1. Shi, X.; Lingerak, R.; Herting, C. J.; Ge, Y.; Kim, S.; Toth, P.; Wang, W.; Brown, B. P.; Meiler, J.; Sossey-Alaoui, K.; et al. Time-resolved live-cell spectroscopy reveals EphA2 multimeric assembly. Science 2023, 382 (6674), 1042-1050. DOI: https://doi.org/10.1126/science.adg5314.

  2. Shi, X.; Lingerak, R.; Shrestha, P.; Buck, M.; Wang, B.-C.; Smith, A. W. The SAM Domain of EphA2 Inhibits Ligand-Independent Clustering and Activation. bioRxiv 2023, 2023.2010.2005.561050. DOI: https://doi.org/10.1101/2023.10.05.561050.

  3. Rybak, J. A.; Sahoo, A. R.; Kim, S.; Pyron, R. J.; Pitts, S. B.; Guleryuz, S.; Smith, A. W.; Buck, M.; Barrera, F. N. Allosteric inhibition of the epidermal growth factor receptor through disruption of transmembrane interactions. J Biol Chem 2023, 104914. DOI: https://doi.org/10.1016/j.jbc.2023.104914.

  4. Mallory, D. P.; Freedman, A.; Kaliszewski, M. J.; Montenegro-Galindo, G. R.; Pugh, C.; Smith, A. W. Direct Quantification of Serum Protein Interactions with PEGylated Micelle Nanocarriers. Biomacromolecules 2023, 24 (6), 2479-2488. DOI: https://doi.org/10.1021/acs.biomac.2c01538.

  5. Brown, B. P.; Zhang, Y. K.; Kim, S.; Finneran, P.; Yan, Y.; Du, Z.; Kim, J.; Hartzler, A. L.; LeNoue-Newton, M. L.; Smith, A. W.; et al. Allele-specific activation, enzyme kinetics, and inhibitor sensitivities of EGFR exon 19 deletion mutations in lung cancer. Proc Natl Acad Sci USA 2022, 119 (30), e2206588119. DOI: https://doi.org/10.1073/pnas.2206588119.

  6. Feng, J.; Khakipoor, B.; May, J.; Mulford, M.; Davis, J.; Siman, K.; Russell, G.; Smith, A. W.; King, H. An open-source dual-beam spectrophotometer for citizen-science-based water quality monitoring. HardwareX 2021, 10, e00241. DOI: https://doi.org/10.1016/j.ohx.2021.e00241.

  7. Du, Z.; Brown, B. P.; Kim, S.; Ferguson, D.; Pavlick, D. C.; Jayakumaran, G.; Benayed, R.; Gallant, J. N.; Zhang, Y. K.; Yan, Y.; et al. Structure-function analysis of oncogenic EGFR Kinase Domain Duplication reveals insights into activation and a potential approach for therapeutic targeting. Nat Commun 2021, 12 (1), 1382. DOI: https://doi.org/10.1038/s41467-021-21613-6.

  8. Christie, S. M.; Hao, J.; Tracy, E.; Buck, M.; Yu, J. S.; Smith, A. W. Interactions between semaphorins and plexin-neuropilin receptor complexes in the membranes of live cells. J Biol Chem 2021, 297 (2), 100965. DOI: https://doi.org/10.1016/j.jbc.2021.100965.

  9. Asher, W. B.; Geggier, P.; Holsey, M. D.; Gilmore, G. T.; Pati, A. K.; Meszaros, J.; Terry, D. S.; Mathiasen, S.; Kaliszewski, M. J.; McCauley, M. D.; et al. Single-molecule FRET imaging of GPCR dimers in living cells. Nat Methods 2021, 18 (4), 397-405. DOI: https://doi.org/10.1038/s41592-021-01081-y.

  10. Ge, Y.; Shi, X.; Boopathy, S.; McDonald, J.; Smith, A. W.; Chao, L. H. Two forms of Opa1 cooperate to complete fusion of the mitochondrial inner-membrane. eLife 2020, 9. DOI: https://doi.org/10.7554/eLife.50973.

  11. Ge, Y.; Boopathy, S.; Smith, A.; Chao, L. H. A model membrane platform for reconstituting mitochondrial membrane dynamics. J Vis Exp 2020,  (163). DOI: https://doi.org/10.3791/61620.

  12. Christie, S. M.; Ham, T. R.; Gilmore, G. T.; Toth, P. D.; Leipzig, N. D.; Smith, A. W. Covalently immobilizing interferon-γ drives filopodia Production through Specific Receptor-Ligand Interactions Independently of Canonical Downstream Signaling. Bioconjug Chem 2020, 31 (5), 1362-1369. DOI: https://doi.org/10.1021/acs.bioconjchem.0c00105.

  13. Christie, S.; Shi, X.; Smith, A. W. Resolving membrane protein-protein interactions in live cells with pulsed interleaved excitation fluorescence cross-correlation spectroscopy. Acc Chem Res 2020, 53 (4), 792-799. DOI: https://doi.org/10.1021/acs.accounts.9b00625.

  14. Li, X.; Smith, A. W. Quantifying Lipid Mobility and Peptide Binding for Gram-Negative and Gram-Positive Model Supported Lipid Bilayers. J Phys Chem B 2019, 123 (49), 10433-10440. DOI: https://doi.org/10.1021/acs.jpcb.9b09709.

  15. Li, X.; Shi, X.; Kaliszewski, M. J.; Smith, A. W. Chapter Three - Fluorescence cross-correlation spectroscopy of lipid-peptide interactions on supported lipid bilayers. Adv Biomem and Lip Self-Assem 2019, 29, 49-68. DOI: https://doi.org/10.1016/bs.abl.2019.01.005.

  16. Bogucki, R.; Greggila, M.; Mallory, P.; Feng, J.; Siman, K.; Khakipoor, B.; King, H.; Smith, A. W. A 3D-Printable Dual Beam Spectrophotometer with Multiplatform Smartphone Adaptor. J Chem Edu 2019, 96 (7), 1527-1531. DOI: https://doi.org/10.1021/acs.jchemed.8b00870.

  17. Agarwal, G.; Smith, A. W.; Jones, B. Discoidin domain receptors: Micro insights into macro assemblies. Biochim Biophys Acta Mol Cell Res 2019, 1866 (11), 118496. DOI: https://doi.org/10.1016/j.bbamcr.2019.06.010.

  18. Mallory, D. P.; Gutierrez, E.; Pinkevitch, M.; Klinginsmith, C.; Comar, W. D.; Roushar, F. J.; Schlebach, J. P.; Smith, A. W.; Jastrzebska, B. The Retinitis Pigmentosa-Linked Mutations in Transmembrane Helix 5 of Rhodopsin Disrupt Cellular Trafficking Regardless of Oligomerization State. Biochemistry 2018, 57 (35), 5188-5201. DOI: https://doi.org/10.1021/acs.biochem.8b00403.

  19. Kaliszewski, M. J.; Shi, X.; Hou, Y.; Lingerak, R.; Kim, S.; Mallory, P.; Smith, A. W. Quantifying membrane protein oligomerization with fluorescence cross- correlation spectroscopy. Methods 2018, 140-141, 40-51. DOI: https://doi.org/10.1016/j.ymeth.2018.02.002.

  20. Alves, D. S.; Westerfield, J. M.; Shi, X.; Nguyen, V. P.; Stefanski, K. M.; Booth, K. R.; Kim, S.; Morrell-Falvey, J.; Wang, B.-C.; Abel, S. M.; et al. A novel pH-dependent membrane peptide that binds to EphA2 and inhibits cell migration. eLife 2018, 7, e36645. DOI: https://doi.org/10.7554/eLife.36645.

  21. Zeng, Z.; Shi, X.; Mabe, T.; Christie, S.; Gilmore, G.; Smith, A. W.; Wei, J. Protein Trapping in Plasmonic Nanoslit and Nanoledge Cavities: The Behavior and Sensing. Anal Chem 2017, 89 (10), 5221-5229. DOI: https://doi.org/10.1021/acs.analchem.6b04493.

  22. Shi, X.; Hapiak, V.; Zheng, J.; Muller-Greven, J.; Bowman, D.; Lingerak, R.; Buck, M.; Wang, B. C.; Smith, A. W. A role of the SAM domain in EphA2 receptor activation. Sci Rep 2017, 7, 45084. DOI: https://doi.org/10.1038/srep45084.

  23. Jastrzebska, B.; Comar, W. D.; Kaliszewski, M. J.; Skinner, K. C.; Torcasio, M. H.; Esway, A. S.; Jin, H.; Palczewski, K.; Smith, A. W. A G Protein-Coupled Receptor Dimerization Interface in Human Cone Opsins. Biochemistry 2017, 56 (1), 61-72. DOI: https://doi.org/10.1021/acs.biochem.6b00877.

  24. Smith, A. W.; Huang, H. H.; Endres, N. F.; Rhodes, C.; Groves, J. T. Dynamic Organization of Myristoylated Src in the Live Cell Plasma Membrane. J Phys Chem B 2016, 120 (5), 867-876. DOI: https://doi.org/10.1021/acs.jpcb.5b08887.

  25. Shi, X.; Kohram, M.; Zhuang, X.; Smith, A. W. Interactions and Translational Dynamics of Phosphatidylinositol Bisphosphate (PIP2) Lipids in Asymmetric Lipid Bilayers. Langmuir 2016, 32 (7), 1732-1741. DOI: https://doi.org/10.1021/acs.langmuir.5b02814.

  26. Liu, C.; Wang, K.; Yi, C.; Shi, X.; Smith, A. W.; Gong, X.; Heeger, A. J. Efficient Perovskite Hybrid Photovoltaics via Alcohol-Vapor Annealing Treatment. Adv Func Mater 2016, 26 (1), 101-110. DOI: https://doi.org/10.1002/adfm.201504041.

  27. Huang, Y.; Bharill, S.; Karandur, D.; Peterson, S. M.; Marita, M.; Shi, X.; Kaliszewski, M. J.; Smith, A. W.; Isacoff, E. Y.; Kuriyan, J. Molecular basis for multimerization in the activation of the epidermal growth factor receptor. eLife 2016, 5, e14107. DOI: https://doi.org/10.7554/eLife.14107.

  28. Grasse, E. K.; Torcasio, M. H.; Smith, A. W. Teaching UV–Vis Spectroscopy with a 3D-Printable Smartphone Spectrophotometer. J Chem Edu 2016, 93 (1), 146-151. DOI: https://doi.org/10.1021/acs.jchemed.5b00654.

  29. Smith, A. W. Detection of rhodopsin dimerization in situ by PIE-FCCS, a time-resolved fluorescence spectroscopy. Methods Mol Biol 2015, 1271, 205-219. DOI: https://doi.org/10.1007/978-1-4939-2330-4_14.

  30. Shi, X.; Li, X.; Kaliszewski, M. J.; Zhuang, X.; Smith, A. W. Tuning the Mobility Coupling of Quaternized Polyvinylpyridine and Anionic Phospholipids in Supported Lipid Bilayers. Langmuir 2015, 31 (5), 1784-1791. DOI: https://doi.org/10.1021/la504241w.

  31. Marita, M.; Wang, Y.; Kaliszewski, Megan J.; Skinner, Kevin C.; Comar, William D.; Shi, X.; Dasari, P.; Zhang, X.; Smith, Adam W. Class A Plexins Are Organized as Preformed Inactive Dimers on the Cell Surface. Biophys J 2015, 109 (9), 1937-1945. DOI: https://doi.org/10.1016/j.bpj.2015.04.043.

  32. Liu, C.; Wang, K.; Yi, C.; Shi, X.; Du, P.; Smith, A. W.; Karim, A.; Gong, X. Ultrasensitive solution-processed perovskite hybrid photodetectors. Journal of Materials Chemistry C 2015, 3 (26), 6600-6606. DOI: https://doi.org/10.1039/C5TC00673B.

  33. Biswas, K. H.; Hartman, K. L.; Yu, C.-h.; Harrison, O. J.; Song, H.; Smith, A. W.; Huang, W. Y. C.; Lin, W.-C.; Guo, Z.; Padmanabhan, A.; et al. E-cadherin junction formation involves an active kinetic nucleation process. Proc Natl Acad Sci USA 2015, 112 (35), 10932-10937. DOI: https://doi.org/10.1073/pnas.1513775112.

  34. Comar, W. D.; Schubert, S. M.; Jastrzebska, B.; Palczewski, K.; Smith, A. W. Time-Resolved Fluorescence Spectroscopy Measures Clustering and Mobility of a G Protein-Coupled Receptor Opsin in Live Cell Membranes. J Am Chem Soc 2014, 136 (23), 8342-8349. DOI: https://doi.org/10.1021/ja501948w.

  35. Smoligovets, Alexander A.; Smith, Adam W.; Groves, Jay T. Ratiometric Imaging of the T-Cell Actin Cytoskeleton Reveals the Nature of Receptor-Induced Cytoskeletal Enrichment. Biophys J 2013, 105 (3), L11-L13. DOI: https://doi.org/10.1016/j.bpj.2013.06.031.

  36. Endres, N. F.; Das, R.; Smith, A. W.; Arkhipov, A.; Kovacs, E.; Huang, Y.; Pelton, J. G.; Shan, Y.; Shaw, D. E.; Wemmer, D. E.; et al. Conformational coupling across the plasma membrane in activation of the EGF receptor. Cell 2013, 152 (3), 543-556. DOI: https://doi.org/10.1016/j.cell.2012.12.032.

  37. Triffo, S. B.; Huang, H. H.; Smith, A. W.; Chou, E. T.; Groves, J. T. Monitoring lipid anchor organization in cell membranes by PIE-FCCS. J Am Chem Soc 2012, 134 (26), 10833-10842. DOI: https://doi.org/10.1021/ja300374c.

  38. Smoligovets, A. A.; Smith, A. W.; Wu, H. J.; Petit, R. S.; Groves, J. T. Characterization of dynamic actin associations with T-cell receptor microclusters in primary T cells. J Cell Sci 2012, 125 (Pt 3), 735-742. DOI: https://doi.org/10.1242/jcs.092825.

  39. Smith, A. W. Lipid-protein interactions in biological membranes: a dynamic perspective. Biochim Biophys Acta 2012, 1818 (2), 172-177. DOI: https://doi.org/10.1016/j.bbamem.2011.06.015.

  40. Belardi, B.; O’Donoghue, G. P.; Smith, A. W.; Groves, J. T.; Bertozzi, C. R. Investigating Cell Surface Galectin-Mediated Cross-Linking on Glycoengineered Cells. J Am Chem Soc 2012, 134 (23), 9549-9552. DOI: https://doi.org/10.1021/ja301694s.

  41. Smith, A. W.; Smoligovets, A. A.; Groves, J. T. Patterned Two-Photon Photoactivation Illuminates Spatial Reorganization in Live Cells. J Phys Chem A 2011, 115 (16), 3867-3875. DOI: https://doi.org/10.1021/jp108295s.

  42. Smith, A. W.; Lessing, J.; Ganim, Z.; Peng, C. S.; Tokmakoff, A.; Roy, S.; Jansen, T. L. C.; Knoester, J. Melting of a β-Hairpin Peptide Using Isotope-Edited 2D IR Spectroscopy and Simulations. J Phys Chem B 2010, 114 (34), 10913-10924. DOI: https://doi.org/10.1021/jp104017h.

  43. Ganim, Z.; Chung, H. S.; Smith, A. W.; DeFlores, L. P.; Jones, K. C.; Tokmakoff, A. Amide I Two-Dimensional Infrared Spectroscopy of Proteins. Acc Chem Res 2008, 41 (3), 432-441. DOI: https://doi.org/10.1021/ar700188n.

  44. Smith, A. W.; Tokmakoff, A. Probing local structural events in β-hairpin unfolding with transient nonlinear infrared spectroscopy. Angew Chem Int Ed Engl 2007, 46 (42), 7984-7987. DOI: https://doi.org/10.1002/anie.200701172.

  45. Smith, A. W.; Tokmakoff, A. Amide I two-dimensional infrared spectroscopy of β-hairpin peptides. J Chem Phys 2007, 126 (4), 045109. DOI: https://doi.org/10.1063/1.2428300.

  46. Smith, A. W.; Chung, H. S.; Ganim, Z.; Tokmakoff, A. Multidimensional IR Spectroscopy of Site-Specific Hairpin Folding. In Ultrafast Phenom XV, Berlin, Heidelberg, 2007; Corkum, P., Jonas, D. M., Miller, R. J. D., Weiner, A. M., Eds.; Springer Berlin Heidelberg: pp 350-352. DOI: https://doi.org/10.1007/978-3-540-68781-8_113.

  47. Chung, H. S.; Khalil, M.; Smith, A. W.; Tokmakoff, A. Transient two-dimensional IR spectrometer for probing nanosecond temperature-jump kinetics. Rev Sci Instrum 2007, 78 (6), 063101. DOI: https://doi.org/10.1063/1.2743168.

  48. Smith, A. W.; Chung, H. S.; Ganim, Z.; Tokmakoff, A. Residual native structure in a thermally denatured β-hairpin. J Phys Chem B 2005, 109 (36), 17025-17027. DOI: https://doi.org/10.1021/jp053949m.

  49. Chung, H. S.; Khalil, M.; Smith, A. W.; Ganim, Z.; Tokmakoff, A. Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin. Proc Natl Acad Sci USA 2005, 102 (3), 612-617. DOI: https://doi.org/10.1073/pnas.0408646102.

  50. Sickafoose, S. M.; Smith, A. W.; Morse, M. D. Optical spectroscopy of tungsten carbide (WC). The Journal of Chemical Physics 2002, 116 (3), 993-1002. DOI: https://doi.org/10.1063/1.1427068.