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Human colonic organoid monolayers self organize into regularly spaced stem and differentiated cell compartments, which are maintained by waves of ERK activity originating from extruded/dying cells.

The budding yeast gained a novel regulator of TORC1 signaling, called Ait1, 150–200 million years ago, around the same time they lost functional Rheb and Tsc1/2.

The absence of negative selection observed in most cancer genomes can be explained by the intrinsic genome-wide linkage in somatic evolution and creates a substantial proteotoxic load.

Host cell acid ceramidase activity contributes to the regulation of erythrocyte maturation and thereby affects the frequency of target cells for rodent Plasmodium yoelii parasites.

Unique sequence feature requirements for the plasmid centromere pSM19035-parS for ParA_pSM-ATPase activation byribbon-helix-helix-ParB_pSM, a non-CTPase centromere-binding protein, evince complex interaction gymnastics among the three reaction components necessary for plasmid partition, which is distinct from ParABS-systems involving helix-turn-helix-ParB-CTPases.

As a Russian doll, mimivirus dsDNA genome is folded in a nucleocapsid-like structure enclosed in the nucleoid compartment, encased in the icosahedral capsid itself decorated by long glycosylated fibrils surprisingly made of the same protein as the genomic fiber.

Cryo-EM and particle classification techniques reveal how the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima multimerizes to connect distant active sites and reveal different conformational states that enable catalysis.

RNA-level regulation of gene expression is negatively associated with protein-level regulation across cellular pathways in normal tissues and cancer.

A mathematical model of neurotransmitter release predicts that a mutual stabilization of calcium and membrane phospholipids binding to synaptotagmin proteins allows several synaptotagmins to work together for fast synaptic transmission.

Mutagenesis and activity assays in vitro and in vivo identify residues in the tethered agonist of GPR116, as well as those within the extracellular loops, that are critical for mediating the response to the tethered agonist.