{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,20]],"date-time":"2026-03-20T10:27:28Z","timestamp":1774002448614,"version":"3.50.1"},"reference-count":53,"publisher":"Biophysical Society of Japan","issue":"0","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["BIOPHYSICS"],"published-print":{"date-parts":[[2022]]},"DOI":"10.2142\/biophysico.bppb-v19.0045","type":"journal-article","created":{"date-parts":[[2022,11,18]],"date-time":"2022-11-18T22:13:14Z","timestamp":1668809594000},"page":"n\/a","source":"Crossref","is-referenced-by-count":2,"title":["Development of the force field for cyclosporine A"],"prefix":"10.2142","volume":"19","author":[{"given":"Tsutomu","family":"Yamane","sequence":"first","affiliation":[{"name":"Graduate School of Medical Life Science, Yokohama City University"},{"name":"HPC- and AI-driven Drug Development Platform Division, Center for Computational Science, RIKEN"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Toru","family":"Ekimoto","sequence":"additional","affiliation":[{"name":"Graduate School of Medical Life Science, Yokohama City University"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3199-6931","authenticated-orcid":false,"given":"Mitsunori","family":"Ikeguchi","sequence":"additional","affiliation":[{"name":"Graduate School of Medical Life Science, Yokohama City University"},{"name":"HPC- and AI-driven Drug Development Platform Division, Center for Computational Science, RIKEN"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"909","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"[1] Tamamura, H., Kobayakawa, T., Ohashi, N. Mid-size drugs based on peptides and peptidomimetics: A new drug category. SpringerBriefs in Pharmaceutical Science &amp; Drug Development (Springer, Singapore, 2018). https:\/\/doi.org\/10.1007\/978-981-10-7691-6","DOI":"10.1007\/978-981-10-7691-6"},{"key":"2","doi-asserted-by":"crossref","unstructured":"[2] Ruegger, A., Kuhn, M., Lichti, H., Loosli, H. R., Huguenin, R., Quiquerez, C., et al. Cyclosporin A, a peptide metabolite from Trichoderma polysporum (Link ex Pers.) Rifai, with a remarkable immunosuppressive activity. Helv. Chim. Acta 59, 1075\u20131092 (1976). https:\/\/doi.org\/10.1002\/hlca.19760590412","DOI":"10.1002\/hlca.19760590412"},{"key":"3","doi-asserted-by":"crossref","unstructured":"[3] Wenger, R. M. Synthesis of cyclosporine and analogs - structural requirements for immunosuppressive activity. Angew. Chem. Int. Ed. Engl. 24, 77\u201385 (1985). https:\/\/doi.org\/10.1002\/anie.198500773","DOI":"10.1002\/anie.198500773"},{"key":"4","doi-asserted-by":"crossref","unstructured":"[4] Hiestand, P. C., Gubler, H. U. Cyclosporins: Immunopharmacologic properties of natural cyclosporins. in The Pharmacology of Lymphocytes. (Bray, M. A., Morley, J. eds.), pp. 487\u2013502 (Springer Berlin Heidelberg, Berlin, Heidelberg, 1988).","DOI":"10.1007\/978-3-642-73217-1_22"},{"key":"5","doi-asserted-by":"crossref","unstructured":"[5] Liu, J., Farmer, J. D., Jr., Lane, W. S., Friedman, J., Weissman, I., Schreiber, S. L. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66, 807\u2013815 (1991). https:\/\/doi.org\/10.1016\/0092-8674(91)90124-h","DOI":"10.1016\/0092-8674(91)90124-H"},{"key":"6","doi-asserted-by":"crossref","unstructured":"[6] Liu, J., Albers, M. W., Wandless, T. J., Luan, S., Alberg, D. G., Belshaw, P. J., et al. Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activity. Biochemistry 31, 3896\u20133901 (1992). https:\/\/doi.org\/10.1021\/bi00131a002","DOI":"10.1021\/bi00131a002"},{"key":"7","doi-asserted-by":"crossref","unstructured":"[7] Mikol, V., Kallen, J., Pflugl, G., Walkinshaw, M. D. X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. J. Mol. Biol. 234, 1119\u20131130 (1993). https:\/\/doi.org\/10.1006\/jmbi.1993.1664","DOI":"10.1006\/jmbi.1993.1664"},{"key":"8","doi-asserted-by":"crossref","unstructured":"[8] Fesik, S. W., Gampe, R. T., Jr., Holzman, T. F., Egan, D. A., Edalji, R., Luly, J. R., et al. Isotope-edited NMR of cyclosporin A bound to cyclophilin: Evidence for a trans 9, 10 amide bond. Science 250, 1406\u20131409 (1990). https:\/\/doi.org\/10.1126\/science.2255910","DOI":"10.1126\/science.2255910"},{"key":"9","doi-asserted-by":"crossref","unstructured":"[9] Weber, C., Wider, G., von Freyberg, B., Traber, R., Braun, W., Widmer, H., et al. The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution. Biochemistry 30, 6563\u20136574 (1991). https:\/\/doi.org\/10.1021\/bi00240a029","DOI":"10.1021\/bi00240a029"},{"key":"10","doi-asserted-by":"crossref","unstructured":"[10] Fesik, S. W., Neri, P., Meadows, R., Olejniczak, E. T., Gemmecker, G. A model of the cyclophilin\/cyclosporin A (CSA) complex from NMR and X-ray data suggests that CSA binds as a transition-state analog. J. Am. Chem. Soc. 114, 3165\u20133166 (1992). https:\/\/doi.org\/10.1021\/ja00034a087","DOI":"10.1021\/ja00034a087"},{"key":"11","doi-asserted-by":"crossref","unstructured":"[11] Kofron, J. L., Kuzmic, P., Kishore, V., Gemmecker, G., Fesik, S. W., Rich, D. H. Lithium chloride perturbation of cis-trans peptide bond equilibria: Effect on conformational equilibria in cyclosporin A and on time-dependent inhibition of cyclophilin. J. Am. Chem. Soc. 114, 2670\u20132675 (1992). https:\/\/doi.org\/10.1021\/ja00033a047","DOI":"10.1021\/ja00033a047"},{"key":"12","doi-asserted-by":"crossref","unstructured":"[12] Loosli, H.-R., Kessler, H., Oschkinat, H., Weber, H.-P., Petcher, T. J., Widmer, A. Peptide conformations. Part 31. The conformation of cyclosporin a in the crystal and in solution. Helv. Chim. Acta 68, 682\u2013704 (1985). https:\/\/doi.org\/10.1002\/hlca.19850680319","DOI":"10.1002\/hlca.19850680319"},{"key":"13","doi-asserted-by":"crossref","unstructured":"[13] Witek, J., Keller, B. G., Blatter, M., Meissner, A., Wagner, T., Riniker, S. Kinetic models of cyclosporin A in polar and apolar environments reveal multiple congruent conformational States. J. Chem. Inf. Model. 56, 1547\u20131562 (2016). https:\/\/doi.org\/10.1021\/acs.jcim.6b00251","DOI":"10.1021\/acs.jcim.6b00251"},{"key":"14","doi-asserted-by":"crossref","unstructured":"[14] Wang, C. K., Swedberg, J. E., Harvey, P. J., Kaas, Q., Craik, D. J. Conformational flexibility is a determinant of permeability for cyclosporin. J. Phys. Chem. B 122, 2261\u20132276 (2018). https:\/\/doi.org\/10.1021\/acs.jpcb.7b12419","DOI":"10.1021\/acs.jpcb.7b12419"},{"key":"15","unstructured":"[15] Schrodinger, LLC The PyMOL Molecular Graphics System, Version 1.8. (2015)."},{"key":"16","doi-asserted-by":"crossref","unstructured":"[16] Rezai, T., Bock, J. E., Zhou, M. V., Kalyanaraman, C., Lokey, R. S., Jacobson, M. P. Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: Successful in silico prediction of the relative permeabilities of cyclic peptides. J. Am. Chem. Soc. 128, 14073\u201314080 (2006). https:\/\/doi.org\/10.1021\/ja063076p","DOI":"10.1021\/ja063076p"},{"key":"17","doi-asserted-by":"crossref","unstructured":"[17] Rezai, T., Yu, B., Millhauser, G. L., Jacobson, M. P., Lokey, R. S. Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers. J. Am. Chem. Soc. 128, 2510\u20132511 (2006). https:\/\/doi.org\/10.1021\/ja0563455","DOI":"10.1021\/ja0563455"},{"key":"18","doi-asserted-by":"crossref","unstructured":"[18] Biron, E., Chatterjee, J., Ovadia, O., Langenegger, D., Brueggen, J., Hoyer, D., et al. Improving oral bioavailability of peptides by multiple N-methylation: Somatostatin analogues. Angew. Chem. Int. Ed. Engl. 47, 2595\u20132599 (2008). https:\/\/doi.org\/10.1002\/anie.200705797","DOI":"10.1002\/anie.200705797"},{"key":"19","doi-asserted-by":"crossref","unstructured":"[19] White, T. R., Renzelman, C. M., Rand, A. C., Rezai, T., McEwen, C. M., Gelev, V. M., et al. On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds. Nat. Chem. Biol. 7, 810\u2013817 (2011). https:\/\/doi.org\/10.1038\/nchembio.664","DOI":"10.1038\/nchembio.664"},{"key":"20","doi-asserted-by":"crossref","unstructured":"[20] Ahlbach, C. L., Lexa, K. W., Bockus, A. T., Chen, V., Crews, P., Jacobson, M. P., et al. Beyond cyclosporine A: conformation-dependent passive membrane permeabilities of cyclic peptide natural products. Future Med. Chem. 7, 2121\u20132130 (2015). https:\/\/doi.org\/10.4155\/fmc.15.78","DOI":"10.4155\/fmc.15.78"},{"key":"21","doi-asserted-by":"crossref","unstructured":"[21] Md. Abdur Rauf, S., Arvidsson, P. I., Albericio, F., Govender, T., Maguire, G. E. M., Kruger, H. G., et al. The effect of N-methylation of amino acids (Ac-X-OMe) on solubility and conformation: A DFT study. Org. Biomol. Chem. 13, 9993\u201310006 (2015). https:\/\/doi.org\/10.1039\/C5OB01565K","DOI":"10.1039\/C5OB01565K"},{"key":"22","doi-asserted-by":"crossref","unstructured":"[22] Shinoda, W. Permeability across lipid membranes. Biochim. Biophys. Acta 1858, 2254\u20132265 (2016). https:\/\/doi.org\/10.1016\/j.bbamem.2016.03.032","DOI":"10.1016\/j.bbamem.2016.03.032"},{"key":"23","doi-asserted-by":"crossref","unstructured":"[23] Dickson, C. J., Hornak, V., Bednarczyk, D., Duca, J. S. Using membrane partitioning simulations to predict permeability of forty-nine drug-like molecules. J. Chem. Inf. Model. 59, 236\u2013244 (2019). https:\/\/doi.org\/10.1021\/acs.jcim.8b00744","DOI":"10.1021\/acs.jcim.8b00744"},{"key":"24","doi-asserted-by":"crossref","unstructured":"[24] Witek, J., Muhlbauer, M., Keller, B. G., Blatter, M., Meissner, A., Wagner, T., et al. Interconversion rates between conformational states as rationale for the membrane permeability of Cyclosporines. Chemphyschem 18, 3309\u20133314 (2017). https:\/\/doi.org\/10.1002\/cphc.201700995","DOI":"10.1002\/cphc.201700995"},{"key":"25","doi-asserted-by":"crossref","unstructured":"[25] Witek, J., Wang, S., Schroeder, B., Lingwood, R., Dounas, A., Roth, H. J., et al. Rationalization of the membrane permeability differences in a series of analogue cyclic decapeptides. J. Chem. Inf. Model. 59, 294\u2013308 (2019). https:\/\/doi.org\/10.1021\/acs.jcim.8b00485","DOI":"10.1021\/acs.jcim.8b00485"},{"key":"26","doi-asserted-by":"crossref","unstructured":"[26] Ono, S., Naylor, M. R., Townsend, C. E., Okumura, C., Okada, O., Lee, H. W., et al. Cyclosporin A: Conformational complexity and chameleonicity. J. Chem. Inf. Model. 61, 5601\u20135613 (2021). https:\/\/doi.org\/10.1021\/acs.jcim.1c00771","DOI":"10.1021\/acs.jcim.1c00771"},{"key":"27","doi-asserted-by":"crossref","unstructured":"[27] Sugita, M., Sugiyama, S., Fujie, T., Yoshikawa, Y., Yanagisawa, K., Ohue, M., et al. Large-scale membrane permeability prediction of cyclic peptides crossing a lipid bilayer based on enhanced sampling molecular dynamics simulations. J. Chem. Inf. Model. 61, 3681\u20133695 (2021). https:\/\/doi.org\/10.1021\/acs.jcim.1c00380","DOI":"10.1021\/acs.jcim.1c00380"},{"key":"28","doi-asserted-by":"crossref","unstructured":"[28] Mackerell, A. D., Jr., Feig, M., Brooks, C. L., 3rd. Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25, 1400\u20131415 (2004). https:\/\/doi.org\/10.1002\/jcc.20065","DOI":"10.1002\/jcc.20065"},{"key":"29","doi-asserted-by":"crossref","unstructured":"[29] Mirijanian, D. T., Mannige, R. V., Zuckermann, R. N., Whitelam, S. Development and use of an atomistic CHARMM-based forcefield for peptoid simulation. J. Comput. Chem. 35, 360\u2013370 (2014). https:\/\/doi.org\/10.1002\/jcc.23478","DOI":"10.1002\/jcc.23478"},{"key":"30","doi-asserted-by":"crossref","unstructured":"[30] Weiser, L. J., Santiso, E. E. A CGenFF-based force field for simulations of peptoids with both cis and trans peptide bonds. J. Comput. Chem. 40, 1946\u20131956 (2019). https:\/\/doi.org\/10.1002\/jcc.25850","DOI":"10.1002\/jcc.25850"},{"key":"31","doi-asserted-by":"crossref","unstructured":"[31] Kamiya, M., Sugita, Y. Flexible selection of the solute region in replica exchange with solute tempering: Application to protein-folding simulations. J. Chem. Phys. 149, 072304 (2018). https:\/\/doi.org\/10.1063\/1.5016222","DOI":"10.1063\/1.5016222"},{"key":"32","doi-asserted-by":"crossref","unstructured":"[32] Best, R. B., Zhu, X., Shim, J., Lopes, P. E., Mittal, J., Feig, M., et al. Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone phi, psi and side-chain chi(1) and chi(2) dihedral angles. J. Chem. Theory Comput. 8, 3257\u20133273 (2012). https:\/\/doi.org\/10.1021\/ct300400x","DOI":"10.1021\/ct300400x"},{"key":"33","doi-asserted-by":"crossref","unstructured":"[33] Vanommeslaeghe, K., Hatcher, E., Acharya, C., Kundu, S., Zhong, S., Shim, J., et al. CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields. J. Comput. Chem. 31, 671\u2013690 (2010). https:\/\/doi.org\/10.1002\/jcc.21367","DOI":"10.1002\/jcc.21367"},{"key":"34","doi-asserted-by":"crossref","unstructured":"[34] Vanommeslaeghe, K., MacKerell, A. D., Jr. Automation of the CHARMM General Force Field (CGenFF) I: Bond perception and atom typing. J. Chem. Inf. Model. 52, 3144\u20133154 (2012). https:\/\/doi.org\/10.1021\/ci300363c","DOI":"10.1021\/ci300363c"},{"key":"35","doi-asserted-by":"crossref","unstructured":"[35] Vanommeslaeghe, K., Raman, E. P., MacKerell, A. D., Jr. Automation of the CHARMM General Force Field (CGenFF) II: Assignment of bonded parameters and partial atomic charges. J. Chem. Inf. Model. 52, 3155\u20133168 (2012). https:\/\/doi.org\/10.1021\/ci3003649","DOI":"10.1021\/ci3003649"},{"key":"36","doi-asserted-by":"crossref","unstructured":"[36] Yu, W., He, X., Vanommeslaeghe, K., MacKerell, A. D., Jr. Extension of the CHARMM General Force Field to sulfonyl-containing compounds and its utility in biomolecular simulations. J. Comput. Chem. 33, 2451\u20132468 (2012). https:\/\/doi.org\/10.1002\/jcc.23067","DOI":"10.1002\/jcc.23067"},{"key":"37","doi-asserted-by":"crossref","unstructured":"[37] Soteras Gutierrez, I., Lin, F. Y., Vanommeslaeghe, K., Lemkul, J. A., Armacost, K. A., Brooks, C. L., 3rd, et al. Parametrization of halogen bonds in the CHARMM general force field: Improved treatment of ligand-protein interactions. Bioorg. Med. Chem. 24, 4812\u20134825 (2016). https:\/\/doi.org\/10.1016\/j.bmc.2016.06.034","DOI":"10.1016\/j.bmc.2016.06.034"},{"key":"38","unstructured":"[38] Frisch, M. J., Trucks, G. W., Schlegel, H. B., Scuseria, G. E., Robb, M. A., Cheeseman, J. R., et al. Gaussian 09, Revision A.02 (Gaussian, Inc., Wallingford CT, 2016)."},{"key":"39","doi-asserted-by":"crossref","unstructured":"[39] Shao, Y., Gan, Z., Epifanovsky, E., Gilbert, A. T. B., Wormit, M., Kussmann, J., et al. Advances in molecular quantum chemistry contained in the Q-Chem 4 program package. Mol. Phys. 113, 184\u2013215 (2015). https:\/\/doi.org\/10.1080\/00268976.2014.952696","DOI":"10.1080\/00268976.2014.952696"},{"key":"40","doi-asserted-by":"crossref","unstructured":"[40] Halkier, A., Helgaker, T., J\u00f8rgensen, P., Klopper, W., Koch, H., Olsen, J., et al. Basis-set convergence in correlated calculations on Ne, N2, and H2O. Chem. Phys. Lett. 286, 243\u2013252 (1998). https:\/\/doi.org\/10.1016\/S0009-2614(98)00111-0","DOI":"10.1016\/S0009-2614(98)00111-0"},{"key":"41","doi-asserted-by":"crossref","unstructured":"[41] Liu, P., Kim, B., Friesner, R. A., Berne, B. J. Replica exchange with solute tempering: a method for sampling biological systems in explicit water. Proc. Natl. Acad. Sci. U.S.A. 102, 13749\u201313754 (2005). https:\/\/doi.org\/10.1073\/pnas.0506346102","DOI":"10.1073\/pnas.0506346102"},{"key":"42","doi-asserted-by":"crossref","unstructured":"[42] Wang, L., Friesner, R. A., Berne, B. J. Replica exchange with solute scaling: a more efficient version of replica exchange with solute tempering (REST2). J. Phys. Chem. B 115, 9431\u20139438 (2011). https:\/\/doi.org\/10.1021\/jp204407d","DOI":"10.1021\/jp204407d"},{"key":"43","doi-asserted-by":"crossref","unstructured":"[43] Kobayashi, C., Jung, J., Matsunaga, Y., Mori, T., Ando, T., Tamura, K., et al. GENESIS 1.1: A hybrid-parallel molecular dynamics simulator with enhanced sampling algorithms on multiple computational platforms. J. Comput. Chem. 38, 2193\u20132206 (2017). https:\/\/doi.org\/10.1002\/jcc.24874","DOI":"10.1002\/jcc.24874"},{"key":"44","doi-asserted-by":"crossref","unstructured":"[44] Jung, J., Mori, T., Kobayashi, C., Matsunaga, Y., Yoda, T., Feig, M., et al. GENESIS: A hybrid-parallel and multi-scale molecular dynamics simulator with enhanced sampling algorithms for biomolecular and cellular simulations. Wiley Interdiscip. Rev. Comput. Mol. Sci. 5, 310\u2013323 (2015). https:\/\/doi.org\/10.1002\/wcms.1220","DOI":"10.1002\/wcms.1220"},{"key":"45","doi-asserted-by":"crossref","unstructured":"[45] Jo, S., Kim, T., Iyer, V. G., Im, W. CHARMM-GUI: A web-based graphical user interface for CHARMM. J. Comput. Chem. 29, 1859\u20131865 (2008). https:\/\/doi.org\/10.1002\/jcc.20945","DOI":"10.1002\/jcc.20945"},{"key":"46","doi-asserted-by":"crossref","unstructured":"[46] Lee, J., Cheng, X., Swails, J. M., Yeom, M. S., Eastman, P. K., Lemkul, J. A., et al. CHARMM-GUI input generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM\/OpenMM simulations using the CHARMM36 additive force field. J. Chem. Theory Comput. 12, 405\u2013413 (2016). https:\/\/doi.org\/10.1021\/acs.jctc.5b00935","DOI":"10.1021\/acs.jctc.5b00935"},{"key":"47","doi-asserted-by":"crossref","unstructured":"[47] Huang, J., Rauscher, S., Nawrocki, G., Ran, T., Feig, M., de Groot, B. L., et al. CHARMM36m: An improved force field for folded and intrinsically disordered proteins. Nat. Methods 14, 71\u201373 (2017). https:\/\/doi.org\/10.1038\/nmeth.4067","DOI":"10.1038\/nmeth.4067"},{"key":"48","doi-asserted-by":"crossref","unstructured":"[48] Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W., Klein, M. L. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79, 926\u2013935 (1983). https:\/\/doi.org\/10.1063\/1.445869","DOI":"10.1063\/1.445869"},{"key":"49","doi-asserted-by":"crossref","unstructured":"[49] Dietz, W., Heinzinger, K. A Molecular Dynamics study of liquid chloroform. Berichte der Bunsengesellschaft f\u00fcr physikalische Chemie 89, 968\u2013977 (1985). https:\/\/doi.org\/10.1002\/bbpc.19850890909","DOI":"10.1002\/bbpc.19850890909"},{"key":"50","doi-asserted-by":"crossref","unstructured":"[50] Mayne, C. G., Saam, J., Schulten, K., Tajkhorshid, E., Gumbart, J. C. Rapid parameterization of small molecules using the Force Field Toolkit. J. Comput. Chem. 34, 2757\u20132770 (2013). https:\/\/doi.org\/10.1002\/jcc.23422","DOI":"10.1002\/jcc.23422"},{"key":"51","doi-asserted-by":"crossref","unstructured":"[51] Abraham, M. J., Murtola, T., Schulz, R., P\u00e1ll, S., Smith, J. C., Hess, B., et al. GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX 1\u20132, 19\u201325 (2015). https:\/\/doi.org\/10.1016\/j.softx.2015.06.001","DOI":"10.1016\/j.softx.2015.06.001"},{"key":"52","doi-asserted-by":"crossref","unstructured":"[52] Brooks, C., Case, D. A. Simulations of peptide conformational dynamics and thermodynamics. Chem. Rev. 93, 2487\u20132502 (1993). https:\/\/doi.org\/10.1021\/cr00023a008","DOI":"10.1021\/cr00023a008"},{"key":"53","doi-asserted-by":"crossref","unstructured":"[53] Ko, S. Y., Dalvit, C. Conformation of cyclosporin A in polar solvents. Int. J. Pept. Protein Res. 40, 380\u2013382 (1992). https:\/\/doi.org\/10.1111\/j.1399-3011.1992.tb00314.x","DOI":"10.1111\/j.1399-3011.1992.tb00314.x"}],"container-title":["Biophysics and Physicobiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/biophysico\/19\/0\/19_e190045\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,5,10]],"date-time":"2024-05-10T04:21:30Z","timestamp":1715314890000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/biophysico\/19\/0\/19_e190045\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022]]},"references-count":53,"journal-issue":{"issue":"0","published-print":{"date-parts":[[2022]]}},"URL":"https:\/\/doi.org\/10.2142\/biophysico.bppb-v19.0045","relation":{},"ISSN":["2189-4779"],"issn-type":[{"value":"2189-4779","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022]]},"article-number":"e190045"}}