ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform
mechanical work during targeted protein degradation within cells. ClpXP consists of …

AAA+ proteolytic machines use energy from ATP hydrolysis to degrade damaged, misfolded,
or unneeded proteins. Protein degradation occurs within a barrel-shaped self …

The αβ T-cell receptor (TCR) on each T lymphocyte mediates exquisite specificity for a
particular foreign peptide bound to a major histocompatibility complex molecule (pMHC) …

ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and
translocates specific protein substrates into the degradation chamber of ClpP. We present …

All cells employ ATP-powered proteases for protein-quality control and regulation. In the
ClpXP protease, ClpX is a AAA+ machine that recognizes specific protein substrates …

AAA+ unfoldases denature and translocate polypeptides into associated peptidases. We
report direct observations of mechanical, force-induced protein unfolding by the ClpX …

ClpXP and other AAA+ proteases recognize, mechanically unfold, and translocate target
proteins into a chamber for proteolysis. It is not known whether these remarkable molecular …

Proteomic analyses provide essential information on molecular pathways of cellular systems
and the state of a living organism. Mass spectrometry is currently the first choice for …

Mesoporous silica nanoparticles (MSNs) are thought to be an attractive drug delivery
material because of their advantages including high specific surface area, tunable pore size …

The unbalanced distribution of carbon flux in microbial cell factories can lead to inefficient
production and poor cell growth. Uncoupling cell growth and chemical synthesis can …