Aggregation condition–structure relationship of mouse prion protein fibrils
Fridmanis, J., Toleikis, Z., Sneideris, T., Ziaunys, M., Bobrovs, R., Smirnovas, V., Jaudzems, K.
International Journal of Molecular Sciences, 22 (17), 9635, 2021.
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S100a9 alters the pathway of alpha-synuclein amyloid aggregation
Toleikis, Z., Ziaunys, M., Baranauskiene, L., Petrauskas, V., Jaudzems, K., Smirnovas, V.
International Journal of Molecular Sciences, 22 (15), 7972, 2021.
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Potent SARS-CoV-2 mRNA Cap Methyltransferase Inhibitors by Bioisosteric Replacement of Methionine in SAM Cosubstrate
Bobiļeva, O., Bobrovs, R., Kaņepe, I., Patetko, L., Kalniņš, G., Šišovs, M., Bula, A.L., Grīnberga, S., Borodušķis, M.R., Ramata-Stunda, A., Rostoks, N., Jirgensons, A., Tārs, K., Jaudzems, K.
ACS Medicinal Chemistry Letters, 12 (7), 1102-1107, 2021.
DOI: 10.1021/acsmedchemlett.1c00140
Structural Analysis of an Antigen Chemically Coupled on Virus-Like Particles in Vaccine Formulation
Jaudzems, K., Kirsteina, A., Schubeis, T., Casano, G., Ouari, O., Bogans, J., Kazaks, A., Tars, K., Lesage, A., Pintacuda, G.
Angewandte Chemie – International Edition, 60 (23), 12847-12851, 2021.
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Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications
Altincekic, N., … Bula, A., Jaudzems, K., Kaņepe, I., et. al.
Frontiers in Molecular Biosciences, 8, 653148, 2021.
DOI: 10.3389/fmolb.2021.653148
Total Synthesis of the Proposed Structure of Uncarialin A
Ūdris, N.V., Jaudzems, K., Smits, G.
Journal of Organic Chemistry, 86 (9), 6927-6930, 2021.
DOI: 10.1021/acs.joc.1c00324
Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family
Fridmanis, J., Otikovs, M., Brangulis, K., Tārs, K., Jaudzems, K.
Proteins: Structure, Function and Bioinformatics, 89 (5), 588-594, 2021.
DOI: 10.1002/prot.26011
Residual Solvent Signal of CDCl3 as a qNMR Internal Standard for Application in Organic Chemistry Laboratory
Muhamadejev, R., Melngaile, R., Paegle, P., Zibarte, I., Petrova, M., Jaudzems, K., Veliks, J.
Journal of Organic Chemistry, 86 (5), 3890-3896, 2021.
DOI: 10.1021/acs.joc.0c02744
Polymorph-Selective Role of Hydrogen Bonding and π-πStacking in p-Aminobenzoic Acid Solutions
Bobrovs, R., Drunka, L., Auzins, A.A., Jaudzems, K., Salvalaglio, M.
Crystal Growth and Design, 21 (1), 436-448, 2021.
DOI: 10.1021/acs.cgd.0c01257
Fused isoselenazolium salts suppress breast cancer cell growth by dramatic increase in pyruvate-dependent mitochondrial ROS production
Makrecka-Kuka, M., Dimitrijevs, P., Domracheva, I., Jaudzems, K., Dambrova, M., Arsenyan, P.
Scientific Reports, 10 (1), 21595, 2020.
DOI: 10.1038/s41598-020-78620-8
High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain
Abelein, A., Chen, G., Kitoka, K., Aleksis, R., Oleskovs, F., Sarr, M., Landreh, M., Pahnke, J., Nordling, K., Kronqvist, N., Jaudzems, K., Rising, A., Johansson, J., Biverstål, H.
Scientific Reports, 10 (1), 235, 2020.
DOI: 10.1038/s41598-019-57143-x
Synthesis of 2-aminopyridopyrimidinones and their plasmepsin I, II, IV inhibition potency
Rasina, D., Stakanovs, G., Kanepe-Lapsa, I., Bobrovs, R., Jaudzems, K., Jirgensons, A.
Chemistry of Heterocyclic Compounds, 56 (6), 786-792, 2020.
DOI: 10.1007/s10593-020-02731-3
BBE31 from the Lyme disease agent Borrelia burgdorferi, known to play an important role in successful colonization of the mammalian host, shows the ability to bind glutathione
Brangulis, K., Akopjana, I., Petrovskis, I., Kazaks, A., Zelencova, D., Jekabsons, A., Jaudzems, K., Tars, K.
Biochimica et Biophysica Acta – General Subjects, 1864 (3), 129499, 2020.
DOI: 10.1016/j.bbagen.2019.129499
Targeting Bacterial Sortase A with Covalent Inhibitors: 27 New Starting Points for Structure-Based Hit-to-Lead Optimization
Jaudzems, K., Kurbatska, V., Jekabsons, A., Bobrovs, R., Rudevica, Z., Leonchiks, A.
ACS Infectious Diseases, 6 (2), 186-194, 2020.
DOI: 10.1021/acsinfecdis.9b00265
Structural and functional analysis of bba03, borrelia burgdorferi competitive advantage promoting outer surface lipoprotein
Fridmanis, J., Bobrovs, R., Brangulis, K., Tārs, K., Jaudzems, K.
Pathogens, 9 (10), art. no. 826, 1-13, 2020.
DOI: 10.3390/pathogens9100826
Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection
Brangulis, K., Akopjana, I., Petrovskis, I., Kazaks, A., Jekabsons, A., Jaudzems, K., Viksna, A., Bertins, M., Tars, K.
FEBS Letters, 594 (2), 317-326, 2020.
DOI: 10.1002/1873-3468.13594
Exploiting Structural Dynamics to Design Open-Flap Inhibitors of Malarial Aspartic Proteases
Bobrovs, R., Jaudzems, K., Jirgensons, A.
Journal of Medicinal Chemistry, 62 (20), 8931-8950, 2019.
DOI: 10.1021/acs.jmedchem.9b00184
Biomimetic composites with enhanced toughening using silk-inspired triblock proteins and aligned nanocellulose reinforcements
Mohammadi, P., Sesilja Aranko, A., Landowski, C.P., Ikkala, O., Jaudzems, K., Wagermaier, W., Linder, M.B.
Science Advances, 5 (9), eaaw2541, 2019.
DOI: 10.1126/sciadv.aaw2541
Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies
Gupta, R., Zhang, H., Lu, M., Hou, G., Caporini, M., Rosay, M., Maas, W., Struppe, J., Ahn, J., Byeon, I.-J.L., Oschkinat, H., Jaudzems, K., Barbet-Massin, E., Emsley, L., Pintacuda, G., Lesage, A., Gronenborn, A.M., Polenova, T.
Journal of Physical Chemistry B, 123 (24), 5048-5058, 2019.
DOI: 10.1021/acs.jpcb.9b02293
DNP NMR of biomolecular assemblies
Jaudzems, K., Polenova, T., Pintacuda, G., Oschkinat, H., Lesage, A.
Journal of Structural Biology, 206 (1), 90-98, 2019.
DOI: 10.1016/j.jsb.2018.09.011
Peptidomimetic plasmepsin inhibitors with potent anti-malarial activity and selectivity against cathepsin D
Zogota, R., Kinena, L., Withers-Martinez, C., Blackman, M.J., Bobrovs, R., Pantelejevs, T., Kanepe-Lapsa, I., Ozola, V., Jaudzems, K., Suna, E., Jirgensons, A.
European Journal of Medicinal Chemistry, 163, 344-352, 2019.
DOI: 10.1016/j.ejmech.2018.11.068
Azole-based non-peptidomimetic plasmepsin inhibitors
Kinena, L., Leitis, G., Kanepe-Lapsa, I., Bobrovs, R., Jaudzems, K., Ozola, V., Suna, E., Jirgensons, A.
Archiv der Pharmazie, 351 (9), 1800151, 2018.
DOI: 10.1002/ardp.201800151
Dynamic Nuclear Polarization-Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic-Angle Spinning
Jaudzems, K., Bertarello, A., Chaudhari, S.R., Pica, A., Cala-De Paepe, D., Barbet-Massin, E., Pell, A.J., Akopjana, I., Kotelovica, S., Gajan, D., Ouari, O., Tars, K., Pintacuda, G., Lesage, A.
Angewandte Chemie – International Edition, 57 (25), 7458-7462, 2018.
DOI: 10.1002/anie.201801016
2-Aminoquinazolin-4(3H)-one based plasmepsin inhibitors with improved hydrophilicity and selectivity
Rasina, D., Stakanovs, G., Borysov, O.V., Pantelejevs, T., Bobrovs, R., Kanepe-Lapsa, I., Tars, K., Jaudzems, K., Jirgensons, A.
Bioorganic and Medicinal Chemistry, 26 (9), 2488-2500, 2018.
DOI: 10.1016/j.bmc.2018.04.012
A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein
Sarr, M., Kronqvist, N., Chen, G., Aleksis, R., Purhonen, P., Hebert, H., Jaudzems, K., Rising, A., Johansson, J.
FEBS Journal, 285 (10), 1873-1885, 2018.
DOI: 10.1111/febs.14451
N-Leucinyl Benzenesulfonamides as Structurally Simplified Leucyl-tRNA Synthetase Inhibitors
Charlton, M.H., Aleksis, R., Saint-Leger, A., Gupta, A., Loza, E., Ribas De Pouplana, L., Kaula, I., Gustina, D., Madre, M., Lola, D., Jaudzems, K., Edmund, G., Randall, C.P., Kime, L., O’Neill, A.J., Goessens, W., Jirgensons, A., Finn, P.W.
ACS Medicinal Chemistry Letters, 9 (2), 84-88, 2018.
DOI: 10.1021/acsmedchemlett.7b00374
Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy
Otikovs, M., Andersson, M., Jia, Q., Nordling, K., Meng, Q., Andreas, L.B., Pintacuda, G., Johansson, J., Rising, A., Jaudzems, K.
Angewandte Chemie – International Edition, 56 (41), 12571-12575, 2017.
DOI: 10.1002/anie.201706649
Is protein deuteration beneficial for proton detected solid-state NMR at and above 100 kHz magic-angle spinning?
Cala-De Paepe, D., Stanek, J., Jaudzems, K., Tars, K., Andreas, L.B., Pintacuda, G.
Solid State Nuclear Magnetic Resonance, 87, 126-136, 2017.
DOI: 10.1016/j.ssnmr.2017.07.004
Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity
Aleksis, R., Oleskovs, F., Jaudzems, K., Pahnke, J., Biverstål, H.
Biochimie, 140, 176-192, 2017.
DOI: 10.1016/j.biochi.2017.07.011
Efficient protein production inspired by how spiders make silk
Kronqvist, N., Sarr, M., Lindqvist, A., Nordling, K., Otikovs, M., Venturi, L., Pioselli, B., Purhonen, P., Landreh, M., Biverstål, H., Toleikis, Z., Sjöberg, L., Robinson, C.V., Pelizzi, N., Jörnvall, H., Hebert, H., Jaudzems, K., Curstedt, T., Rising, A., Johansson, J.
Nature Communications, 8, 15504, 2017.
DOI: 10.1038/ncomms15504
NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils
Stanek, J., Andreas, L.B., Jaudzems, K., Cala, D., Lalli, D., Bertarello, A., Schubeis, T., Akopjana, I., Kotelovica, S., Tars, K., Pica, A., Leone, S., Picone, D., Xu, Z.-Q., Dixon, N.E., Martinez, D., Berbon, M., El Mammeri, N., Noubhani, A., Saupe, S., Habenstein, B., Loquet, A., Pintacuda, G.
Angewandte Chemie – International Edition, 55 (50), 15504-15509, 2016.
DOI: 10.1002/anie.201607084
Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions
Aleksis, R., Jaudzems, K., Muceniece, R., Liepinsh, E.
Peptides, 85, 56-62, 2016.
DOI: 10.1016/j.peptides.2016.09.006
Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages
Shishovs, M., Rumnieks, J., Diebolder, C., Jaudzems, K., Andreas, L.B., Stanek, J., Kazaks, A., Kotelovica, S., Akopjana, I., Pintacuda, G., Koning, R.I., Tars, K.
Journal of Molecular Biology, 428 (21), 4267-4279, 2016.
DOI: 10.1016/j.jmb.2016.08.025
Crystal structure of Plasmodium falciparum proplasmepsin IV: The plasticity of proplasmepsins
Recacha, R., Jaudzems, K., Akopjana, I., Jirgensons, A., Tars, K.
Acta Crystallographica Section:F Structural Biology Communications, 72, 659-666, 2016.
DOI: 10.1107/S2053230X16011663
Structure of fully protonated proteins by proton-detected magic- Angle spinning NMR
Andreas, L.B., Jaudzems, K., Stanek, J., Lalli, D., Bertarelloa, A., Marchand, T.L., De Paepe, D.C., Kotelovica, S., Akopjana, I., Knott, B., Wegner, S., Engelke, F., Lesage, A., Emsley, L., Tars, K., Herrmann, T., Pintacuda, G.
Proceedings of the National Academy of Sciences of the United States of America, 113 (33), 9187-9192, 2016.
DOI: 10.1073/pnas.1602248113
Transmissible amyloid
Tjernberg, L.O., Rising, A., Johansson, J., Jaudzems, K., Westermark, P.
Journal of Internal Medicine, 280 (2), 153-163, 2016.
DOI: 10.1111/joim.12499
Fragment-Based Discovery of 2-Aminoquinazolin-4(3H)-ones As Novel Class Nonpeptidomimetic Inhibitors of the Plasmepsins I, II, and IV
Rasina, D., Otikovs, M., Leitans, J., Recacha, R., Borysov, O.V., Kanepe-Lapsa, I., Domraceva, I., Pantelejevs, T., Tars, K., Blackman, M.J., Jaudzems, K., Jirgensons, A.
Journal of Medicinal Chemistry, 59 (1), 374-387, 2016.
DOI: 10.1021/acs.jmedchem.5b01558
Diversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal Domains
Otikovs, M., Chen, G., Nordling, K., Landreh, M., Meng, Q., Jörnvall, H., Kronqvist, N., Rising, A., Johansson, J., Jaudzems, K.
ChemBioChem, 16 (12), 1720-1724, 2015.
DOI: 10.1002/cbic.201500263
O – Tert -Butyltyrosine, an NMR Tag for High-Molecular-Weight Systems and Measurements of Submicromolar Ligand Binding Affinities
Chen, W.-N., Kuppan, K.V., Lee, M.D., Jaudzems, K., Huber, T., Otting, G.
Journal of the American Chemical Society, 137 (13), 4581-4586, 2015.
DOI: 10.1021/jacs.5b01918
Structures of plasmepsin II from Plasmodium falciparum in complex with two hydroxyethylamine-based inhibitors
Recacha, R., Leitans, J., Akopjana, I., Aprupe, L., Trapencieris, P., Jaudzems, K., Jirgensons, A., Tars, K.
Acta Crystallographica Section:F Structural Biology Communications, 71, 1531-1539, 2015.
DOI: 10.1107/S2053230X15022049
Structural and functional analysis of BB0689 from Borrelia burgdorferi, a member of the bacterial CAP superfamily
Brangulis, K., Jaudzems, K., Petrovskis, I., Akopjana, I., Kazaks, A., Tars, K.
Journal of Structural Biology, 192 (3), 320-330, 2015.
DOI: 10.1016/j.jsb.2015.09.007
High-resolution proton-detected NMR of proteins at very fast MAS
Andreas, L.B., Le Marchand, T., Jaudzems, K., Pintacuda, G.
Journal of Magnetic Resonance, 253, art. no. 5586, 36-49, 2015.
DOI: 10.1016/j.jmr.2015.01.003
J-UNIO protocol used for NMR structure determination of the 206-residue protein NP-346487.1 from Streptococcus pneumoniae TIGR4
Jaudzems, K., Pedrini, B., Geralt, M., Serrano, P., Wüthrich, K.
Journal of Biomolecular NMR, 61 (1), 65-72, 2015.
DOI: 10.1007/s10858-014-9886-3
Discovery and structure-activity relationship studies of irreversible benzisothiazolinone-based inhibitors against Staphylococcus aureus sortase A transpeptidase
Zhulenkovs, D., Rudevica, Z., Jaudzems, K., Turks, M., Leonchiks, A.
Bioorganic and Medicinal Chemistry, 22 (21), 5988-6003, 2014.
DOI: 10.1016/j.bmc.2014.09.011
Rapid proton-detected NMR assignment for proteins with fast magic angle spinning
Barbet-Massin, E., Pell, A.J., Retel, J.S., Andreas, L.B., Jaudzems, K., Franks, W.T., Nieuwkoop, A.J., Hiller, M., Higman, V., Guerry, P., Bertarello, A., Knight, M.J., Felletti, M., Le Marchand, T., Kotelovica, S., Akopjana, I., Tars, K., Stoppini, M., Bellotti, V., Bolognesi, M., Ricagno, S., Chou, J.J., Griffin, R.G., Oschkinat, H., Lesage, A., Emsley, L., Herrmann, T., Pintacuda, G.
Journal of the American Chemical Society, 136 (35), 12489-12497, 2014.
DOI: 10.1021/ja507382j
Carbonic Anhydrase Generates CO2 and H+ That Drive Spider Silk Formation Via Opposite Effects on the Terminal Domains
Andersson, M., Chen, G., Otikovs, M., Landreh, M., Nordling, K., Kronqvist, N., Westermark, P., Jörnvall, H., Knight, S., Ridderstråle, Y., Holm, L., Meng, Q., Jaudzems, K., Chesler, M., Johansson, J., Rising, A.
PLoS Biology, 12 (8), e1001921, 2014.
DOI: 10.1371/journal.pbio.1001921
Plasmepsin inhibitory activity and structure-guided optimization of a potent hydroxyethylamine-based antimalarial hit
Jaudzems, K., Tars, K., Maurops, G., Ivdra, N., Otikovs, M., Leitans, J., Kanepe-Lapsa, I., Domraceva, I., Mutule, I., Trapencieris, P., Blackman, M.J., Jirgensons, A.
ACS Medicinal Chemistry Letters, 5 (4), 373-377, 2014.
DOI: 10.1021/ml4004952
Reactivity of aziridine-2-carboxamide (leakadine) with nucleophiles in aqueous solutions
Aleksis, R., Jaudzems, K., Ivanova, J., Žalubovskis, R., Kalvinsh, I., Liepinsh, E.
Chemistry of Heterocyclic Compounds, 49 (11), 1589-1598, 2014.
DOI: 10.1007/s10593-014-1410-x
Enzymatic activity of circular sortase A under denaturing conditions: An advanced tool for protein ligation
Zhulenkovs, D., Jaudzems, K., Zajakina, A., Leonchiks, A.
Biochemical Engineering Journal, 82, 200-209, 2014.
DOI: 10.1016/j.bej.2013.11.018
Structural characterization of CspZ, a complement regulator factor H and FHL-1 binding protein from Borrelia burgdorferi
Brangulis, K., Petrovskis, I., Kazaks, A., Bogans, J., Otikovs, M., Jaudzems, K., Ranka, R., Tars, K.
FEBS Journal, 281 (11), 2613-2622, 2014.
DOI: 10.1111/febs.12808
Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation
Kronqvist, N., Otikovs, M., Chmyrov, V., Chen, G., Andersson, M., Nordling, K., Landreh, M., Sarr, M., Jörnvall, H., Wennmalm, S., Widengren, J., Meng, Q., Rising, A., Otzen, D., Knight, S.D., Jaudzems, K., Johansson, J.
Nature communications, 5, 3254, 3254, 2014.
DOI: 10.1038/ncomms4254
Out-and-back 13C-13C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS
Barbet-Massin, E., Pell, A.J., Jaudzems, K., Franks, W.T., Retel, J.S., Kotelovica, S., Akopjana, I., Tars, K., Emsley, L., Oschkinat, H., Lesage, A., Pintacuda, G.
Journal of Biomolecular NMR, 56 (4), 379-386, 2013.
DOI: 10.1007/s10858-013-9757-3
Structural basis for 5′-end-specific recognition of single-stranded DNA by the R3H domain from human Sμbp-2
Jaudzems, K., Jia, X., Yagi, H., Zhulenkovs, D., Graham, B., Otting, G., Liepinsh, E.
Journal of Molecular Biology, 424 (1-2), 42-53, 2012.
DOI: 10.1016/j.jmb.2012.09.010
PH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain
Jaudzems, K., Askarieh, G., Landreh, M., Nordling, K., Hedhammar, M., Jörnvall, H., Rising, A., Knight, S.D., Johansson, J.
Journal of Molecular Biology, 422 (4), 477-487, 2012.
DOI: 10.1016/j.jmb.2012.06.004
Comparison of NMR and crystal structures for the proteins TM1112 and TM1367
Mohanty, B., Serrano, P., Pedrini, B., Jaudzems, K., Geralt, M., Horst, R., Herrmann, T., Elsliger, M.-A., Wilson, I.A., Wüthrich, K.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (10), 1381-1392, 2010.
DOI: 10.1107/S1744309110020956
Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites
Serrano, P., Pedrini, B., Geralt, M., Jaudzems, K., Mohanty, B., Horst, R., Herrmann, T., Elsliger, M.-A., Wilson, I.A., Wüthrich, K.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (10), 1393-1405, 2010.
DOI: 10.1107/S1744309110033658
NMR structure of the protein NP-247299.1: Comparison with the crystal structure
Jaudzems, K., Geralt, M., Serrano, P., Mohanty, B., Horst, R., Pedrini, B., Elsliger, M.-A., Wilson, I.A., Wüthrich, K.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (10), pp. 1367-1380, 2010.
DOI: 10.1107/S1744309110005890
NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH6.5
Johnson, M.A., Jaudzems, K., Wüthrich, K.
Journal of Molecular Biology, 402 (4), 619-628, 2010.
DOI: 10.1016/j.jmb.2010.07.043
Inhibition of carnitine acetyltransferase by mildronate, a regulator of energy metabolism
Jaudzems, K., Kuka, J., Gutsaits, A., Zinovjevs, K., Kalvinsh, I., Liepinsh, E., Liepinsh, E., Dambrova, M.
Journal of Enzyme Inhibition and Medicinal Chemistry, 24 (6), 1269-1275, 2009.
DOI: 10.3109/14756360902829527
A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader
Loscha, K.V., Jaudzems, K., Ioannou, C., Su, X.-C., Hill, F.R., Otting, G., Dixon, N.E., Liepinsh, E.
Nucleic Acids Research, 37 (7), 2395-2404, 2009.
DOI: 10.1093/nar/gkp092