Project description:Does the RiPP compound bind Cu2+, Cu+, or Fe2+? Assessing to see whether this Novel RiPP compound binds or not since it possesses the properties of methanobactin
Project description:Does the RiPP compound bind Cu2+, Cu+, or Fe2+? Assessing to see whether this Novel RiPP compound binds or not since it possesses the properties of methanobactin
Project description:This study compares flare type self-expandable metal stent with conventional D-type self-expandable metal stent for malignant colorectal obstruction.
Project description:Metal-binding proteins (MBPs) play diverse and critical functions in all living systems and many human diseases are closely related to dysfunctional MBPs. Here we developed a chemoproteomic method named METAL-TPP for global discovery of MBPs in proteomes, which operates by extracting metals from MBPs with chelators and logging the resulting structural perturbation of MBPs with thermal proteome profiling. We applied METAL-TPP to the human proteomes and identified 2856 proteins with significant thermal shifts, including not only many known MBPs but also 75 proteins without previous annotation of metal-binding activity.
Project description:The natural product holomycin contains a unique cyclic disulfide and exhibits broad-spectrum antimicrobial activities. Reduced holomycin chelates metal ions with high affinity and disrupts metal homeostasis in the cell. To identify cellular metalloproteins that are affected by holomycin, reactive-cysteine profiling was performed using isotopic Tandem Orthogonal Proteolysis–Activity-based Protein Profiling. This chemoproteomic analysis showed that holomycin treatment increases the reactivity of metal-coordinating cysteine residues in several zinc-dependent and iron-sulfur cluster-dependent enzymes. Whole-proteome abundance analysis revealed that holomycin treatment induces zinc starvation, iron starvation, and cellular stress. This study sets the stage for investigating the impact of metal-binding molecules on metalloproteomes using chemoproteomics.