@article{zhang_li_wu_post_lanson_liu_hu_wang_zhang_hong_et al._2022, title={Effects of cobalt doping on the reactivity of hausmannite for As(III) oxidation and As(V) adsorption}, volume={122}, ISSN={["1878-7320"]}, DOI={10.1016/j.jes.2022.02.004}, abstractNote={Hausmannite is a common low valence Mn oxide mineral, with a distorted spinel structure, in surficial sediments. Although natural Mn oxides often contain various impurities of transitional metals (TMs), few studies have addressed the effect and related mechanism of TM doping on the reactivity of hausmannite with metal pollutants. Here, the reactivity of cobalt (Co) doped hausmannite with aqueous As(III) and As(V) was studied. Co doping decreased the point of zero charge of hausmannite and its adsorption capacity for As(V). Despite a reduction of the initial As(III) oxidation rate, Co-doped hausmannite could effectively oxidize As(III) to As(V), followed by the adsorption and fixation of a large amount of As(V) on the mineral surface. Arsenic K-edge EXAFS analysis of the samples after As(V) adsorption and As(III) oxidation revealed that only As(V) was adsorbed on the mineral surface, with an average As-Mn distance of 3.25-3.30 Å, indicating the formation of bidentate binuclear complexes. These results provide new insights into the interaction mechanism between TMs and low valence Mn oxides and their effect on the geochemical behaviors of metal pollutants.}, journal={JOURNAL OF ENVIRONMENTAL SCIENCES}, author={Zhang, Shuang and Li, Hui and Wu, Zhongkuan and Post, Jeffrey E. and Lanson, Bruno and Liu, Yurong and Hu, Biyun and Wang, Mingxia and Zhang, Limei and Hong, Mei and et al.}, year={2022}, month={Dec}, pages={217–226} }
 @article{argo_shi_liu_goshe_2015, title={Performing protein crosslinking using gas-phase cleavable chemical crosslinkers and liquid chromatography-tandem mass spectrometry}, volume={89}, ISSN={["1095-9130"]}, DOI={10.1016/j.ymeth.2015.06.011}, abstractNote={In this article, we describe our methods and protocols using collision-induced dissociative chemical crosslinking-tandem mass spectrometry (CID-CXL-MS/MS) analysis and the practical considerations when implementing these reagents and methodology for protein crosslinking studies. The synthesis of our novel chemical crosslinkers is described as well as their use for effectively labeling protein and protein complexes. Several sample preparation methods for liquid chromatography-tandem mass spectrometry are provided including the enrichment of interpeptide crosslinks. For identification of CID-CXL-MS/MS crosslinks, details regarding MS acquisition parameters and the utilization of various mass spectrometers are addressed along with post-data acquisition analysis to identify interpeptide crosslinks. Once the CID-CXL-MS/MS approach is optimized for a protein target or a set of targets, it can be used as a tool for biological research for studying protein structure when integrated with data obtained using other techniques, such as NMR, X-ray crystallography, and cryo-electron microscopy, or extended to the study of protein-protein interactions in physiological environments.}, journal={METHODS}, author={Argo, Andrew S. and Shi, Chunxiao and Liu, Fan and Goshe, Michael B.}, year={2015}, month={Nov}, pages={64–73} }
 @article{olson_liu_tucker_goshe_cavanagh_2013, title={Chemical crosslinking and LC/MS analysis to determine protein domain orientation: Application to AbrB}, volume={431}, ISSN={["1090-2104"]}, DOI={10.1016/j.bbrc.2012.12.124}, abstractNote={To fully understand the modes of action of multi-protein complexes, it is essential to determine their overall global architecture and the specific relationships between domains and subunits. The transcription factor AbrB is a functional homotetramer consisting of two domains per monomer. Obtaining the high-resolution structure of tetrameric AbrB has been extremely challenging due to the independent character of these domains. To facilitate the structure determination process, we solved the NMR structures of both domains independently and utilized gas-phase cleavable chemical crosslinking and LC/MS(n) analysis to correctly position the domains within the full tetrameric AbrB protein structure.}, number={2}, journal={BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS}, author={Olson, Andrew L. and Liu, Fan and Tucker, Ashley T. and Goshe, Michael B. and Cavanagh, John}, year={2013}, month={Feb}, pages={253–257} }
 @article{liu_wu_sweedler_goshe_2012, title={An enhanced protein crosslink identification strategy using CID-cleavable chemical crosslinkers and LC/MSn analysis}, volume={12}, ISSN={["1615-9861"]}, DOI={10.1002/pmic.201100352}, abstractNote={Abstract}, number={3}, journal={PROTEOMICS}, author={Liu, Fan and Wu, Cong and Sweedler, Jonathan V. and Goshe, Michael B.}, year={2012}, month={Feb}, pages={401–405} }