Laboratorijas vadītājs
E-pasts: kristaps.jaudzems@osi.lv
Tālrunis: (+371) 67014817
Curriculum Vitae
Izglītība |
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03/2011 | Doktora grāds ķīmijā, Rīgas Tehniskā universitāte Doktora darbs: “NMR studies of protein structure, function and ligand interactions”. Zinātniskie vadītāji: prof. E. Liepiņš un prof. K. Wüthrich |
07/2008 | Maģistra grāds ķīmijas tehnoloģijā, Rīgas Tehniskā universitāte Maģistra darbs: “Proteīnu KMR spektroskopija un telpiskā uzbūve: DnaI un cikliskās Sortāzes A piemēri”. Zinātniskais vadītājs: prof. E. Liepiņš |
07/2006 | Bakalaura grāds ķīmijas tehnoloģijā, Rīgas Tehniskā universitāte Bakalaura darbs: “Selektīvi aizsargātu glikozes-6-fosfāta analogu sintēze”. Zinātniskā vadītāja: prof. Ē. Bizdēna |
Pētniecības pieredze |
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09/2017-tagad | Laboratorijas vadītājs Latvijas Organiskās sintēzes institūtā |
09/2015-08/2017 | Marie Skłodowska-Curie pēcdoktorantūras pētnieks Augsta lauka kodolu magnētiskās rezonanases centrā, Lionā, Francijā Dr. Anne Lesage grupā |
11/2011-08/2015 | vadošais pētnieks Latvijas Organiskās sintēzes institūtā |
10-12/2014 | vies-pētnieks Austrālijas Nacionālajā universitātē, Kanberā, Austrālijā. Apmācība bezšūnu proteīnu sintēzē un paramagnētiskajā KMR prof. Gottfried Otting vadībā |
10-12/2012 | vies-pētnieks Augsta lauka kodolu magnētiskās rezonanases centrā (Centre de RMN à Très Hauts Champs), Lionā, Francijā. Apmācība cietvielu KMR Dr. Guido Pintacuda vadībā |
06-09/2011 | vies-postdoks, The Scripps Research Institute, La Jolla, Kalifornijā, ASV prof. Kurt Wüthrich grupā |
07/2010-05/2011 | zinātniskais asistents Latvijas Organiskās sintēzes institūtā. Vadītājs: prof. Edvards Liepiņš |
09/2008-06/2010 | ārējais doktorants,The Scripps Research Institute, La Jolla, Kalifornija, ASV. Biomolekulu KMR pētījumi prof. Kurt Wüthrich vadībā |
01/2007-08/2008 | zinātniskais asistents Latvijas Organiskās sintēzes institūtā. Vadītājs: prof. Edvards Liepiņš |
05/2006-12/2006 | laborants Latvijas Organiskās sintēzes institūtā |
09/2002-05/2006 | laborants Rīgas Tehniskajā universitātē |
Pasniedzēja pieredze |
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02/2021- | profesors Latvijas Universitātē. Kursi: KMR spektroskopija, Dabasvielu ķīmija, Stereoķīmija, Organiskā ķīmija |
03/2018-02/2021 | asociētais profesors Latvijas Universitātē. Kursi: KMR spektroskopija, Dabasvielu ķīmija, Stereoķīmija |
03/2018-01/2019 | vies-asociētais profesors Rīgas Tehniskajā universitātē. Kursi: Fizikālās pētīšanas metodes, KMR spektroskopija |
02/2012-02/2018 | docents Rīgas Tehniskajā universitātē. Kursi: Fizikālās pētīšanas metodes, KMR spektroskopija |
2013-2017 | pasniedzējs Latvijas Universitātē. Kurss: KMR spektroskopija |
Valodu zināšanas |
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Latviešu (dzimtā), angļu un vācu (tekoši), krievu (pamatzināšanas) | |
Apbalvojumi un stipendijas |
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02/2022 | LZA diploms par vienu no nozīmīgākajiem sasniegumiem Latvijas zinātnē 2021. gadā |
12/2019 | LZA īstenais loceklis |
02/2018 | LZA diploms par vienu no nozīmīgākajiem sasniegumiem Latvijas zinātnē 2017. gadā |
12/2017 | LZA korespondētājloceklis |
10/2017 | Eiropas Zinātņu un mākslu akadēmijas veicināšanas balva |
09/2015-08/2017 | Marie Skłodowska-Curie indivuālais grants |
2013, 2015, 2017 | RTU un A/S OlainFarm piešķirtā Solomona Hillera balva studiju noslēguma darba vadītājam |
09/2010-05/2011 | Eiropas Sociālā fonda stipendija |
04/2009 | Prof. Emīlijas Gudrinieces balva labākajam jaunajam zinātniekam ķīmijā |
07/2006 | A/S OlainFarm balva par labāko bakalaura darbu |
Publikācijas
- Mikolka P., Kronqvist N., Haegerstrand-Björkman M., Jaudzems K., Kosutova P., Kolomaznik M., Saluri M., Landreh M., Calkovska A., Curstedt T., Johansson J. Synthetic surfactant with a combined SP-B and SP-C analogue is efficient in rabbit models of adult and neonatal respiratory distress syndrome. Transl. Res. (2023) in press. DOI
- Kovada V., Withers-Martinez C., Bobrovs R., Ce Rule H.N., Liepins E., Grinberga S., Hackett F., Collins C.R., Kreicberga A., Jiménez-Díaz M.B., Angulo-Barturen I., Rasina D., Suna E., Jaudzems K., Blackman M.J., Jirgensons A. Macrocyclic Peptidomimetic Plasmepsin X Inhibitors with Potent In Vitro and In Vivo Antimalarial Activity J. Med. Chem. (2023) 66: 10658-10680. DOI
- Torres F., Bütikofer M., Stadler G.R., Renn A., Kadavath H., Bobrovs R., Jaudzems K., Riek R. Ultrafast Fragment Screening Using Photo-Hyperpolarized (CIDNP) NMR. J. Am. Chem. Soc. (2023) 145: 12066-12080. DOI
- Zelencova-Gopejenko D., Videja M., Grandane A., Pudnika-Okinčica L., Sipola A., Vilks K., Dambrova M., Jaudzems K., Liepinsh E. Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity. Int. J. Mol. Sci. (2023) 24: 5528. DOI
- Bobileva O., Bobrovs R., Sirma E.E., Kanepe I., Bula A.L., Patetko L., Ramata-Stunda A., Grinberga S., Jirgensons A., Jaudzems K. 3-(Adenosylthio)benzoic Acid Derivatives as SARS-CoV-2 Nsp14 Methyltransferase Inhibitors. Molecules (2023) 28: 768. DOI
- Guo H., Puttreddy R., Salminen T., Lends A., Jaudzems K., Zeng H., Priimagi A. Halogen-bonded shape memory polymers. Nat. Commun. (2022) 13: 7436. DOI
- Lends A., Daskalov A., Maleckis A., Delamare A., Berbon M., Grélard A., Morvan E., Shenoy J., Dutour A., Tolchard J., Noubhani A., Giraud M.F., Sanchez C., Habenstein B., Guichard G., Compain G., Jaudzems K., Saupe S.J., Loquet A. Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis. Commun. Biol. (2022) 5: 1202. DOI
- Zelencova-Gopejenko D., Grandane A., Loza E., Lola D., Sipola A., Liepinsh E., Arsenyan P., Jaudzems K. Binding versus Enzymatic Processing of ε-Trimethyllysine Dioxygenase Substrate Analogues. ACS Med. Chem. Lett. (2022) 13: 1723-1729. DOI
- Berg H., Wirtz Martin M.A., Altincekic N., Alshamleh I., Kaur Bains J., Blechar J., Ceylan B., de Jesus V., Dhamotharan K., Fuks C., Gande S.L., Hargittay B., Hohmann K.F., Hutchison M.T., Marianne Korn S., Krishnathas R., Kutz F., Linhard V., Matzel T., Meiser N., Niesteruk A., Pyper D.J., Schulte L., Trucks S., Azzaoui K., Blommers M.J.J., Gadiya Y., Karki R., Zaliani A., Gribbon P., da Silva Almeida M., Dinis Anobom C., Bula A.L., Bütikofer M., Putinhon Caruso Í., Caterina Felli I., Da Poian A.T., Cardoso de Amorim G., Fourkiotis N.K., Gallo A., Ghosh D., Gomes-Neto F., Gorbatyuk O., Hao B., Kurauskas V., Lecoq L., Li Y., Cunha Mebus-Antunes N., Mompeán M., Cristtina Neves-Martins T., Ninot-Pedrosa M., Pinheiro A.S., Pontoriero L., Pustovalova Y., Riek R., Robertson A.J., Jose Abi Saad M., Treviño M.Á., Tsika A.C., Almeida F.C.L., Bax A., Henzler-Wildman K., Hoch J.C., Jaudzems K., Laurents D.V., Orts J., Pierattelli R., Spyroulias G.A., Duchardt-Ferner E., Ferner J., Fürtig B., Hengesbach M., Löhr F., Qureshi N., Richter C., Saxena K., Schlundt A., Sreeramulu S., Wacker A., Weigand J.E., Wirmer-Bartoschek J., Wöhnert J., Schwalbe H. Comprehensive Fragment Screening of the SARS-CoV-2 Proteome Explores Novel Chemical Space for Drug Development. Angew. Chem. Int. Ed. (2022) 61: e202205858. DOI
- Arndt T., Jaudzems K., Shilkova O., Francis J., Johansson M., Laity P.R., Sahin C., Chatterjee U., Kronqvist N., Barajas-Ledesma E., Kumar R., Chen G., Strömberg R., Abelein A., Langton M., Landreh M., Barth A., Holland C., Johansson J., Rising A. Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform. Nat. Commun. (2022) 13: 4695. DOI
- Bobrovs R., Basens E.E., Drunka L., Kanepe I., Matisone S., Velins K.K., Andrianov V., Leitis G., Zelencova-Gopejenko D., Rasina D., Jirgensons A., Jaudzems K. Exploring Aspartic Protease Inhibitor Binding to Design-Selective Antimalarials. J. Chem. Inf. Model. (2022) 62: 3263–3273. DOI
- Toleikis Z., Bobrovs R., Janoniene A., Lends A., Ziaunys M., Baronaite I., Petrauskas V., Kitoka K., Smirnovas V., Jaudzems K. Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy. Int. J. Mol. Sci. (2022) 23: 6781. DOI
- Šede M., Fridmanis J., Otikovs M., Johansson J., Rising A., Kronqvist N., Jaudzems K. Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization. Front. Mol. Biosci. (2022) 9: 936887. DOI
- Spunde K., Vigante B., Dubova U.N., Sipola A., Timofejeva I., Zajakina A., Jansons J., Plotniece A., Pajuste K., Sobolev A., Muhamadejev R., Jaudzems K., Duburs G., Kozlovska T. Design and Synthesis of Hepatitis B Virus (HBV) Capsid Assembly Modulators and Evaluation of Their Activity in Mammalian Cell Model. Pharmaceuticals (2022) 15: 773. DOI
- Le Marchand T., Schubeis T., Bonaccorsi M., Paluch P., Lalli D., Pell A.J., Andreas L.B., Jaudzems K., Stanek J., Pintacuda G. 1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning. Chem. Rev. (2022) 122: 9943-10018. DOI
- Sarr M., Kitoka K., Walsh-White K.A., Kaldmäe M., Metlāns R., Tārs K., Mantese A., Shah D., Landreh M., Rising A., Johansson J., Jaudzems K., Kronqvist N. The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence. J. Biol. Chem. (2022) 298: 101913. DOI
- Arndt T., Greco G., Schmuck B., Bunz J., Shilkova O., Francis J., Pugno N.M., Jaudzems K., Barth A., Johansson J., Rising A. Engineered Spider Silk Proteins for Biomimetic Spinning of Fibers with Toughness Equal to Dragline Silks. Adv. Funct. Mater. (2022) 32: 2200986. DOI
- Bahri S., Silvers R., Michael B., Jaudzems K., Lalli D., Casano G., Ouari O., Lesage A., Pintacuda G., Linse S., Griffin R.G. 1H detection and dynamic nuclear polarization–enhanced NMR of Aβ1-42 fibrils. Proc. Natl. Acad. Sci. USA (2022) 119: e2114413119. DOI
- Bobrovs R., Kanepe I., Narvaiss N., Patetko L., Kalnins G., Sisovs M, Bula A.L., Grinberga S., Boroduskis M., Ramata-Stunda A., Rostoks N., Jirgensons A., Tars K., Jaudzems K. Discovery of SARS-CoV-2 Nsp14 and Nsp16 Methyltransferase Inhibitors by High-Throughput Virtual Screening. Pharmaceuticals (2021) 14: 1243. DOI
- Kitoka K., Skrabana R., Gasparik N., Hritz J., Jaudzems K. NMR Studies of Tau Protein in Tauopathies. Front. Mol. Biosci. (2021) 8: 761227. DOI
- Bobrovs R., Auzins A.A., Drunka L., Metlans R., Muhamadejevs R., Jaudzems K. Using HOESY NMR Spectroscopy to Characterize Prenucleation Aggregates. Cryst. Growth Des. (2021) 21: 6166–6172. DOI
- Fridmanis J., Toleikis Z., Sneideris T., Ziaunys M., Bobrovs R., Smirnovas V., Jaudzems K. Aggregation Condition–Structure Relationship of Mouse Prion Protein Fibrils. Int. J. Mol. Sci. (2021) 22: 9635. DOI
- Toleikis Z., Ziaunys M., Baranauskiene L., Petrauskas V., Jaudzems K., Smirnovas V. S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation. Int. J. Mol. Sci. (2021) 22: 7972. DOI
- Bobiļeva O., Bobrovs R., Kaņepe I., Patetko L., Kalniņš G., Šišovs M, Bula A.L., Grīnberga S., Borodušķis M., Ramata-Stunda A., Rostoks N., Jirgensons A., Ta̅rs K., Jaudzems K. Potent SARS-CoV-2 mRNA Cap Methyltransferase Inhibitors by Bioisosteric Replacement of Methionine in SAM Cosubstrate. ACS Med. Chem. Lett. (2021) 12: 1102-1107. DOI
- Jaudzems K., Kirsteina A., Schubeis T., Casano G., Ouari O., Bogans J., Kazaks A., Tars K., Lesage A., Pintacuda G. Structural Analysis of an Antigen Chemically‐Coupled on Virus‐Like Particles in Vaccine Formulation. Angew. Chem. Int. Ed. (2021) 60: 12847-12851. DOI
- Ūdris N., Jaudzems K., Smits G. Total Synthesis of the Proposed Structure of Uncarialin A. J. Org. Chem. (2021) 86: 6927–6930. DOI
- Altincekic N., Korn S.M., Qureshi N.S., Dujardin M., Ninot-Pedrosa M., Abele R., Abi Saad M.J., Alfano C., Almeida F.C.L., Alshamleh I., de Amorim G.C., Anderson T.K., Anobom C.D., Anorma C., Bains J.K., Bax A., Blackledge M., Blechar J., Böckmann A., Brigandat L., Bula A., Bütikofer M., Camacho-Zarco A.R., Carlomagno T., Caruso I.P., Ceylan B., Chaikuad A., Chu F., Cole L., Crosby M.G., de Jesus V., Dhamotharan K., Felli I.C., Ferner J., Fleischmann Y., Fogeron M.-L., Fourkiotis N.K., Fuks C., Fürtig B., Gallo A., Gande S.L., Gerez J.A., Ghosh D., Gomes-Neto F., Gorbatyuk O., Guseva S., Hacker C., Häfner S., Hao B., Hargittay B., Henzler-Wildman K., Hoch J.C., Hohmann K.F., Hutchison M.T., Jaudzems K., Jović K., Kaderli J., Kalniņš G., Kaņepe I., Kirchdoerfer R.N., Kirkpatrick J., Knapp S., Krishnathas R., Kutz F., zur Lage S., Lambertz R., Lang A., Laurents D., Lecoq L., Linhard V., Löhr F., Malki A., Bessa L.M., Martin R.W., Matzel T., Maurin D., McNutt S.W., Mebus-Antunes N.C., Meier B.H., Meiser N., Mompeán M., Monaca E., Montserret R., Mariño Perez L., Moser C., Muhle-Goll C., Neves-Martins T.C., Ni X., Norton-Baker B., Pierattelli R., Pontoriero L., Pustovalova Y., Ohlenschläger O., Orts J., Da Poian A.T., Pyper D.J., Richter C., Riek R., Rienstra C.M., Robertson A., Pinheiro A.S., Sabbatella R., Salvi N., Saxena K., Schulte L., Schiavina M., Schwalbe H., Silber M., Almeida M.dS., Sprague-Piercy M.A., Spyroulias G.A., Sreeramulu S., Tants J.-N., Tārs K., Torres F., Töws S., Treviño M.Á., Trucks S., Tsika A.C., Varga K., Wang Y., Weber M.E., Weigand J.E., Wiedemann C., Wirmer-Bartoschek J., Wirtz Martin M.A., Zehnder J., Hengesbach M. and Schlundt A. Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications. Front. Mol. Biosci. (2021) 8: 653148. DOI
- Muhamadejev R., Melngaile R., Paegle P., Zibarte I., Petrova M., Jaudzems K., Veliks J. Residual Solvent Signal of CDCl3 as a qNMR Internal Standard for Application in Organic Chemistry Laboratory. J. Org. Chem. (2021) 86: 3890–3896. DOI
- Fridmanis J., Otikovs M., Brangulis K., Tārs K., Jaudzems K. Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family. Proteins (2021) 89: 588–594. DOI
- Bobrovs R., Drunka L., Auzins A.A., Jaudzems K., Salvalaglio M. Polymorph-Selective Role of Hydrogen Bonding and π–π Stacking in p-Aminobenzoic Acid Solutions. Cryst. Growth Des. (2021) 21: 436–448. DOI
- Makrecka-Kuka M., Dimitrijevs P., Domracheva I., Jaudzems K., Dambrova M., Arsenyan P. Fused isoselenazolium salts suppress breast cancer cell growth by dramatic increase in pyruvate-dependent mitochondrial ROS production. Sci. Rep. (2020) 10: 21595. DOI
- Fridmanis J., Bobrovs R., Brangulis K., Tārs K., Jaudzems K. Structural and Functional Analysis of BBA03, Borrelia burgdorferi Competitive Advantage Promoting Outer Surface Lipoprotein. Pathogens (2020) 9: 826. DOI
- Rasina D., Stakanovs G., Kanepe-Lapsa I., Bobrovs R., Jaudzems K., Jirgensons A. Synthesis of 2-aminopyridopyrimidinones and their plasmepsin I, II, IV inhibition potency. Chem. Heterocycl. Compd. (2020) 56: 786–792. DOI
- 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. High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain. Sci. Rep. (2020) 10: 235. DOI
- Brangulis K., Akopjana I., Petrovskis I., Kazaks A., Zelencova D., Jekabsons A., Jaudzems K., Tars K. 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. Biochim. Biophys. Acta Gen. Subj. (2020) 1864: 129499. DOI
- Jaudzems K., Kurbatska V., Jēkabsons A., Bobrovs R., Rudevica Z., Leonchiks A. Targeting Bacterial Sortase A with Covalent Inhibitors: 27 New Starting Points for Structure-Based Hit-to-Lead Optimization. ACS Infect. Dis. (2020) 6: 186-194. DOI
- Brangulis K., Akopjana I., Petrovskis I., Kazaks A., Jekabsons A., Jaudzems K., Viksna A., Bertins M., Tars K. Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection. FEBS Lett. (2020) 594: 317-326. DOI
- Mohammadi P., Aranko A.S., Landowski C.P., Ikkala O., Jaudzems K., Wagermaier W., Linder M.B. Biomimetic composites with enhanced toughening using silk-inspired triblock proteins and aligned nanocellulose reinforcements. Sci. Adv. (2019) 5: eaaw2541. DOI
- Bobrovs R., Jaudzems K., Jirgensons A. Exploiting Structural Dynamics To Design Open-Flap Inhibitors of Malarial Aspartic Proteases. J. Med. Chem. (2019) 62: 8931-8950. DOI
- Gupta R., Zhang H., Lu M., Hou G., Caporini M., Rosay M., Maas W., Struppe J., Ahn J., Byeon I.L., Oschkinat H., Jaudzems K., Barbet-Massin E., Emsley L., Pintacuda G., Lesage A., Gronenborn A.M., Polenova T. Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies. J. Phys. Chem. B (2019) 123: 5048-5058. DOI
- Jaudzems K., Polenova T., Pintacuda G., Oschkinat H., Lesage A. DNP NMR of biomolecular assemblies. J. Struct. Biol. (2019) 206: 90–98. DOI
- 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. Peptidomimetic plasmepsin inhibitors with potent anti-malarial activity and selectivity against cathepsin D. Eur. J. Med. Chem. (2019) 163: 344-352. DOI
- Kinena L., Leitis G., Kanepe‐Lapsa I., Bobrovs R., Jaudzems K., Ozola V., Suna E., Jirgensons A. Azole‐based non‐peptidomimetic plasmepsin inhibitors. Arch. Pharm. Chem. Life Sci. (2018) 351: 1800151. DOI
- Sarr M., Kronqvist N., Chen G., Aleksis R., Purhonen P., Hebert H., Jaudzems K., Rising A., Johansson J. A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein. FEBS J. (2018) 285: 1873–1885. DOI
- Rasina D., Stakanovs G., Borysov O.V., Pantelejevs T., Bobrovs R., Kanepe-Lapsa I., Tars K., Jaudzems K., Jirgensons A. 2-Aminoquinazolin-4(3H)-one based plasmepsin inhibitors with improved hydrophilicity and selectivity. Bioorg. Med. Chem. (2018) 26: 2488–2500. DOI
- 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. Dynamic nuclear polarization enhanced biomolecular NMR spectroscopy at high magnetic field with fast magic-angle spinning. Angew. Chem. Int. Ed. (2018) 57: 7458-7462. DOI
- 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. N-Leucinyl Benzenesulfonamides as Structurally Simplified Leucyl-tRNA Synthetase Inhibitors. ACS Med. Chem. Lett. (2018) 9: 84–88. DOI
- Otikovs M., Andersson M., Jia Q., Nordling K., Meng Q., Andreas L.B., Pintacuda G., Johansson J., Rising A., Jaudzems K. Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy. Angew. Chem. Int. Ed. (2017) 56: 12571–12575. DOI
- Cala-De Paepe D., Stanek J., Jaudzems K., Tars K., Andreas L.B., Pintacuda G. Is protein deuteration beneficial for proton detected solid-state NMR at and above 100 kHz magic-angle spinning? Solid State Nucl. Magn. Reson. (2017) 87: 126–136. DOI
- Aleksis R., Oleskovs F., Jaudzems K., Pahnke J., Biverstål H. Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity. Biochimie (2017) 140: 176-192. DOI
- Kronqvist N., Sarr M., Lindqvist A., Nordling K., Otikovs M., Venturi L., Pioselli B., Purhonen P., Landreh M., Biverstål H., Toleikis Z., Sjoberg L., Robinson C.V., Pelizzi N., Jornvall H., Hebert H., Jaudzems K., Curstedt T., Rising A., Johansson J. Efficient protein production inspired by how spiders make silk. Nat. Commun. (2017) 8: 15504. DOI (Full text)
- 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. NMR spectroscopic assignment of backbone and side-chain protons in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils. Angew. Chem. Int. Ed. (2016) 55: 15504-15509. DOI
- Aleksis R., Jaudzems K., Muceniece R., Liepinsh E. Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions. Peptides (2016) 85: 56–62. DOI
- Recacha R., Jaudzems K., Akopjana I., Jirgensons A., Tars K. Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins. Acta Cryst. (2016) F72: 659–666. DOI
- 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. Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages. J. Mol. Biol. (2016) 428: 4267–4279. DOI
- Andreas L.B., Jaudzems K., Stanek J., Lalli D., Bertarello A., Le Marchand T., Cala-De Paepe D., Kotelovica S., Akopjana I., Knott B., Wegner S., Engelke F., Lesage A., Emsley L., Tars K., Herrmann T., Pintacuda G. Structure of fully protonated proteins by proton-detected magic-angle spinning NMR. Proc. Natl. Acad. Sci. USA (2016) 113: 9187–9192. DOI
- Tjernberg L.O., Rising A., Johansson J., Jaudzems K. and Westermark P. Transmissible amyloid. J. Intern. Med. (2016) 280: 153–163. DOI
- 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. Fragment-Based Discovery of 2-Aminoquinazolin-4(3H)-ones As Novel Class Nonpeptidomimetic Inhibitors of the Plasmepsins I, II, and IV. J. Med. Chem. (2016) 59: 374–387. DOI
- Recacha R., Leitans J., Akopjana I., Aprupe L., Trapencieris P., Jaudzems K., Jirgensons A., Tars K. Structures of plasmepsin II from Plasmodium falciparum in complex with two hydroxyethylamine-based inhibitors. Acta Cryst. (2015) F71: 1531–1539. DOI
- Brangulis K., Jaudzems K., Petrovskis I., Akopjana I., Kazaks A., Tars K. Structural and functional analysis of BB0689 from Borrelia burgdorferi, a member of the bacterial CAP superfamily. J. Struct. Biol. (2015) 192: 320–330. DOI
- Otikovs M., Chen G., Nordling K., Landreh M., Meng Q., Jörnvall H., Kronqvist N., Rising A., Johansson J., Jaudzems K. Diversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal Domains. ChemBioChem (2015) 16: 1720–1724. DOI | Back Cover
- Chen W.N., Kuppan K.V., Lee M.D., Jaudzems K., Huber T., Otting G. O-tert-Butyltyrosine, an NMR tag for high-molecular weight systems and measurements of submicromolar ligand binding affinities. J. Am. Chem. Soc. (2015) 137: 4581–4586. DOI
- Andreas L.B., Le Marchand T., Jaudzems K., Pintacuda G. High-resolution proton-detected NMR of proteins at very fast MAS. J. Magn. Reson. (2015) 253: 36–49. DOI
- Jaudzems K., Pedrini B., Geralt M., Serrano P., Wüthrich K. J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4. J. Biomol. NMR (2015) 61: 65–72. DOI
- Zhulenkovs D., Rudevica Z., Jaudzems K., Turks M., Leonchiks A. Discovery and structure–activity relationship studies of irreversible benzisothiazolinone-based inhibitors against Staphylococcus aureus sortase A transpeptidase. Bioorg. Med. Chem. (2014) 22: 5988–6003. DOI
- 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. Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning. J. Am. Chem. Soc. (2014) 136: 12489–12497. DOI
- 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. Carbonic Anhydrase Generates CO2 and H+ That Drive Spider Silk Formation Via Opposite Effects on the Terminal Domains. PLoS Biol. (2014) 12: e1001921. DOI (Full text)
- Brangulis K., Petrovskis I., Kazaks A., Bogans J., Otikovs M., Jaudzems K., Ranka R., Tars K. Structural characterization of CspZ, a complement regulator factor H and FHL-1 binding protein from Borrelia burgdorferi. FEBS J. (2014) 281: 2613-2622. DOI
- 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. Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Nat. Commun. (2014) 5: 3254. DOI
- 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. Plasmepsin Inhibitory Activity and Structure-Guided Optimization of a Potent Hydroxyethylamine-Based Antimalarial Hit. ACS Med. Chem. Lett. (2014) 5: 373-377. DOI
- Zhulenkovs D., Jaudzems K., Zajakina A., Leonchiks A. Enzymatic activity of circular sortase A under denaturing conditions: An advanced tool for protein ligation. Biochem. Eng. J. (2014) 82: 200-209. DOI
- Aleksis R., Jaudzems K., Ivanova J., Žalubovskis R., Kalvinsh I., Liepinsh E. Reactivity of aziridine-2-carboxamide (Leakadine) with nucleophiles in aqueous solutions. Chem. Heterocycl. Comp. (2014) 49: 1589-1598. DOI
- 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. Out-and-back (13)C-(13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS. J. Biomol. NMR (2013) 56: 379-386. DOI
- Jaudzems K., Jia X., Yagi H., Zhulenkovs D., Graham B., Otting G., Liepinsh E. Structural Basis for 5′-End-Specific Recognition of Single-Stranded DNA by the R3H Domain from Human Sμbp-2. J. Mol. Biol. (2012) 424: 42-53. DOI
- Jaudzems K., Askarieh G., Landreh M., Nordling K., Hedhammar M., Jörnvall H., Rising A., Knight S.D., Johansson J. pH-Dependent Dimerization of Spider Silk N-Terminal Domain Requires Relocation of a Wedged Tryptophan Side Chain. J. Mol. Biol. (2012) 422: 477-487. DOI
- Johnson M.A., Jaudzems K., Wüthrich K. NMR structure of the SARS coronavirus nonstructural protein Nsp7 in solution at pH 6.5. J. Mol. Biol. (2010) 402: 619-628. DOI Full text
- Jaudzems K., Geralt M., Serrano P., Mohanty B., Horst R., Pedrini B., Elsliger M.-A., Wilson I.A., Wüthrich K. NMR structure of the protein NP_247299.1: comparison with the crystal structure. Acta Cryst. (2010) F66: 1367-1380. DOI (Full text)
- Mohanty B., Serrano P., Pedrini B., Jaudzems K., Geralt M., Horst R., Herrmann T., Elsliger M.-A., Wilson I.A., Wüthrich K. Comparison of NMR and crystal structures for the proteins TM1112 and TM1367. Acta Cryst. (2010) F66: 1381-1392. DOI (Full text)
- Serrano P., Pedrini B., Geralt M., Jaudzems K., Mohanty B., Horst R., Herrmann T., Elsliger M.-A., Wilson I.A., Wüthrich K. Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites. Acta Cryst. (2010) F66: 1393-1405. DOI (Full text)
- Jaudzems K., Kuka J., Gutsaits A., Zinovjevs K., Kalvinsh I., Liepinsh E., Liepinsh E., Dambrova M. Inhibition of carnitine acetyltransferase by mildronate, a regulator of energy metabolism. J. Enz. Inhib. Med. Chem. (2009) 24: 1269-1275. DOI
- Loscha K.V., Jaudzems K., Ioannou C., Su X.-C., Hill F.R., Otting G., Dixon N.E., Liepinsh E. A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader. Nucleic Acids Res. (2009) 37: 2395-2404. DOI (Full text)
Patenti
- Kinena L., Ozola V., Suna E., Leitis G., Jirgensons A., Jaudzems K., Kanepe-Lapsa I., Domracheva I. Substituted aminoalkylazoles as malarial aspartic protease inhibitors. WO2017069601.
- Pelšs J., Domračeva I., Žalubovskis R., Jaudzems K. Derivatives of 2,6-diaza-bicyclo[2.2.2]octane-3,5-ditione as potential anti-cancer agents. LV15160.
- Jirgensons A., Domraceva I., Kanepe-Lapsa I., Rasina D., Jaudzems K., Otikovs M. Novel substituted 2-aminoquinazolin-4(3H)-one derivatives as malarial aspartic protease inhibitors. WO2015063544.
- Zhulenkovs D., Rudevica Z., Leonchiks A., Jaudzems K., Zicane D., Turks M. N-(3-hydroxy-5,7-dimethyladamantan-1-yl)-2-(3-oxobenzo[d]isothiazol-2(3h)-yl)acetamide as a novel inhibitor for staphylococcus aureus sortase a. EP2875816.
- Zhulenkovs D., Rudevica Z., Leonchiks A., Jaudzems K., Zicane D., Turks M. N’-(2-(3-oxobenzo[d]isothiazol-2(3h)-yl)acetyl)adamantane-1-carbohydrazide as a novel inhibitor for staphylococcus aureus sortase A. EP2875815.