Dr. Kristaps Jaudzems

Group Leader

E-mail: kristaps.jaudzems@osi.lv
Tel.: (+371) 67014817

CV | Publications

Curriculum Vitae

Born February 5th, 1984 in Riga, Latvia

Education
03/2011 Ph. D. in Chemistry, Riga Technical University
Thesis: “NMR studies of protein structure, function and ligand interactions”. Supervisors: Prof. E. Liepinsh and prof. K. Wüthrich.
07/2008 M. Sc. in Chemical Technology, Riga Technical University
Thesis: “Protein NMR spectroscopy and spatial structure: examples of DnaI and cyclic Sortase A”. Supervisor: Prof. E. Liepinsh
07/2006 B. Sc. in Chemical Technology, Riga Technical University
Thesis: “Synthesis of selectively protected analogues of glucose-6-phosphate”. Supervisor: Prof. E. Bizdena

Research Positions and Training
09/2017-present Group Leader, Latvian Institute of Organic Synthesis
09/2015-08/2017 Marie Skłodowska-Curie Postdoctoral Fellow, Center for High Field NMR, Institute of Analytical Sciences, Lyon, France. Principal Investigator: Dr. Anne Lesage
11/2011-08/2015 Senior Researcher, Latvian Institute of Organic Synthesis
10-12/2014 Visiting Fellow, Australian National University, Canberra, Australia. Training in cell-free protein synthesis and paramagnetic NMR with Prof. Gottfried Otting
10-12/2012 Visiting Researcher, The Center for High-Field NMR, Lyon, France. Training in biomolecular solid-state NMR with Dr. Guido Pintacuda
06-09/2011 Postdoctoral Fellow (visiting), The Scripps Research Institute, La Jolla, CA, USA. Principal Investigator: Prof. Kurt Wüthrich
07/2010-05/2011 Research Assistant (Graduate Student), Latvian Institute of Organic Synthesis. Advisor: Prof. Edvards Liepinsh
09/2008-06/2010 External Graduate Student, The Scripps Research Institute, La Jolla, CA, USA. Advisor: Prof. Kurt Wüthrich
01/2007-08/2008 Research Assistant (Graduate Student), Latvian Institute of Organic Synthesis. Advisor: Prof. Edvards Liepinsh
05/2006-12/2006 Laboratory Assistant, Latvian Institute of Organic Synthesis
09/2002-05/2006 Laboratory Assistant, Riga Technical University

Teaching Experience
02/2021-present Professor, University of Latvia. Courses: NMR spectroscopy, Chemistry of natural compounds, Stereochemistry, Physical organic chemistry
03/2018-02/2021 Associate Professor, University of Latvia. Courses: NMR spectroscopy, Chemistry of natural compounds, Stereochemistry
03/2018-01/2019 Guest Associate Professor, Riga Technical University. Courses: Physical methods, NMR spectroscopy
02/2012-02/2018 Docent, Riga Technical University. Courses: Physical methods, NMR spectroscopy
2013-2017 Lecturer, University of Latvia. Course: NMR spectroscopy

Language skills
Latvian (native), english and german (fluent), russian (basic)

Awards and Fellowships
02/2022 Latvian Academy of Sciences diploma for one of most significant science achievements in Latvia in 2021
12/2019 Full member of Latvian Academy of Sciences
02/2018 Latvian Academy of Sciences diploma for one of most significant science achievements in Latvia in 2017
12/2017 Corresponding member of Latvian Academy of Sciences
10/2017 European Academy of Sciences and Arts promotion prize for young scientists
09/2015-08/2017 Marie Skłodowska-Curie individual fellowship
2013, 2015, 2017 Solomon Hiller award for BSc thesis supervisors (awarded by Riga Technical University and JSC OlainFarm)
09/2010-05/2011 European Social Fund fellowship
04/2009 Prof. Emīlija Gudriniece award to the best young scientist in chemistry
07/2006 JSC OlainFarm award for best BSc thesis

Publications

  1. 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
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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
  7. 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
  8. 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
  9. 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
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. Kitoka K., Skrabana R., Gasparik N., Hritz J., Jaudzems K. NMR Studies of Tau Protein in Tauopathies. Front. Mol. Biosci. (2021) 8: 761227. DOI
  16. 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
  17. 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
  18. 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
  19. 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
  20. 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
  21. Ūdris N., Jaudzems K., Smits G. Total Synthesis of the Proposed Structure of Uncarialin A. J. Org. Chem. (2021) 86: 6927–6930. DOI
  22. 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
  23. 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
  24. 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
  25. 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
  26. 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
  27. 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
  28. 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
  29. 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
  30. 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
  31. 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
  32. 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
  33. 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
  34. 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
  35. 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
  36. Jaudzems K., Polenova T., Pintacuda G., Oschkinat H., Lesage A. DNP NMR of biomolecular assemblies. J. Struct. Biol. (2019) 206: 90–98. DOI
  37. 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
  38. 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
  39. 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
  40. 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
  41. 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
  42. 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
  43. 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
  44. 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
  45. 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
  46. 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)
  47. 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
  48. 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
  49. 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
  50. 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
  51. 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
  52. Tjernberg L.O., Rising A., Johansson J., Jaudzems K. and Westermark P. Transmissible amyloid. J. Intern. Med. (2016) 280: 153–163. DOI
  53. 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
  54. 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
  55. 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
  56. 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
  57. 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
  58. 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
  59. 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
  60. 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
  61. 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
  62. 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)
  63. 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
  64. 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
  65. 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
  66. 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
  67. 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
  68. 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
  69. 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
  70. 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
  71. 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
  72. 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)
  73. 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)
  74. 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)
  75. 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
  76. 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)

Patents

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.

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