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Tutkimusryhmät
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Etusivu
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Juha Rouvinen

Juha Rouvinen

Laitoksen varajohtaja

Professori

Orgaanisen kemian, erityisesti biomolekyylien rakennetutkimuksen professori

Kemian laitos, Luonnontieteiden, metsätieteiden ja tekniikan tiedekunta

juha.rouvinen@uef.fi | 050 409 6387

Tiedot Julkaisut

S. 1960, FM 1986 (Joensuun yliopisto), vieraileva tutkija 1986 (Greifswaldin yliopisto), tohtorikoulutettava 1987-1990 (Uppsalan yliopisto). FT 1991 (Joensuun yliopisto), nuorempi tutkija 1990-1993 (Suomen akatemia) kristallografisen lääkeainesuunnittelun dosentti 1993 (Kuopion yliopisto), yliassistentti (Joensuun yliopisto) 1993-1996, akatemiatutkija 1996-2001, professori 2001- (Joensuun yliopisto/Itä-Suomen yliopisto), matemaattis-luonnontieteellisen tiedekunnan dekaani 2007-2009 (Joensuun yliopisto).

Tutkimusryhmät

Bio-orgaaninen kemia 01.01.2010 -

Avainsanat

allergia entsyymit proteiinikristallografia rakennebiologia

Julkaisut

103/104 kappaletta

Robust Approach for Quantifying Glucocorticoid Binding to the Anti-Cortisol Fab Fragment via Native Mass Spectrometry
Eronen, Veikko; Iljin, Kristiina; Paakkonen, Johan; Janis, Janne; Rouvinen, Juha; Nevanen, Tarja K; Hakulinen, Nina. 2024. ACS omega. [Publication Date: April 3, 2024]: 1-8
Structural insight to elucidate the binding specificity of the anti-cortisol Fab fragment with glucocorticoids
Eronen, Veikko; Tullila, Antti; Iljin, Kristiina; Rouvinen, Juha; Nevanen, Tarja K; Hakulinen, Nina. 2023. Journal of structural biology. 215:
Calculation and Visualization of Binding Equilibria in Protein Studies
Pääkkönen, Johan; Jänis, Janne; Rouvinen, Juha. 2022. ACS omega. 7: 10789-10795
Allergens and their associated small molecule ligands - their dual role in sensitization
Chruszcz, Maksymilian; Chew, Fook Tim; Hoffmann-Sommergruber, Karin; Hurlburt, Barry K; Mueller, Geoffrey A; Pomes, Anna; Rouvinen, Juha; Villalba, Mayte; Woehrl, Birgitta M; Breiteneder, Heimo. 2021. Allergy. 76: 2367-2382
Current state of and need for enzyme engineering of 2-deoxy-D-ribose 5-phosphate aldolases and its impact
Rouvinen, Juha; Andberg, Martina; Pääkkönen, Johan; Hakulinen, Nina; Koivula, Anu. 2021. Applied microbiology and biotechnology. 105: 6215-6228
Structural Insights into the Mechanisms Underlying the Kinetic Stability of GH28 Endo-Polygalacturonase
Tu, Tao; Wang, Zhiyun; Luo, Yan; Li, Yeqing; Su, Xiaoyun; Wang, Yuan; Zhang, Jie; Rouvinen, Juha; Yao, Bin; Hakulinen, Nina; Luo, Huiying. 2021. Journal of agricultural and food chemistry. 69: 815-823
Three-dimensional structure of xylonolactonase from Caulobacter crescentus: A mononuclear iron enzyme of the 6-bladed ß-propeller hydrolase family
Pääkkönen, Johan; Hakulinen, Nina; Andberg, Martina; Koivula, Anu; Rouvinen, Juha. 2021. Protein science. 2022; 31: 371-383
Xylonolactonase from Caulobacter crescentus Is a Mononuclear Nonheme Iron Hydrolase
Pääkkönen, Johan; Penttinen, Leena; Andberg, Martina; Koivula, Anu; Hakulinen, Nina; Rouvinen, Juha; Jänis, Janne. 2021. Biochemistry. 60: 3046-3049
Substrate specificity of 2-deoxy-D-ribose 5-phosphate aldolase (DERA) assessed by different protein engineering and machine learning methods
Voutilainen, Sanni; Heinonen, Markus; Andberg, Martina; Jokinen, Emmi; Maaheimo, Hannu; Pääkkönen, Johan; Hakulinen, Nina; Rouvinen, Juha; Lähdesmäki, Harri; Kaski, Samuel; Rousu, Juho; Penttilä, Merja; Koivula, Anu. 2020. Applied microbiology and biotechnology. 104: 10515-10529
Allergeenien ja IgE-vasta-aineiden rakennetutkimuksesta uuden sukupolven allergiarokotteiden kehitykseen
Takkinen, Kristiina; Rouvinen, Juha. 2019. Dosis. 35: 176-185
Bioconjugation with Aminoalkylhydrazine for Efficient Mass Spectrometry-Based Detection of Small Carbonyl Compounds
Thangaraj, SK; Voutilainen, S; Andberg, M; Koivula, A; Jänis, J; Rouvinen, J. 2019. ACS omega. 4: 13447-13453
Development of hypoallergenic variants of the major horse allergen Equ c 1 for immunotherapy by rational structure based engineering
Haka, J; Niemi, MH; Mattila, P; Jänis, J; Takkinen, K; Rouvinen, J. 2019. Scientific reports. 9: 20148
Quantitation of Thyroid Hormone Binding to Anti-Thyroxine Antibody Fab Fragment by Native Mass Spectrometry
Thangaraj, SK; Arola, H; Tullila, A; Nevanen, TK; Rouvinen, J; Jänis, J. 2019. ACS omega. 4: 18718-18724
The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry
Kiema, TR; Thapa, CJ; Laitaoja, M; Schmitz, W; Maksimainen, MM; Fukao, T; Rouvinen, J; Jänis, J; Wierenga, RK. 2019. Biochemical journal. 476: 307-332
Thermokinetic Analysis of Protein Subunit Exchange by Variable-Temperature Native Mass Spectrometry
Thangaraj, Senthil K; James, Salman; Rouvinen, Juha; Jänis, Janne. 2019. Biochemistry. 58: 5025-5029
A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes
Penttinen, L; Rutanen, C; Saloheimo, M; Kruus, K; Rouvinen, J; Hakulinen, N. 2018. PLoS ONE. 13: e0196691
Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes
Abbott, Wade; Alber, Orly; Bayer, Ed; Berrin, Jean-Guy; Boraston, Alisdair; Brumer, Harry; Brzezinski, Ryszard; Clarke, Anthony; Cobucci-Ponzano, Beatrice; Cockburn, Darrell; Coutinho, Pedro; Czjzek, Mirjam; Dassa, Bareket; Davies, Gideon John; Eijsink, Vincent; Eklof, Jens; Felice, Alfons; Ficko-Blean, Elizabeth; Pincher, Geoff; Fontaine, Thierry et al. (Incl. Rouvinen, Juha). 2018. Glycobiology. 28: 3-8
The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family
Rahman, MM; Andberg, M; Koivula, A; Rouvinen, J; Hakulinen, N. 2018. Scientific reports. 8: 865
Unraveling substrate specificity and catalytic promiscuity of Aspergillus oryzae catechol oxidase
Penttinen, Leena; Rutanen, Chiara; Jänis, Janne; Rouvinen, Juha; Hakulinen, Nina. 2018. Chembiochem. 19: 2348-2352
Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose
Chu Yindi, Tu Tao, Penttinen Leena, Xue Xianli, Wang Xiaoyu, Yi Zhuolin, Gong Li, Rouvinen Juha, Luo Huiying, Hakulinen Nina, Yao Bin, Su Xiaoyun. 2017. Journal of biological chemistry. 292: 19315-19327
The Crystal Structure of a Bacterial L-Arabinonate Dehydratase Contains a [2Fe-2S] Cluster
Rahman Mohammad Mubinur, Andberg Martina, Thangaraj Senthil Kumar, Parkkinen Tarja, Penttilä Merja, Jänis Janne, Koivula Anu, Rouvinen Juha, Hakulinen Nina. 2017. Acs chemical biology. 12: 1919-1927
Crystallization and X-ray diffraction analysis of an L-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii and a D-xylonate dehydratase from Caulobacter crescentus
Rahman Mohammad Mubinur, Andberg Martina, Koivula Aanu, Rouvinen Juha, Hakulinen Nina. 2016. Acta crystallographica section F : structural biology and crystallization communications. 72: 604-608
Identification of Small Molecule Compounds for Pharmacological Chaperone Therapy of Aspartylglucosaminuria
Banning A, Gülec C, Rouvinen J, Gray SJ, Tikkanen R. 2016. Scientific reports. 6: 37583
Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases
Taberman Helena, Parkkinen Tarja, Rouvinen Juha. 2016. Protein science. 25: 778-786
Dimerization of lipocalin allergens
Niemi Merja H, Rytkönen-Nissinen Marja, Miettinen Ilja, Jänis Janne, Virtanen Tuomas, Rouvinen Juha. 2015. Scientific reports. 5: 13841
Effect of active site mutation on pH activity and transglycosylation of Sulfolobus acidocaldarius ß-glycosidase
Anbarasan Sasikala, Timoharju Tommi, Barthomeuf Janice, Pastinen Ossi, Rouvinen Juha, Leisola Matti, Turunen Ossi. 2015. Journal of molecular catalysis B : enzymatic. 118: 62-69
Structure and function of Caulobacter crescentus aldose-aldose oxidoreductase
Taberman Helena, Andberg Martina, Koivula Anu, Hakulinen Nina, Penttilä Merja, Rouvinen Juha, Parkkinen Tarja. 2015. Biochemical journal. 472: 297-307
Three-dimensional structures of laccases
Hakulinen Nina, Rouvinen Juha. 2015. Cellular and molecular life sciences. 72: 857-868
Varpasalon Hirvoset
Rouvinen Juha. 2015. Suomen sukututkimusseuran vuosikirja. 48: 3-71
Antigenic Differences between AS03 Adjuvanted Influenza A (H1N1) Pandemic Vaccines: Implications for Pandemrix-Associated Narcolepsy Risk
Vaarala O, Vuorela A, Partinen M, Baumann M, Freitag TL, Meri S, Saavalainen P, Jauhiainen M, Soliymani R, Kirjavainen T, Olsen P, Saarenpää-Heikkilä O, Rouvinen J, Roivainen M, Nohynek H, Jokinen J, Julkunen I, Kilpi T. 2014. PLoS ONE. 9: e114361
Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens
Taberman H, Andberg M, Parkkinen Y, Richard P, Hakulinen N, Koivula A, Rouvinen J. 2014. Acta crystallographica section F : structural biology and crystallization communications. 70: 49-52
Structural aspects of dog allergies: The crystal structure of a dog dander allergen Can f 4
Niemi Merja H, Rytkönen-Nissinen Marja, Jänis Janne, Virtanen Tuomas, Rouvinen Juha. 2014. Molecular immunology. 61: 7-15
Structure and function of a decarboxylating Agrobacterium tumefaciens keto-deoxy-D-galactarate dehydratase
Taberman H, Andberg A, Parkkinen T, Jänis J, Penttilä M, Hakulinen N, Koivula A, Rouvinen J. 2014. Biochemistry. 53: 8052-8060
The crystal structure of acidic beta-galactosidase from Aspergillus oryzae
Maksimainen MM, Lampio A, Mertanen M, Turunen, O, Rouvinen J. 2013. International journal of biological macromolecules. 60: 109-115
The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae
Hakulinen N, Gasparetti C, Kaljunen H, Kruus K, Rouvinen J. 2013. Journal of biological inorganic chemistry. 18: 917-929
Structural analysis, enzymatic characterization, and catalytic mechanisms of beta-galactosidase from Bacillus circulans sp alkalophilus
Maksimainen M, Paavilainen S, Hakulinen N, Rouvinen J. 2012. Febs journal. 279: 1788-1798
Amphiphilic nanotubes in the crystal structure of a biosurfactant protein hydrophobin HFBII
Kallio JM & Rouvinen J. 2011. Chemical communications. 47: 9843-9845
Crystal structure of an ascomycete fungal laccase from Thielavia arenaria: Common features of asco-laccases
Kallio JP, Gasparetti C, Andberg M, Boer H, Koivula A, Kruus K, Rouvinen J & Hakulinen N. 2011. Febs journal. 278: 2283-2295
Crystal structure of uronate dehydrogenase from Agrobacterium tumefaciens
Parkkinen T, Boer H, Jänis J, Andberg M, Penttilä M, Koivula A & Rouvinen J. 2011. Journal of biological chemistry. 286: 27294-27300
Crystal structures of Trichoderma reesei &#946 -galactosidase reveal conformational changes in the active site
Maksimainen M, Hakulinen N, Kallio JM, Timoharju T, Turunen O & Rouvinen J.. 2011. Journal of structural biology. 174: 156-163
Crystallization and preliminary X-ray analysis of Aspergillus oryzae catechol oxidase
Kaljunen H, Gasparetti C, Kruus K, Rouvinen J & Hakulinen N. 2011. Acta crystallographica section F : structural biology and crystallization communications. 67: 672-674
Polysaccharides as Precipitants in Protein Crystallization for X-Ray Diffraction Studies
Laura Vepsäläinen, Katja Palmunen, Sinikka Uotila, Kalevi Visuri, Juha Rouvinen, and Johanna M. Kallio. 2011. Crystal growth and design. 11: 1152-1158
Probing the dioxygen route in Melanocarpus albomyces laccase with pressurised xenon-gas
Kallio JP, Rouvinen J, Kruus K & Hakulinen N. 2011. Biochemistry. 50: 4396-4398
The testosterone binding mechanism of an antibody derived from a naïve human scFv library
Niemi MH, Takkinen K, Amundsen L, Söderlund H, Rouvinen J & Höyhtyä M. 2011. Journal of molecular recognition. 24: 209-219
A Structural Insight into the Molecular Recognition of a (-) -Delta 9-Tetrahydrocannabinol and the Development of a Sensitive, One-Step, Homogeneous Immunocomplex-Based Assay for Its Detection
Merja H. Niemi, Laura Turunen, Timo Pulli, Tarja K. Nevanen, Matti Höyhtyä, Hans Söderlund, Juha Rouvinen, Kristiina Takkinen. 2010. Journal of molecular biology. 400: 803-814
Transient Dimers of Allergens
Juha Rouvinen, Janne Jänis, Marja-Leena Laukkanen, Sirpa Jylhä, Merja Niemi, Tero Päivinen, Soili Mäkinen-Kiljunen, Tari Haahtela, Hans Söderlund, Kristiina Takkinen. 2010. PLoS ONE. 5: e9037
Crystallization and preliminary diffractoin analysis of a b-galactosidase from Trichoderma reesei
Maksimainen M, Timoharju T, Kallio JM, Hakulinen N, Turunen O & Rouvinen J. 2009. Acta Cryst.. F65: 767-769
Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure
Andberg, M., Hakulinen, N., Auer, S., Saloheimo, M., Koivula, A., Rouvinen, J. and Kruus, K.. 2009. FEBS Journal. 276: 6285-6300
Preliminary X-ray analysis of twinned crystals of sarcosine dimethylglycine methyltransferase from Halorhodospira halochoris
Kallio, J. P., Jänis, J., Nyyssölä, A., Hakulinen, N., and Rouvinen, J.. 2009. Acta Cryst.. F65: 805-808
Structure-function studies of a Melanocarpus albomyces laccase suggest a pathway for oxidation of phenolic compounds
Kallio, J. P., Auer, S., Jänis, J., Andberg, M., Kruus, K., Rouvinen, J., Koivula, A., and Hakulinen, N. 2009. J. Mol. Biol.. 392: 895-909
The contribution of polystyrene nanospheres towards the crystallization of proteins
Kallio JM, Hakulinen N, Kallio JP, Niemi MH, Kärkkäinen S & Rouvinen J. 2009. PLoS ONE. 4: e4198
A near-atomic resolution structure of a Melanocapus albomyces laccase.
N. Hakulinen, M. Andberg, J. Kallio, A. Koivula, K. Kruus, J. Rouvinen. 2008. Journal of Structural Biology. 162: 29-39
Animal-derived lipocalin allergens exhibit immunoglobulin E cross-reactivity
S. Saarelainen, M. Rytkönen-Nissinen, J. Rouvinen, A. Taivainen, S. Auriola, A. Kauppinen, T. Kinnunen and T. Virtanen. 2008. Clinical and Experimental Allergy. 38: 374-381
Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine b- lactoglobulin allergen
Merja Niemi, Janne Jänis, Sirpa Jylhä, Johanna M. Kallio, Nina Hakulinen, Marja-Leena Laukkanen, Kristiina Takkinen and Juha Rouvinen. 2008. Acta crystallographica section F : structural biology and crystallization communications. F64: 25-28
Characterization of the pH-dependent dissociation of a multimeric metalloprotein Streptomyces rubiginosus xylose isomerase by ESI FT-ICR mass spectrometry
Janne Jänis, Salla Pasanen, Juha Rouvinen and Pirjo Vainiotalo. 2008. Journal of Mass Spectrometry. 43: 1376-1380
Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding
Tarja Parkkinen, Anu Koivula, Jari Vehmaanperä and Juha Rouvinen. 2008. Protein science. 17: 1383-1394
Irreversible thermal denaturation of Trichoderma reesei endo-1,4-b- xylanase II and its three disulfide mutants characterized by differential scanning calorimetry
Jänis J, Rouvinen J, Vainiotalo P, Turunen O & Shnyrov VL. 2008. International journal of biological macromolecules. 42: 75-80
Determination of steady-state kinetic parameters for a xylanase-catalyzed hydrolysis of neutral underivatized xylooligosaccharides by mass spectrometry
J. Jänis;P. Pulkkinen;J. Rouvinen;P. Vainiotalo. 2007. Anal. Biochem. 365: 165-173
Heterologous expression of Melanocarpus albomyces cellobiohydrolase Cel7B, and random mutagenesis to improve its thermostability
Voutilainen S.;Boer H.;Linder M.;Puranen T.;Rouvinen J.;Vehmaanperä J.;Koivula A.. 2007. Enzyme Microbiol Technology. 41: 234-243
Molecular dynamics studies on thermostability of family 11 xylanases
Purmonen M.;Valjakka J.;Takkinen K.;Laitinen T.;Rouvinen J.. 2007. Protein Engineering, Design & Selection. 20: 551-559
Molecular interactions between a recombinant IgE antibody and the b- lactoglobulin allergen
Niemi M.;Jylhä S.;Laukkanen M-L.;Söderlund H.;Mäkinen-Kiljunen S.;Kallio J.;Hakulinen N.;Haahtela T.;Takkinen K.;Rouvinen J.. 2007. Structure. 15: 1413-1421
Preliminary X- ray analysis of cellobiohydrolase Cel7B from Melanocarpus albomyces
Parkkinen T.;Koivula A.;Vehmaanperä J.;Rouvinen J.. 2007. Acta crystallographica section F : structural biology and crystallization communications. 63: 754-757
A crystallographic and spectroscopic study on the effect of X-ray radiation on the crystal structure of Melanocarpus albomyces laccase
Hakulinen Nina;Kruus Kristiina;Koivula Anu;Rouvinen Juha. 2006. Biochemical Biophysical Research Communications. 350: 929-934
Crystal Structures of an Enantioselective Fab-fragment in Free and Complex Forms
Parkkinen Tarja;Nevanen Tarja;Koivula Anu;Rouvinen Juha. 2006. Journal of Molecular Biology. 357: 471-480
Hydrophobin HFBII in detail - ultrahigh resolution structure of 0.75 Å
Hakanpää J.;Linder M.;Popov A.;Schmidt A.;Rouvinen J.. 2006. Acta Crystallographica Section D: Biological Crystallography. D62: 356-367
Structure-based stability engineering of the mouse IgG1 fab fragment by modifying constant domains
Teerinen Tuija;Valjakka Jarkko;Rouvinen Juha;Takkinen Kristiina. 2006. Journal of Molecular Biology. 361: 687-697
Two crystal structures of Trichoderma reesei hydrophobin HFBI - a structure of a protein amphiphile with and without detergent interaction
Hakanpää J.;Szilvay G.;Kaljunen H.;Maksimainen M.;Linder M.;Rouvinen J.. 2006. Protein science. 15: 2129-2140
Determination of Thiooxylo-oligosaccharide Binding to Family 11 Xylanases Using Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry and X-Ray Crystallography
Jänis J;Hakanpää J;Hakulinen N;Ibatullin FM;Hoxha A;Derrick PJ;Rouvinen J;Vainiotalo P. 2005. FEBS Journal. 272: 2317-2333
Analysis of microfibril angle of wood fibers using laser microscope polarimetry
Jari Palviainen;Juha Rouvinen and Raimo Silvennoinen. 2004. Optical engineering. 43: 186-191
Atomic Resolution Structure of the HFBII Hydrophobin, a Self-assembling Amphiphile
Hakanpää J;Paananen A;Askolin S;Nakari-Setälä T;Parkkinen T;Penttilä M;Linder MB & Rouvinen J. 2004. J. Biol. Chem.. 279: 534-539
Autoproteolytic activation of human aspartylglucosaminidase
Saarela J;Oinonen C;Jalanko A;Rouvinen J & Peltonen L. 2004. Biochem. J.. 378: 363-371
Characterization of Mutant Xylanases Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry: Stabilizing Contributions of Disulfide Bridges and N- Terminal Extensions
Jänis J;Turunen O;Leisola M;Derrick PJ;Rouvinen J & Vainiotalo P. 2004. Biochemistry. 43: 9556-9866
Characterization of the 3'exonuclease subunit DP1 of Methanococcus jannaschii replicative DNA polymerase D
Jokela M;Eskelinen A;Pospiech H;Rouvinen J;and Syväoja JE.. 2004. Nucl Acids Res. 32: 2430-2440
Crystallization and preliminary X-ray analysis of a novel Trichoderma reesei xylanase IV belonging to glycoside hydrolase family 5
Parkkinen T;Hakulinen N;Tenkanen M;Siika-aho M & Rouvinen J. 2004. Acta Cryst. D. 60: 542-544
Crystallization and preliminary X-ray characterization of Trichoderma reesei hydrophobin HFBII
Hakanpää J;Parkkinen T;Hakulinen N;Linder M & Rouvinen J. 2004. Acta Cryst. D. 60: 163-165
Laser light scattering from wood samples soaked in water or in benzyl benzoate
Simonaho S-P;Tolonen Y;Rouvinen J & Silvennoinen R. 2004. Optik. 114: 445-448
Crystal structure of 20k endoglucanase from Melanocarpus albomyces at 1.8 Å resolution.
Valjakka J & Rouvinen J. 2003. Acta Cryst. D. 59: 765-768
Laser light scattering from wood samples soaked in water and in bentzyl benzoate
Simo-Pekka Simonaho;Yrjö Tolonen;Juha Rouvinen and Raimo Silvennoinen. 2003. Optik. 114: 445-448
MMPBSA free energy analysis of endo1,4xylanase II (XynII)substrate complexes: binding of the reactive sugar in a skewboat and chair conformation.
Laitinen T;Rouvinen J & Peräkylä M. 2003. Org. Biomolec. Chem.. 1: 3535-3540
Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa
Hakulinen N;Turunen O;Jänis J;Leisola M & Rouvinen J:. 2003. Eur. J. Biochem.. 270: 1399-1412
A Mass Spectrometric Study of Metal-Binding to Osteocalcin
Nousiainen Marjaana;Derrick Peter;Kaartinen;Mäenpää Pekka;Rouvinen Juha;Vainiotalo Pirjo. 2002. Chemistry & Biology. 9: 195-202
Crystal structure of an in vitro affinity- and specificity-matured anti-testosterone Fab in complex with testosterone. Improved affinity results from small structural changes within tghe variable domains
Valjakka J.;Hemminki A.;Niemi S.;Söderlund H.;Takkinen K. & Rouvinen J.. 2002. J. Biol. Chem.. 277: 44021-44027
Structural insights into steroid hormone binding. The Crystal structures of a recombinant anti-testosterone Fab fragment in free and testosterone-bound forms
Valjakka J.;Takkinen K.;Teerinen T.;Söderlund H. & Rouvinen J.. 2002. J. Biol. Chem.. 277: 4183-4190
Combination of weakly stabilizing mutations with a disulfide bridge in the a-helix region of Trichoderma reesei endo-1,4-b-xylanase II increases the thermal stability through synergism
Turunen O;Etuaho K;Fenel F;Vehmaanperä J;Wu X;Rouvinen J;Leisola M. 2001. J. Biotechnol.. 88: 37-46
Improved Synthesis and Characterization of 1,3,4,6-tetra-O-acetyl-2-(N-acetylacetamido)-2-deoxy-beta-D-glucopyranose
Suihko Mona;Ahlgren Markku;Aulaskari Paula;Rouvinen Juha. 2001. Carbohydrate Research. 334: 337-341
Improved synthesis and characterization of 1,3,4,6-tetra-O-acetyl-2-(N-acetylacetamido)-2-deoxy-b-D-glucopyranose
Suihko M;Ahlgrén M;Aulaskari P;Rouvinen J. 2001. Carbohydrate Res.. 334: 337-341
Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations
Saarela J;Laine M;Oinonen C;von Schantz C;Jalanko A;Rouvinen J;Peltonen L. 2001. Human Mol. Genet.. 10: 983-995
Searching for the determinants of allergenicity in proteins of the lipocalin family
Rouvinen J;Virtanen T;Mäntyjärvi R. 2001. J. Chromatogr. B.. 756: 199-206
Thermostability of endo-1,4-beeta-Xylanase II from Trichoderma Reesei Studied by Electrospray Ionization Fourier-Transform Ion Cyclotron Resonance MS, Hydrogen/Deuterium-Exchange Reactions and Dynamic Light Scattering
Jänis Janne;Rouvinen Juha;Leisola Matti;Turunen Ossi;Vainiotalo Pirjo. 2001. Biochemical Journal. 356: 453-460
Ab initio quantum mechanical and density functional theory calculations of nucleophile- and nucleophile and acid-catalyzed opening of an epoxide ring: A model for the covalent binding of epoxyalkyl inhibitors to the active site of glycosidases
Laitinen T;Rouvinen J;Peräkylä M. 1998. J. Org. Chem.. 63: 8157-8162
Conformational changes and the catalytic cycle of endo-1,4-xylanase II from Trichoderma reesei: A molecular dynamics study
Muilu J;Törrönen A;Peräkylä M & Rouvinen J. 1998. Proteins. 31: 434-444
Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei
Hakulinen N;Tenkanen M;Rouvinen J. 1998. Acta Cryst. D. 54: 430-432
The role of the T-box for the function of the vitamin D receptor on different types of response elements
Quack M;Szafranski K;Rouvinen J & Carlberg C. 1998. Nucl. Acids Res.. 26: 5372-5378
Tryptophan 272: an essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A
Koivula A.;Kinnari T;Harjunpää V;Ruohonen L;Teleman A;Drakenberg;T;Rouvinen J;Jones TA;Teeri TT. 1998. FEBS Lett.. 429: 341-346
Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase
Tikkanen R;Peltola M;Oinonen C;Rouvinen J;Peltonen L. 1997. EMBO J.. 16: 6684-6693
Structural and functional properties of low molecular weight endo-1,4-b-xylanases
Törrönen A;Rouvinen J. 1997. Biotech.. 57: 137-149
Ab Initio Quantum Mechanical Study on the Catalytic Mechanism of Aspartylglucosaminidase (AGA): A Serine Protease-like Mechanism with an N-terminal Threonine and Substrate-Assisted Catalysis
Peräkylä M;Rouvinen J. 1996. Chem. Eur. J.. 2: 150-154
Covalent Binding of Three Epoxyalkyl-Xylosides to the Active Site of Endo-1,4-Xylanase II from Trichoderma reesei
Havukainen R;Törrönen A;Laitinen T;Rouvinen J. 1996. Biochemistry. 35: 9617-9624
Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation
Tikkanen R;Riikonen A;Oinonen C;Rouvinen J;Peltonen L. 1996. EMBO J.. 15: 2954-2960
Large-Scale Purification and Preliminary X-ray Diffraction Studies of Human Aspartylglucosaminidase
Tikkanen R;Rouvinen J;Törrönen A;Kalkkinen N;Peltonen L. 1996. Proteins. 24: 253-258
Preparation and Structure Determination of 1-Benzyl-, 1-Methyl- and 1H-5-[(2-Nitro-2-phenyl)ethenyl]imidazoles
Aulaskari;Paula;Ahlgren;Markku;Rouvinen;Juha;Vainiotalo;Pirjo;Pohjala;Esko;Vepsäläinen;Jouko. 1996. Journal of Heterocyclic Chemistry. 33: 1345-1354
The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169
Koivula A;Reinikainen T;Ruohonen L;Valkeajärvi A;Claeyssens M;Teleman O;Kleywegt GJ;Szardenings M;Rouvinen J;Jones TA;Teeri TT. 1996. Protein Eng.. 9: 691-699
Studies on the Reaction of 2-Aminoacetophenone with Thiophosgene
Morgenstern Olaf;Richter Peter;Rouvinen Juha;Mälkönen Pentti J.;Vainiotalo Pirjo;Hänninen Kari;Ahlgren Markku;Vepsäläinen Jouko. 1991. Journal of Heterocyclic Chemistry. 28: 1091-1097

University of Eastern Finland Joensuu, Kuopio © University of Eastern Finland

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Näytä asetukset

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Tarkenna hakuasi

Juha Rouvinen

Tutkimusryhmät

Avainsanat

Robust Approach for Quantifying Glucocorticoid Binding to the Anti-Cortisol Fab Fragment via Native Mass Spectrometry

Structural insight to elucidate the binding specificity of the anti-cortisol Fab fragment with glucocorticoids

Calculation and Visualization of Binding Equilibria in Protein Studies

Allergens and their associated small molecule ligands - their dual role in sensitization

Current state of and need for enzyme engineering of 2-deoxy-D-ribose 5-phosphate aldolases and its impact

Structural Insights into the Mechanisms Underlying the Kinetic Stability of GH28 Endo-Polygalacturonase

Three-dimensional structure of xylonolactonase from Caulobacter crescentus: A mononuclear iron enzyme of the 6-bladed ß-propeller hydrolase family

Xylonolactonase from Caulobacter crescentus Is a Mononuclear Nonheme Iron Hydrolase

Substrate specificity of 2-deoxy-D-ribose 5-phosphate aldolase (DERA) assessed by different protein engineering and machine learning methods

Allergeenien ja IgE-vasta-aineiden rakennetutkimuksesta uuden sukupolven allergiarokotteiden kehitykseen

Bioconjugation with Aminoalkylhydrazine for Efficient Mass Spectrometry-Based Detection of Small Carbonyl Compounds

Development of hypoallergenic variants of the major horse allergen Equ c 1 for immunotherapy by rational structure based engineering

Quantitation of Thyroid Hormone Binding to Anti-Thyroxine Antibody Fab Fragment by Native Mass Spectrometry

The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry

Thermokinetic Analysis of Protein Subunit Exchange by Variable-Temperature Native Mass Spectrometry

A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes

Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes

The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family

Unraveling substrate specificity and catalytic promiscuity of Aspergillus oryzae catechol oxidase

Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose

The Crystal Structure of a Bacterial L-Arabinonate Dehydratase Contains a [2Fe-2S] Cluster

Crystallization and X-ray diffraction analysis of an L-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii and a D-xylonate dehydratase from Caulobacter crescentus

Identification of Small Molecule Compounds for Pharmacological Chaperone Therapy of Aspartylglucosaminuria

Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases

Dimerization of lipocalin allergens

Effect of active site mutation on pH activity and transglycosylation of Sulfolobus acidocaldarius ß-glycosidase

Structure and function of Caulobacter crescentus aldose-aldose oxidoreductase

Three-dimensional structures of laccases

Varpasalon Hirvoset

Antigenic Differences between AS03 Adjuvanted Influenza A (H1N1) Pandemic Vaccines: Implications for Pandemrix-Associated Narcolepsy Risk

Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens

Structural aspects of dog allergies: The crystal structure of a dog dander allergen Can f 4

Structure and function of a decarboxylating Agrobacterium tumefaciens keto-deoxy-D-galactarate dehydratase

The crystal structure of acidic beta-galactosidase from Aspergillus oryzae

The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae

Structural analysis, enzymatic characterization, and catalytic mechanisms of beta-galactosidase from Bacillus circulans sp alkalophilus

Amphiphilic nanotubes in the crystal structure of a biosurfactant protein hydrophobin HFBII

Crystal structure of an ascomycete fungal laccase from Thielavia arenaria: Common features of asco-laccases

Crystal structure of uronate dehydrogenase from Agrobacterium tumefaciens

Crystal structures of Trichoderma reesei &#946 -galactosidase reveal conformational changes in the active site

Crystallization and preliminary X-ray analysis of Aspergillus oryzae catechol oxidase

Polysaccharides as Precipitants in Protein Crystallization for X-Ray Diffraction Studies

Probing the dioxygen route in Melanocarpus albomyces laccase with pressurised xenon-gas

The testosterone binding mechanism of an antibody derived from a naïve human scFv library

A Structural Insight into the Molecular Recognition of a (-) -Delta 9-Tetrahydrocannabinol and the Development of a Sensitive, One-Step, Homogeneous Immunocomplex-Based Assay for Its Detection

Transient Dimers of Allergens

Crystallization and preliminary diffractoin analysis of a b-galactosidase from Trichoderma reesei

Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure

Preliminary X-ray analysis of twinned crystals of sarcosine dimethylglycine methyltransferase from Halorhodospira halochoris

Structure-function studies of a Melanocarpus albomyces laccase suggest a pathway for oxidation of phenolic compounds

The contribution of polystyrene nanospheres towards the crystallization of proteins

A near-atomic resolution structure of a Melanocapus albomyces laccase.

Animal-derived lipocalin allergens exhibit immunoglobulin E cross-reactivity

Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine b- lactoglobulin allergen

Characterization of the pH-dependent dissociation of a multimeric metalloprotein Streptomyces rubiginosus xylose isomerase by ESI FT-ICR mass spectrometry

Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding

Irreversible thermal denaturation of Trichoderma reesei endo-1,4-b- xylanase II and its three disulfide mutants characterized by differential scanning calorimetry

Determination of steady-state kinetic parameters for a xylanase-catalyzed hydrolysis of neutral underivatized xylooligosaccharides by mass spectrometry

Heterologous expression of Melanocarpus albomyces cellobiohydrolase Cel7B, and random mutagenesis to improve its thermostability

Molecular dynamics studies on thermostability of family 11 xylanases

Molecular interactions between a recombinant IgE antibody and the b- lactoglobulin allergen

Preliminary X- ray analysis of cellobiohydrolase Cel7B from Melanocarpus albomyces

A crystallographic and spectroscopic study on the effect of X-ray radiation on the crystal structure of Melanocarpus albomyces laccase

Crystal Structures of an Enantioselective Fab-fragment in Free and Complex Forms

Hydrophobin HFBII in detail - ultrahigh resolution structure of 0.75 Å

Structure-based stability engineering of the mouse IgG1 fab fragment by modifying constant domains

Two crystal structures of Trichoderma reesei hydrophobin HFBI - a structure of a protein amphiphile with and without detergent interaction

Determination of Thiooxylo-oligosaccharide Binding to Family 11 Xylanases Using Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry and X-Ray Crystallography

Analysis of microfibril angle of wood fibers using laser microscope polarimetry

Atomic Resolution Structure of the HFBII Hydrophobin, a Self-assembling Amphiphile

Autoproteolytic activation of human aspartylglucosaminidase

Characterization of Mutant Xylanases Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry: Stabilizing Contributions of Disulfide Bridges and N- Terminal Extensions

Characterization of the 3'exonuclease subunit DP1 of Methanococcus jannaschii replicative DNA polymerase D

Crystallization and preliminary X-ray analysis of a novel Trichoderma reesei xylanase IV belonging to glycoside hydrolase family 5

Crystallization and preliminary X-ray characterization of Trichoderma reesei hydrophobin HFBII

Laser light scattering from wood samples soaked in water or in benzyl benzoate