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Simone Codispoti, Valerio G. Giacobelli, Matúš Friček, Václav Verner, Julie Nováková, Martin Mašek, Anton Bokač, Robin Kryštůfek, Radko Souček, Michal Kolář, Giuliano Zanchetta, Klára Hlouchová. (2026) Protoribosomal condensate formation across cationic chemistries. BiorXiv https://doi.org/10.64898/2026.09.29.755306

Buchel F., Giacobelli V. G., Hlouchová K. (2026) Minimal-alphabet proteins by evolution, engineering, and design. Trends in Biochemical Sciences https://doi.org/10.1016/j.tibs.2026.08.002

Brown S M, Kalvoda T, Kryštůfek R, Kormaník J M, Makarov M, Verner V, Hexnerová R, Srb P, Andris E, Bednárová L, Pazderková M, Lepšík M, Řezáč J, Konvalinka J, Veverka V, Rulíšek L, Freeland S, Hlouchová K (2026) Xeno amino acid alphabets form peptides with familiar secondary structure. https://doi.org/10.64898/2026.01.28.701962

Bartlett S, Gupta A, Phung D, Goldford JE, Yang J, Hlouchova K, Fischer W, Yung YL. (2026) A highly limited amino acid library from asteroid Bennu yields wide-ranging protein folds. Nat Commun. doi: 10.1038/s41467-026-71509-6.

Fried SD, Hochberg G, Hlouchova K. (2026) Reconstructing ancient protein alphabets: what can we truly infer? Trends Genet. 26:S0168-9525(26)00063-6. doi: 10.1016/j.tig.2026.03.002.

Giacobelli V G, Andersson S, Srb P, Neuwirthová T, Ruszová Z, Marhoul J, Pšenička S, Knetl A, Bednárová L, Veverka V, Hlouchová K, André I. (2025) Ancient amino acid sets enable stable protein folds. https://doi.org/10.1101/2025.10.29.685319

Cherepashuk I, Makarov M, Soucek R, Verner V, Krystufek R, Hadravova R, Giacobelli V G G, Fujishima K, Jordan S F, Longo L M, Hlouchova K. (2025) Peptides at vesicle and mineral prebiotic interfaces. bioRxiv 2025.06.13.659467; doi: https://doi.org/10.1101/2025.06.13.659467

Makarov M, Kryštůfek R, Friček M, Manriquez-Sandoval E, Dutta S, Kormaník JM, Kalvoda T, Verner V, Bednárová L, Charnavets T, Lebl M, Brown SM, Hadravová R, Konvalinka J, Singharoy A, Fried SD, Hlouchová K. (2025) Prebiotically Plausible Peptides can Self-assemble into β-rich Nanostructures. bioRxiv 10:2025.11.09.687475. doi: 10.1101/2025.11.09.687475.

MH Kolář, K Hlouchová (2025). Evolution of protein – RNA interactions. Current Opinion in Structural Biology, Volume 94, 103109, https://doi.org/10.1016/j.sbi.2025.103109

Hlouchová, K. (2024). Peptides En Route from Prebiotic to Biotic Catalysis. Accounts of Chemical Research, 57(15), 2027-2037. https://doi.org/10.1021/acs.accounts.4c00137

Codispoti S, Yamaguchi T, Makarov M, Giacobelli VG, Mašek M, Kolář MH, Sanchez Rocha AC, Fujishima K*, Zanchetta G*, Hlouchová K.* (2024) The interplay between peptides and RNA is critical for protoribosome compartmentalization and stability. Nucleic Acid Research, gkae823, https://doi.org/10.1093/nar/gkae823

Aubel M, Buchel F, Heames B, Jones A, Honc O, Bornberg-Bauer E*, Hlouchova K.* (2024) High-throughput selection of human de novo-emerged sORFs with high folding potential. Genome Biol Evol. 16(4):evae069. https://doi.org/10.1093/gbe/evae069

Sanchez Rocha CA, Makarov M, Pravda L, Novotny M*, Hlouchova K.* (2024) Coenzyme-Protein Interactions since Early Life. eLife, 13:RP94174. https://doi.org/10.7554/eLife.94174.1

Hlouchova K. (2023) Toxin rescue by a random sequence. Nat. Ecol. Evol. 7(12):1963-1964. doi: 10.1038/s41559-023-02252-0.

Heames B, Buchel F, Aubel M, Tretyachenko V, Loginov D, Novak P, Lange A, Bornberg- Bauer E*, Hlouchova K.* (2023) Experimental characterization of de novo proteins and their unevolved random-sequence counterparts. Nature Ecology & Evolution https://doi.org/10.1038/s41559-023-02010-2

Makarov M, Sanchez Rocha AC, Krystufek R, Cherepashuk I, Dzmitruk V, Charnavets T, Faustino AM, Lebl M, Fujishima K, Fried SD*, Hlouchova K.* (2023) Early selection of the amino acid alphabet was adaptively shaped by biophysical constraints of foldability. J Am Chem Soc. 145(9):5320-5329. https://doi.org/10.1021/jacs.2c12987

Tretyachenko V, Vymetal J, Neuwirthova T, Vondrasek J, Fujishima K, Hlouchova K. (2022) Modern and prebiotic amino acids support distinct structural profiles in proteins. Open Biology 12: 220040.
https://doi.org/10.1098/rsob.220040

Giacobelli VG, Fujishima K, Lepsik M, Tretyachenko V, Kadava T, Makarov M, Bednarova L, Novak P, Hlouchova K. (2022) In vitro evolution reveals non-cationic protein – RNA interaction mediated by metal ions. Molecular Biology and Evolution, msac032. https://doi.org/10.1093/molbev/msac032.

Fried SD*, Fujishima K, Makarov M, Cherepashuk I, Hlouchova K*. (2022) Peptides before and during the nucleotide world: and origins story emphasizing cooperation between proteins and nucleic acids. Journal of Royal Society Interface 19: 20210641. https://doi.org/10.1098/rsif.2021.0641

Makarov M, Meng J, Tretyachenko V, Srb P, Březinová A, Giacobelli VG, Bednárová L, Vondrášek J, Dunker AK* and Hlouchová K.* (2021) Enzyme catalysis prior to aromatic residues: reverse engineering of a dephosphoCoA kinase. Protein Science DOI10.1002/pro.4068

Bornberg-Bauer E, Hlouchova K, Lange A. (2020) Structure and function of naturally evolved de novo proteins. Current Opinions in Structural Biology. 68, 175-183. DOI: 10.1016/j.sbi.2020.11.010

Tretyachenko V, Voráček V, Souček R, FujishimaK, and Hlouchová K. (2020) CoLiDe: Combinatorial Library Design tool for probing protein sequence space. Bioinformatics DOI: 10.1093/bioinformatics/btaa804

Vymětal J, Vondrášek J, and Hlouchová, K. (2019). Sequence Versus Composition: What Prescribes IDP Biophysical Properties? Entropy, 21(7), 654. https://doi.org/10.3390/e21070654

Tretyachenko V, Vymětal J, Bednárová L, Kopecký V, Hofbauerová K, Jindrová H, Hubálek M, Souček R, Konvalinka J, Vondrášek J, and Hlouchová K. (2017) Random protein sequences can form defined secondary structure and are well-tolerated in vivo. SciRep 7, 15449. https://doi.org/10.1038/s41598-017-15635-8