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1. Small Molecules with Either Receptor-Selective or Pan-Receptor Activity in the Three LuxR-Type Receptors that Regulate Quorum Sensing in Pseudomonas aeruginosa

   https://doi.org/10.1021/acschembio.2c00675  

   Nyffeler, Kayleigh E. ; Santa, Emma E. ; Blackwell, Helen E. ( November 2022 , ACS Chemical Biology)
2. Mapping Tyrosine Kinase Receptor Dimerization to Receptor Expression and Ligand Affinities

   https://doi.org/10.3390/pr7050288  

   Mamer, Spencer B. ; Palasz, Alexandra A. ; Imoukhuede, P. I. ( May 2019 , Processes)

   Tyrosine kinase receptor (RTK) ligation and dimerization is a key mechanism for translating external cell stimuli into internal signaling events. This process is critical to several key cell and physiological processes, such as in angiogenesis and embryogenesis, among others. While modulating RTK activation is a promising therapeutic target, RTK signaling axes have been shown to involve complicated interactions between ligands and receptors both within and across different protein families. In angiogenesis, for example, several signaling protein families, including vascular endothelial growth factors and platelet-derived growth factors, exhibit significant cross-family interactions that can influence pathway activation. Computational approaches can provide key insight to detangle these signaling pathways but have been limited by the sparse knowledge of these cross-family interactions. Here, we present a framework for studying known and potential non-canonical interactions. We constructed generalized models of RTK ligation and dimerization for systems of two, three and four receptor types and different degrees of cross-family ligation. Across each model, we developed parameter-space maps that fully determine relative pathway activation for any set of ligand-receptor binding constants, ligand concentrations and receptor concentrations. Therefore, our generalized models serve as a powerful reference tool for predicting not only known ligand: Receptor axes but also how unknown interactions could alter signaling dimerization patterns. Accordingly, it will drive the exploration of cross-family interactions and help guide therapeutic developments across processes like cancer and cardiovascular diseases, which depend on RTK-mediated signaling. 

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3. Two unequally redundant "helper" immune receptor families mediate Arabidopsis thaliana intracellular "sensor" immune receptor functions

   https://doi.org/10.1371/journal.pbio.3000783  

   Saile, Svenja C. ; Jacob, Pierre ; Castel, Baptiste ; Jubic, Lance M. ; Salas-Gonzáles, Isai ; Bäcker, Marcel ; Jones, Jonathan D. ; Dangl, Jeffery L. ; El Kasmi, Farid ( September 2020 , PLOS Biology)

   Dong, Xinnian (Ed.)
4. Estrogen Stimulation of Kiss1 Expression in the Medial Amygdala Involves Estrogen Receptor-α But Not Estrogen Receptor-β

   https://doi.org/10.1210/en.2016-1431  

   Stephens, Shannon B. ; Chahal, Navdeep ; Munaganuru, Nagambika ; Parra, Ruby A. ; Kauffman, Alexander S. ( October 2016 , Endocrinology)
5. Intra- and intermolecular atomic-scale interactions in the receptor binding domain of SARS-CoV-2 spike protein: implication for ACE2 receptor binding

   https://doi.org/10.1039/d0cp03145c  

   Adhikari, Puja ; Li, Neng ; Shin, Matthew ; Steinmetz, Nicole F. ; Twarock, Reidun ; Podgornik, Rudolf ; Ching, Wai-Yim ( September 2020 , Physical Chemistry Chemical Physics)

   null (Ed.)

   The COVID-19 pandemic poses a severe threat to human health with unprecedented social and economic disruption. Spike (S) glycoprotein in the SARS-CoV-2 virus is pivotal in understanding the virus anatomy, since it initiates the early contact with the ACE2 receptor in the human cell. The subunit S1 in chain A of S-protein has four structural domains: the receptor binding domain (RBD), the n-terminal domain (NTD) and two subdomains (SD1, SD2). We report details of the intra- and inter-molecular binding mechanism of RBD using density functional theory, including electronic structure, interatomic bonding and partial charge distribution. We identify five strong hydrogen bonds and analyze their roles in binding. This provides a pathway to a quantum-chemical understanding of the interaction between the S-protein and the ACE2 receptor with insights into the function of conserved features in the ACE2 receptor binding domain that could inform vaccine and drug development. 

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