“We acknowledge the MCB Structural Biology Core Facility for valuable support.”
We’d also appreciate a short e-mail notification when your article gets published.
The use of the HZB facilities and the allocation of beamtime must be properly mentioned in any publication based on experiments perfomed at HZB. Please state in the experimental section of the paper: “Measurements were carried out at the XX instrument (beamline/station) at Helmholtz-Zentrum Berlin.”
Please state in the acknowledgements “We thank HZB for the allocation of neutron/synchrotron radiation beamtime.”
We acknowledge the European Synchrotron Radiation Facility (ESRF) for provision of synchrotron radiation facilities under proposal ID ### and on beamline(s) ###. We thank NAME(s) for assistance and support during the beamtime.
https://www.esrf.fr/UsersAndScience/UserGuide/Publications
Data collected at ESRF beamlines are assigned with DOI and will be realeased publicaly after 3-year embargo period. For acknoledgement please contact us to provide the respective session DOI for your published data.
https://www.esrf.fr/datapolicy
We acknowledge the MAX IV Laboratory for beamtime on the [insert Beamline name here] beamline under proposal [insert proposal ID here]. Research conducted at MAX IV, a Swedish national user facility, is supported by Vetenskapsrådet (Swedish Research Council, VR) under contract 2018-07152, Vinnova (Swedish Governmental Agency for Innovation Systems) under contract 2018-04969 and Formas under contract 2019-02496.
https://www.maxiv.lu.se/user-access/practical-information/user-policies/
1. Chrzanowski J, Nowicka J, Koralewski R, Joachimiak L, Gzik A, Borek B, Brzezinska J, Kusmirek D, Olejniczak S, Matyszewski K, Mazur M, Olczak J, Glatt S, Grudnik P, Wilk P, Muchowicz A, Kikulska A, Gluchowska KM, Drzewicka K, Belczyk-Ciesielska A, Wachowska M, Sipak-Bujanowicz Z, Mulewski K, Tkaczyk A, Rejczak T, Golebiowski A, Zaslona Z, Blaszczyk R.; Structure-Guided Discovery of OAT-4828 as Potent, Selective, and Orally Bioavailable USP7 Inhibitor with In Vivo Antileukemic Activity. J Med Chem 10.1021/acs.jmedchem.6c00407
2. Wilk P, Wątor-Wilk E, Muszak D, Kochanowski P, Krojer T, Grudnik P.; Crystallographic fragment screening supports tool compound discovery and reveals conformational flexibility in human deoxyhypusine synthase. Communications Chemistry 10.1038/s42004-026-01897-9
1. Wątor E, Rutkiewicz M, Weiss MS, Wilk P.; Co-expression with chaperones can affect protein 3D structure as exemplified by loss-of-function variants of human prolidase. FEBS Lett 10.1002/1873-3468.13877
2. Wątor E, Wilk P, Grudnik P.; Half Way to Hypusine-Structural Basis for Substrate Recognition by Human Deoxyhypusine Synthase. Biomolecules 10.3390/biom10040522
3. Janczak M, Hyz K, Bukowski M, Lyzen R, Hydzik M, Wegrzyn G, Szalewska-Palasz A, Grudnik P, Dubin G, Wladyka B.; Chromosomal localization of PemIK toxin-antitoxin system results in the loss of toxicity – Characterization of pemIKSa1-Sp from Staphylococcus pseudintermedius. Microbiol Res. 10.1016/j.micres.2020.126529
4. Krutyhołowa R, Reinhardt-Tews A, Chramiec-Głąbik A, Breunig KD, Glatt S.; Fungal Kti12 proteins display unusual linker regions and unique ATPase p-loops. Curr Genet 10.1007/s00294-020-01070-2
5. Kluza A, Wojdyla Z, Mrugala B, Kurpiewska K, Porebski PJ, Niedzialkowska E, Minor W, Weiss MS, Borowski T.; Regioselectivity of hyoscyamine 6β-hydroxylase-catalysed hydroxylation as revealed by high-resolution structural information and QM/MM calculations. Dalton Trans. 10.1039/d0dt00302f
1. Krysiak K, Grudnik P, Glatt S.; Structural and functional insights into the Elongator complex. Nucleic Acids Res. 10.1093/nar/gkae165
2. Musiał B, Skalniak Ł, Holak TA, Grudnik P.; Recent advances in PD-1/PD-L1 protein–protein interaction inhibitors. Int J Biol Macromol. 10.1016/j.ijbiomac.2024.131392
3. Wilk P, Grudnik P, Wątor-Wilk E.; Structural characterization of human deoxyhypusine synthase variants. bioRxiv 10.1101/2024.04.12.589215
4. Nowak M, Kluza A, Borowski T.; Structural biology approaches in plant stress signaling. Front Plant Sci. 10.3389/fpls.2024.1343980
5. Kaczmarek M, Glatt S, Grudnik P.; Analytical strategies for structural characterization of biomolecular complexes. Trends Anal Chem. 10.1016/j.trac.2024.117716
6. Wątor E, Weiss MS, Wilk P.; Advances in prolidase structural studies and molecular chaperone interactions. Int J Biol Macromol. 10.1016/j.ijbiomac.2024.130136
7. Skalniak Ł, Holak TA, Musielak B.; Small-molecule modulation of immune checkpoint signaling. MedChemComm 10.1039/D3MD00746D
8. Grudnik P, Wilk P, Glatt S.; Structural basis of substrate recognition in human deoxyhypusine synthase. Nat Commun. 10.1038/s41467-024-48251-y
9. Muchowicz A, Kikulska A, Grudnik P.; Discovery of selective USP7 inhibitors with antileukemic activity. ACS Med Chem Lett. 10.1021/acsmedchemlett.4c00042
10. Wątor-Wilk E, Wilk P, Grudnik P.; Crystallographic fragment screening for deoxyhypusine synthase inhibitor discovery. Acta Crystallogr D Struct Biol. 10.1107/S2059798324006594
11. Wilk P, Grudnik P, Weiss MS.; Structural studies of hypusination pathway enzymes. bioRxiv 10.1101/2024.06.20.599981
12. Grudnik P, Glatt S.; Functional implications of Elongator-associated ATPases. FEBS J. 10.1111/febs.17207
13. Wątor E, Wilk P, Grudnik P.; Structural determinants of substrate specificity in human deoxyhypusine synthase. bioRxiv 10.1101/2024.08.15.608090
14. Kaczmarek P, Holak TA, Skalniak Ł.; Functional polymers for biomolecular targeting applications. Macromol Rapid Commun. 10.1002/marc.202400712
15. Grudnik P, Wilk P, Glatt S.; Molecular basis of deoxyhypusine synthase regulation. Proc Natl Acad Sci USA 10.1073/pnas.2407398121
16. Wątor-Wilk E, Weiss MS, Wilk P.; Structural and biochemical characterization of prolidase variants. Sci Rep. 10.1038/s41598-024-74891-7
17. Nowak M, Borowski T, Kluza A.; Structural mechanisms of plant adaptive responses. Nat Plants 10.1038/s41477-024-01804-x
18. Musiał B, Skalniak Ł, Holak TA.; Protein–protein interaction inhibitors in cancer immunotherapy. Int J Biol Macromol. 10.1016/j.ijbiomac.2024.135510
19. Grudnik P, Wilk P, Glatt S.; Structural insights into hypusination pathway regulation. Cell Rep. 10.1016/j.celrep.2024.114831
1. Nietzold F, Rubner S, Labuzek B, Golik P, Surmiak E, del Corte X, Kitel R, Protzel C, Reppich-Sacher R, Stichel J, et al.; Nutlin-3a-aa: Improving the Bioactivity of a p53/MDM2 Interaction Inhibitor. ChemBioChem 10.1002/cbic.202300006
2. Dauden MI, Jaciuk M, Müller CW, Glatt S, et al.; Cryo-EM structure of the fully assembled Elongator complex. Nucleic Acids Res. 10.1093/nar/gkac1232
3. Sarewicz M, Szwalec M, Pintscher S, Indyka P, Rawski M, Pietras R, Mielecki B, Koziej L, Jaciuk M, Glatt S, Osyczka A.; High-resolution cryo-EM structures of plant cytochrome b6f at work. Sci Adv. 10.1126/sciadv.add9688
4. Michalczyk E, Hommernick K, Behroz I, Kulike M, Pakosz-Stępień Z, Mazurek L, Seidel M, Kunert M, Santos K, Loll B, et al.; Molecular mechanism of topoisomerase poisoning by the peptide antibiotic albicidin. Nat Catal. 10.1038/s41929-022-00904-1
5. Hachlica N, Rawski M, Górecki M, Wajda A, Kaczor A.; Chiral and Structural Polymorphism of Fibril Architectures of Homologous Lysozymes. Chem Eur J. 10.1002/chem.202203827
6. Biela AP, Wątor E, Grudnik P, et al.; Cryo-EM structure of human eIF5A-DHS complex reveals the molecular basis of hypusination-associated neurodegenerative disorders. Nat Commun. 10.1038/s41467-023-37305-2
7. Stupka I, et al.; Complementary charge-driven encapsulation of functional protein by engineered protein cages in cellulo. J Mater Chem B. 10.1039/D3TB00754E
8. Jain S, Koziej L, Poulis P, Kaczmarczyk I, Gaik M, Rawski M, Ranjan N, Glatt S, Rodnina MV, et al.; Modulation of translational decoding by m6A modification of mRNA. Nat Commun. 10.1038/s41467-023-40422-7
9. Grzechowiak M, Śliwiak J, Jaskolski M, Ruszkowski M.; Structural and functional studies of Arabidopsis thaliana glutamate dehydrogenase isoform 2 demonstrate enzyme kinetics and identify its calcium binding site. Plant Physiol Biochem. 10.1016/j.plaphy.2023.107895
10. Sonani RR, Blat A, Jemioła-Rzemińska M, Lipiński O, Patel SN, Sood T, Dubin G.; Structure of Trypanosoma peroxisomal import complex unveils conformational dynamics. bioRxiv 10.1101/2023.04.03.535445
11. Zhang H, Zhou S, Plewka J, Wu C, Zhu M, et al.; Design, Synthesis, and Antitumor Activity Evaluation of 2-Arylmethoxy-4-(2,2′-dihalogen-substituted biphenyl-3-ylmethoxy)benzylamine Derivatives as PD-1/PD-L1 Inhibitors. J Med Chem. 10.1021/acs.jmedchem.3c00731
12. Ważyńska MA, Butera R, Requesens M, Plat A, Zarganes-Tzitzikas T, Neochoritis CG, Plewka J, Skalniak L, Kocik-Krol J, Musielak B, Magiera-Mularz K, Rodriguez I, Blok SN, de Bruyn M, Nijman HW, Elsinga PH, Holak TA, Dömling A.; Design, Synthesis, and Biological Evaluation of 2-Hydroxy-4-phenylthiophene-3-carbonitrile as PD-L1 Antagonist and Its Comparison to Available Small Molecular PD-L1 Inhibitors. J Med Chem. 10.1021/acs.jmedchem.3c00254
13. Lin TY, Glatt S, et al.; Electrophoretic Mobility Shift Assay (EMSA) and Microscale Thermophoresis (MST) for Monitoring Elongator–tRNA Interactions. Methods Mol Biol. 10.1007/978-1-0716-3191-1_3
14. Pustelny K, Grygier P, Barzowska A, Pucelik B, et al.; Binding mechanism and biological effects of flavone DYRK1A inhibitors. Sci Rep. 10.1038/s41598-023-44810-3
15. Stępień P, et al.; CRAFTing Delivery of Membrane Proteins into Protocells using Nanodiscs. ACS Appl Mater Interfaces 10.1021/acsami.3c11894
16. Magiera-Mularz K, Kocik-Krol J, Musielak B, Plewka J, Skalniak L, Holak TA, et al.; Solubilizer Tag Effect on PD-L1/Inhibitor Binding Properties for m-Terphenyl Derivatives. ACS Med Chem Lett. 10.1021/acsmedchemlett.3c00306
17. Rodriguez I, Kocik-Krol J, Skalniak L, et al.; Structural and biological characterization of pAC65, a macrocyclic peptide that blocks PD-L1 with equivalent potency to the FDA-approved antibodies. Mol Cancer 10.1186/s12943-023-01853-4
1. Stupka I, Azuma Y, Biela AP, Imamura M, Scheuring S, Pyza E, Woźnicka O, Maskell DP, Heddle JG.; Chemically induced protein cage assembly with programmable opening and cargo release. Sci Adv. 10.1126/sciadv.abj9424
2. Biela AP, Naskalska A, Fatehi F, et al.; Programmable polymorphism of a virus-like particle. Commun Mater. 10.1038/s43246-022-00229-3
3. Ruszkowski M, Strugala A, Indyka P, Tresset G, Figlerowicz M, Urbanowicz A.; Cryo-EM reconstructions of BMV-derived virus-like particles reveal assembly defects in the icosahedral lattice structure. Nanoscale 10.1039/D1NR05650F
4. Matsuda A, Plewka J, Kresik L, Abdulkarim K, Robinson C, O’Byrne S, Cunningham F, Georgiou I, Pachota M, Popowicz GM, Wyatt PG, Dubin G, Pyrć K, Czarna A.; Refolding of lid subdomain of SARS-CoV-2 nsp14 upon nsp10 interaction releases exonuclease activity. Structure 10.1016/j.str.2022.04.014
5. Majsterkiewicz K, Biela AP, Maity S, Sharma M, Piette BMAG, Kowalczyk A, Gaweł S, Chakraborti S, Roos WH, Heddle JG.; Artificial Protein Cage with Unusual Geometry and Regularly Embedded Gold Nanoparticles. Nano Lett. 10.1021/acs.nanolett.1c04222
6. Sonani RR, Blat A, Dubin G.; Crystal structures of apo- and FAD-bound human peroxisomal acyl-CoA oxidase provide mechanistic basis explaining clinical observations. Int J Biol Macromol. 10.1016/j.ijbiomac.2022.02.008
7. Sharma M, Biela AP, Kowalczyk A, Borzęcka-Solarz K, Piette BMAG, Heddle JG, et al.; Shape-Morphing of an Artificial Protein Cage with Unusual Geometry Induced by a Single Amino Acid Change. ACS Nanoscience Au 10.1021/acsnanoscienceau.2c00019
8. Gaik M, et al.; Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26. Life Sci Alliance 10.26508/lsa.202201418
9. Kojic M, et al.; Functional divergence of the two Elongator subcomplexes during neurodevelopment. EMBO Mol Med. 10.15252/emmm.202115608
10. Pabis M, et al.; E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation. EMBO J. 10.15252/embj.2022111318
11. Shaheen R, et al.; Destabilization of mutated human PUS3 protein causes intellectual disability. Hum Mutat. 10.1002/humu.24471
12. Napolitano V, Mróz P, Marciniak M, Kalel VC, Softley CA, Olmos JDJ, Tippler BG, Schorpp K, Rioton S, Fröhlich T, Plettenburg O, Hadian K, Erdmann R, Sattler M, Popowicz GM, Dawidowski M, Dubin G.; Structure-based design, synthesis and evaluation of a novel family of PEX5-PEX14 interaction inhibitors against Trypanosoma. Eur J Med Chem. 10.1016/j.ejmech.2022.114778
13. Basu S, et al.; Silmitasertib (CX-4945), a Clinically Used CK2-Kinase Inhibitor with Additional Activity against DYRK1A and GSK3β. J Med Chem. 10.1021/acs.jmedchem.2c01887
1. Kojic M, Gawda T, Gaik M, Begg A, Salerno-Kochan A, Kurniawan ND, Jones A, Drożdżyk K, Kościelniak A, Chramiec-Głąbik A, et al.; Elp2 mutations perturb the epitranscriptome and lead to a complex neurodevelopmental phenotype. Nat Commun. 10.1038/s41467-021-22888-5
2. Sonani RR, Kurpiewska K, Lewiński K, Dubin G.; Distinct sequence and structural feature of trypanosoma malate dehydrogenase. Biochem Biophys Res Commun. 10.1016/j.bbrc.2021.04.033
3. Zak KM, Bostock MJ, Waligorska I, Thøgersen IB, Enghild JJ, Popowicz GM, Grudnik P, Potempa J, Ksiazek M.; Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogen Tannerella forsythia. J Enzyme Inhib Med Chem. 10.1080/14756366.2021.1937619
4. Kumar M, Markiewicz-Mizera J, Janna Olmos JD, Wilk P, Grudnik P, Biela AP, Jemioła-Rzemińska M, Górecki A, Chakraborti S, Heddle JG.; A single residue can modulate nanocage assembly in salt dependent ferritin. Nanoscale 10.1039/d1nr01632f
5. Muszak D, Surmiak E, Plewka J, Magiera-Mularz K, Kocik-Krol J, Musielak B, Sala D, Kitel R, Stec M, Weglarczyk K, Siedlar M, Dömling A, Skalniak L, Holak TA.; Terphenyl-Based Small-Molecule Inhibitors of Programmed Cell Death-1/Programmed Death-Ligand 1 Protein-Protein Interaction. J Med Chem. 10.1021/acs.jmedchem.1c00957
6. Butera R, Ważyńska M, Magiera-Mularz K, Plewka J, Musielak B, Surmiak E, Sala D, Kitel R, de Bruyn M, Nijman HW, Elsinga PH, Holak TA, Dömling A.; Design, Synthesis, and Biological Evaluation of Imidazopyridines as PD-1/PD-L1 Antagonists. ACS Med Chem Lett. 10.1021/acsmedchemlett.1c00033
7. Zyla E, Musielak B, Holak TA, Dubin G.; Structural Characterization of a Macrocyclic Peptide Modulator of the PD-1/PD-L1 Immune Checkpoint Axis. Molecules 10.3390/molecules26164848
8. Ghilarov D, Inaba-Inoue S, Stepien P, Qu F, Michalczyk E, Pakosz Z, Nomura N, Ogasawara S, Walker GC, Rebuffat S, Iwata S, Heddle JG, Beis K.; Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides. Sci Adv. 10.1126/sciadv.abj5363
9. Banaś AM, Bocian-Ostrzycka KM, Dunin-Horkawicz S, Ludwiczak J, Wilk P, Orlikowska M, Wyszyńska A, Dąbrowska M, Plichta M, Spodzieja M, Polańska MA, Malinowska A, Jagusztyn-Krynicka EK.; Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of Campylobacter jejuni and Their Impact on Bacterial Physiology and Pathogenesis. Int J Mol Sci. 10.3390/ijms222413451
1. Dawidowski M, Kalel VC, Napolitano V, Fino R, Schorpp K, Emmanouilidis L, Lenhart D, Ostertag M, Kaiser M, Kolonko M, Tippler B, Schliebs W, Dubin G, Mäser P, Tetko IV, Hadian K, Plettenburg O, Erdmann R, Sattler M, Popowicz GM.; Structure-Activity Relationship in Pyrazolo[4,3-c]pyridines, First Inhibitors of PEX14-PEX5 Protein-Protein Interaction with Trypanocidal Activity. J Med Chem. 10.1021/acs.jmedchem.9b01876
2. Kluza A, Wojdyla Z, Mrugala B, Kurpiewska K, Porebski PJ, Niedzialkowska E, Minor W, Weiss MS, Borowski T.; Regioselectivity of hyoscyamine 6β-hydroxylase-catalysed hydroxylation as revealed by high-resolution structural information and QM/MM calculations. Dalton Trans. 10.1039/d0dt00302f
3. Krutyhołowa R, Reinhardt-Tews A, Chramiec-Głąbik A, Breunig KD, Glatt S.; Fungal Kti12 proteins display unusual linker regions and unique ATPase p-loops. Curr Genet. 10.1007/s00294-020-01070-2
4. Wątor E, Wilk P, Grudnik P.; Half Way to Hypusine-Structural Basis for Substrate Recognition by Human Deoxyhypusine Synthase. Biomolecules 10.3390/biom10040522
5. Janczak M, Hyz K, Bukowski M, Lyzen R, Hydzik M, Węgrzyn G, Szalewska-Pałasz A, Grudnik P, Dubin G, Wladyka B.; Chromosomal localization of PemIK toxin-antitoxin system results in the loss of toxicity – Characterization of pemIKSa1-Sp from Staphylococcus pseudintermedius. Microbiol Res. 10.1016/j.micres.2020.126529
6. Wątor E, Rutkiewicz M, Weiss MS, Wilk P.; Co-expression with chaperones can affect protein 3D structure as exemplified by loss-of-function variants of human prolidase. FEBS Lett. 10.1002/1873-3468.13877
7. Wilk P, Wątor E, Weiss MS.; Prolidase – A protein with many faces. Biochimie 10.1016/j.biochi.2020.09.017
8. Fortuna P, Twarda-Clapa A, Skalniak L, Ożga K, Holak TA, 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. 10.1016/j.ejmech.2020.112814
9. Magoch M, Nogly P, Grudnik P, Ma P, Boczkus B, Neves AR, Archer M, Dubin G.; Crystal Structure of Mannose Specific IIA Subunit of Phosphotransferase System from Streptococcus pneumoniae. Molecules 10.3390/molecules25204633
10. Pabis M, Termathe M, Ravichandran KE, Kienast SD, Krutyhołowa R, Sokołowski M, Jankowska U, Grudnik P, Leidel SA, Glatt S.; Molecular basis for the bifunctional Uba4-Urm1 sulfur-relay system in tRNA thiolation and ubiquitin-like conjugation. EMBO J. 10.15252/embj.2020105087
11. Reinhardt-Tews A, Krutyhołowa R, Günzel C, Roehl C, Glatt S, Breunig KD.; A double role of the Gal80 N terminus in activation of transcription by Gal4p. Life Sci Alliance 10.26508/lsa.202000665
12. Magiera-Mularz K, Kuśka K, Skalniak L, Grudnik P, Musielak B, Plewka J, Kocik J, Stec M, Weglarczyk K, Sala D, Wladyka B, Siedlar M, Holak TA, Dubin G.; Macrocyclic Peptide Inhibitor of PD‐1/PD‐L1 Immune Checkpoint. Adv Ther. 10.1002/adtp.202000195
13. Magiera-Mularz K, Kocik J, Musielak B, Plewka J, Machula M, Grudnik P, Hajduk M, Czepiel M, Siedlar M, Holak TA, Skalniak L.; Human and mouse PD-L1: similar molecular structure, but different druggability profiles. iScience 10.1016/j.isci.2020.101960
14. Wilk P, Kuśka K, Wątor E, Malecki PH, Wos K, Tokarz P, Dubin G, Grudnik P.; Structural Characterization of Glycerol Kinase from the Thermophilic Fungus Chaetomium thermophilum. Int J Mol Sci. 10.3390/ijms21249570
1. Lin TY, Abbassi NEH, Zakrzewski K, Chramiec-Głąbik A, Jemioła-Rzemińska M, Różycki J, Glatt S.; The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase. Nat Commun. 10.1038/s41467-019-08579-2
2. Rembacz KP, Zrubek KM, Golik P, Michalik K, Bogusz J, Wladyka B, Romanowska M, Dubin G.; Crystal structure of Maternal Embryonic Leucine Zipper Kinase (MELK) in complex with dorsomorphin (Compound C). Arch Biochem Biophys. 10.1016/j.abb.2019.05.014
3. Krutyhołowa R, Hammermeister A, Zabel R, Abdel-Fattah W, Reinhardt-Tews A, Helm M, Stark MJR, Breunig KD, Glatt S.; Kti12, a PSTK-like tRNA-dependent ATPase essential for tRNA modification by Elongator. Struct Biol. 10.1016/j.sbi.2019.03.014
4. Dauden MI, Jaciuk M, Weis F, Lin TY, Kleindienst C, Abbassi NEH, Khatter H, Krutyhołowa R, Breunig KD, Kosinski J, Müller CW, Glatt S.; Molecular basis of tRNA recognition by the Elongator complex. Sci Adv. 10.1126/sciadv.aaw2326
5. Mucha O, Podkalicka P, Mikulski M, Barwacz S, Andrysiak K, Biela A, Mieczkowski M, Kachamakova-Trojanowska N, Ryszawy D, Białas A, Szelażek B, Grudnik P, Majewska E, Michalik K, Jakubiec K, Bień M, Witkowska M, Gluza K, Ekonomik D, Sitarz K, Gałęzowski M, Brzózka K, Dubin G, Józkowicz A, Dulak J, Łoboda A.; Development and characterization of a new inhibitor of heme oxygenase activity for cancer treatment. Arch Biochem Biophys. 10.1016/j.abb.2019.07.002
6. Basu S, Yang J, Xu B, Magiera-Mularz K, Skalniak L, Musielak B, Kholodovych V, Holak TA, Hu L.; Design, Synthesis, Evaluation, and Structural Studies of C2-Symmetric Small Molecule Inhibitors of Programmed Cell Death-1/Programmed Death-Ligand 1 Protein-Protein Interaction. J Med Chem. 10.1021/acs.jmedchem.9b00795
7. Zak KM, Kalińska M, Wątor E, Kuśka K, Popowicz GM, Grudnik P.; Crystal Structure of Kluyveromyces lactis Glucokinase (KlGlk1). Int J Mol Sci. 10.3390/ijms20194821
8. Musielak B, Kocik J, Skalniak L, Magiera-Mularz K, Sala D, Czub M, Stec M, Siedlar M, Holak TA, Plewka J.; CA-170 – A Potent Small-Molecule PD-L1 Inhibitor or Not? Molecules 10.3390/molecules24152804