The small molecule ML233 is a direct inhibitor of tyrosinase function.

Melanogenesis is the biological process regulating the synthesis of melanin pigments in melanocytes. Defective melanogenesis is associated with numerous human skin diseases, including, but not limited to, albinism, vitiligo, melasma, and hypo- and hyperpigmentation disorders. Tyrosinase is the rate-limiting enzyme controlling melanogenesis, and hence tremendous efforts have been made to identify potent and safe inhibitors of tyrosinase function.

Electrochemically Driven Optical Dynamics of Reflectin Protein Films.

Neuronally triggered phosphorylation drives the dynamic condensation of reflectin proteins, enabling squid to fine tune the colors reflected from specialized skin cells (iridocytes) for camouflage and communication. Reflectin, the primary component of iridocyte lamellae, forms alternating layers of protein and low refractive index extracellular space within membrane-encapsulated structures, acting as a biologically tunable distributed Bragg reflector. In vivo, reflectin condensation induces osmotic dehydration of these lamellae, reducing their thickness and shifting the wavelength of reflected light.

Search for New Resonances Decaying to Pairs of Merged Diphotons in Proton-Proton Collisions at sqrt[s]=13 TeV.

A search is presented for an extended Higgs sector with two new particles, X and ϕ, in the process X→ϕϕ→(γγ)(γγ). Novel neural networks classify events with diphotons that are merged and determine the diphoton masses. The search uses LHC proton-proton collision data at sqrt[s]=13  TeV collected with the CMS detector, corresponding to an integrated luminosity of 138  fb^{-1}.

Charge screening and hydrophobicity drive progressive assembly and liquid-liquid phase separation of reflectin protein.

The intrinsically disordered reflectin proteins drive tunable reflectivity for dynamic camouflage and communication in the recently evolved Loliginidae family of squid. Previous work revealed that reflectin A1 forms discrete assemblies whose size is precisely predicted by protein net charge density and charge screening by the local anion concentration. Using dynamic light scattering, FRET, and confocal microscopy, we show that these assemblies, of which 95 to 99% of bulk protein in solution is partitioned into, are dynamic intermediates to liquid protein-dense condensates formed by liquid-liquid phase separation (LLPS).