Departments

Evaluation of transient protein states, Project code J1-4400

Principal investigator: prof. dr. Simona Golič Grdadolnik

       1. PROJECT SUMMARY:

Despite recent advances in biophysical techniques and computational approaches for the investigation of biomolecular systems, the characterization of the dynamic equilibria of protein states remains a demanding challenge due to the elusive nature of the dynamic processes that regulate these equilibria. In particular, the sparsely populated, transient states are difficult to characterize at the atomic level because they are "invisible" to the biophysical methods that detect protein states with the lowest energy or the highest abundance. There is growing evidence for the importance of transient, thermally accessible protein states in the biological function of proteins.

The main goal of the proposed project is to develop a combined experimental and theoretical approach for the physicochemical characterization at the atomic level of transient protein states close to physiological conditions in aqueous environments. The characterization will allow to relate them to the specific dynamic event that is important for their function. To overcome the problems of averaging and signal assignment, a combination of solution NMR and vibrational spectroscopy operating on different time scales will be used. Together, these spectroscopies can provide access to transient molecular states in dynamic exchange on time scales from picoseconds to milliseconds. To obtain a model-based understanding of the correlation between each type of motion and its effect on dynamic equilibria of states, we will use atomistic molecular dynamic simulations. Algorithms for numerical analysis of the correlation between experimental and computational results will be developed to understand the influence of the individual contributions of the coupled motions on the distribution of protein states. Proteins of different families will be studied, covering a wide range of dynamic events that can cause transitions between thermally accessible protein states. The functional role of the selected proteins in biological processes cannot be comprehensively understood without examining the dynamic equilibria between their possible states without and/or with their binding partners. The expected results may provide presently unforeseen insights into the function of these proteins in health and disease. 

The developed approach will be widely applicable to the characterization of transient protein states at the atomic level in aqueous environments. The results of the proposed studies can contribute significantly to the understanding of protein function in health and disease and will be of great interest to many specific research areas, such as molecular recognition, molecular signal transduction, enzyme catalysis, protein folding and binding, and target-based design and drug discovery.

Participating organizations: 

• University of Ljubljana, Faculty of Pharmacy

                 - basic information regarding financing

The project is co-financed by ARRS with 2481 annual hours of price class B for a period of 3 years. Funding starts on October 1, 2022.

                 - composition of the project group with links to SICRIS

At the National Institute of Chemistry, the project group includes:

At the Faculty of Pharmacy (University of Ljubljana), the project group includes:

       2. phases of the project and their realization

Work was organized into three work packages (WP). 

WP1: Identification and evaluation of transient conformational states of aegerolysins with intrinsically disordered regions.

This work package addressed the role of protein dynamics and intrinsically disordered regions (IDRs) in aegerolysins relevant for lipid interactions. During the reporting period, complete backbone and side‑chain NMR chemical shift assignments were obtained for two target proteins: the atypical aegerolysin fusver and the Nep1‑like protein NLPPp. Based on experimentally derived NMR restraints (interproton distances and dihedral angles), high‑resolution solution structures were determined for both proteins. The originally planned protein phiatt was replaced by NLPPp due to insufficient stability, allowing full completion of the objectives within the project timeframe.

Both proteins exhibit a combination of structured and intrinsically disordered regions. Comparison of solution NMR structures with predicted or crystallographic models revealed pronounced deviations in regions implicated in biological function, highlighting limitations of static structural descriptions. NMR relaxation measurements provided clear evidence for μs–ms timescale conformational exchange in both proteins, demonstrating that dynamic processes are intrinsic to their functional states.

For fusver, AlphaFold2 predicted the formation of an N‑terminal α‑helix with potential membrane‑interaction capability. In contrast, solution NMR data showed that this region remains intrinsically disordered and is characterized by enhanced ps–ns dynamics without detectable μs–ms ordering. These results demonstrate that static structure prediction does not capture dynamic behaviour relevant to function in this system.

In the case of NLPPp, combined NMR relaxation analyses and molecular dynamics simulations indicated that functional disorder arises predominately from μs–ms conformational exchange rather than fast ps–ns flexibility. The results support a conformational selection mechanism underlying lipid binding. Based on these findings, originally planned vibrational spectroscopy experiments were replaced by targeted NMR interaction studies. Lipid binding did not measurably affect the conformational exchange process, but induced chemical shift perturbations in regions not previously associated with binding, revealing additional protein regions relevant for lipid interaction.

WP2: Identification and evaluation of transient conformational states of MurD related to substrate and inhibitor binding.

The aim of this work package was to characterize conformational dynamics of the bacterial enzyme MurD and their relevance for ligand recognition and inhibition. Complete methyl group (AILV^proR) NMR assignments were achieved, together with ¹³C methyl and ¹⁵N backbone relaxation measurements for MurD in its free form and in complexes with substrates and inhibitors. This enabled comprehensive coverage of both the protein backbone and hydrophobic cores for dynamic analysis.

Extensive molecular dynamics simulations were performed for all relevant states. Integration of experimental NMR relaxation data with computational analyses led to the development of a novel, unbiased methodology for identifying specific dynamic mechanisms directly from relaxation parameters. The approach provided improved prediction of μs–ms conformational exchange compared to commonly used methods and was independently validated using NMR CPMG relaxation dispersion experiments.

The results revealed pronounced dynamic heterogeneity and multiple transient conformational states within MurD–substrate and MurD–inhibitor complexes. These findings rationalize earlier difficulties in designing effective MurD inhibitors based exclusively on static crystallographic structures. The data provide concrete guidelines for structure‑based design strategies that explicitly incorporate protein dynamics and support the development of multitarget Mur inhibitors.

Furthermore, the study uncovered a previously unrecognized dynamic feature of MurD suggestive of an allosteric regulatory mechanism. Collective motions on the μs–ms timescale were detected in regions distant from ligand‑binding sites, connected through loop regions exhibiting ps–ns flexibility. This behavior indicates the presence of an internal dynamic network. Recent independent studies (2025) reporting modulation of MurD activity through protein–protein interactions further reinforce the relevance of these findings and highlight protein dynamics as a key determinant of MurD regulation. Methodological advances developed in this work package were successfully transferred, in collaboration with project partners, to the design of new structural classes of inhibitors targeting HSP90.

WP3: Identification and evaluation of transient conformational states of NGF related to the binding of small endogenous ligands.

This work package focused on elucidating how small endogenous ligands modulate the structural and functional states of nerve growth factor (NGF) and its precursor proNGF. Using an integrated biophysical approach combining NMR spectroscopy, vibrational spectroscopy, molecular dynamics simulations, and small‑angle X‑ray scattering (SAXS), ligand binding was characterized at atomic resolution. SAXS measurements were performed in collaboration with international partners at the CNR Institute of Crystallography.

We demonstrated that ATP binds selectively to the intrinsically disordered propeptide region of proNGF and induces a global conformational rearrangement that inhibits proteolytic maturation into NGF. This identifies ATP as an allosteric modulator of proNGF. Considering that extracellular ATP concentrations are elevated under pathological conditions, this mechanism represents a plausible stress‑responsive regulatory pathway affecting the proNGF:NGF balance, previously associated with cognitive dysfunction. In contrast, ATP binding to mature NGF was significantly weaker and did not result in detectable global conformational changes.

The interaction of NGF with the two most abundant brain lysophosphatidylserines (LysoPS 18:0 and LysoPS 18:1) was also characterized. Due to solubility constraints, lipids were introduced via DMSO‑d₆, necessitating prior characterization of specific DMSO–NGF interactions. Selected systems were further analyzed using ¹⁵N NMR relaxation measurements. No μs–ms conformational exchange was detected in NGF regions involved in ligand binding or receptor recognition. Functional assays showed that lipid binding had only a weak effect on NGF interaction with the TrkA and p75^NTR receptors, while the contribution of DMSO itself was negligible.

       3. bibliographic references that derive directly from the implementation of the project

           Original scientific articles:

1. OGRIS, Iza, ZUPANČIČ, Barbara, SOSIČ, Izidor, MERZEL, Franci, GOLIČ GRDADOLNIK, Simona. Mechanistic insight into the dynamics of Mur ligase through a comprehensive timescale-specific approach. Communications chemistry. 2025, vol. 8, [article no.] 285. https://www.nature.com/articles/s42004-025-01675-z, DOI: 10.1038/s42004-025-01675-z. [COBISS.SI-ID 250979587]

2. PAOLETTI, Francesca, GORIČAN, Tjaša, CASSETTA, Alberto, GRDADOLNIK, Jože, TOPORASH, Mykola, LAMBA, Doriano, GOLIČ GRDADOLNIK, Simona, COVACEUSZACH, Sonia. Unveiling the solvent effect : DMSO interaction with human nerve growth factor and its implications for drug discovery. Molecules. 2025, vol. 30, iss. 14, [article no.] 3030. https://www.mdpi.com/1420-3049/30/14/3030, DOI: 10.3390/molecules30143030. [COBISS.SI-ID 244001795]

3. VENIANAKIS, Themistoklis, GORIČAN, Tjaša, PAPAMOKOS, Georgios, GOLIČ GRDADOLNIK, Simona, SISKOSA, Michael G., GEROTHANASSIS, Ioannis P. Are the pKₐ values of free fatty acids in aqueous solution abnormally high? An NMR and computational perspective. Chemical communications. 2025, vol. 61, iss. 100, str. 19890-19893. https://pubs.rsc.org/en/content/articlelanding/2025/cc/d5cc05822h. [COBISS.SI-ID 261330435] 

4. DERNOVŠEK, Jaka, ZAJEC, Živa, POJE, Goran, URBANČIČ, Dunja, GORIČAN, Tjaša, GOLIČ GRDADOLNIK, Simona, MLINARIČ-RAŠČAN, Irena, COTMAN, Andrej Emanuel, ZIDAR, Nace, TOMAŠIČ, Tihomir, et al. Exploration and optimisation of structure-activity relationships of new triazole-based C-terminal Hsp90 inhibitors towards in vivo anticancer potency. Biomedicine & pharmacotherapy.. 2024, vol. 177, [article no.] 16941 https://www.sciencedirect.com/science/article/pii/S0753332224008254, DOI: 10.1016/j.biopha.2024.116941. [COBISS.SI-ID 199197699].

5. ZAJEC, Živa, DERNOVŠEK, Jaka, CINGL, Jernej, OGRIS, Iza, GEDGAUDAS, Marius, ZUBRIENÉ, Asta, MITROVIĆ, Ana, GOLIČ GRDADOLNIK, Simona, GOBEC, Martina, TOMAŠIČ, Tihomir. New class of Hsp90 C-terminal domain inhibitors with anti-tumor properties against triple-negative breast cancer. Journal of medicinal chemistry. [Online ed.]. 2024, vol. 67, no. 15, str. 12984-13018. https://pubs.acs.org/doi/10.1021/acs.jmedchem.4c00932, DOI: 10.1021/acs.jmedchem.4c00932. [COBISS.SI-ID 203626243]

6. VENIANAKIS, Themistoklis, PARISIS, Nikolaos, CHRISTOU, Atalanti, GOULAS, Vlasios, NIKOLOUDAKIS, Nikolaos, BOTSARIS, George, GORIČAN, Tjaša, GOLIČ GRDADOLNIK, Simona, TZAKOS, Andreas G., GEROTHANASSIS, Ioannis P. Phytochemical analysis and biological evaluation of carob leaf (Ceratonia siliqua L.) crude extracts using NMR and mass spectroscopic techniques. Molecules. 2024, vol. 29, no. 22, [article no.] 5273. https://www.mdpi.com/1420-3049/29/22/5273, DOI: 10.3390/molecules29225273. [COBISS.SI-ID 214778371]

7. PAOLETTI, Francesca, COVACEUSZACH, Sonia, CASSETTA, Alberto, CALABRESE, Antonio N., NOVAK, Urban, KONAREV, Peter, GRDADOLNIK, Jože, LAMBA, Doriano, GOLIČ GRDADOLNIK, Simona. Distinct conformational changes occur within the intrinsically unstructured pro-domain of pro-Nerve Growth Factor in the presence of ATP and Mg2+. Protein science. vol. 32, iss. 2, e4563. https://onlinelibrary.wiley.com/doi/epdf/10.1002/pro.4563 DOI:  10.1002/pro.4563. [COBISS.SI-ID 139671043]

8. DIAMANTIS, Dimitrios A., TSIAILANIS, Antonios D., PAPAEMMANOUIL, Christina, NIKA, Maria-Christina, KANAKI, Zoi, GOLIČ GRDADOLNIK, Simona, BABIČ, Andrej, TZAKOS, Eleftherios Paraskevas, FOURNIER, Isabelle, SALZET, Michel, KUSHWAHA, Prem Prakash, THOMAIDIS, Nikolaos S., RAMPIAS, Theodoros, SHANKAR, Eswar, KARAKURT, Serdar, GUPTA, Sanjay Kumar, TZAKOS, Andreas G. Development of a novel apigenin prodrug programmed for alkaline-phosphatase instructed self-inhibition to combat cancer. Journal of biomolecular structure & dynamics. 2023, str. 1-22, https://www.tandfonline.com/doi/epdf/10.1080/07391102.2023.2247083?needAccess=true&role=buttonDOI: 10.1080/07391102.2023.2247083. [COBISS.SI-ID 163337219]

Invited lectures:

1. GOLIČ GRDADOLNIK, Simona. NMR-assisted development of muramyl ligase inhibitors: toward new antibacterial agents : invited lecture at Round table on “Solution NMR applications in molecular biophysics”, March 27, 2026, Institute of Crystallography-C.N.R., Trieste, Italy. [COBISS.SI-ID 274517251]

2. OGRIS, Iza, ZUPANČIČ, Barbara, MERZEL, Franci, GOLIČ GRDADOLNIK, Simona. Mechanistic insights into the dynamics of an antibiotic target revealed by NMR relaxation. V: Mini symposium at establishment of a collaboration between National Institute of Chemistry (NIC) and Institute of Crystallography (IC), CNR : May 7, 2025, Grand lecture hall, National Institute of Chemistry, Ljubljana: Book of abstracts. https://www.ki.si/fileadmin/user_upload/datoteke-splosno/Novice/2022/Book_of_Abstracts.pdf. [COBISS.SI-ID 236087299]

3. GOLIČ GRDADOLNIK, Simona. NMR-assisted studies of ligand-protein interactions in solution : joint workshop between Istituto di Cristallografia (CNR) and Kemijski inštitut : Integrative structural biology: 21. 6. 2023 [COBISS.SI-ID 157436675]

Presentations at conferences:

1. OGRIS, Iza, ZUPANČIČ, Barbara, MERZEL, Franci, GOLIČ GRDADOLNIK, Simona. Exploring mur ligase dynamics across timescales : implications for mechanism and inhibitor design. V: NMR: a tool for biology: 14th International Conference : May 26-28, 2025 : Paris, France. 2025. Str. 107. https://www.nmr2025.conferences-pasteur.org/images/public/Programme-book-NMR2025.pdf. [COBISS.SI-ID 239584259]
2. GORIČAN, Tjaša, ZUPANČIČ, Barbara, ANDERLUH, Gregor, GOLIČ GRDADOLNIK, Simona. Investigation of the structure and dynamics of an atypical aegerolysin. V: NMR: a tool for biology: 14th International Conference : May 26-28, 2025 : Paris, France. 2025. Str. 99. https://www.nmr2025.conferences-pasteur.org/images/public/Programme-book-NMR2025.pdf. [COBISS.SI-ID 239595523]
3. GORIČAN, Tjaša, DERNOVŠEK, Jaka, OGRIS, Iza, ZAJEC, Živa, TOMAŠIČ, Tihomir, GOLIČ GRDADOLNIK, Simona. The binding of new structural classes of C-terminal inhibitors to P20 human Hsp90 studied by ligand-based NMR methods. V: ANDERLUH, Gregor (ur.), CRNKOVIĆ, Ana (ur.). 3rd MOSBRI Scientific Conference : 10th - 13th June 2024, Ljubljana, Slovenia : programme & abstracts. Str.129. https://www.mosbri.eu/events/conferences/ljubljana-2024/programme-ljubljana/. [COBISS.SI-ID 199722499]
4. PAOLETTI, Francesca, MERZEL, Franci, COVACEUSZACH, Sonia, CASSETTA, Alberto, CALABRESE, Antonio N., OGRIS, Iza, NOVAK, Urban, GRDADOLNIK, Jože, LAMBA, Doriano, GOLIČ GRDADOLNIK, Simona. Differential interactions between ATP and NGF/proNGF revealed P32 ATP as modulator of Neurotrophins biological activity. V: ANDERLUH, Gregor (ur.), CRNKOVIĆ, Ana (ur.). 3rd MOSBRI Scientific Conference : 10th - 13th June 2024, Ljubljana, Slovenia : programme & abstracts. Str. 141. https://www.mosbri.eu/events/conferences/ljubljana-2024/programme-ljubljana/. [COBISS.SI-ID 199723779]
5. OGRIS, Iza, ZUPANČIČ, Barbara, HERLAH, Barbara, PERDIH, Andrej, MERZEL, Franci, GOLIČ GRDADOLNIK, Simona. Exploring the impact of MurD conformational dynamics on ligand P21 binding with NMR and MD simulations. V: ANDERLUH, Gregor (ur.), CRNKOVIĆ, Ana (ur.). 3rd MOSBRI Scientific Conference : 10th - 13th June 2024, Ljubljana, Slovenia : programme & abstracts. Ljubljana: National Institute of Chemistry, 2024. Str. 130. https://www.mosbri.eu/events/conferences/ljubljana-2024/programme-ljubljana/. [COBISS.SI-ID 199722755]
6. GORIČAN, Tjaša, DERNOVŠEK, Jaka, OGRIS, Iza, ZAJEC, Živa, TOMAŠIČ, Tihomir, GOLIČ GRDADOLNIK, Simona. Interactions between new structural classes of C-terminal inhibitors and human Hsp90 investigated by ligand-based NMR methods. V: AILM2024 : Advanced Isotope Labelling Methods for Integrated Structural Biology : May 28-31, Grenoble, France. 2024. Str. 65. https://www.ailm2024.org/. [COBISS.SI-ID 200680451]
7. DERNOVŠEK, Jaka, GORIČAN, Tjaša, ZAJEC, Živa, TRUNKELJ, Natalija, ZIDAR, Nace, ILAŠ, Janez, URBANČIČ, Dunja, ZUBRIENÉ, Asta, MATULIS, Daumantas, GOLIČ GRDADOLNIK, Simona, TOMAŠIČ, Tihomir. New N- and C-terminal Hsp90 inhibitors with anticancer activity and without heat shock response induction. V: Book of abstracts : 4th Alpine Winter Conference on Medicinal and Synthetic Chemistry, St. Anton, Austria, January 28-February 1, 2024. Str. 99, p013, https://www.alpinewinterconference.org/auth.php?langue=english&cle_menus=1049119092&ant_file_redirect=content.php%3Flangue%3Denglish%26amp%3Bcle_menus%3D1238918051. [COBISS.SI-ID 199446531]
8. DERNOVŠEK, Jaka, ZAJEC, Živa, URBANČIČ, Dunja, STURTZEL, Caterina, GORIČAN, Tjaša, CINGL, Jernej, GRISSENBERGER, Sarah, GOLIČ GRDADOLNIK, Simona, ZIDAR, Nace, DISTEL, Martin, TOMAŠIČ, Tihomir, et al. Development of allosteric Hsp90 inhibitors for the treatment of Ewing sarcoma. V: Book of abstracts : EFMC ISMC : International Symposium on Medicinal Chemistry, Rome, Italy, September 1-5, 2024. Str. 519, p645. https://www.efmc-ismc.org/v2/data/1725266112EFMC-ISMC-2024-BoA-web-FINAL.pdf. [COBISS.SI-ID 206896643]
9. DERNOVŠEK, Jaka, ZAJEC, Živa, URBANČIČ, Dunja, STURTZEL, Caterina, GORIČAN, Tjaša, CINGL, Jernej, GRISSENBERGER, Sarah, GOLIČ GRDADOLNIK, Simona, ZIDAR, Nace, DISTEL, Martin. Development of Hsp90 C-terminal domain inhibitors for the treatment of Ewing sarcoma. V: Molecular chaperones in cancer and protein quality control : CNIO – CaixaResearch Frontiers Meeting : Madrid, 10th – 12th June, 2024. CNIO – CaixaResearch Frontiers Meeting eMadrid, 10th – 12th June, 2024. Str. 133. https://apps.cnio.es/eventos/descargas/CFM/1306333_1750,32_booklet.pdf. [COBISS.SI-ID 209870595]
10. DERNOVŠEK, Jaka, ZIDAR, Nace, ZAJEC, Živa, GORIČAN, Tjaša, GOLIČ GRDADOLNIK, Simona, STURTZEL, Caterina, GRISSENBERGER, Sarah, DISTEL, Martin, COTMAN, Andrej Emanuel, TOMAŠIČ, Tihomir. Triazolni C-končni zaviralci Hsp90 : od β-CF [sub] 3 benzilnih alkoholov do serije zaviralcev s protitumornim delovanjem. V: PINTAR, Albin (ur.). Slovenski kemijski dnevi 2024 : zbornik povzetkov = book of abstracts : 30 let = 30 years : 18.-20. september 2024, Bernardin, Portorož. Elektronska izd. Ljubljana: Slovensko kemijsko društvo, 2024. Str. 74. https://skd2024.chem-soc.si/wp-content/uploads/2024/08/SKD-2024-Zbornik-povzetkov_compressed.pdf. [COBISS.SI-ID 210715907]
11. PAOLETTI, Francesca, MERZEL, Franci, COVACEUSZACH, Sonia, CASSETTA, Alberto, CALABRESE, Antonio N., OGRIS, Iza, NOVAK, Urban, KONAREV, Peter, GRDADOLNIK, Jože, LAMBA, Doriano, GOLIČ GRDADOLNIK, Simona. Differential interactions between ATP and NGF / proNGF: chance or necessity? V: 62° congress SIB : 7-9 September [2023], Firenze : abstract book. Str. 42. https://www.congressosib2023.it/wp-content/uploads/2023/09/Abstract-Book_CongressoSIB-2023.pdf, https://www.congressosib2023.it/abstract-book/. [COBISS.SI-ID 176813315]
12. ŽIBRAT, Nika, PODOBNIK, Marjetka, GOLIČ GRDADOLNIK, Simona, ANDERLUH, Gregor. Phytophthora parasitica NLP shares three-dimensional fold and pore-forming activity of model Nep1-like protein, NLPPya. V: SEPČIĆ, Kristina (ur.), PAVŠIČ, Miha (ur.). 15th Meeting of the Slovenian Biochemical Society with International Participation = 15. srečanje Slovenskega biokemijskega društva z mednarodno udeležbo: book of abstracts = zbornik povzetkov : Portorož, 20-23 September 2023 = [20.–23. september 2023, Portorož, Slovenija]. Ljubljana: Slovenian Biochemical Society: = Slovensko biokemijsko društvo, 2023. Str. 171. https://portoroz2023.sbd.si/upload/docs/SBD2023_Portoroz-Book_of_Abstracts.pdf. [COBISS.SI-ID 170124035]
13. HERLAH, Barbara, OGRIS, Iza, GOLIČ GRDADOLNIK, Simona, SOSIČ, Izidor, GOBEC, Stanislav, PERDIH, Andrej. Simulation-based optimization of 4,6-substituted-1,3,5-triazin-2(1H)-ones as catalytic inhibitors of the human DNA Topoisomerase IIΑ. V: Abstracts book : Lisbon 2023, at the edge of Europe and Science. [S. l.]: [s. n.], 2023. Str. 88. https://annualmeeting.eufeps.org/programme.html. [COBISS.SI-ID 156434691].
14. DERNOVŠEK, Jaka, GORIČAN, Tjaša, ZAJEC, Živa, ZIDAR, Nace, ILAŠ, Janez, URBANČIČ, Dunja, ZUBRIENÉ, Asta, MATULIS, Daumantas, GOLIČ GRDADOLNIK, Simona, TOMAŠIČ, Tihomir. Development of new HSP90β-selective inhibitors based on topoisomerase II ligands. V: JAKOPIN, Žiga (ur.), TOMAŠIČ, Tihomir (ur.). Crossing the Boundaries of Medicinal Chemistry: book of abstracts: University of Ljubljana, Faculty of Pharmacy, September 28, 2023. Ljubljana: Fakulteta za farmacijo, 2023. Str. 21 https://www.ffa.uni-lj.si/docs/default-source/e-knjige/book-of-abstracts---crossing-the-boundaries-of-medicinal-chemistry.pdf?sfvrsn=2. [COBISS.SI-ID 173421059]
15. HERLAH, Barbara, OGRIS, Iza, GOLIČ GRDADOLNIK, Simona, GOBEC, Stanislav, SOSIČ, Izidor, PERDIH, Andrej. Structure-based optimization of 4,6-substituted-1,3,5-triazin2(1H)-ones as catalytic inhibitors of human DNA topoisomerase IIα. V: PINTAR, Albin (ur.). Slovenski kemijski dnevi 2023 = 29th Annual Meeting of the Slovenian Chemical Society: zbornik povzetkov = book of abstracts: 13.-15. september 2023, Portorož, Portorose, Slovenija. Ljubljana: Slovensko kemijsko društvo, 2023. Str. 118. https://www.conftool.org/scs-annual-meeting-2023/index.php?page=browseSessions&form_session=47#paperID119, https://www.conftool.org/scs-annual-meeting-2023/index.php/Herlah-Structure-based_optimization_of_4%2C6-substituted-1%2C3%2C5-triazin-2-119.pdf?page=downloadPaper&filename=Herlah-Structure-based_optimization_of_4%2C6-substituted-1%2C3%2C5-triazin-2-119.pdf&form_id=119. [COBISS.SI-ID 167932931]