A combination of advanced optical imaging and cryogenic electron microscopy has been used to explore membrane fusion in a synthetic system and provide new insights into neurotransmitter release.

A protein that can recognize regions of DNA with a high proportion of unmethylated CpG dinucleotides, and then recruit polycomb group proteins to these CpG islands, has been identified.

The enzyme that collaborates with ubiquitin ligases to promote the release of defective polypeptides from stalled ribosomes in a process named ribosome-associated degradations has been identified as the ATPase Cdc48.

Structure-function analysis of the super elongation complex formed when HIV replicates inside cells reveals that the HIV-1 Tat protein binds to a cleft between P-TEFb, an enzyme that is involved in normal transcription, and AFF4, a protein that is used to build the super elongation complex

The details of how the enzyme DNA polymerase α initiates the polymerization of nucleotides in DNA replication, a critical step in the synthesis of new chromosomal DNA, have been revealed in atomic detail.

Experiments on synthetic models of synaptic vesicles have shed new light on the role of the protein α-synuclein in the central nervous system.

Cryo-electron tomography reveals how a chaperone protein called TRiC reduces the ability of pathogenic mutant huntingtin proteins to form aggregates.

By using structural methods to screen compounds for their ability to interact with amyloid beta, researchers have identified small molecules that stabilize amyloid fibers and reduce the toxic effect of smaller aggregates on cells.

A key activator of Ras signaling adopts an autoinhibited, dimeric conformation that is activated by membrane and calcium binding.

Structural studies reveal the mechanism by which a HECT E3 ubiquitin ligase carries out E2-to-E3-to-substrate ubiquitin transfer and prioritizes target lysines for ubiquitination.