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1. Ligand Decomposition during Nanoparticle Synthesis: Influence of Ligand Structure and Precursor Selection

   https://doi.org/10.1021/acs.chemmater.2c03006  

   Sperry, Breena M.; Kukhta, Nadzeya A.; Huang, Yunping; Luscombe, Christine K. (January 2023, Chemistry of Materials)
2. Ion-Mediated Ligand Exchange and Size Focusing of Semiconductor Nanocrystals in Ligand-Saturated Solutions

   https://doi.org/10.1021/acs.jpcc.8b09215  

   Kholmicheva, Natalia; Yang, Mingrui; Moroz, Pavel; Eckard, Holly; Vore, Abigail; Cassidy, James; Pushina, Mariia; Boddy, Anthony; Porotnikov, Dmitry; Anzenbacher, Pavel; et al (June 2018, The Journal of Physical Chemistry C)
3. Quantifying the Interdependence of Metal–Ligand Covalency and Bond Distance Using Ligand K‐edge XAS

   https://doi.org/10.1002/anie.201905635  

   Lee, Kyounghoon; Blake, Anastasia V.; Donahue, Courtney M.; Spielvogel, Kyle D.; Bellott, Brian J.; Daly, Scott R. (August 2019, Angewandte Chemie International Edition)

   Abstract Bond distance is a common structural metric used to assess changes in metal–ligand bonds, but it is not clear how sensitive changes in bond distances are with respect to changes in metal–ligand covalency. Here we report ligand K‐edge XAS studies on Ni and Pd complexes containing different phosphorus(III) ligands. Despite the large number of electronic and structural permutations, P K‐edge pre‐edge peak intensities reveal a remarkable correlation that spectroscopically quantifies the linear interdependence of covalent M−P σ bonding and bond distance. Cl K‐edge studies conducted on many of the same Ni and Pd compounds revealed a poor correlation between M−Cl bond distance and covalency, but a strong correlation was established by analyzing Cl K‐edge data for Ti complexes with a wider range of Ti−Cl bond distances. Together these results establish a quantitative framework to begin making more accurate assessments of metal–ligand covalency using bond distances from readily‐available crystallographic data. 

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4. Quantification of ligand and mutation-induced bias in EGFR phosphorylation in direct response to ligand binding

   https://doi.org/10.1038/s41467-023-42926-8  

   Wirth, Daniel; Özdemir, Ece; Hristova, Kalina (December 2023, Nature Communications)

   Signaling bias is the ability of a receptor to differentially activate downstream signaling pathways in response to different ligands. Bias investigations have been hindered by inconsistent results in different cellular contexts. Here we introduce a methodology to identify and quantify bias in signal transduction across the plasma membrane without contributions from feedback loops and system bias. We apply the methodology to quantify phosphorylation efficiencies and determine absolute bias coefficients. We show that the signaling of epidermal growth factor receptor (EGFR) to EGF and TGFα is biased towards Y1068 and against Y1173 phosphorylation, but has no bias for epiregulin. We further show that the L834R mutation found in non-small-cell lung cancer induces signaling bias as it switches the preferences to Y1173 phosphorylation. The knowledge gained here challenges the current understanding of EGFR signaling in health and disease and opens avenues for the exploration of biased inhibitors as anti-cancer therapies. 

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5. Unconventional Site Selectivity in Palladium-Catalyzed Cross-Couplings of Dichloroheteroarenes under Ligand-Controlled and Ligand-Free Systems

   https://doi.org/10.1021/acs.joc.2c00665  

   Norman, Jacob P.; Larson, Nathaniel G.; Entz, Emily D.; Neufeldt, Sharon R. (June 2022, The Journal of Organic Chemistry)