Harries, L. W. RNA biology provides new therapeutic targets for human disease. Front. Genet. 10, 205 (2019).<\/p>\n
CAS<\/a>\u00a0 Zhu, Y., Zhu, L., Wang, X. & Jin, H. RNA-based therapeutics: an overview and prospectus. Cell Death Dis. 13, 644 (2022).<\/p>\n CAS<\/a>\u00a0 Yu, A.-M., Choi, Y. H. & Tu, M.-J. RNA drugs and RNA targets for small molecules: principles, progress, and challenges. Pharmacol. Rev. 72, 862\u2013898 (2020).<\/p>\n CAS<\/a>\u00a0 Lightfoot, H. L. & Smith, G. F. Targeting RNA with small molecules-a safety perspective. Br. J. Pharmacol. 182, 4201\u20134220 (2023).<\/p>\n Bennett, C. F. Therapeutic antisense oligonucleotides are coming of age. Annu. Rev. Med. 70, 307\u2013321 (2019).<\/p>\n CAS<\/a>\u00a0 Luther, D., Lee, Y., Nagaraj, H., Scaletti, F. & Rotello, V. Delivery approaches for crispr\/cas9 therapeutics in vivo: advances and challenges. Expert Opin. Drug Deliv. 15, 905\u2013913 (2018).<\/p>\n CAS<\/a>\u00a0 Wu, P. Inhibition of RNA-binding proteins with small molecules. Nat. Rev. Chem. 4, 441\u2013458 (2020).<\/p>\n CAS<\/a>\u00a0 Childs-Disney, J. L. et al. Targeting RNA structures with small molecules. Nat. Rev. Drug Discov. 21, 736\u2013762 (2022).<\/p>\n CAS<\/a>\u00a0 Howe, J. A. et al. Selective small-molecule inhibition of an RNA structural element. Nature 526, 672\u2013677 (2015).<\/p>\n CAS<\/a>\u00a0 Dibrov, S. M. et al. Hepatitis C virus translation inhibitors targeting the internal ribosomal entry site: miniperspective. J. Med. Chem. 57, 1694\u20131707 (2014).<\/p>\n CAS<\/a>\u00a0 Palacino, J. et al. Smn2 splice modulators enhance u1\u2013pre-mRNA association and rescue sma mice. Nat. Chem. Biol. 11, 511\u2013517 (2015).<\/p>\n CAS<\/a>\u00a0 Ratni, H. et al. Discovery of risdiplam, a selective survival of motor neuron-2 (smn2) gene splicing modifier for the treatment of spinal muscular atrophy (SMA). J Med Chem. 61, 6501\u20136517 (2018).<\/p>\n Gresh, N. et al. Addressing the issues of non-isotropy and non-additivity in the development of quantum chemistry-grounded polarizable molecular mechanics. in Quantum Modeling of Complex Molecular Systems, 1\u201349 (Springer, 2015).<\/p>\n Jing, Z. et al. Polarizable force fields for biomolecular simulations: recent advances and applications. Annu. Rev. Biophys. 48, 371\u2013394 (2019).<\/p>\n CAS<\/a>\u00a0 Shi, Y., Ren, P., Schnieders, M. & Piquemal, J.-P. Polarizable force fields for biomolecular modeling. Rev. Comput. Chem. 28, 51\u201386 (2015).<\/p>\n Melcr, J. & Piquemal, J.-P. Accurate biomolecular simulations account for electronic polarization. Front. Mol. Biosci. 6, 143 (2019).<\/p>\n CAS<\/a>\u00a0 El Khoury, L. et al. Computationally driven discovery of SARS-CoV-2 M pro inhibitors: from design to experimental validation. Chem. Sci. 13, 3674\u20133687 (2022).<\/p>\n CAS<\/a>\u00a0 Ponder, J. W. et al. Current status of the amoeba polarizable force field. J. Phys. Chem. B 114, 2549\u20132564 (2010).<\/p>\n CAS<\/a>\u00a0 Zhang, C. et al. Amoeba polarizable atomic multipole force field for nucleic acids. J. Chem. Theory Comput. 14, 2084\u20132108 (2018).<\/p>\n CAS<\/a>\u00a0 Gresh, N., Cisneros, G. A., Darden, T. A. & Piquemal, J.-P. Anisotropic, polarizable molecular mechanics studies of inter-and intramolecular interactions and ligand- macromolecule complexes. a bottom-up strategy. J. Chem. Theory Comput. 3, 1960\u20131986 (2007).<\/p>\n CAS<\/a>\u00a0 El Hage, K., Piquemal, J.-P., Hobaika, Z., Maroun, R. G. & Gresh, N. Substituent-modulated affinities of halobenzene derivatives to the HIV-1 integrase recognition site. Analyses of the interaction energies by parallel quantum chemical and polarizable molecular mechanics. J. Phys. Chem. A 118, 9772\u20139782 (2014).<\/p>\n CAS<\/a>\u00a0 Adjoua, O. et al. Tinker-hp: Accelerating molecular dynamics simulations of large complex systems with advanced point dipole polarizable force fields using GPUs and multi-GPU systems. J. Chem. Theory Comput. 17, 2034\u20132053 (2021).<\/p>\n CAS<\/a>\u00a0 Lagard\u00e8re, L., Aviat, F. & Piquemal, J.-P. Pushing the limits of multiple-time-step strategies for polarizable point dipole molecular dynamics. J. Phys. Chem. Lett. 10, 2593\u20132599 (2019).<\/p>\n PubMed<\/a>\u00a0 Jaffrelot-Inizan, T. et al. High-resolution mining of SARS-CoV-2 main protease conformational space: Supercomputer-driven unsupervised adaptive sampling. Chem. Sci. 12, 4889\u20134907 (2021).<\/p>\n CAS<\/a>\u00a0 C\u00e9lerse, F. et al. An efficient Gaussian-accelerated molecular dynamics (GAMD) multilevel enhanced sampling strategy: application to polarizable force fields simulations of large biological systems. J. Chem. Theory Comput. 18, 968\u2013977 (2022).<\/p>\n PubMed<\/a>\u00a0 C\u00e9lerse, F., Lagard\u00e8re, L., Derat, E. & Piquemal, J.-P. Massively parallel implementation of steered molecular dynamics in tinker-hp: Comparisons of polarizable and non-polarizable simulations of realistic systems. J. Chem. Theory Comput. 15, 3694\u20133709 (2019).<\/p>\n PubMed<\/a>\u00a0 Lagard\u00e8re, L. et al. Lambda-abf: Simplified, portable, accurate, and cost-effective alchemical free-energy computation. J. Chem. Theory Comput. 20, 4481\u20134498 (2024).<\/p>\n PubMed<\/a>\u00a0 Blazhynska, M. et al. Water\u2013glycan interactions drive the SARS-CoV-2 spike dynamics: insights into glycan-gate control and camouflage mechanisms. Chem. Sci. 15, 14177\u201314187 (2024).<\/p>\n CAS<\/a>\u00a0 Wang, L. et al. Accurate and reliable prediction of relative ligand binding potency in prospective drug discovery by way of a modern free-energy calculation protocol and force field. J. Am. Chem. Soc. 137, 2695\u20132703 (2015).<\/p>\n CAS<\/a>\u00a0 Zhang, C.-H. et al. Potent noncovalent inhibitors of the main protease of sars-cov-2 from molecular sculpting of the drug perampanel guided by free energy perturbation calculations. ACS Cent. Sci. 7, 467\u2013475 (2021).<\/p>\n CAS<\/a>\u00a0 Chodera, J. D. et al. Alchemical free energy methods for drug discovery: progress and challenges. Curr. Opin. Struct. Biol. 21, 150\u2013160 (2011).<\/p>\n CAS<\/a>\u00a0 El Hage, K. et al. Targeting the major groove of the palindromic d (ggcgcc) 2 sequence by oligopeptide derivatives of anthraquinone intercalators. J. Chem. Inf. Model. 62, 6649\u20136666 (2022).<\/p>\n CAS<\/a>\u00a0 Gresh, N. et al. Enforcing local DNA kinks by sequence-selective trisintercalating oligopeptides of a tricationic porphyrin: a polarizable molecular dynamics study. ChemPhysChem 25, e202300776 (2024).<\/p>\n CAS<\/a>\u00a0 El Hage, K., Mondal, P. & Meuwly, M. Free energy simulations for protein ligand binding and stability. Mol. Sim. 44, 1044\u20131061 (2018).<\/p>\n CAS<\/a>\u00a0 Rasouli, A., Pickard IV, F. C., Sur, S., Grossfield, A. & I\u015f\u0131k Bennett, M. Essential considerations for free energy calculations of RNA-small molecule complexes: lessons from the theophylline-binding RNA aptamer. J. Chem. Inf. Model. 65, 223\u2013239 (2025).<\/p>\n Abramyan, A. M. et al. Accurate physics-based prediction of binding affinities of RNA- and DNA-targeting ligands. J. Chem. Inf. Model. 65, 1392\u20131403 (2025).<\/p>\n Clark, F., Robb, G., Cole, D. J. & Michel, J. Comparison of receptor\u2013ligand restraint schemes for alchemical absolute binding free energy calculations. J. Chem. Theory Comput. 19, 3686\u20133704 (2023).<\/p>\n CAS<\/a>\u00a0 Salari, R., Joseph, T., Lohia, R., H\u00e9nin, J. & Brannigan, G. A streamlined, general approach for computing ligand binding free energies and its application to GPCR-bound cholesterol. J. Chem. Theory Comput. 14, 6560\u20136573 (2018).<\/p>\n CAS<\/a>\u00a0 Zhang, H. et al. Accurate estimation of the standard binding free energy of netropsin with DNA. Molecules 23, 228 (2018).<\/p>\n PubMed<\/a>\u00a0 Gapsys, V. et al. Accurate absolute free energies for ligand\u2013protein binding based on non-equilibrium approaches. Commun. Chem. 4, 61 (2021).<\/p>\n CAS<\/a>\u00a0 Dibrov, S. M. et al. Structure of a hepatitis C virus RNA domain in complex with a translation inhibitor reveals a binding mode reminiscent of riboswitches. Proc. Natl Acad. Sci. 109, 5223\u20135228 (2012).<\/p>\n CAS<\/a>\u00a0 Seth, P. P. et al. Sar by ms: discovery of a new class of RNA-binding small molecules for the hepatitis C virus: internal ribosome entry site IIA subdomain. J. Med. Chem. 48, 7099\u20137102 (2005).<\/p>\n CAS<\/a>\u00a0 Wu, J. C., Chattree, G. & Ren, P. Automation of amoeba polarizable force field parameterization for small molecules. Theor. Chem. Acc. 131, 1\u201311 (2012).<\/p>\n Shi, Y. et al. Polarizable atomic multipole-based amoeba force field for proteins. J. Chem. Theory Comput. 9, 4046\u20134063 (2013).<\/p>\n CAS<\/a>\u00a0 Yang, X., Liu, C., Kuo, Y.-A., Yeh, H.-C. & Ren, P. Computational study on the binding of mango-II RNA aptamer and fluorogen using the polarizable force field amoeba. Front. Mol. Biosci. 9, 946708 (2022).<\/p>\n CAS<\/a>\u00a0 Lagard\u00e8re, L. et al. Tinker-hp: a massively parallel molecular dynamics package for multiscale simulations of large complex systems with advanced point dipole polarizable force fields. Chem. Sci. 9, 956\u2013972 (2018).<\/p>\n PubMed<\/a>\u00a0 Jolly, L.-H. et al. Raising the performance of the tinker-hp molecular modeling package [article v1.0]. Living J. Comput. Mol. Sci. 1, 10409 (2019).<\/p>\n Fiorin, G., Klein, M. L. & H\u00e9nin, J. Using collective variables to drive molecular dynamics simulations. Mol. Phys. 111, 3345\u20133362 (2013).<\/p>\n CAS<\/a>\u00a0 Bonati, L., Rizzi, V. & Parrinello, M. Data-driven collective variables for enhanced sampling. J. Phys. Chem. Lett. 11, 2998\u20133004 (2020).<\/p>\n CAS<\/a>\u00a0 Padroni, G., Patwardhan, N., Schapira, M. & Hargrove, A. Systematic analysis of the interactions driving small molecule\u2013rna recognition. RSC Med. Chem. 11, 802\u2013813 (2020).<\/p>\n CAS<\/a>\u00a0 Chen, W. et al. Enhancing hit discovery in virtual screening through absolute protein\u2013ligand binding free-energy calculations. J. Chem. Inf. Model. 63, 3171\u20133185 (2023).<\/p>\n CAS<\/a>\u00a0 Parsons, J. et al. Conformational inhibition of the hepatitis C virus internal ribosome entry site RNA. Nat. Chem. Biol. 5, 823\u2013825 (2009).<\/p>\n CAS<\/a>\u00a0 Santiago-McRae, E., Ebrahimi, M., Sandberg, J. W., Brannigan, G. & H\u00e9nin, J. Computing absolute binding affinities by streamlined alchemical free energy perturbation (safep)[article v1. 0]. Living J. Comput. Mol. Sci. 5, 2067\u20132067 (2023).<\/p>\n Invernizzi, M. & Parrinello, M. Rethinking metadynamics: from bias potentials to probability distributions. J. Phys. Chem. Lett. 11, 2731\u20132736 (2020).<\/p>\n CAS<\/a>\u00a0 Invernizzi, M. & Parrinello, M. Exploration vs convergence speed in adaptive-bias enhanced sampling. J. Chem. Theory Comput. 18, 3988\u20133996 (2022).<\/p>\n CAS<\/a>\u00a0 Walker, B., Liu, C., Wait, E. & Ren, P. Automation of amoeba polarizable force field for small molecules: Poltype 2. J. Comput. Chem. 43, 1530\u20131542 (2022).<\/p>\n CAS<\/a>\u00a0 Turney, J. M. et al. Psi4: an open-source ab initio electronic structure program. Wiley Interdiscip. Rev. Comput. Mol. Sci. 2, 556\u2013565 (2012).<\/p>\n CAS<\/a>\u00a0 Stone, A. J. & Alderton, M. Distributed multipole analysis: methods and applications. Mol. Phys. 56, 1047\u20131064 (1985).<\/p>\n CAS<\/a>\u00a0 Rackers, J. A. et al. Tinker 8: software tools for molecular design. J. Chem. theory Comput. 14, 5273\u20135289 (2018).<\/p>\n CAS<\/a>\u00a0 Ren, P., Wu, C. & Ponder, J. W. Polarizable atomic multipole-based molecular mechanics for organic molecules. J. Chem. Theory Comput. 7, 3143\u20133161 (2011).<\/p>\n CAS<\/a>\u00a0 Zhang, C., Bell, D., Harger, M. & Ren, P. Polarizable multipole-based force field for aromatic molecules and nucleobases. J. Chem. Theory Comput. 13, 666\u2013678 (2017).<\/p>\n CAS<\/a>\u00a0 Bannwarth, C. et al. Extended tight-binding quantum chemistry methods. Wiley Interdiscip. Rev. Comput. Mol. Sci. 11, e1493 (2021).<\/p>\n CAS<\/a>\u00a0 Bannwarth, C., Ehlert, S. & Grimme, S. Gfn2-xtb-an accurate and broadly parametrized self-consistent tight-binding quantum chemical method with multipole electrostatics and density-dependent dispersion contributions. J. Chem. Theory Comput. 15, 1652\u20131671 (2019).<\/p>\n CAS<\/a>\u00a0 Chai, J.-D. & Head-Gordon, M. Long-range corrected hybrid density functionals with damped atom\u2013atom dispersion corrections. Phys. Chem. Chem. Phys. 10, 6615\u20136620 (2008).<\/p>\n CAS<\/a>\u00a0 Tuckerman, M., Berne, B. J. & Martyna, G. J. Reversible multiple time scale molecular dynamics. J. Chem. Phys. 97, 1990\u20132001 (1992).<\/p>\n CAS<\/a>\u00a0 Bussi, G., Donadio, D. & Parrinello, M. Canonical sampling through velocity rescaling. J. Chem. Phys. 126, 014101 (2007).<\/p>\n Berendsen, H. J., Postma, J. V., Van Gunsteren, W. F., DiNola, A. & Haak, J. R. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81, 3684\u20133690 (1984).<\/p>\n CAS<\/a>\u00a0 Essmann, U. et al. A smooth particle mesh ewald method. J. Chem. Phys. 103, 8577\u20138593 (1995).<\/p>\n CAS<\/a>\u00a0 Lagard\u00e8re, L. et al. Scalable evaluation of polarization energy and associated forces in polarizable molecular dynamics: Ii. toward massively parallel computations using smooth particle mesh ewald. J. Chem. Theory Comput. 11, 2589\u20132599 (2015).<\/p>\n PubMed<\/a>\u00a0 Laury, M. L., Wang, Z., Gordon, A. S. & Ponder, J. W. Absolute binding free energies for the sampl6 cucurbit [8] uril host\u2013guest challenge via the amoeba polarizable force field. J. Comput. Aided Mol. Des. 32, 1087\u20131095 (2018).<\/p>\n CAS<\/a>\u00a0 Boresch, S., Tettinger, F., Leitgeb, M. & Karplus, M. Absolute binding free energies: a quantitative approach for their calculation. J. Phys. Chem. B 107, 9535\u20139551 (2003).<\/p>\n CAS<\/a>\u00a0 H\u00e9nin, J., Lopes, L. J. & Fiorin, G. Human learning for molecular simulations: the collective variables dashboard in VMD. J. Chem. Theory Comput. 18, 1945\u20131956 (2022).<\/p>\n PubMed<\/a>\u00a0 Humphrey, W., Dalke, A. & Schulten, K. Vmd: visual molecular dynamics. J. Mol. Graph. 14, 33\u201338 (1996).<\/p>\n CAS<\/a>\u00a0 Straatsma, T. P. & McCammon, J. A. Multiconfiguration thermodynamic integration. J. Chem. Phys. 95, 1175\u20131188 (1991).<\/p>\n CAS<\/a>\u00a0 Zwanzig, R. W. High-temperature equation of state by a perturbation method. i. nonpolar gases. J. Chem. Phys. 22, 1420\u20131426 (1954).<\/p>\n CAS<\/a>\u00a0 Jiang, W. & Roux, B. Free energy perturbation hamiltonian replica-exchange molecular dynamics (fep\/h-remd) for absolute ligand binding free energy calculations. J. Chem. Theory Comput. 6, 2559\u20132565 (2010).<\/p>\n CAS<\/a>\u00a0 Lyubartsev, A., Martsinovski, A., Shevkunov, S. & Vorontsov-Velyaminov, P. New approach to Monte Carlo calculation of the free energy: method of expanded ensembles. J. Chem. Phys. 96, 1776\u20131783 (1992).<\/p>\n CAS<\/a>\u00a0 Thomas, J. R. & Hergenrother, P. J. Targeting RNA with small molecules. Chem. Rev. 108, 1171\u20131224 (2008).<\/p>\n CAS<\/a>\u00a0 Far, S. et al. Bis-and tris-DNA intercalating porphyrins designed to target the major groove: Synthesis of acridylbis-arginyl-porphyrins, molecular modelling of their DNA complexes, and experimental tests. Eur. J. Org. Chem. 2004, 1781\u20131797 (2004).<\/p>\n Petrov, D., Perthold, J. W., Oostenbrink, C., de Groot, B. L. & Gapsys, V. Guidelines for free-energy calculations involving charge changes. J. Chem. Theory Comput. 20, 914\u2013925 (2024).<\/p>\n CAS<\/a>\u00a0 Barducci, A., Bonomi, M. & Parrinello, M. Metadynamics. WIREs Comput. Mol. Sci. 1, 826\u2013843 (2011).<\/p>\n CAS<\/a>\u00a0 Welling, M. Fisher Linear Discriminant Analysis. Tech. Rep., Dep. Comput. Sci. Univ. Toronto (2005).<\/p>\n Rizzi, V., Bonati, L., Ansari, N. & Parrinello, M. The role of water in host-guest interaction. Nat. Commun. 12, 93 (2021).<\/p>\n CAS<\/a>\u00a0 Ansari, N., Rizzi, V., Carloni, P. & Parrinello, M. Water-triggered, irreversible conformational change of SARS-CoV-2 main protease on passing from the solid state to aqueous solution. J. Am. Chem. Soc. 143, 12930\u201312934 (2021).<\/p>\n CAS<\/a>\u00a0 Ansari, N., Rizzi, V. & Parrinello, M. Water regulates the residence time of benzamidine in trypsin. Nat. Commun. 13, 5438 (2022).<\/p>\n CAS<\/a>\u00a0 Bjelobrk, Z. et al. Naphthalene crystal shape prediction from molecular dynamics simulations. Cryst. Eng. Comm. 21, 3280\u20133288 (2019).<\/p>\n CAS<\/a>\u00a0 Leontis, N. B., Stombaugh, J. & Westhof, E. The non\u2013Watson\u2013Crick base pairs and their associated isostericity matrices. Nucleic Acids Res. 30, 3497\u20133531 (2002).<\/p>\n CAS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
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\n Google Scholar<\/a>\u00a0\n <\/p>\n
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\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n
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