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2024
Ożga, K.; Rudzińska-Szostak, E.; Berlicki, Ł. Optimization of peptide foldamer-based artificial retro-aldolase, Cat. Sci. Tech. 2024, accepted. View at Publisher. | |
Ciesiołkiewicz, A.; Lizandra Perez, J.; Skalniak, L.; Noceń, P.; Berlicki, Ł. Miniprotein engineering for inhibition of PD‐1/PD‐L1 interaction, Protein Sci. 2024, 33, e5106. View at Publisher |
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Kovalenko, V.; Rudzińska-Szostak, E.; Ślepokura, K.; Berlicki, Ł. Scalable Synthesis of All Stereoisomers of 2-Aminocyclopentanecarboxylic Acid─A Toolbox for Peptide Foldamer Chemistry. J Org Chem 2024, 89 (7), 4760–4767. View at Publisher. | |
Marković, V.; Szczepańska, A.; Berlicki, Ł. Antiviral Protein–Protein Interaction Inhibitors. J Med Chem 2024, 67 (5), 3205–3231. View at Publisher. | |
Grelich-Mucha, M.; Bachelart, T.; Torbeev, V.; Ożga, K.; Berlicki, Ł.; Olesiak-Bańska, J. Biomaterials Science 2024, 12 (6), 1590-1602. View at Publisher. |
2023
Rodriguez, I.; Kocik-Krol, J.; Skalniak, L.; Musielak, B.; Wisniewska, A.; Ciesiołkiewicz, A.; Berlicki, Ł.; Plewka, J.; Grudnik, P.; Stec, M.; Siedlar, M.; Holak, T. A.; Magiera-Mularz, K. Structural and Biological Characterization of PAC65, a Macrocyclic Peptide That Blocks PD-L1 with Equivalent Potency to the FDA-Approved Antibodies. Mol Cancer 2023, 22 (1), 150. View at Publisher. | |
Tabor, W.; Katsogiannou, A.; Karta, D.; Andrianopoulou, E.; Berlicki, Ł.; Vassiliou, S.; Grabowiecka, A. Exploration of Thiourea-Based Scaffolds for the Construction of Bacterial Ureases Inhibitors. ACS Omega 2023, 8 (31), 28783–28796. View at Publisher. | |
Maślanka, M.; Tabor, W.; Krzyżek, P.; Grabowiecka, A.; Berlicki, Ł.; Mucha, A. Inhibitory Activity of Catecholic Phosphonic and Phosphinic Acids against Helicobacter Pylori Ureolysis. Eur J Med Chem 2023, 257, 115528. View at Publisher. | |
Szefczyk, M.; Szulc, N.; Gąsior-Głogowska, M.; Bystranowska, D.; Żak, A.; Sikora, A.; Polańska, O.; Ożyhar, A.; Berlicki, Ł. The Application of the Hierarchical Approach for the Construction of Foldameric Peptide Self-Assembled Nanostructures. Soft Matter 2023, 19 (21), 3828–3840. View at Publisher. | |
Marković, V.; Shaik, J. B.; Ożga, K.; Ciesiołkiewicz, A.; Lizandra Perez, J.; Rudzińska-Szostak, E.; Berlicki, Ł. Peptide Foldamer-Based Inhibitors of the SARS-CoV-2 S Protein–Human ACE2 Interaction. J Enzyme Inhib Med Chem 2023, 38 (1), 2244693. View at Publisher. | |
Macegoniuk, K.; Tabor, W.; Mazzei, L.; Cianci, M.; Giurg, M.; Olech, K.; Burda-Grabowska, M.; Kaleta, R.; Grabowiecka, A.; Mucha, A.; Ciurli, S.; Berlicki, Ł. Optimized Ebselen-Based Inhibitors of Bacterial Ureases with Nontypical Mode of Action. J Med Chem 2023, 66 (3), 2054–2063. View at Publisher. |
2022
Ożga, K.; Berlicki, Ł. Miniprotein-based artificial retroaldolase. ACS Catalysis 2022, 12(24), 15424-15430. View at Publisher
Loharch, S.; Berlicki, Ł. Rational Development of Bacterial Ureases Inhibitors. The Chemical Record 2022, 22 (8), e202200026. View at Publisher.
Berlicki, Ł. Tailoring Peptides and Peptidomimetics for Targeting Protein–Protein Interactions. In Peptide and Peptidomimetic Therapeutics; Elsevier, 2022; pp 57–71. View at Publisher.
Vassiliou, S.; Pagoni, A.; Węglarz-Tomczak, E.; Talma, M.; Tabor, W.; Grabowiecka, A.; Berlicki, Ł.; Mucha, A. Phosphinic Acid-Based Enzyme Inhibitors. Phosphorus Sulfur Silicon Relat Elem 2022, 197 (5–6), 451–456. View at Publisher.
Szefczyk, M.; Ożga, K.; Drewniak-Świtalska, M.; Rudzińska-Szostak, E.; Hołubowicz, R.; Ożyhar, A.; Berlicki, Ł. Controlling the Conformational Stability of Coiled-Coil Peptides with a Single Stereogenic Center of a Peripheral β-Amino Acid Residue. RSC Adv 2022, 12 (8), 4640–4647. View at Publisher.
Ożga, K.; Berlicki, Ł. Design and Engineering of Miniproteins. ACS Bio & Med Chem Au 2022, 2 (4), 316–327. View at Publisher.
Ciesiołkiewicz, A.; Lizandra Perez, J.; Berlicki, Ł. Miniproteins in Medicinal Chemistry. Bioorg Med Chem Lett 2022, 71, 128806. View at Publisher.
Stanojlovic, V.; Müller, A.; Moazzam, A.; Hinterholzer, A.; Ożga, K.; Berlicki, Ł.; Schubert, M.; Cabrele, C. A Conformationally Stable Acyclic Β‐Hairpin Scaffold Tolerating the Incorporation of Poorly Β‐Sheet‐Prone Amino Acids. ChemBioChem 2022, 23 (4). View at Publisher.
2021
Pagoni, A.; Grabowiecka, A.; Tabor, W.; Mucha, A.; Vassiliou, S.; Berlicki, Ł. Covalent Inhibition of Bacterial Urease by Bifunctional Catechol-Based Phosphonates and Phosphinates. J Med Chem 2021, 64 (1), 404–416. View at Publisher.
Ożga, K.; Drewniak‐Świtalska, M.; Rudzińska‐Szostak, E.; Berlicki, Ł. Towards Foldameric Miniproteins: A Helix‐Turn‐Helix Motif. ChemPlusChem 2021, 86 (4), 646–649. View at Publisher.
Szefczyk, M.; Szulc, N.; Gąsior-Głogowska, M.; Modrak-Wójcik, A.; Bzowska, A.; Majstrzyk, W.; Taube, M.; Kozak, M.; Gotszalk, T.; Rudzińska-Szostak, E.; Berlicki, Ł. Hierarchical Approach for the Rational Construction of Helix-Containing Nanofibrils Using α,β-Peptides. Nanoscale 2021, 13 (7), 4000–4015. View at Publisher.
Drewniak-Świtalska, M.; Barycza, B.; Rudzińska-Szostak, E.; Morawiak, P.; Berlicki, Ł. Constrained Beta-Amino Acid-Containing Miniproteins. Org Biomol Chem 2021, 19 (19), 4272–4278. View at Publisher.
Bejger, M.; Fortuna, P.; Drewniak-Świtalska, M.; Plewka, J.; Rypniewski, W.; Berlicki, Ł. A Computationally Designed β-Amino Acid-Containing Miniprotein. Chemical Communications 2021, 57 (49), 6015–6018. View at Publisher.
Grelich-Mucha, M.; Garcia, A. M.; Torbeev, V.; Ożga, K.; Berlicki, Ł.; Olesiak-Bańska, J. Autofluorescence of Amyloids Determined by Enantiomeric Composition of Peptides. J Phys Chem B 2021, 125 (21), 5502–5510. View at Publisher.
2020
Fortuna, P.; Twarda-Clapa, A.; Skalniak, L.; Ożga, K.; Holak, T. A.; Berlicki, Ł. Systematic ‘Foldamerization’ of Peptide Inhibiting P53-MDM2/X Interactions by the Incorporation of Trans- or Cis-2-Aminocyclopentanecarboxylic Acid Residues. Eur J Med Chem 2020, 208, 112814. https://doi.org/10.1016/j.ejmech.2020.112814.
Tarczewska, A.; Wycisk, K.; Orłowski, M.; Waligórska, A.; Dobrucki, J.; Drewniak-Świtalska, M.; Berlicki, Ł.; Ożyhar, A. Nuclear Immunophilin FKBP39 from Drosophila Melanogaster Drives Spontaneous Liquid-Liquid Phase Separation. Int J Biol Macromol 2020, 163, 108–119. https://doi.org/10.1016/j.ijbiomac.2020.06.255.
2019
Fortuna, P.; Linhares, B. M.; Purohit, T.; Pollock, J.; Cierpicki, T.; Grembecka, J.; Berlicki, Ł. Covalent and Noncovalent Constraints Yield a Figure Eight-like Conformation of a Peptide Inhibiting the Menin-MLL Interaction. Eur J Med Chem 2020, 207, 112748. https://doi.org/10.1016/j.ejmech.2020.112748.
Pagoni, A.; Daliani, T.; Macegoniuk, K.; Vassiliou, S.; Berlicki, Ł. Catechol-Based Inhibitors of Bacterial Urease. Bioorg Med Chem Lett 2019, 29 (9), 1085–1089. https://doi.org/10.1016/j.bmcl.2019.02.032.
Burda‐Grabowska, M.; Macegoniuk, K.; Flick, R.; Nocek, B. P.; Joachimiak, A.; Yakunin, A. F.; Mucha, A.; Berlicki, Ł. Bisphosphonic Acids and Related Compounds as Inhibitors of Nucleotide‐ and Polyphosphate‐processing Enzymes: A PPK1 and PPK2 Case Study. Chem Biol Drug Des 2019, 93 (6), 1197–1206. https://doi.org/10.1111/cbdd.13439.
2018
Ntatsopoulos, V.; Macegoniuk, K.; Mucha, A.; Vassiliou, S.; Berlicki, Ł. Structural Exploration of Cinnamate-Based Phosphonic Acids as Inhibitors of Bacterial Ureases. Eur J Med Chem 2018, 159, 307–316. https://doi.org/10.1016/j.ejmech.2018.09.074.
Nocek, B. P.; Khusnutdinova, A. N.; Ruszkowski, M.; Flick, R.; Burda, M.; Batyrova, K.; Brown, G.; Mucha, A.; Joachimiak, A.; Berlicki, Ł.; Yakunin, A. F. Structural Insights into Substrate Selectivity and Activity of Bacterial Polyphosphate Kinases. ACS Catal 2018, 8 (11), 10746–10760. https://doi.org/10.1021/acscatal.8b03151.
Drewniak, M.; Węglarz-Tomczak, E.; Ożga, K.; Rudzińska-Szostak, E.; Macegoniuk, K.; Tomczak, J. M.; Bejger, M.; Rypniewski, W.; Berlicki, Ł. Helix-Loop-Helix Peptide Foldamers and Their Use in the Construction of Hydrolase Mimetics. Bioorg Chem 2018, 81, 356–361. https://doi.org/10.1016/j.bioorg.2018.07.012.
2017
Giberti, S.; Bertazzini, M.; Liboni, M.; Berlicki, Ł.; Kafarski, P.; Forlani, G. Phytotoxicity of Aminobisphosphonates Targeting Both δ 1 -Pyrroline-5-Carboxylate Reductase and Glutamine Synthetase. Pest Manag Sci 2017, 73 (2), 435–443. https://doi.org/10.1002/ps.4299.
Macegoniuk, K.; Grela, E.; Biernat, M.; Psurski, M.; Gościniak, G.; Dziełak, A.; Mucha, A.; Wietrzyk, J.; Berlicki, Ł.; Grabowiecka, A. Aminophosphinates against Helicobacter Pylori Ureolysis—Biochemical and Whole-Cell Inhibition Characteristics. PLoS One 2017, 12 (8), e0182437. https://doi.org/10.1371/journal.pone.0182437.
Szefczyk, M.; Węglarz‐Tomczak, E.; Fortuna, P.; Krzysztoń, A.; Rudzińska‐Szostak, E.; Berlicki, Ł. Controlling the Helix Handedness of Ααβ‐Peptide Foldamers through Sequence Shifting. Angewandte Chemie International Edition 2017, 56 (8), 2087–2091. https://doi.org/10.1002/anie.201610154.
Macegoniuk, K.; Kowalczyk, R.; Rudzińska, A.; Psurski, M.; Wietrzyk, J.; Berlicki, Ł. Potent Covalent Inhibitors of Bacterial Urease Identified by Activity-Reactivity Profiling. Bioorg Med Chem Lett 2017, 27 (6), 1346–1350. https://doi.org/10.1016/j.bmcl.2017.02.022.
Ntatsopoulos, V.; Vassiliou, S.; Macegoniuk, K.; Berlicki, Ł.; Mucha, A. Novel Organophosphorus Scaffolds of Urease Inhibitors Obtained by Substitution of Morita-Baylis-Hillman Adducts with Phosphorus Nucleophiles. Eur J Med Chem 2017, 133, 107–120. https://doi.org/10.1016/j.ejmech.2017.03.070.
Rudzińska‐Szostak, E.; Berlicki, Ł. Sequence Engineering to Control the Helix Handedness of Peptide Foldamers. Chemistry – A European Journal 2017, 23 (60), 14980–14986. https://doi.org/10.1002/chem.201702730.
Magiera‐Mularz, K.; Skalniak, L.; Zak, K. M.; Musielak, B.; Rudzinska‐Szostak, E.; Berlicki, Ł.; Kocik, J.; Grudnik, P.; Sala, D.; Zarganes‐Tzitzikas, T.; Shaabani, S.; Dömling, A.; Dubin, G.; Holak, T. A. Bioactive Macrocyclic Inhibitors of the PD‐1/PD‐L1 Immune Checkpoint. Angewandte Chemie International Edition 2017, 56 (44), 13732–13735. https://doi.org/10.1002/anie.201707707.
Wavhale, R. D.; Martis, E. A. F.; Ambre, P. K.; Wan, B.; Franzblau, S. G.; Iyer, K. R.; Raikuvar, K.; Macegoniuk, K.; Berlicki, Ł.; Nandan, S. R.; Coutinho, E. C. Discovery of New Leads against Mycobacterium Tuberculosis Using Scaffold Hopping and Shape Based Similarity. Bioorg Med Chem 2017, 25 (17), 4835–4844. https://doi.org/10.1016/j.bmc.2017.07.034.
2016
Macegoniuk, K.; Grela, E.; Palus, J.; Rudzińska-Szostak, E.; Grabowiecka, A.; Biernat, M.; Berlicki, Ł. 1,2-Benzisoselenazol-3(2 H )-One Derivatives As a New Class of Bacterial Urease Inhibitors. J Med Chem 2016, 59 (17), 8125–8133. https://doi.org/10.1021/acs.jmedchem.6b00986.
Węglarz-Tomczak, E.; Berlicki, Ł.; Pawełczak, M.; Nocek, B.; Joachimiak, A.; Mucha, A. A Structural Insight into the P1 S1 Binding Mode of Diaminoethylphosphonic and Phosphinic Acids, Selective Inhibitors of Alanine Aminopeptidases. Eur J Med Chem 2016, 117, 187–196. https://doi.org/10.1016/j.ejmech.2016.04.018.
Wójcik, P.; Berlicki, Ł. Peptide-Based Inhibitors of Protein–Protein Interactions. Bioorg Med Chem Lett 2016, 26 (3), 707–713. https://doi.org/10.1016/j.bmcl.2015.12.084.
Kosikowska, P.; Bochno, M.; Macegoniuk, K.; Forlani, G.; Kafarski, P.; Berlicki, Ł. Bisphosphonic Acids as Effective Inhibitors of Mycobacterium Tuberculosis Glutamine Synthetase. J Enzyme Inhib Med Chem 2016, 31 (6), 931–938. https://doi.org/10.3109/14756366.2015.1070846.
2015
Macegoniuk, K.; Dziełak, A.; Mucha, A.; Berlicki, Ł. Bis(Aminomethyl)Phosphinic Acid, a Highly Promising Scaffold for the Development of Bacterial Urease Inhibitors. ACS Med Chem Lett 2015, 6 (2), 146–150. https://doi.org/10.1021/ml500380f.
Rudzińska-Szostak, E.; Gõrecki, Ł.; Berlicki, Ł.; ͆lepokura, K.; Mucha, A. Zwitterionic Phosphorylated Quinines as Chiral Solvating Agents for NMR Spectroscopy. Chirality 2015, 27 (10), 752–760. https://doi.org/10.1002/chir.22494.
2014
Cabrele, C.; Martinek, T. A.; Reiser, O.; Berlicki, Ł. Peptides Containing β-Amino Acid Patterns: Challenges and Successes in Medicinal Chemistry. J Med Chem 2014, 57 (23), 9718–9739. https://doi.org/10.1021/jm5010896.
Vassiliou, S.; Węglarz-Tomczak, E.; Berlicki, Ł.; Pawełczak, M.; Nocek, B.; Mulligan, R.; Joachimiak, A.; Mucha, A. Structure-Guided, Single-Point Modifications in the Phosphinic Dipeptide Structure Yield Highly Potent and Selective Inhibitors of Neutral Aminopeptidases. J Med Chem 2014, 57 (19), 8140–8151. https://doi.org/10.1021/jm501071f.
Bochno, M.; Berlicki, Ł. A Three-Component Synthesis of Aminomethylenebis-H-Phosphinates. Tetrahedron Lett 2014, 55 (1), 219–223. https://doi.org/10.1016/j.tetlet.2013.10.153.
2013
Benini, S.; Kosikowska, P.; Cianci, M.; Mazzei, L.; Vara, A. G.; Berlicki, Ł.; Ciurli, S. The Crystal Structure of Sporosarcina Pasteurii Urease in a Complex with Citrate Provides New Hints for Inhibitor Design. JBIC Journal of Biological Inorganic Chemistry 2013, 18 (3), 391–399. https://doi.org/10.1007/s00775-013-0983-7.
Wȩglarz-Tomczak, E.; Porȩba, M.; Byzia, A.; Berlicki, Ł.; Nocek, B.; Mulligan, R.; Joachimiak, A.; Dra̧g, M.; Mucha, A. An Integrated Approach to the Ligand Binding Specificity of Neisseria Meningitidis M1 Alanine Aminopeptidase by Fluorogenic Substrate Profiling, Inhibitory Studies and Molecular Modeling. Biochimie 2013, 95 (2), 419–428. https://doi.org/10.1016/j.biochi.2012.10.018.
Dra̧g, M.; Wieczerzak, E.; Pawełczak, M.; Berlicki, Ł.; Grzonka, Z.; Kafarski, P. Toward Very Potent, Non-Covalent Organophosphonate Inhibitors of Cathepsin C and Related Enzymes by 2-Amino-1-Hydroxy-Alkanephosphonates Dipeptides. Biochimie 2013, 95 (8), 1640–1649. https://doi.org/10.1016/j.biochi.2013.05.006.
Berlicki, L.; Kaske, M.; Gutiérrez-Abad, R.; Bernhardt, G.; Illa, O.; Ortuño, R. M.; Cabrele, C.; Buschauer, A.; Reiser, O. Replacement of Thr32 and Gln34 in the C -Terminal Neuropeptide y Fragment 25-36 by Cis -Cyclobutane and Cis -Cyclopentane β-Amino Acids Shifts Selectivity toward the Y4 Receptor. J Med Chem 2013, 56 (21), 8422–8431. https://doi.org/10.1021/jm4008505.
Forlani, G.; Berlicki, Ł.; Duò, M.; Dzièdzioła, G.; Giberti, S.; Bertazzini, M.; Kafarski, P. Synthesis and Evaluation of Effective Inhibitors of Plant Δ1-Pyrroline-5-Carboxylate Reductase. J Agric Food Chem 2013, 61 (28), 6792–6798. https://doi.org/10.1021/jf401234s.
2012
Forlani, G.; Petrollino, D.; Fusetti, M.; Romanini, L.; Nocek, B.; Joachimiak, A.; Berlicki, Ł.; Kafarski, P. Δ1-Pyrroline-5-Carboxylate Reductase as a New Target for Therapeutics: Inhibition of the Enzyme from Streptococcus Pyogenes and Effects in Vivo. Amino Acids 2012, 42 (6), 2283–2291. https://doi.org/10.1007/s00726-011-0970-7.
Berlicki, Ł.; Pilsl, L.; Wéber, E.; Mándity, I. M.; Cabrele, C.; Martinek, T. A.; Fülöp, F.; Reiser, O. Unique α,Β‐ and α,α,β,Β‐Peptide Foldamers Based on Cis ‐β‐Aminocyclopentanecarboxylic Acid. Angewandte Chemie International Edition 2012, 51 (9), 2208–2212. https://doi.org/10.1002/anie.201107702.
Berlicki, Ł.; Bochno, M.; Grabowiecka, A.; Białas, A.; Kosikowska, P.; Kafarski, P. N-Substituted Aminomethanephosphonic and Aminomethane-P-Methylphosphinic Acids as Inhibitors of Ureases. Amino Acids 2012, 42 (5), 1937–1945. https://doi.org/10.1007/s00726-011-0920-4.
Vassiliou, S.; Grabowiecka, A.; Kosikowska, P.; Berlicki, L. Three Component Kabachnik-Fields Condensation Leading to Substituted Aminomethane-P-Hydroxymethylphosphonic Acids as Atool for Screening of Bacterial Urease Inhibitors. Arkivoc 2012, 2012 (4), 33–43.
Górecki, L.; Berlicki, L.; Mucha, A.; Kafarski, P.; Łlepokura, K.; Rudzińska-Szostak, E. Phosphorylation as a Method of Tuning the Enantiodiscrimination Potency of Quinine-An NMR Study. Chirality 2012, 24 (4), 318–328. https://doi.org/10.1002/chir.22000.
2011
Kosikowska, P.; Berlicki, Ł. Urease Inhibitors as Potential Drugs for Gastric and Urinary Tract Infections: A Patent Review. Expert Opin Ther Pat 2011, 21 (6), 945–957. https://doi.org/10.1517/13543776.2011.574615.
Mucha, A.; Kafarski, P.; Berlicki, Ł. Remarkable Potential of the α-Aminophosphonate/Phosphinate Structural Motif in Medicinal Chemistry. J Med Chem 2011, 54 (17), 5955–5980. https://doi.org/10.1021/jm200587f.
2010
Rudzińska, E.; Dziędzioła, G.; Berlicki, Å.; Kafarski, P. Enantiodifferentiation of alpha-Hydroxyalkanephosphonic Acids in 31 P NMR with Application of alpha-Cyclodextrin as Chiral Discriminating Agent. Chirality 2010, 22 (1), 63–68. https://doi.org/10.1002/chir.20707.
Vassiliou, S.; Kosikowska, P.; Grabowiecka, A.; Yiotakis, A.; Kafarski, P.; Berlicki, Ł. Computer-Aided Optimization of Phosphinic Inhibitors of Bacterial Ureases. J Med Chem 2010, 53 (15), 5597–5606. https://doi.org/10.1021/jm100340m.
Occhipinti, A.; Berlicki, Ł.; Giberti, S.; Dziȩdzioła, G.; Kafarski, P.; Forlani, G. Effectiveness and Mode of Action of Phosphonate Inhibitors of Plant Glutamine Synthetase. Pest Manag Sci 2010, 66 (1), 51–58. https://doi.org/10.1002/ps.1830.
2009
Dąbrowska, E.; Burzyńska, A.; Mucha, A.; Matczak-Jon, E.; Sawka-Dobrowolska, W.; Berlicki, Ł.; Kafarski, P. Insight into the Mechanism of Three Component Condensation Leading to Aminomethylenebisphosphonates. J Organomet Chem 2009, 694 (23), 3806–3813. https://doi.org/10.1016/j.jorganchem.2009.07.025.
Rudzińska, E.; Berlicki, Ł.; Kafarski, P.; Lämmerhofer, M.; Mucha, A. Cinchona Alkaloids as Privileged Chiral Solvating Agents for the Enantiodiscrimination of N-Protected Aminoalkanephosphonates—a Comparative NMR Study. Tetrahedron Asymmetry 2009, 20 (23), 2709–2714. https://doi.org/10.1016/j.tetasy.2009.11.003.
2008
Vassiliou, S.; Grabowiecka, A.; Kosikowska, P.; Yiotakis, A.; Kafarski, P.; Berlicki, Ł. Design, Synthesis, and Evaluation of Novel Organophosphorus Inhibitors of Bacterial Ureases. J Med Chem 2008, 51 (18), 5736–5744. https://doi.org/10.1021/jm800570q.
Forlani, G.; Occhipinti, A.; Berlicki, Ł.; Dziedzioła, G.; Wieczorek, A.; Kafarski, P. Tailoring the Structure of Aminobisphosphonates To Target Plant P5C Reductase. J Agric Food Chem 2008, 56 (9), 3193–3199. https://doi.org/10.1021/jf800029t.
2007
Berlicki, Ł.; Mucha, A.; Kafarski, P. A Mild and Convenient Oxidation of H-Phosphinic Acids. Pol J Chem 2007, 81 (11), 1959–1962.
Kafarski, P.; Mlynarz, P.; Rudzinska, E.; Berlicki, L. Organophosphorus Supramolecular Chemistry. Part 2. Organophosphorus Receptors. Curr Org Chem 2007, 11 (18), 1593–1609. https://doi.org/10.2174/138527207783221192.
Rudzińska, E.; Berlicki, Ł.; Mucha, A.; Kafarski, P. Analysis of PD‐Dependent Complexation of N ‐benzyloxycarbonylaminophosphonic Acids by Α‐cyclodextrin. Enantiodifferentiation of Phosphonic Acid p K a Values. Chirality 2007, 19 (10), 764–768. https://doi.org/10.1002/chir.20450.
Forlani, G.; Giberti, S.; Berlicki, Ł.; Petrollino, D.; Kafarski, P. Plant P5C Reductase as a New Target for Aminomethylenebisphosphonates. J Agric Food Chem 2007, 55 (11), 4340–4347. https://doi.org/10.1021/jf0701032.
Rudzińska, E.; Berlicki, Ł.; Mucha, A.; Kafarski, P. Chiral Discrimination of Ethyl and Phenyl N-Benzyloxycarbonylaminophosphonates by Cyclodextrins. Tetrahedron Asymmetry 2007, 18 (13), 1579–1584. https://doi.org/10.1016/j.tetasy.2007.06.021.
Rudzińska, E.; Poliwoda, A.; Berlicki, Ł.; Mucha, A.; Dżygiel, P.; Wieczorek, P. P.; Kafarski, P. Enantiodifferentiation of N-Benzyloxycarbonylaminophosphonic and Phosphinic Acids and Their Esters Using Cyclodextrins by Means of Capillary Electrophoresis. J Chromatogr A 2007, 1138 (1–2), 284–290. https://doi.org/10.1016/j.chroma.2006.10.065.
2006
Berlicki, L.; Rudziska, E.; Mlynarza, P.; Kafarski, P. Organophosphorus Supramolecular Chemistry Part 1. Receptors for Organophosphorus Compounds. Curr Org Chem 2006, 10 (18), 2285–2306. https://doi.org/10.2174/138527206778992699.
Berlicki, Ł.; Kafarski, P. Computer-Aided Analysis of the Interactions of Glutamine Synthetase with Its Inhibitors. Bioorg Med Chem 2006, 14 (13), 4578–4585. https://doi.org/10.1016/j.bmc.2006.02.022.
Forlani, G.; Obojska, A.; Berlicki, Ł.; Kafarski, P. Phosphinothricin Analogues as Inhibitors of Plant Glutamine Synthetases. J Agric Food Chem 2006, 54 (3), 796–802. https://doi.org/10.1021/jf0526285.
2005
Berlicki, L.; Kafarski, P. Computer-Aided Analysis and Design of Phosphonic and Phosphinic Enzyme Inhibitors as Potential Drugs and Agrochemicals. Curr Org Chem 2005, 9 (18), 1829–1850. https://doi.org/10.2174/138527205774913088.
Berlicki, Ł.; Obojska, A.; Forlani, G.; Kafarski, P. Design, Synthesis, and Activity of Analogues of Phosphinothricin as Inhibitors of Glutamine Synthetase. J Med Chem 2005, 48 (20), 6340–6349. https://doi.org/10.1021/jm050474e.
Berlicki, Ł.; Rudzińska, E.; Mucha, A.; Kafarski, P. Cyclodextrins as NMR Probes in the Study of the Enantiomeric Compositions of N-Benzyloxycarbonylamino-Phosphonic and Phosphinic Acids. Tetrahedron Asymmetry 2004, 15 (10), 1597–1602. https://doi.org/10.1016/j.tetasy.2004.03.037.
Obojska, A.; Berlicki, L.; Kafarski, P.; Lejczak, B.; Chicca, M.; Forlani, G. Herbicidal Pyridyl Derivatives of Aminomethylene-Bisphosphonic Acid Inhibit Plant Glutamine Synthetase. J Agric Food Chem 2004, 52 (11), 3337–3344. https://doi.org/10.1021/jf049843q.
2003
Berlicki, Ł.; Rudzińska, E.; Kafarski, P. Enantiodifferentiation of Aminophosphonic and Aminophosphinic Acids with α- and β-Cyclodextrins. Tetrahedron Asymmetry 2003, 14 (11), 1535–1539. https://doi.org/10.1016/S0957-4166(03)00273-8.
2002
Berlicki, Ł.; Kafarski, P. The Use of Molecular Modelling for Comparison of Three Possible Modes of Action of Herbicidally Active Derivatives of Aminomethylenebisphosphonic Acid. Pestic Biochem Physiol 2002, 73 (2), 94–103. https://doi.org/10.1016/S0048-3575(02)00026-3.