Publications
Vasudevan, S., Senapati, S., Pendergast, M., and Park, P. S.-H. (2024) Aggregation of rhodopsin mutants in mouse models of autosomal dominant retinitis pigmentosa. Nat. Commun. 15, 1451. [PubMed Link]
Vasudevan, S., Samuels, I. S., and Park, P. S.-H. (2023) Gpr75 knockout mice display age-dependent cone photoreceptor cell loss. J. Neurochem. 167, 538-555. [PubMed Link]
Senapati, S. and Park, P. S.-H. (2023) Understanding the rhodopsin worldview through atomic force microscopy (AFM): structure, stability, and activity studies. Chem. Rec. 23, e202300113. [PubMed Link]
Widjaja-Adhi, M. A. K., Kolesnikov, A. V., Vasudevan, S., Park, P. S-H., Kefalov, V. J., and Golczak, M. (2022) Acyl-CoA:wax alcohol acyltransferase 2 modulates the cone visual cycle in mouse retina. FASEB J 36, e22390. [PubMed Link]
Park, P. S.-H. (2021) Supramolecular organization of rhodopsin in rod photoceptor cell membranes. Pflugers Arch. 473, 1361-1376. [PubMed Link]
Wang, X., Pierre, V., Senapati, S., Park, P. S.-H., and Senyo, S. E. (2021) Microenvironment stiffness amplifies post-ischemia heart regeneration in response to exogenous extracellular matrix proteins in neonatal mice. Fron. Cardiovasc. Med. 8, 773978. [PubMed Link]
Adhikari, D. P., Biener, G., Stoneman, M. R., Badu, D. N., Paprocki, J. D., Eis, A., Park, P. S.-H., Popa, I., and Raicu, V. (2021) Comparative photophysical properties of some widely used fluorescent proteins under two-photon excitation conditions. Spectrochim. Acta A Mol. Biomol. Spectrosc. 262, 120133. [PubMed Link]
Wang, X., Pierre, V., Liu, C., Senapati, S., Park, P. S.-H., and Senyo, S. E. (2021) Exogenous extracellular matrix proteins decrease cardiac fibroblast activation in stiffening microenvironment through CAPG. J. Mol. Cell. Cardiol. 159, 105-119. [PubMed Link]
Vasudevan, S. and Park, P. S.-H. (2021) Differential aggregation properties of mutant human and bovine rhodopsin. Biochemistry 60, 6-18. [PubMed Link]
Senapati, S. and Park, P. S.-H. (2020) Differential adaptations in rod outer segment disc membranes in different models of congenital stationary night blindness. Biochim. Biophys. Acta 1862, 183396. [PubMed Link]
Sechrest, E. R., Murphy, J., Senapati, S., Goldberg, A. F. X., Park, P. S.-H., and Kolandaivelu, S. (2020) Loss of PRCD alters number and packaging density of rhodopsin in rod photoreceptor disc membranes. Sci. Rep. 10, 17885. [PubMed Link]
Wang, X., Senapati, S., Akinbote, A., Gnanasambandam, B., Park, P. S.-H., and Senyo, S. E. (2020) Microenvironment stiffness requires decellularized cardiac extracellular matrix to promote heart regeneration in the neonatal mouse heart. Acta Biomater. 113, 380-392. [PubMed Link]
Colozo, A. T., Vasudevan, S., and Park, P. S.-H. (2020) Retinal degeneration in mice expressing the constitutively active G90D rhodopsin mutant. Hum. Mol. Genet. 29, 881-891. [PubMed Link]
Park, P. S.-H. (2019) Rhodopsin oligomerization and aggregation. J. Membr. Biol. 262, 413-423. [PubMed Link]
Senapati, S., Poma, A. B., Cieplak, M., Filipek, S., and Park, P. S.-H. (2019) Differentiating between inactive and active states of rhodopsin by atomic force microscopy in native membranes. Anal. Chem. 91, 7226-7235. [PubMed Link]
Senapati, S. and Park, P. S.-H. (2019) Investigating the nanodomain organization of rhodopsin in native membranes by atomic force microscopy. Methods Mol. Biol. 1886, 61-74. [PubMed Link]
Gragg, M. and Park, P. S.-H. (2019) Detection of misfolded rhodopsin aggregates in cells by Forster resonance energy transfer. Methods Cell Biol. 149, 87-105. [PubMed Link]
Gragg, M. and Park, P. S.-H. (2018) Misfolded rhodopsin mutants display variable aggregation properties. Biochim. Biophys. Acta 1864, 2938-2948. [PubMed Link]
Senapati, S., Gragg, M., Samuels, I. S., Parmar, V. M., Maeda, A., and Park, P. S.-H. (2018) Effect of dietary docosahexaenoic acid on rhodopsin content and packing in photoreceptor cell membranes. Biochim. Biophys. Acta 1860, 1403-1413. [PubMed Link]
Rakshit, T., Senapati, S., Parmar, V. M., Sahu, B., Maeda, A., and Park, P. S.-H. (2017) Adaptations in rod outer segment disc membranes in response to environmental lighting conditions. Biochim. Biophys. Acta 1864, 1691-1702. [PubMed Link]
Mishra, A. K., Gragg, M., Stoneman, M., Biener, G., Oliver, J. A., Miszta, P., Filipek, S., Raicu, V., and Park, P. S.-H. (2016) Quaternary structures of opsin in live cells revealed by FRET spectrometry. Biochem. J. 473, 3819-3836. [PubMed Link]
Gragg, M., Kim, T. G., Howell, S., and Park, P. S.-H. (2016) Wild-type opsin does not aggregate with a misfolded opsin mutant. Biochim. Biophys. Acta 1858, 1850-1859. [PubMed Link]
Han, X., Tang, J., Wang, J., Ren, F., Zheng, J., Gragg, M., Kiser, P., Park, P. S.-H., Palczewski, K., Yao, X., and Zhang, Y. (2016) Conformational change of human checkpoint kinase 1 (Chk1) induced by DNA damage. J. Biol. Chem. 921, 12951-12959. [PubMed Link]
Rakshit, T., Senapati, S., Sinha, S., Whited, A. M., and Park, P. S.-H. (2015) Rhodopsin forms nanodomains in rod outer segment disc membranes of the cold blooded Xenopus laevis. PLoS One 10,e0141114. [PubMed Link]
Miller, L. M., Gragg, M., Kim, T. G., and Park, P. S.-H. (2015) Misfolded opsin mutants display elevated β-sheet structure. FEBS Lett. 589, 3119-3125. [PubMed Link]
Rakshit, T. and Park, P. S.-H. (2015) Impact of reduced rhodopsin expressionon the structure of rod outer segment disc membranes. Biochemistry 54,2885-2894. [PubMed Link]
Park, P. S.-H., and Müller, D. J. (2015) Dynamic single-molecule force spectroscopy of rhodopsin in native membranes. Methods Mol. Biol. 1271, 173-185. [PubMed Link]
Whited, A. M. and Park, P. S.-H. (2015) Nanodomain organization of rhodopsin in native human and murine rod outer segment disc membranes. Biochim. Biophys. Acta 1848, 26-34. [PubMed Link]
Park, P. S.-H. (2014) Constitutively active rhodopsin and retinal disease. Adv. Pharmacol. 70, 1-36. [PubMed Link]
Whited, A. M. and Park, P. S.-H. (2014) Atomic force microscopy: A multifaceted tool to study membrane proteins and their interactions with ligands. Biochim. Biophys. Acta, 1838, 56-68. [PubMed Link]
Kawamura, S., Gerstung, M., Colozo, A. T., Helenius, J., Maeda, A., Beerenwinkel, N., Park, P. S.-H., and Müller, D. J. (2013) Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin. Structure, 21, 426-437. [PubMed Link]
Kawamura, S., Colozo, A. T., Ge, L., Müller, D. J., and Park, P. S.-H. (2012) Structural, energetic, and mechanical perturbations in a rhodopsin mutant that causes congenital stationary night blindness. J. Biol. Chem. 287, 21826-21835. [PubMed Link]
Park, P. S.-H. (2012) Ensemble of G protein-coupled receptor active states. Curr. Med. Chem. 19, 1146-1154. [PubMed Link]
Kawamura, S., Colozo, A. T., Müller, D. J., and Park, P. S.-H. (2010) Conservation of molecular interactions stabilizing bovine and mouse rhodopsin. Biochemistry 49, 10412-10420. [PubMed Link]
Hovan, S. C., Howell, S., and Park, P. S.-H. (2010) Forster resonance energy transfer as a tool to study photoreceptor biology. J. Biomed. Opt. 15, 067001. [PubMed Link]