Multi-modal structural data fusion questions the specificity of fMRI-behavior associations by providing strong evidence relating human brain structure to a wide range of behavioral measures previously associated to functional connectivity.
Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.
Construction of a first atomic model for an intact bacterial ATP synthase allows for a structural understanding of the roles of individual amino acids in the mechanism of ATP synthesis.
Operonic mRNAs in bacteria are comprised of ORF (open reading frame)-wide units of secondary structure, which are intrinsically distinct between adjacent ORFs and encode a rough blueprint for ORF-specific translation efficiency.
Discovery of the structural basis for recognition and uptake of a human precursor for body odour production reveals an important role for bacterial peptide transport and novel routes to prevent its production in humans.
A structural and functional analysis of the electron transfer complex between a sulfite oxidase and its redox protein partner reveals an elegant compromise between the requirements for fast and efficient electron transfer and reaction specificity.
Distinct binding of viral proteins to the same region on the nucleosome surface can result in contrasting changes to higher-order chromatin structure in the host cell.
Structural analysis of the kinesin-13 MCAK bound to its C-terminal tail reveals the molecular basis for the conformation of kinesin-13 in solution and the mechanism that triggers long-range conformational changes upon microtubule binding.
A domain-general structure learning mechanism, supported by anterior insula, moves beyond explicit category labels and dyadic similarity as the sole inputs to social group representations and predicts ally-choice behavior.
Structure-based virtual screening reveals multiple novel TRPV5 inhibitors that bind and exert their effect from previously unidentified binding sites as characterized by cryo-electron microscopy and electrophysiology.
