Disulfide bonds are an important class of protein post-translational modifications, yet this
structurally crucial modification type is commonly overlooked in mass spectrometry (MS) …

Disulfide linkage is critical to protein folding and structural stability. The location of disulfide
linkages for antibodies is routinely discovered by comparing the chromatograms of the …

A versatile protocol for the direct thiolation of an inert sp2 C–H bond is presented via a
catalytic amount of copper catalysis, by switching related Brønsted bases and regulating the …

Oxidation–reduction post-translational modifications (redox-PTMs) are chemical alterations
to amino acids of proteins. Redox-PTMs participate in the regulation of protein conformation …

Low‐valent chromium catalysts are cheap and less toxic compared to other transition metal
catalysts. Here in, we reported a ligand‐free chromium (III)‐catalyzed manganese reductive …

A transition‐metal‐free approach to synthesize unsymmetrical disulfides is reported that
relies on a K2CO3‐promoted one‐pot reaction of thiosulfonates, thiourea and alkyl halides …

Polysulfides are significant compounds in life science, pharmaceutical science, and material
science. Therefore, polysulfide construction is in great demand. The controllable sequential …

Self‐assembled virus‐like particles (VLPs) hold great potential as natural nanomaterials for
applications in many fields. For such purposes, monodisperse size distribution is a desirable …

Significance: Reactive oxygen species are produced during normal metabolism in cells, and
their excesses have been implicated in protein damage and toxicity, as well as in the …

Disulfide bonds (SS) are post-translational modifications important for the proper folding and
stabilization of many cellular proteins with therapeutic uses, including antibodies and other …