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-present 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

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