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Lactic acid bacteria engage a hybrid metabolism which blends features of fermentation and respiration when they perform extracellular electron transfer.

Structured RNA elements bind to the human methyltransferase like-3 (METTL3)-METTL14 enzyme complex with high affinity and restrict the formation of N⁶-deoxymethyladenosine in DNA.

A single origin–recognition complex (ORC) directs loading of a pair of head-to-head Mcm2-7 replicative DNA helicases by forming a protein tether to the first helicase, releasing from its initial DNA-binding site, and rebinding the origin DNA in the opposite orientation.

Celastrol covalently inhibited the chaperone activity of GRP78 and could disconnect the transduction of ER stress signal to downstream inflammatory response and lipid metabolism.

As a cell prepares to divide, a molecular actor known as the Origin Recognition Complex makes intricate ATP-driven movements to recruit proteins required to duplicate DNA.

Multiple solution-state structures are used for the DNA double-strand break repair functions of the Mre11-Rad50 protein complex.

An in-depth map of ATR signaling during mouse meiosis is revealed using a combination of genetic and pharmacological approaches coupled to quantitative mass spectrometry.

The intrinsically disordered regions (IDRs) of metazoan DNA replication licensing factors phase separate through synergistic electrostatic DNA-IDR and hydrophobic inter-IDR interactions.

A deep mutational scan of the ADAR2 deaminase domain creates a map for designing tailored ADAR2 variants, and splitting the deaminase between residues 468 and 469 enables highly transcript-specific RNA editing.

Biochemical analysis on hetero-mutated c₁₀ subunits ring and molecular dynamics simulations demonstrate the cooperation among c-subunits of F_oF₁-ATP synthase in rotation-coupled proton translocation.