Dr. Kristaps Jaudzems

Laboratorijas vadītājs

E-pasts: kristaps.jaudzems@osi.lv
Tālrunis: (+371) 67014817

CV | Publikācijas

Curriculum Vitae

Dzimšanas dati 1984. gada 5. februāris, Rīga, Latvija

Izglītība

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

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

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

Latviešu (dzimtā), angļu un vācu (tekoši), krievu (pamatzināšanas)

Apbalvojumi un stipendijas

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

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

  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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