The structural and mechanistic characterization of competitive inhibition of human DMT1 offers a promising route for the development of compounds for the treatment of iron overload disorders.
The first structure of a bacteriophage-encoded S-adenosyl methionine degrading enzyme was solved and demonstrated to catalyze a unimolecular lyase reaction occurring at the domain interface of a trimeric structure.
The analysis of the first 1000 revertible protein trap alleles in zebrafish resulted in new functional genomic annotations and produced a panel of potential new models of human disease.
ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.
Encapsulin-associated ferritin proteins form metal-dependent decamers that are active as ferroxidase enzymes, but require encapsulation to form an iron store.
The initiation of human genome replication requires the six-subunit origin recognition complex (ORC) and CDC6, with ORC playing additional roles during mitosis and in organization of the cell nucleus.
Polymerase θ is among the most proficient terminal transferases known and switches between three different mechanisms of terminal transferase activity.
The intermediate state conformation of the human KCNQ1 potassium channel voltage sensor domain was determined, validated, and shown to be conductive under physiological conditions.
