals the structural mechanism of enzyme inhibition by AMPylation.

The paper shows PII interacts with NAGK in two steps, with the B-loop initiating contact and the T-loop completing the complex formation.

This study identifies CdgR as a c-di-GMP receptor in Synechocystis that regulates type IV pilus-dependent functions through interactions with transcription factors SyCRP1 and SyCRP2.

This study identifies the sucrose metabolism pathways in Ustilago maydis, revealing alternative strategies for carbon acquisition during different growth stages.

This study investigates the metabolic and physiological effects of L-lysine on Synechocystis sp. PCC 6803, identifying key genes involved in Lys resistance and metabolic disruption.

The paper identifies pteridines, including lumazine dehydroxyxanthopterin B2, as natural ligands of CutA that modulate copper binding and redox homeostasis in E. coli and Synechococcus elongatus.

The paper identifies ComFB as a new family of c-di-NMP receptors in bacteria, showing they bind c-di-GMP and c-di-AMP and regulate cellular processes like motility.

The paper shows ComFB binds c-di-GMP to inhibit motility in B. subtilis by affecting flagellar activity, independent of MotI.

This study identifies CSE as a Ca2+-binding protein that links intracellular Ca2+-signaling to cell-cell communication in multicellular cyanobacteria by regulating nanopore and septal junction formation.

This paper shows cyanobacteria can use guanidine as a nitrogen source, regulated by NtcA and a riboswitch, enabling precise gene control for synthetic biology.

This study identifies SbtB as a redox-regulated apyrase that modulates bicarbonate transporter SbtA activity in cyanobacteria by integrating metabolic and carbon status signals.

This study uses native metabolomics to identify a family of protease inhibitors from cyanobacteria, revealing their structure and potent biological activity.