Elevated Titanium Levels After Revision Total Hip Caused by Previously Unreported Mechanism.

Introduction: Metallosis from total hip arthroplasty is usually due to trunnionosis and is associated with elevated serum cobalt and chromium levels. Titanium levels usually remain normal.

Methods: Here, we report two rare cases of elevated titanium levels, both with the same mechanism, which is a previously unreported cause of titanium metallosis.

Vulnerability to climate change of United States marine mammal stocks in the western North Atlantic, Gulf of Mexico, and Caribbean.

Climate change and climate variability are affecting marine mammal species and these impacts are projected to continue in the coming decades. Vulnerability assessments provide a framework for evaluating climate impacts over a broad range of species using currently available information. We conducted a trait-based climate vulnerability assessment using expert elicitation for 108 marine mammal stocks and stock groups in the western North Atlantic, Gulf of Mexico, and Caribbean Sea.

Carbon-Centered Radicals in Protein Manipulation.

Methods to directly post-translationally modify proteins are perhaps the most straightforward and operationally simple ways to create and study protein post-translational modifications (PTMs). However, precisely altering or constructing the C-C scaffolds pervasive throughout biology is difficult with common two-electron chemical approaches. Recently, there has been a surge of new methods that have utilized single electron/radical chemistry applied to site-specifically "edit" proteins that have started to create this potential-one that in principle could be near free-ranging.

Posttranslational, site-directed photochemical fluorine editing of protein sidechains to probe residue oxidation state via F-nuclear magnetic resonance.

The fluorination of amino acid residues represents a near-isosteric alteration with the potential to report on biological pathways, yet the site-directed editing of carbon-hydrogen (C-H) bonds in complex biomolecules to carbon-fluorine (C-F) bonds is challenging, resulting in its limited exploitation. Here, we describe a protocol for the posttranslational and site-directed alteration of native γCH to γCF in protein sidechains. This alteration allows the installation of difluorinated sidechain analogs of proteinogenic amino acids, in both native and modified states.