44. M. Spichty, H. Zipse, S. Majouri, K.M. Fromm, B. Giese
“50 Years of Giese Reaction–a Personal View”
Angew. Chem. Int. Ed. Engl. 65: e24825 (2026); https://doi.org/10.1002/anie.202524825
43. L. Mamede, G. W. Rangel, M. Schmitt, S. Albrecht, M. Spichty, J. Bero, C. Beaufay, I. Florent, M. Llinás, M. Frédérich, J. Quetin-Leclercq
“Natural triterpenic phenolic esters target PfA-M17 in Plasmodium falciparum”
Malaria J. 25: 74 (2026); https://doi.org/10.1186/s12936-025-05762-3
42. Andréa Engel, F. Ferrari, M. Meyer, J.-M. Strub, M. Spichty, C. Bertsch, C. Schaeffer-Reiss, C. Tarnus, S. Albrecht, M.-L. Goddard
“Understanding the mode of action of arsenic(III) on the fungus Neofusicoccum parvum: Target protein identification”
Anal. Biochem. 708: 115988 (2026); https://doi.org/10.1016/j.ab.2025.115988
41. A. Bianchi, F. Marquenet, L. Manciocchi, M. Spichty, K. M. Fromm*
“Toward predicting silver ion binding in proteins”
Chem. Commun. 61: 5309 (2025); https://doi.org/10.1039/D4CC06612J
40. L. Manciocchi, A. Bianchi, V. Mazan, M. Potapov, K. M. Fromm, M. Spichty*
“Modeling the Interaction Between Silver(I) Ion and Proteins with 12-6 Lennard-Jones Potential: A Bottom-Up Parameterization Approach ”
Biophysica 5: 7 (2025); https://doi.org/10.3390/biophysica5010007
39. Y. Liang, R. Schettini, N. Kern, L. Manciocchi, I. Izzo, M. Spichty, A. Bodlenner, P. Compain*
“Deconstructing Best-in-Class Neoglycoclusters as a Tool for Dissecting Key Multivalent Processes in Glycosidase Inhibition”
Chem. Eur. J. 30: e202304126 (2024); https://doi.org/10.1002/chem.202304126
38. D. Neshchadin, A.-M. Kelterer, C. Houée-Levin, E. Stadler, M. Spichty, G. Gescheidt*
“Methionine-Based Radicals: Time Scales and Species”
Appl. Magn., Reson. 53: 1331 (2022); https://doi.org/10.1007/s00723-022-01469-9
37. D. Cluet, B. Vergier, N.-P. Levy, L. Dehau, A. Thurman, I. Amri, M. Spichty*
“Titration of Apparent In-Cellula Affinities of Protein-Protein Interactions”
ChemBioChem 4: e202100640 (2021); https://doi.org/10.1002/cbic.202100640
36. H. Duplus-Bottin, M. Spichty, G. Triqueneaux, C. Place, P. E. Mangeot, T. Ohlmann, F. Vittoz, G. Yvert*
“A single-chain and fast-responding light-inducible Cre recombinase as a novel optogenetic switch”
eLife 10: e61268 (2021); https://doi.org/10.7554/eLife.61268
35. L. Mourot, M. Schmitt, E. Mouray, M. Spichty, I. Florent, S. Albrecht*
“Structure-activity relationship and molecular modelling studies of quinazolinedione derivatives MMV665916 as potential antimalarial agent”
Bioorg. Med. Chem. 51: 116513 (2021); https://doi.org/10.1016/j.bmc.2021.116513
34. H. Quast, G. Gescheidt,* M. Spichty*
“Topological Dynamics of a Radical Ion Pair: Experimental and Computational Assessment at the Relevant Nanosecond Timescale”
Chemistry 2: 219 (2020); https://doi.org/10.3390/chemistry2020014
33. D. Cluet, I. Amri, B. Vergier, J. Léault, A. Audibert, C. Grosjean, D. Calabrési, M. Spichty*
“A quantitative tri-fluorescent yeast two-hybrid system: from flow cytometry to in-cellula affinities”
Mol. Cell. Proteom. 19: 701 (2020); https://doi.org/10.1074/mcp.TIR119.001692
32. F. Beurton, P. Stempor, M. Caron, A. Appert, Y. Dong, R. A-j Chen, D. Cluet, Y. Couté, M. Herbette, N. Huang, H. Polveche, M. Spichty, C. Bedet, J. Ahringer,* F. Palladino*
“Physical and functional interaction between SET1/COMPASS complex component CFP-1 and a Sin3S HDAC complex in C. elegans”
Nucl. Acids Res. 47: 11164 (2019); https://doi.org/10.1093/nar/gkz880
31. M. Richard, F. Chuffart, H. Duplus-Bottin, F. Pouyet, M. Spichty, E. Fulcrand, M. Entrevan, A. Barthelaix, M. Springer, D. Jost* and G. Yvert*
“Assigning function to natural allelic variation via dynamic modeling of gene network induction”
Mol. Sys. Biol. 14: e7803 (2018); https://doi.org/10.15252/msb.20177803
30. M. Rossi, M. Spichty, L. Attorri, C. Distante, C. Nervi, S. Salvati, L. Vitelli* “Eicosapentaenoic acid modulates the synergistic action of CREB1 and ID/E2A family members in the rat pup brain and mouse embryonic stem cells”
Biochim. Biophys. Acta, Gene Regul. Mech. 1860: 870 (2017); https://doi.org/10.1016/j.bbagrm.2017.06.002
29. D.E. Fast, M. Zalibera, A. Lauer, A. Eibel, C. Schweigert, A.-M. Kelterer, M. Spichty, D. Neshchadin, D. Voll, H. Ernst, Y. Liang, K. Dietliker, A.-N. Unterreiner, C. Barner-Kowollik, H. Grützmacher, G. Gescheidt*
“Bis (mesitoyl) phosphinic acid: photo-triggered release of metaphosphorous acid in solution”
Chem. Comm. 52: 9917 (2016); https://doi.org/10.1039/C6CC05219C
28. M. Zalibera, K. Dietliker, P. N. Stébé, H. J. Grützmacher, M. Spichty, G. Gescheidt*
“The Redox Chemistry of Mono- and Bis(acyl)phosphane Oxides”
Eur. J. Org. Chem. 2014: 331 (2014); https://doi.org/10.1002/ejoc.201301214
27. D. Cluet, P.-N. Stébé, S. Riche, M. Spichty*, M. Delattre*
“Automated High-Throughput Quantification of Mitotic Spindle Positioning from DIC Movies of Caenorhabditis Embryos”
PLoS One 9: e93718 (2014); https://doi.org/10.1371/journal.pone.0093718
26. Silvia Dibenedetto, David Cluet, Pierre Nicolas Stébé, Veronique Baumle, Jeremie Leault, Raphael Terreux, Marc Bickle, Benoit de Chassey, Ivan Mikaelian, Pierre Colas, Martin Spichty, Michele Zoli and Brian B. Rudkin*
“Calcineurin A vs NS5A-TP2/HDDC2: a case study of site-directed low-frequency random mutagenesis for dissecting target specificity of peptide aptamers”
Mol. Cell. Proteom. 12:1939 (2013); https://doi.org/10.1074/mcp.m112.024612
25. Francesco Rao* and Martin Spichty*
“Thermodynamics and Kinetics of Large-Time-Step Molecular Dynamics”
J. Comput. Chem. 33: 475 (2012); https://doi.org/10.1002/jcc.21990
24. Kamel Meguellati, Sylvain Ladame and Martin Spichty*
“A conceptually improved TD-DFT approach for predicting the maximum absorption wavelength of cyanine dyes”
Dyes Pigm. 90:114 (2011); https://doi.org/10.1016/j.dyepig.2010.12.001
23. Martin Spichty*, Marco Cecchini and Martin Karplus*
“Conformational free-energy difference of a Miniprotein from Nonequilibrium Simulations”
J. Phys. Chem. Lett. 1: 1922 (2010); https://doi.org/10.1021/jz1005016
22. Marco Cecchini*, Sergei V. Krivov, Martin Spichty, and Martin Karplus*
“Correction: Calculation of Free-Energy Differences by Confinement Simulations. Application to Peptide Conformers [J. Phys. Chem. B. 113, 9728 (2009)]”
J. Phys. Chem. B 114: 19, 6763 (2010); https://doi.org/10.1021/jp102878c
21. Kamel Meguellati, Martin Spichty and Sylvain Ladame*
“Synthesis, spectroscopic and DNA alkylating properties of malondialdehyde (MDA) bis-imine fluorescent adducts”
Mol. BioSyst. 6: 1694 (2010); https://doi.org/10.1039/C002157A
20. Marco Cecchini*, Sergei V. Krivov, Martin Spichty and Martin Karplus*
“The Calculation of Free-Energy Differences between Peptide Conformers by Confinement Simulations”
J. Phys. Chem. B. 113: 9728 (2009); https://doi.org/10.1021/jp9020646
19. Martin Spichty*, Antoine Taly, Franz Hagn, Horst Kessler, Sofia Barluenga, Nicolas Winssinger* and Martin Karplus*
“The HSP90 binding mode of a radicicol-like E-oxime from docking, binding free energy estimations, and NMR 15N chemical shifts”
Biophys. Chem. 143: 111 (2009); https://doi.org/10.1016/j.bpc.2009.04.003
18. Kamel Meguellati, Martin Spichty and Sylvain Ladame*
“Reversible Synthesis and Characterization of Dynamic Imino Analogues of Trimethine and Pentamethine Cyanine Dyes“
Org. Lett. 11: 1123 (2009); https://doi.org/10.1021/ol802913b
17. Martin Spichty*, Klaus J. Kulicke, Markus Neuburger, Silvia Schaffner and Jürgen F. K. Müller*
“Heterobimetallic bisphosphonate titanium complexes: carbene-like carbanions?”
Eur. J. Inorg. Chem. 32: 5024 (2008); https://doi.org/10.1002/ejic.200800747
16. Martin Spichty*a, Paul Maragakis*a and Martin Karplus*
“A differential fluctuation theorem”
J. Phys. Chem. B. 112: 6168 (2008); https://doi.org/10.1021/jp077037r
15. Paul Maragakis, Martin Spichty and Martin Karplus
“Erratum: Optimal estimates of free energies from multi-state nonequilibrium work data”
Phys. Rev. Lett. 98: 259901 (2007); https://doi.org/10.1103/PhysRevLett.98.259901
14. Paul Maragakis, Martin Spichty and Martin Karplus
“Optimal estimates of free energies from multi-state nonequilibrium work data”
Phys. Rev. Lett. 96: 100602 (2006); https://doi.org/10.1103/PhysRevLett.96.100602
13. Markus Seeligera, Martin Spichtya, Sadie E. Kelly, Mark Bycroft, Stefan M. V. Freund*, Martin Karplus* and Laura Itzhaki*
“Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins”
J. Biol. Chem. 280: 30448 (2005); https://doi.org/10.1074/jbc.m501450200
12. Martin Spichty, Nicholas Turro, Günther Rist, Jean-Luc Birbaum, Kurt Dietliker, Jean-Pierre Wolf and Georg Gescheidt*
“Bond cleavage in the excited state of acyl phosphene oxides. Insight on the role of conformation by model calculations: a concept”
J. Photochem. Photobiol. A-Chem. 142: 209 (2001); https://doi.org/10.1016/S1010-6030(01)00515-9
11. Jürgen F. K. Müller*, Klaus J. Kulicke, Markus Neuburger and Martin Spichty
“Carbanions substituted by transition metals: synthesis, structure, and configurational restrictions of a lithium titanium phosphonate”
Angew. Chem. Int. Ed. Engl. 40: 2890 (2001); https://doi.org/10.1002/1521-3773(20010803)40:15%3C2890::AID-ANIE2890%3E3.0.CO;2-T
10. Bernd Giese*, Martin Spichty and Stephan Wessely
“Long-distance charge transport through DNA. An extended hopping model”
Pure Appl. Chem. 73: 449 (2001); http://dx.doi.org/10.1351/pac200173030449
9. Martin Spichty, Bernd Giese, Akikazu Matsumoto, Hanns Fischer and Georg Gescheidt*
“Conformational Dynamics in a Methacrylate-Derived Radical: A Computational and EPR Study”
Macromolecules 34: 723 (2001); https://doi.org/10.1021/ma001217g
8. Bernd Giese* and Martin Spichty
“Long distance charge transport through DNA: quantification and extension of the hopping model”
ChemPhysChem 1: 195 (2000); https://doi.org/10.1002/1439-7641(20001215)1:4%3C195::AID-CPHC195%3E3.0.CO;2-B
7. Martin Spichty, Gianfranco Fragale and Thomas Wirth*
“Theoretical Investigations on the Stereoselective Selenenylation Reaction of Alkenes”
J. Am. Chem. Soc. 122: 10914 (2000); https://doi.org/10.1021/ja001602l
6. Ralf Glatthar, Martin Spichty, Andreas Gugger, Rohit Batra, Wolfgang Damm, Matthias Mohr, Hendrik Zipse* and Bernd Giese*
“Mechanistic studies in the radical induced DNA strand cleavage - formation and reactivity of the radical cation intermediate”
Tetrahedron 56: 4117 (2000); https://doi.org/10.1016/S0040-4020(00)00335-5
5. Xue Wang, Kendall N. Houk*, Martin Spichty and Thomas Wirth
“Origin of Stereoselectivities in Asymmetric Alkoxyselenenylations”
J. Am. Chem. Soc. 121: 8567 (1999); https://doi.org/10.1021/ja990473+
4. Andreas Marx, Martin Spichty, Mario Amacker, Urs Schwitter, Ulrich Hübscher, Thomas A. Bickle, Giovanni Maga and Bernd Giese*
“Probing interactions between HIV-1 reverse transcriptase and its DNA substrate with backbone modified nucleotides”
Chem. Biol. 6: 111 (1999); https://doi.org/10.1016/s1074-5521(99)80007-6
3. Thomas Wirth*, Gianfranco Fragale and Martin Spichty
“Mechanistic Course of the Asymmetric Methoxyselenylation Reaction”
J. Am. Chem. Soc. 120: 3376 (1998); https://doi.org/10.1021/ja974177d
2. Eric Meggers, Dirk Kusch, Martin Spichty, Uta Wille and Bernd Giese*
“Electron transfer through DNA in the course of radical-induced strand cleavage”
Angew. Chem. Int. Ed., 37: 460 (1998); https://doi.org/10.1002/(sici)1521-3773(19980302)37:4%3C460::aid-anie460%3E3.0.co;2-u
1. Rohit Batra*, Bernd Giese, Martin Spichty, Georg Gescheidt* and Kendall N. Houk
“Calculations of Isotropic Hyperfine Coupling Constants of Organic Radicals. The Evaluation of Semiempirical, Hartree-Fock, and Density Functional Methods”
J. Phys. Chem. 100: 18371 (1996); https://doi.org/10.1021/jp961696e