The translocon is a membrane‐embedded protein assembly that catalyzes protein
movement across membranes. The core translocon, the SecYEG complex, forms oligomers …

The small heat shock protein 27 (Hsp27) is an oligomeric, molecular chaperone in vitro. This
chaperone activity and other physiological roles attributed to Hsp27 have been reported to …

Human Hsp27 oligomerizes in vivo in a phosphorylation-dependent manner that regulates
the functional activity of the protein. We have studied the self-association of wild-type Hsp27 …

HSP27 is highly expressed in, and supports oncogene addiction of, many cancers. HSP27
phosphorylation is a limiting step for activation of this protein and a target for inhibition, but …

Non–small cell lung cancer (NSCLC) is the most frequent cause of death from cancer
worldwide. Despite the availability of active chemotherapy regimens and EGFR tyrosine …

The small heat shock protein 27 (Hsp27 or HSPB1) is an oligomeric molecular chaperone in
vitro that is associated with several neuromuscular, neurological, and neoplastic diseases …

Campylobacter jejuni is a leading bacterial cause of food-borne illness in the developed
world. Like most pathogens, C. jejuni requires iron that must be acquired from the host …

Binding of divalent metal ions to human hemopexin (Hx) purified by a new protocol has
been characterized by metal ion affinity chromatography and potentiometric titration in the …

The functional properties of the recombinant C-terminal dimerization domain of the
Pseudomonas aeruginosa Fur (ferric uptake regulator) protein expressed in and purified …

Calmodulin (CaM) is composed of two EF-hand domains tethered by a flexible linker. Upon
Ca2+-binding, a fragment of CaM encompassing EF-hands 2 and 3 (CaM2/3; residues 46 …