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1. Covalent Capture of Collagen Triple Helices Using Lysine–Aspartate and Lysine–Glutamate Pairs

   https://doi.org/10.1021/acs.biomac.0c00878  

   Hulgan, Sarah A. ; Jalan, Abhishek A. ; Li, I-Che ; Walker, Douglas R. ; Miller, Mitchell D. ; Kosgei, Abigael J. ; Xu, Weijun ; Phillips, George N. ; Hartgerink, Jeffrey D. ( September 2020 , Biomacromolecules)
2. Structural Determination of Lysine-Linked Cisplatin Complexes via IRMPD Action Spectroscopy: NN _s and NO ^– Binding Modes of Lysine to Platinum Coexist

   https://doi.org/10.1021/acs.jpcb.2c06234  

   He, C. C. ; Hamlow, L. A. ; Roy, H. A. ; Devereaux, Zachary. J. ; Hasan, M. A. ; Israel, E. ; Cunningham, N. A. ; Martens, J. ; Berden, G. ; Oomens, J. ; et al ( November 2022 , The Journal of Physical Chemistry B)
3. Lysine-Dependent Entropy Effects in the B. subtilis Lysine Riboswitch: Insights from Single-Molecule Thermodynamic Studies

   https://doi.org/10.1021/acs.jpcb.1c07833  

   Marton Menendez, Andrea ; Nesbitt, David J. ( January 2022 , The Journal of Physical Chemistry B)
4. Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance

   https://doi.org/10.1038/s41467-021-23474-5  

   Garcia, Laura Ramos ; Tenev, Tencho ; Newman, Richard ; Haich, Rachel O. ; Liccardi, Gianmaria ; John, Sidonie Wicky ; Annibaldi, Alessandro ; Yu, Lu ; Pardo, Mercedes ; Young, Samuel N. ; et al ( December 2021 , Nature Communications)

   Abstract Necroptosis is a lytic, inflammatory form of cell death that not only contributes to pathogen clearance but can also lead to disease pathogenesis. Necroptosis is triggered by RIPK3-mediated phosphorylation of MLKL, which is thought to initiate MLKL oligomerisation, membrane translocation and membrane rupture, although the precise mechanism is incompletely understood. Here, we show that K63-linked ubiquitin chains are attached to MLKL during necroptosis and that ubiquitylation of MLKL at K219 significantly contributes to the cytotoxic potential of phosphorylated MLKL. The K219R MLKL mutation protects animals from necroptosis-induced skin damage and renders cells resistant to pathogen-induced necroptosis. Mechanistically, we show that ubiquitylation of MLKL at K219 is required for higher-order assembly of MLKL at membranes, facilitating its rupture and necroptosis. We demonstrate that K219 ubiquitylation licenses MLKL activity to induce lytic cell death, suggesting that necroptotic clearance of pathogens as well as MLKL-dependent pathologies are influenced by the ubiquitin-signalling system.
5. Lysine Deacetylase Substrate Selectivity: A Dynamic Ionic Interaction Specific to KDAC8

   https://doi.org/10.1021/acs.biochem.1c00384  

   Toro, Tasha B. ; Swanier, Jordan S. ; Bezue, Jada A. ; Broussard, Christian G. ; Watt, Terry J. ( August 2021 , Biochemistry)