| Year |
Citation |
Score |
| 2023 |
Pijning T, Vujičić-Žagar A, van der Laan JM, de Jong RM, Ramirez-Palacios C, Vente A, Edens L, Dijkstra BW. Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger. Protein Science : a Publication of the Protein Society. 33: e4856. PMID 38059672 DOI: 10.1002/pro.4856 |
0.326 |
|
| 2020 |
Ismaya WT, Tjandrawinata RR, Dijkstra BW, Beintema JJ, Nabila N, Rachmawati H. Relationship of Agaricus bisporus mannose-binding protein to lectins with β-trefoil fold. Biochemical and Biophysical Research Communications. PMID 32439171 DOI: 10.1016/J.Bbrc.2020.05.030 |
0.357 |
|
| 2020 |
Lai X, Wichers HJ, Soler-Lopez M, Dijkstra BW. Phenylthiourea Binding to Human Tyrosinase-Related Protein 1. International Journal of Molecular Sciences. 21. PMID 32019241 DOI: 10.3390/Ijms21030915 |
0.417 |
|
| 2019 |
Rohman A, Dijkstra BW, Puspaningsih NNT. β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides. International Journal of Molecular Sciences. 20. PMID 31698702 DOI: 10.3390/Ijms20225524 |
0.372 |
|
| 2019 |
Rohman A, Dijkstra BW. The role and mechanism of microbial 3-ketosteroid Δ-dehydrogenases in steroid breakdown. The Journal of Steroid Biochemistry and Molecular Biology. PMID 30991094 DOI: 10.1016/J.Jsbmb.2019.04.015 |
0.401 |
|
| 2018 |
Rohman A, van Oosterwijk N, Puspaningsih NNT, Dijkstra BW. Structural basis of product inhibition by arabinose and xylose of the thermostable GH43 β-1,4-xylosidase from Geobacillus thermoleovorans IT-08. Plos One. 13: e0196358. PMID 29698436 DOI: 10.1371/Journal.Pone.0196358 |
0.43 |
|
| 2017 |
Lai X, Wichers HJ, Soler-Lopez M, Dijkstra BW. Structure and Function of Human Tyrosinase and Tyrosinase-related Proteins. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 29052256 DOI: 10.1002/chem.201704410 |
0.32 |
|
| 2016 |
Bai Y, Gangoiti J, Dijkstra BW, Dijkhuizen L, Pijning T. Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria. Structure (London, England : 1993). PMID 28065507 DOI: 10.1016/J.Str.2016.11.023 |
0.351 |
|
| 2016 |
Lai X, Soler-Lopez M, Wichers HJ, Dijkstra BW. Large-Scale Recombinant Expression and Purification of Human Tyrosinase Suitable for Structural Studies. Plos One. 11: e0161697. PMID 27551823 DOI: 10.1371/journal.pone.0161697 |
0.331 |
|
| 2016 |
van Oosterwijk N, Willies SC, Hekelaar J, Terwisscha van Scheltinga AC, Turner NJ, Dijkstra BW. Structural basis of substrate range and enantioselectivity of two (S)-selective ω-transaminases. Biochemistry. PMID 27428867 DOI: 10.1021/Acs.Biochem.6B00370 |
0.496 |
|
| 2016 |
Lai X, Soler-Lopez M, Ismaya WT, Wichers HJ, Dijkstra BW. Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35 Å resolution. Acta Crystallographica. Section F, Structural Biology Communications. 72: 244-50. PMID 26919530 DOI: 10.1107/S2053230X16002107 |
0.443 |
|
| 2016 |
Hartanti L, Rohman A, Suwandi A, Dijkstra BW, Nurahman Z, Puspaningsih NNT. Mutation Analysis of the pKa Modulator Residue in β-D-xylosidase from Geobacillus Thermoleovorans IT-08: Activity Adaptation to Alkaline and High-Temperature Conditions Procedia Chemistry. 18: 39-48. DOI: 10.1016/J.Proche.2016.01.008 |
0.399 |
|
| 2016 |
Dijkstra BW, van Oosterwijk N, Rohman A. Structure and Catalytic Mechanism of 3-Ketosteroid Dehydrogenases Procedia Chemistry. 18: 3-11. DOI: 10.1016/J.Proche.2016.01.006 |
0.375 |
|
| 2015 |
Ballut L, Violot S, Shivakumaraswamy S, Thota LP, Sathya M, Kunala J, Dijkstra BW, Terreux R, Haser R, Balaram H, Aghajari N. Active site coupling in Plasmodium falciparum GMP synthetase is triggered by domain rotation. Nature Communications. 6: 8930. PMID 26592566 DOI: 10.1038/ncomms9930 |
0.331 |
|
| 2015 |
Rozeboom HJ, Yu S, Mikkelsen R, Nikolaev I, Mulder HJ, Dijkstra BW. Crystal structure of quinone-dependent alcohol dehydrogenase from Pseudogluconobacter saccharoketogenes. Protein Science : a Publication of the Protein Society. PMID 26440996 DOI: 10.1002/Pro.2818 |
0.379 |
|
| 2015 |
Floor RJ, Wijma HJ, Jekel PA, Terwisscha van Scheltinga AC, Dijkstra BW, Janssen DB. X-ray crystallographic validation of structure predictions used in computational design for protein stabilization. Proteins. 83: 940-51. PMID 25739581 DOI: 10.1002/Prot.24791 |
0.43 |
|
| 2015 |
Natalia D, Vidilaseris K, Ismaya WT, Puspasari F, Prawira I, Hasan K, Fibriansah G, Permentier HP, Nurachman Z, Subroto T, Dijkstra BW, Soemitro S. Effect of introducing a disulphide bond between the A and C domains on the activity and stability of Saccharomycopsis fibuligera R64 α-amylase. Journal of Biotechnology. 195: 8-14. PMID 25533400 DOI: 10.1016/J.Jbiotec.2014.12.002 |
0.389 |
|
| 2015 |
Heberling MM, Masman MF, Bartsch S, Wybenga GG, Dijkstra BW, Marrink SJ, Janssen DB. Ironing out their differences: dissecting the structural determinants of a phenylalanine aminomutase and ammonia lyase. Acs Chemical Biology. 10: 989-97. PMID 25494407 DOI: 10.1021/Cb500794H |
0.419 |
|
| 2015 |
Lai X, Soler-López M, Wichers HJ, Dijkstra BW. Structure and mechanism studies of human tyrosinase Acta Crystallographica Section a Foundations and Advances. 71: s226-s226. DOI: 10.1107/S205327331509659X |
0.3 |
|
| 2014 |
Wybenga GG, Szymanski W, Wu B, Feringa BL, Janssen DB, Dijkstra BW. Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from Taxus chinensis. Biochemistry. 53: 3187-98. PMID 24786474 DOI: 10.1021/Bi500187A |
0.42 |
|
| 2014 |
Pijning T, Vuji?i?-Žagar A, Kralj S, Dijkhuizen L, Dijkstra BW. Flexibility of truncated and full-length glucansucrase GTF180 enzymes from Lactobacillus reuteri 180. The Febs Journal. 281: 2159-71. PMID 24597929 DOI: 10.1111/Febs.12769 |
0.434 |
|
| 2014 |
Koch G, Nadal-Jimenez P, Reis CR, Muntendam R, Bokhove M, Melillo E, Dijkstra BW, Cool RH, Quax WJ. Reducing virulence of the human pathogen Burkholderia by altering the substrate specificity of the quorum-quenching acylase PvdQ. Proceedings of the National Academy of Sciences of the United States of America. 111: 1568-73. PMID 24474783 DOI: 10.1073/Pnas.1311263111 |
0.308 |
|
| 2014 |
Rozeboom HJ, Godinho LF, Nardini M, Quax WJ, Dijkstra BW. Crystal structures of two Bacillus carboxylesterases with different enantioselectivities. Biochimica Et Biophysica Acta. 1844: 567-75. PMID 24418394 DOI: 10.1016/J.Bbapap.2014.01.003 |
0.495 |
|
| 2013 |
Rohman A, van Oosterwijk N, Thunnissen AM, Dijkstra BW. Crystal structure and site-directed mutagenesis of 3-ketosteroid Δ1-dehydrogenase from Rhodococcus erythropolis SQ1 explain its catalytic mechanism. The Journal of Biological Chemistry. 288: 35559-68. PMID 24165124 DOI: 10.1074/Jbc.M113.522771 |
0.497 |
|
| 2013 |
Rozeboom HJ, Beldman G, Schols HA, Dijkstra BW. Crystal structure of endo-xylogalacturonan hydrolase from Aspergillus tubingensis. The Febs Journal. 280: 6061-9. PMID 24034788 DOI: 10.1111/Febs.12524 |
0.547 |
|
| 2013 |
Visweswaran GR, Steen A, Leenhouts K, Szeliga M, Ruban B, Hesseling-Meinders A, Dijkstra BW, Kuipers OP, Kok J, Buist G. AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis. Plos One. 8: e72167. PMID 23951292 DOI: 10.1371/Journal.Pone.0072167 |
0.363 |
|
| 2013 |
Rozeboom HJ, Yu S, Madrid S, Kalk KH, Zhang R, Dijkstra BW. Crystal structure of α-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism. The Journal of Biological Chemistry. 288: 26764-74. PMID 23902768 DOI: 10.1074/Jbc.M113.485896 |
0.492 |
|
| 2013 |
Schallmey M, Floor RJ, Hauer B, Breuer M, Jekel PA, Wijma HJ, Dijkstra BW, Janssen DB. Biocatalytic and structural properties of a highly engineered halohydrin dehalogenase. Chembiochem : a European Journal of Chemical Biology. 14: 870-81. PMID 23585096 DOI: 10.1002/cbic.201300005 |
0.361 |
|
| 2013 |
Crismaru CG, Wybenga GG, Szymanski W, Wijma HJ, Wu B, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB. Biochemical properties and crystal structure of a β-phenylalanine aminotransferase from Variovorax paradoxus. Applied and Environmental Microbiology. 79: 185-95. PMID 23087034 DOI: 10.1128/Aem.02525-12 |
0.458 |
|
| 2013 |
Leemhuis H, Pijning T, Dobruchowska JM, van Leeuwen SS, Kralj S, Dijkstra BW, Dijkhuizen L. Glucansucrases: three-dimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications. Journal of Biotechnology. 163: 250-72. PMID 22796091 DOI: 10.1016/J.Jbiotec.2012.06.037 |
0.336 |
|
| 2013 |
Bartsch S, Wybenga GG, Jansen M, Heberling MM, Wu B, Dijkstra BW, Janssen DB. Redesign of a phenylalanine aminomutase into a phenylalanine ammonia lyase Chemcatchem. 5: 1797-1802. DOI: 10.1002/Cctc.201200871 |
0.425 |
|
| 2012 |
Pijning T, Vuji?i?-Žagar A, Kralj S, Dijkhuizen L, Dijkstra BW. Structure of the α-1,6/α-1,4-specific glucansucrase GTFA from Lactobacillus reuteri 121. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 68: 1448-54. PMID 23192022 DOI: 10.1107/S1744309112044168 |
0.498 |
|
| 2012 |
Ruigrok VJ, Levisson M, Hekelaar J, Smidt H, Dijkstra BW, van der Oost J. Characterization of Aptamer-Protein Complexes by X-ray Crystallography and Alternative Approaches. International Journal of Molecular Sciences. 13: 10537-52. PMID 22949878 DOI: 10.3390/Ijms130810537 |
0.348 |
|
| 2012 |
van Oosterwijk N, Knol J, Dijkhuizen L, van der Geize R, Dijkstra BW. Structure and catalytic mechanism of 3-ketosteroid-Delta4-(5α)-dehydrogenase from Rhodococcus jostii RHA1 genome. The Journal of Biological Chemistry. 287: 30975-83. PMID 22833669 DOI: 10.1074/Jbc.M112.374306 |
0.462 |
|
| 2012 |
Anwar MA, Leemhuis H, Pijning T, Kralj S, Dijkstra BW, Dijkhuizen L. The role of conserved inulosucrase residues in the reaction and product specificity of Lactobacillus reuteri inulosucrase. The Febs Journal. 279: 3612-21. PMID 22823473 DOI: 10.1111/J.1742-4658.2012.08721.X |
0.436 |
|
| 2012 |
Wybenga GG, Crismaru CG, Janssen DB, Dijkstra BW. Structural determinants of the β-selectivity of a bacterial aminotransferase. The Journal of Biological Chemistry. 287: 28495-502. PMID 22745123 DOI: 10.1074/Jbc.M112.375238 |
0.384 |
|
| 2012 |
Rohman A, van Oosterwijk N, Dijkstra BW. Purification, crystallization and preliminary X-ray crystallographic analysis of 3-ketosteroid Δ1-dehydrogenase from Rhodococcus erythropolis SQ1. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 68: 551-6. PMID 22691786 DOI: 10.1107/S1744309112011025 |
0.426 |
|
| 2012 |
Augustyniak W, Brzezinska AA, Pijning T, Wienk H, Boelens R, Dijkstra BW, Reetz MT. Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention Protein Science. 21: 487-497. PMID 22267088 DOI: 10.1002/Pro.2031 |
0.456 |
|
| 2012 |
Brison Y, Pijning T, Malbert Y, Fabre É, Mourey L, Morel S, Potocki-Véronèse G, Monsan P, Tranier S, Remaud-Siméon M, Dijkstra BW. Functional and structural characterization of α-(1->2) branching sucrase derived from DSR-E glucansucrase. The Journal of Biological Chemistry. 287: 7915-24. PMID 22262856 DOI: 10.1074/Jbc.M111.305078 |
0.37 |
|
| 2012 |
Visweswaran GR, Dijkstra BW, Kok J. A genetically engineered protein domain binding to bacterial murein, archaeal pseudomurein, and fungal chitin cell wall material. Applied Microbiology and Biotechnology. 96: 729-37. PMID 22262228 DOI: 10.1007/S00253-012-3871-0 |
0.324 |
|
| 2012 |
Godinho LF, Reis CR, Rozeboom HJ, Dekker FJ, Dijkstra BW, Poelarends GJ, Quax WJ. Enhancement of the enantioselectivity of carboxylesterase A by structure-based mutagenesis. Journal of Biotechnology. 158: 36-43. PMID 22248594 DOI: 10.1016/J.Jbiotec.2011.12.026 |
0.428 |
|
| 2012 |
Wu B, Szyma?ski W, Wybenga GG, Heberling MM, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB. Mechanism-inspired engineering of phenylalanine aminomutase for enhanced β-regioselective asymmetric amination of cinnamates. Angewandte Chemie (International Ed. in English). 51: 482-6. PMID 22113970 DOI: 10.1002/Anie.201106372 |
0.378 |
|
| 2012 |
Opa?i? M, Hesp BH, Fusetti F, Dijkstra BW, Broos J. Structural investigation of the transmembrane C domain of the mannitol permease from Escherichia coli using 5-FTrp fluorescence spectroscopy. Biochimica Et Biophysica Acta. 1818: 861-8. PMID 22100747 DOI: 10.1016/J.Bbamem.2011.11.001 |
0.427 |
|
| 2012 |
Leemhuis H, Pijning T, Dobruchowska JM, Dijkstra BW, Dijkhuizen L. Glycosidic bond specificity of glucansucrases: On the role of acceptor substrate binding residues Biocatalysis and Biotransformation. 30: 366-376. DOI: 10.3109/10242422.2012.676301 |
0.307 |
|
| 2011 |
van Oosterwijk N, Knol J, Dijkhuizen L, van der Geize R, Dijkstra BW. Cloning, overexpression, purification, crystallization and preliminary X-ray analysis of 3-ketosteroid Δ(4)-(5α)-dehydrogenase from Rhodococcus jostii RHA1. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 1269-73. PMID 22102045 DOI: 10.1107/S1744309111028727 |
0.311 |
|
| 2011 |
Visweswaran GR, Dijkstra BW, Kok J. Murein and pseudomurein cell wall binding domains of bacteria and archaea--a comparative view. Applied Microbiology and Biotechnology. 92: 921-8. PMID 22012341 DOI: 10.1007/S00253-011-3637-0 |
0.308 |
|
| 2011 |
Pijning T, Anwar MA, Böger M, Dobruchowska JM, Leemhuis H, Kralj S, Dijkhuizen L, Dijkstra BW. Crystal structure of inulosucrase from Lactobacillus: insights into the substrate specificity and product specificity of GH68 fructansucrases. Journal of Molecular Biology. 412: 80-93. PMID 21801732 DOI: 10.1016/J.Jmb.2011.07.031 |
0.456 |
|
| 2011 |
Visweswaran GR, Dijkstra BW, Kok J. A minimum of three motifs is essential for optimal binding of pseudomurein cell wall-binding domain of Methanothermobacter thermautotrophicus. Plos One. 6: e21582. PMID 21738718 DOI: 10.1371/Journal.Pone.0021582 |
0.356 |
|
| 2011 |
Ismaya WT, Rozeboom HJ, Weijn A, Mes JJ, Fusetti F, Wichers HJ, Dijkstra BW. Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone. Biochemistry. 50: 5477-86. PMID 21598903 DOI: 10.1021/Bi200395T |
0.475 |
|
| 2011 |
Palomo M, Pijning T, Booiman T, Dobruchowska JM, van der Vlist J, Kralj S, Planas A, Loos K, Kamerling JP, Dijkstra BW, van der Maarel MJ, Dijkhuizen L, Leemhuis H. Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formed. The Journal of Biological Chemistry. 286: 3520-30. PMID 21097495 DOI: 10.1074/Jbc.M110.179515 |
0.503 |
|
| 2011 |
Natalia D, Vidilaseris K, Satrimafitrah P, Ismaya WT, Purkan, Permentier H, Fibriansah G, Puspasari F, Nurachman Z, Dijkstra BW, Soemitro S. Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64 Biologia. 66: 27-32. DOI: 10.2478/S11756-010-0151-2 |
0.383 |
|
| 2010 |
Vujicic-Zagar A, Pijning T, Kralj S, López CA, Eeuwema W, Dijkhuizen L, Dijkstra BW. Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes. Proceedings of the National Academy of Sciences of the United States of America. 107: 21406-11. PMID 21118988 DOI: 10.1073/Pnas.1007531107 |
0.492 |
|
| 2010 |
Kale A, Pijning T, Sonke T, Dijkstra BW, Thunnissen AM. Crystal structure of the leucine aminopeptidase from Pseudomonas putida reveals the molecular basis for its enantioselectivity and broad substrate specificity. Journal of Molecular Biology. 398: 703-14. PMID 20359484 DOI: 10.1016/J.Jmb.2010.03.042 |
0.444 |
|
| 2010 |
Bokhove M, Yoshida H, Hensgens CM, van der Laan JM, Sutherland JD, Dijkstra BW. Structures of an isopenicillin N converting Ntn-hydrolase reveal different catalytic roles for the active site residues of precursor and mature enzyme. Structure (London, England : 1993). 18: 301-8. PMID 20223213 DOI: 10.1016/J.Str.2010.01.005 |
0.5 |
|
| 2010 |
Bokhove M, Nadal Jimenez P, Quax WJ, Dijkstra BW. The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. Proceedings of the National Academy of Sciences of the United States of America. 107: 686-91. PMID 20080736 DOI: 10.1073/Pnas.0911839107 |
0.431 |
|
| 2009 |
Pijning T, van Pouderoyen G, Kluskens L, van der Oost J, Dijkstra BW. The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer. Febs Letters. 583: 3665-70. PMID 19854184 DOI: 10.1016/J.Febslet.2009.10.047 |
0.494 |
|
| 2009 |
Patel AK, van Oosterwijk N, Singh VK, Rozeboom HJ, Kalk KH, Siezen RJ, Jagannadham MV, Dijkstra BW. Crystallization and preliminary X-ray analysis of carnein, a serine protease from Ipomoea carnea. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 383-5. PMID 19342786 DOI: 10.1107/S1744309109008288 |
0.339 |
|
| 2009 |
Levisson M, Sun L, Hendriks S, Swinkels P, Akveld T, Bultema JB, Barendregt A, van den Heuvel RH, Dijkstra BW, van der Oost J, Kengen SW. Crystal structure and biochemical properties of a novel thermostable esterase containing an immunoglobulin-like domain. Journal of Molecular Biology. 385: 949-62. PMID 19013466 DOI: 10.1016/J.Jmb.2008.10.075 |
0.51 |
|
| 2008 |
Boersma YL, Pijning T, Bosma MS, van der Sloot AM, Godinho LF, Dröge MJ, Winter RT, van Pouderoyen G, Dijkstra BW, Quax WJ. Loop grafting of Bacillus subtilis lipase A: inversion of enantioselectivity. Chemistry & Biology. 15: 782-9. PMID 18721749 DOI: 10.1016/J.Chembiol.2008.06.009 |
0.381 |
|
| 2008 |
Rozeboom HJ, Bjerkan TM, Kalk KH, Ertesvåg H, Holtan S, Aachmann FL, Valla S, Dijkstra BW. Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii. The Journal of Biological Chemistry. 283: 23819-28. PMID 18574239 DOI: 10.1074/Jbc.M804119200 |
0.408 |
|
| 2008 |
Kelly RM, Leemhuis H, Rozeboom HJ, van Oosterwijk N, Dijkstra BW, Dijkhuizen L. Elimination of competing hydrolysis and coupling side reactions of a cyclodextrin glucanotransferase by directed evolution. The Biochemical Journal. 413: 517-25. PMID 18422488 DOI: 10.1042/Bj20080353 |
0.431 |
|
| 2008 |
Boersma YL, Dröge MJ, van der Sloot AM, Pijning T, Cool RH, Dijkstra BW, Quax WJ. A novel genetic selection system for improved enantioselectivity of Bacillus subtilis lipase A. Chembiochem : a European Journal of Chemical Biology. 9: 1110-5. PMID 18383241 DOI: 10.1002/Cbic.200700754 |
0.349 |
|
| 2008 |
Pijning T, Vuji?i?-Žagar A, Kralj S, Eeuwema W, Dijkhuizen L, Dijkstra BW. Biochemical and crystallographic characterization of a glucansucrase from Lactobacillus reuteri 180 Biocatalysis and Biotransformation. 26: 12-17. DOI: 10.1080/10242420701789163 |
0.453 |
|
| 2007 |
Rohman A, van Oosterwijk N, Kralj S, Dijkhuizen L, Dijkstra BW, Puspaningsih NN. Purification, crystallization and preliminary X-ray analysis of a thermostable glycoside hydrolase family 43 beta-xylosidase from Geobacillus thermoleovorans IT-08. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 63: 932-5. PMID 18007043 DOI: 10.1107/S1744309107046015 |
0.369 |
|
| 2007 |
Tiesinga JJ, van Pouderoyen G, Nardini M, Ransac S, Dijkstra BW. Structural basis of phospholipase activity of Staphylococcus hyicus lipase. Journal of Molecular Biology. 371: 447-56. PMID 17582438 DOI: 10.1016/J.Jmb.2007.05.041 |
0.483 |
|
| 2007 |
van Straaten KE, Barends TR, Dijkstra BW, Thunnissen AM. Structure of Escherichia coli Lytic transglycosylase MltA with bound chitohexaose: implications for peptidoglycan binding and cleavage. The Journal of Biological Chemistry. 282: 21197-205. PMID 17502382 DOI: 10.1074/Jbc.M701818200 |
0.805 |
|
| 2007 |
Barends TR, Bultema JB, Kaper T, van der Maarel MJ, Dijkhuizen L, Dijkstra BW. Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-amylase-like transglycosylase. The Journal of Biological Chemistry. 282: 17242-9. PMID 17420245 DOI: 10.1074/Jbc.M701444200 |
0.474 |
|
| 2007 |
Kaper T, Leemhuis H, Uitdehaag JC, van der Veen BA, Dijkstra BW, van der Maarel MJ, Dijkhuizen L. Identification of acceptor substrate binding subsites +2 and +3 in the amylomaltase from Thermus thermophilus HB8. Biochemistry. 46: 5261-9. PMID 17407266 DOI: 10.1021/Bi602408J |
0.441 |
|
| 2007 |
Wolterink-van Loo S, van Eerde A, Siemerink MA, Akerboom J, Dijkstra BW, van der Oost J. Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases. The Biochemical Journal. 403: 421-30. PMID 17176250 DOI: 10.1042/Bj20061419 |
0.464 |
|
| 2007 |
de Jong RM, Bazzacco P, Poelarends GJ, Johnson WH, Kim YJ, Burks EA, Serrano H, Thunnissen AM, Whitman CP, Dijkstra BW. Crystal structures of native and inactivated cis-3-chloroacrylic acid dehalogenase. Structural basis for substrate specificity and inactivation by (R)-oxirane-2-carboxylate. The Journal of Biological Chemistry. 282: 2440-9. PMID 17121835 DOI: 10.1074/Jbc.M608134200 |
0.447 |
|
| 2006 |
van Eerde A, Wolterink-van Loo S, van der Oost J, Dijkstra BW. Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 1061-6. PMID 17077480 DOI: 10.1107/S1744309106039583 |
0.323 |
|
| 2006 |
Vujici?-Zagar A, Dijkstra BW. Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 angstroms resolution. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 716-21. PMID 16880540 DOI: 10.1107/S1744309106024729 |
0.348 |
|
| 2006 |
Hamiaux C, van Eerde A, Parsot C, Broos J, Dijkstra BW. Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri. Embo Reports. 7: 794-9. PMID 16826238 DOI: 10.1038/Sj.Embor.7400753 |
0.419 |
|
| 2006 |
de Jong RM, Kalk KH, Tang L, Janssen DB, Dijkstra BW. The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family. Journal of Bacteriology. 188: 4051-6. PMID 16707696 DOI: 10.1128/Jb.01866-05 |
0.382 |
|
| 2006 |
Barends TR, Polderman-Tijmes JJ, Jekel PA, Williams C, Wybenga G, Janssen DB, Dijkstra BW. Acetobacter turbidans alpha-amino acid ester hydrolase: how a single mutation improves an antibiotic-producing enzyme. The Journal of Biological Chemistry. 281: 5804-10. PMID 16377627 DOI: 10.1074/Jbc.M511187200 |
0.483 |
|
| 2006 |
Dröge MJ, Boersma YL, van Pouderoyen G, Vrenken TE, Rüggeberg CJ, Reetz MT, Dijkstra BW, Quax WJ. Directed evolution of Bacillus subtilis lipase A by use of enantiomeric phosphonate inhibitors: crystal structures and phage display selection. Chembiochem : a European Journal of Chemical Biology. 7: 149-57. PMID 16342303 DOI: 10.1002/Cbic.200500308 |
0.452 |
|
| 2006 |
Dijkstra BW. Degradation of halogenated compounds: structures and catalytic mechanisms of dehalogenases Acta Crystallographica Section a Foundations of Crystallography. 62: s32-s32. DOI: 10.1107/S0108767306099363 |
0.452 |
|
| 2005 |
de Jong RM, Tiesinga JJ, Villa A, Tang L, Janssen DB, Dijkstra BW. Structural basis for the enantioselectivity of an epoxide ring opening reaction catalyzed by halo alcohol dehalogenase HheC. Journal of the American Chemical Society. 127: 13338-43. PMID 16173767 DOI: 10.1021/Ja0531733 |
0.357 |
|
| 2005 |
van Straaten KE, Dijkstra BW, Vollmer W, Thunnissen AM. Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold. Journal of Molecular Biology. 352: 1068-80. PMID 16139297 DOI: 10.1016/J.Jmb.2005.07.067 |
0.803 |
|
| 2005 |
Alagaratnam S, van Pouderoyen G, Pijning T, Dijkstra BW, Cavazzini D, Rossi GL, Van Dongen WM, van Mierlo CP, van Berkel WJ, Canters GW. A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: structural determinants of redox potential. Protein Science : a Publication of the Protein Society. 14: 2284-95. PMID 16131657 DOI: 10.1110/Ps.051582605 |
0.44 |
|
| 2005 |
Barends TR, de Jong RM, van Straaten KE, Thunnissen AM, Dijkstra BW. Escherichia coli MltA: MAD phasing and refinement of a tetartohedrally twinned protein crystal structure. Acta Crystallographica. Section D, Biological Crystallography. 61: 613-21. PMID 15858272 DOI: 10.1107/S0907444905005743 |
0.766 |
|
| 2005 |
Tang L, Torres Pazmiño DE, Fraaije MW, de Jong RM, Dijkstra BW, Janssen DB. Improved catalytic properties of halohydrin dehalogenase by modification of the halide-binding site. Biochemistry. 44: 6609-18. PMID 15850394 DOI: 10.1021/Bi047613Z |
0.421 |
|
| 2005 |
Yoshida H, Hensgens CM, van der Laan JM, Sutherland JD, Hart DJ, Dijkstra BW. An approach to prevent aggregation during the purification and crystallization of wild type acyl coenzyme A: isopenicillin N acyltransferase from Penicillium chrysogenum. Protein Expression and Purification. 41: 61-7. PMID 15802222 DOI: 10.1016/J.Pep.2005.02.007 |
0.381 |
|
| 2005 |
Krengel U, Rozeboom HJ, Kalk KH, Dijkstra BW. Crystallization and preliminary crystallographic analysis of endo-1,4-beta-xyalanase I from Aspergillus niger. Acta Crystallographica. Section D, Biological Crystallography. 52: 571-6. PMID 15299682 DOI: 10.1107/S0907444995014740 |
0.392 |
|
| 2005 |
Barends TRM, de Jong RM, van Straaten KE, Thunnissen AWH, Dijkstra BW. Escherichia coliMltA: MAD phasing and refinement of a tetartohedrally twinned protein crystal structure. Addendum and erratum Acta Crystallographica Section D Biological Crystallography. 61: 1172-1172. DOI: 10.1107/S0907444905013533 |
0.401 |
|
| 2004 |
Barends TR, Yoshida H, Dijkstra BW. Three-dimensional structures of enzymes useful for beta-lactam antibiotic production. Current Opinion in Biotechnology. 15: 356-63. PMID 15358004 DOI: 10.1016/J.Copbio.2004.06.009 |
0.375 |
|
| 2004 |
Alkema WB, Hensgens CM, Snijder HJ, Keizer E, Dijkstra BW, Janssen DB. Structural and kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase. Protein Engineering, Design & Selection : Peds. 17: 473-80. PMID 15254299 DOI: 10.1093/Protein/Gzh057 |
0.424 |
|
| 2004 |
van Eerde A, Hamiaux C, Pérez J, Parsot C, Dijkstra BW. Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity. Embo Reports. 5: 477-83. PMID 15088068 DOI: 10.1038/Sj.Embor.7400144 |
0.439 |
|
| 2004 |
Van Straaten KE, Dijkstra BW, Thunnissen AM. Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography. 60: 758-60. PMID 15039577 DOI: 10.1107/S0907444904002574 |
0.769 |
|
| 2004 |
Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L. Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge. Proteins. 54: 128-34. PMID 14705029 DOI: 10.1002/Prot.10516 |
0.413 |
|
| 2004 |
de Jong RM, Brugman W, Poelarends GJ, Whitman CP, Dijkstra BW. The X-ray structure of trans-3-chloroacrylic acid dehalogenase reveals a novel hydration mechanism in the tautomerase superfamily. The Journal of Biological Chemistry. 279: 11546-52. PMID 14701869 DOI: 10.1074/Jbc.M311966200 |
0.431 |
|
| 2004 |
Eggert T, Leggewie C, Puls M, Streit W, Van Pouderoyen G, Dijkstra BW, Jaeger KE. Novel biocatalysts by identification and design Biocatalysis and Biotransformation. 22: 139-144. DOI: 10.1080/10242420410001710056 |
0.334 |
|
| 2003 |
de Jong RM, Dijkstra BW. Structure and mechanism of bacterial dehalogenases: different ways to cleave a carbon-halogen bond. Current Opinion in Structural Biology. 13: 722-30. PMID 14675551 DOI: 10.1016/J.Sbi.2003.10.009 |
0.368 |
|
| 2003 |
Dijkstra BW, Matthews RG. Catalysis and regulation - from structure to function. Current Opinion in Structural Biology. 13: 706-8. PMID 14675548 DOI: 10.1016/J.Sbi.2003.10.014 |
0.32 |
|
| 2003 |
Barends TR, Dijkstra BW. Acetobacter turbidans alpha-amino acid ester hydrolase: merohedral twinning in P21 obscured by pseudo-translational NCS. Acta Crystallographica. Section D, Biological Crystallography. 59: 2237-41. PMID 14646082 DOI: 10.1107/S0907444903020729 |
0.399 |
|
| 2003 |
Fittipaldi M, Steiner RA, Matsushita M, Dijkstra BW, Groenen EJ, Huber M. Single-crystal EPR study at 95 GHz of the type 2 copper site of the inhibitor-bound quercetin 2,3-dioxygenase. Biophysical Journal. 85: 4047-54. PMID 14645093 DOI: 10.1016/S0006-3495(03)74818-8 |
0.308 |
|
| 2003 |
van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW. Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger. Febs Letters. 554: 462-6. PMID 14623112 DOI: 10.1016/S0014-5793(03)01221-3 |
0.49 |
|
| 2003 |
Verdon G, Albers SV, van Oosterwijk N, Dijkstra BW, Driessen AJ, Thunnissen AM. Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus. Journal of Molecular Biology. 334: 255-67. PMID 14607117 DOI: 10.1016/J.Jmb.2003.08.065 |
0.371 |
|
| 2003 |
de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW. Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site. The Embo Journal. 22: 4933-44. PMID 14517233 DOI: 10.1093/emboj/cdg479 |
0.375 |
|
| 2003 |
Leemhuis H, Kragh KM, Dijkstra BW, Dijkhuizen L. Engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exo-specificity. Journal of Biotechnology. 103: 203-12. PMID 12890607 DOI: 10.1016/S0168-1656(03)00126-3 |
0.463 |
|
| 2003 |
Fusetti F, Pijning T, Kalk KH, Bos E, Dijkstra BW. Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39. The Journal of Biological Chemistry. 278: 37753-60. PMID 12851408 DOI: 10.1074/Jbc.M303137200 |
0.434 |
|
| 2003 |
Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM. Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. Journal of Molecular Biology. 330: 343-58. PMID 12823973 DOI: 10.1016/S0022-2836(03)00575-8 |
0.443 |
|
| 2003 |
Leemhuis H, Rozeboom HJ, Wilbrink M, Euverink GJ, Dijkstra BW, Dijkhuizen L. Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1. Biochemistry. 42: 7518-26. PMID 12809508 DOI: 10.1021/Bi034439Q |
0.446 |
|
| 2003 |
Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L. The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity. Febs Letters. 541: 47-51. PMID 12706817 DOI: 10.1016/S0014-5793(03)00286-2 |
0.463 |
|
| 2003 |
Barends TR, Polderman-Tijmes JJ, Jekel PA, Hensgens CM, de Vries EJ, Janssen DB, Dijkstra BW. The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases. The Journal of Biological Chemistry. 278: 23076-84. PMID 12684501 DOI: 10.1074/Jbc.M302246200 |
0.406 |
|
| 2003 |
Snijder HJ, Timmins PA, Kalk KH, Dijkstra BW. Detergent organisation in crystals of monomeric outer membrane phospholipase A. Journal of Structural Biology. 141: 122-31. PMID 12615538 DOI: 10.1016/S1047-8477(02)00579-8 |
0.434 |
|
| 2003 |
Barends TR, Hensgens CM, Polderman-Tijmes JJ, Jekel PA, de Vries E, Janssen DB, Dijkstra BW. X-ray analysis of two antibiotic-synthesizing bacterial ester hydrolases: preliminary results. Acta Crystallographica. Section D, Biological Crystallography. 59: 158-60. PMID 12499556 DOI: 10.1107/S090744490201836X |
0.465 |
|
| 2003 |
Leemhuis H, Dijkstra BW, Dijkhuizen L. Thermoanaerobacterium thermosulfurigenes cyclodextrin glycosyltransferase. European Journal of Biochemistry / Febs. 270: 155-62. PMID 12492486 DOI: 10.1046/J.1432-1033.2003.03376.X |
0.36 |
|
| 2003 |
Funke SA, Eipper A, Reetz MT, Otte N, Thiel W, Van Pouderoyen G, Dijkstra BW, Jaeger KE, Eggert T. Directed evolution of an enantioselective Bacillus subtilis lipase Biocatalysis and Biotransformation. 21: 67-73. DOI: 10.1080/1024242031000110847 |
0.351 |
|
| 2002 |
Steiner RA, Kalk KH, Dijkstra BW. Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proceedings of the National Academy of Sciences of the United States of America. 99: 16625-30. PMID 12486225 DOI: 10.1073/Pnas.262506299 |
0.364 |
|
| 2002 |
Kooter IM, Steiner RA, Dijkstra BW, van Noort PI, Egmond MR, Huber M. EPR characterization of the mononuclear Cu-containing Aspergillus japonicus quercetin 2,3-dioxygenase reveals dramatic changes upon anaerobic binding of substrates. European Journal of Biochemistry / Febs. 269: 2971-9. PMID 12071961 DOI: 10.1046/J.1432-1033.2002.02973.X |
0.335 |
|
| 2002 |
Steiner RA, Meyer-Klaucke W, Dijkstra BW. Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 2. X-ray absorption studies of native enzyme and anaerobic complexes with the substrates quercetin and myricetin. Biochemistry. 41: 7963-8. PMID 12069586 DOI: 10.1021/Bi015974Y |
0.383 |
|
| 2002 |
Steiner RA, Kooter IM, Dijkstra BW. Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights. Biochemistry. 41: 7955-62. PMID 12069585 DOI: 10.1021/Bi0159736 |
0.451 |
|
| 2002 |
Kingma RL, Snijder HJ, Dijkstra BW, Dekker N, Egmond MR. Functional importance of calcium binding sites in outer membrane phospholipase A. Biochimica Et Biophysica Acta. 1561: 230-7. PMID 11997123 DOI: 10.1016/S0005-2736(02)00351-6 |
0.377 |
|
| 2002 |
Fusetti F, von Moeller H, Houston D, Rozeboom HJ, Dijkstra BW, Boot RG, Aerts JM, van Aalten DM. Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins. The Journal of Biological Chemistry. 277: 25537-44. PMID 11960986 DOI: 10.1074/jbc.M201636200 |
0.325 |
|
| 2002 |
Leemhuis H, Dijkstra BW, Dijkhuizen L. Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase. Febs Letters. 514: 189-92. PMID 11943149 DOI: 10.1016/S0014-5793(02)02362-1 |
0.397 |
|
| 2002 |
Hensgens CM, Kroezinga EA, van Montfort BA, van der Laan JM, Sutherland JD, Dijkstra BW. Purification, crystallization and preliminary X-ray diffraction of Cys103Ala acyl coenzyme A: isopenicillin N acyltransferase from Penicillium chrysogenum. Acta Crystallographica. Section D, Biological Crystallography. 58: 716-8. PMID 11914506 DOI: 10.1107/S0907444902003244 |
0.457 |
|
| 2002 |
Bokma E, Rozeboom HJ, Sibbald M, Dijkstra BW, Beintema JJ. Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis. European Journal of Biochemistry / Febs. 269: 893-901. PMID 11846790 DOI: 10.1046/J.0014-2956.2001.02721.X |
0.446 |
|
| 2002 |
Fusetti F, Schröter KH, Steiner RA, van Noort PI, Pijning T, Rozeboom HJ, Kalk KH, Egmond MR, Dijkstra BW. Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus. Structure (London, England : 1993). 10: 259-68. PMID 11839311 DOI: 10.1016/S0969-2126(02)00704-9 |
0.474 |
|
| 2002 |
Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM. Purification, crystallization and preliminary X-ray diffraction analysis of an archaeal ABC-ATPase. Acta Crystallographica. Section D, Biological Crystallography. 58: 362-5. PMID 11807278 DOI: 10.1107/S0907444901020765 |
0.395 |
|
| 2002 |
de Jong RM, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW. Crystallization and preliminary X-ray analysis of an enantioselective halohydrin dehalogenase from Agrobacterium radiobacter AD1. Acta Crystallographica. Section D, Biological Crystallography. 58: 176-8. PMID 11752805 DOI: 10.1107/S0907444901019618 |
0.404 |
|
| 2002 |
Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW. Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: Structural basis for substrate oxidation and electron transfer Journal of Biological Chemistry. 277: 3727-3732. PMID 11714714 DOI: 10.1074/Jbc.M109403200 |
0.435 |
|
| 2002 |
Leemhuis H, Uitdehaag JCM, Rozeboom HJ, Dijkstra BW, Dijkhuizen L. The remote substrate binding subsite -6 in cyclodextrin-glycosyltransferase controls the transferase activity of the enzyme via an induced-fit mechanism Journal of Biological Chemistry. 277: 1113-1119. PMID 11696539 DOI: 10.1074/Jbc.M106667200 |
0.425 |
|
| 2002 |
Eggert T, Van Pouderoyen G, Pencreac'h G, Douchet I, Verger R, Dijkstra BW, Jaeger KE. Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis Colloids and Surfaces B: Biointerfaces. 26: 37-46. DOI: 10.1016/S0927-7765(02)00033-4 |
0.471 |
|
| 2002 |
Uitdehaag JCM, Van Der Veen BA, Dijkhuizen L, Dijkstra BW. Catalytic mechanism and product specificity of cyclodextrin glycosyltransferase, a prototypical transglycosylase from the α-amylase family Enzyme and Microbial Technology. 30: 295-304. DOI: 10.1016/S0141-0229(01)00498-7 |
0.31 |
|
| 2001 |
Oubrie A, Huizinga EG, Rozeboom HJ, Kalk KH, De Jong GAH, Duine JA, Dijkstra BW. Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: Crystals with unique optical properties Acta Crystallographica Section D: Biological Crystallography. 57: 1732-1734. PMID 11679760 DOI: 10.1107/S0907444901013002 |
0.383 |
|
| 2001 |
Eggert T, Van Pouderoyen G, Dijkstra BW, Jaeger KE. Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in regulation of gene expression, biochemical properties, and three-dimensional structure Febs Letters. 502: 89-92. PMID 11583117 DOI: 10.1016/S0014-5793(01)02665-5 |
0.447 |
|
| 2001 |
Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW. Structural investigations of the active-site mutant Asn156A1a of outer membrane phospholipase A: Function of the Asn-His interaction in the catalytic triad Protein Science. 10: 1962-1969. PMID 11567087 DOI: 10.1110/Ps.17701 |
0.422 |
|
| 2001 |
Van der Veen BA, Leemhuis H, Kralj S, Uitdehaag JCM, Dijkstra BW, Dijkhuizen L. Hydrophobic Amino Acid Residues in the Acceptor Binding Site Are Main Determinants for Reaction Mechanism and Specificity of Cyclodextrin-glycosyltransferase Journal of Biological Chemistry. 276: 44557-44562. PMID 11555657 DOI: 10.1074/Jbc.M107533200 |
0.415 |
|
| 2001 |
Van Pouderoyen G, Eggert T, Jaeger KE, Dijkstra BW. The crystal structure of Bacillus subtilis lipase: A minimal α/β hydrolase fold enzyme Journal of Molecular Biology. 309: 215-226. PMID 11491291 DOI: 10.1006/Jmbi.2001.4659 |
0.539 |
|
| 2001 |
Snijder HJ, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW. Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli Journal of Molecular Biology. 309: 477-489. PMID 11371166 DOI: 10.1006/Jmbi.2001.4675 |
0.371 |
|
| 2001 |
Uitdehaag JC, van der Veen BA, Dijkhuizen L, Elber R, Dijkstra BW. Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase. Proteins. 43: 327-35. PMID 11288183 DOI: 10.1002/Prot.1044 |
0.376 |
|
| 2001 |
Steiner RA, Rozeboom HJ, De Vries A, Kalk KH, Murshudov GN, Wilson KS, Dijkstra BW. X-ray structure of bovine pancreatic phospholipase A2 at atomic resolution Acta Crystallographica Section D: Biological Crystallography. 57: 516-526. PMID 11264580 DOI: 10.1107/S0907444901002530 |
0.464 |
|
| 2001 |
Pouderoyen Gv, Eggert T, Jaeger KE, Dijkstra BW. The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme. Journal of Molecular Biology. 309: 215-226. DOI: 10.2210/Pdb1I6W/Pdb |
0.513 |
|
| 2001 |
Snijder HJ, Eerde JHv, Kingma RL, Kalk KH, Egmond MR, Dijkstra BW. Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A Protein Science. 10: 1962-1969. DOI: 10.1101/Ps.17701 |
0.354 |
|
| 2001 |
Nardini M, Rink R, Janssen DB, Dijkstra BW. Structure and mechanism of the epoxide hydrolase from Agrobacterium radiobacter AD1 Journal of Molecular Catalysis - B Enzymatic. 11: 1035-1042. DOI: 10.1016/S1381-1177(00)00049-7 |
0.516 |
|
| 2000 |
Alkema WBL, Hensgens CMH, Kroezinga EH, De Vries E, Floris R, Van Der Laan JM, Dijkstra BW, Janssen DB. Characterization of the β-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies Protein Engineering. 13: 857-863. PMID 11239085 DOI: 10.1093/Protein/13.12.857 |
0.49 |
|
| 2000 |
Van der Veen BA, Uitdehaag JCM, Dijkstra BW, Dijkhuizen L. Engineering of cyclodextrin glycosyltransferase reaction and product specificity Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1543: 336-360. PMID 11150613 DOI: 10.1016/S0167-4838(00)00233-8 |
0.363 |
|
| 2000 |
Liebeton K, Zonta A, Schimossek K, Nardini M, Lang D, Dijkstra BW, Reetz MT, Jaeger KE. Directed evolution of an enantioselective lipase. Chemistry & Biology. 7: 709-18. PMID 10980451 DOI: 10.1016/S1074-5521(00)00015-6 |
0.438 |
|
| 2000 |
Kingma RL, Fragiathaki M, Snijder HJ, Dijkstra BW, Verheij HM, Dekker N, Egmond MR. Unusual catalytic triad of Escherichia coli outer membrane phospholipase A. Biochemistry. 39: 10017-22. PMID 10955989 DOI: 10.1021/Bi000786D |
0.491 |
|
| 2000 |
Oubrie A, Dijkstra BW. Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions Protein Science. 9: 1265-1273. PMID 10933491 DOI: 10.1110/Ps.9.7.1265 |
0.483 |
|
| 2000 |
Nardini M, Lang DA, Liebeton K, Jaeger KE, Dijkstra BW. Crystal structure of pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases. The Journal of Biological Chemistry. 275: 31219-25. PMID 10893416 DOI: 10.1074/Jbc.M003903200 |
0.488 |
|
| 2000 |
Uitdehaag JCM, Van Alebeek GJWM, Van Der Veen BA, Dijkhuizen L, Dijkstra BW. Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity Biochemistry. 39: 7772-7780. PMID 10869182 DOI: 10.1021/Bi000340X |
0.465 |
|
| 2000 |
Van Der Veen BA, Uitdehaag JCM, Dijkstra BW, Dijkhuizen L. The role of arginine 47 in the cyclization and coupling reactions of cyclodextrin glycosyltransferase from Bacillus circulans strain 251: Implications for product inhibition and product specificity European Journal of Biochemistry. 267: 3432-3441. PMID 10848958 DOI: 10.1046/J.1432-1327.2000.01353.X |
0.343 |
|
| 2000 |
Van Der Veen BA, Uitdehaag JCM, Penninga D, Van Alebeek GJWM, Smith LM, Dijkstra BW, Dijkhuizen L. Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase α-cyclodextrin production Journal of Molecular Biology. 296: 1027-1038. PMID 10686101 DOI: 10.1006/Jmbi.2000.3528 |
0.451 |
|
| 2000 |
Van Asselt EJ, Kalk KH, Dijkstra BW. Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan Biochemistry. 39: 1924-1934. PMID 10684641 DOI: 10.1021/Bi992161P |
0.46 |
|
| 2000 |
Van Der Veen BA, Van Alebeek GJWM, Uitdehaag JCM, Dijkstra BW, Dijkhuizen L. The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms European Journal of Biochemistry. 267: 658-665. PMID 10651801 DOI: 10.1046/J.1432-1327.2000.01031.X |
0.381 |
|
| 2000 |
Armand S, Wagemaker MJM, Sánchez-Torres P, Kester HCM, Van Santen Y, Dijkstra BW, Visser J, Benen JAE. The active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis Journal of Biological Chemistry. 275: 691-696. PMID 10617668 DOI: 10.1074/Jbc.275.1.691 |
0.427 |
|
| 1999 |
Nardini M, Dijkstra BW. Alpha/beta hydrolase fold enzymes: the family keeps growing. Current Opinion in Structural Biology. 9: 732-7. PMID 10607665 DOI: 10.1016/S0959-440X(99)00037-8 |
0.367 |
|
| 1999 |
Uitdehaag JCM, Kalk KH, Van Der Veen BA, Dijkhuizen L, Dijkstra BW. The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a γ-cyclodextrin-CGTase complex at 1.8-Å resolution Journal of Biological Chemistry. 274: 34868-34876. PMID 10574960 DOI: 10.1074/Jbc.274.49.34868 |
0.439 |
|
| 1999 |
Van Asselt EJ, Dijkstra BW. Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability Febs Letters. 458: 429-435. PMID 10570954 DOI: 10.1016/S0014-5793(99)01198-9 |
0.337 |
|
| 1999 |
Jaeger KE, Dijkstra BW, Reetz MT. Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases Annual Review of Microbiology. 53: 315-351. PMID 10547694 DOI: 10.1146/annurev.micro.53.1.315 |
0.352 |
|
| 1999 |
Van Asselt EJ, Dijkstra AJ, Kalk KH, Takacs B, Keck W, Dijkstra BW. Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand Structure. 7: 1167-1180. PMID 10545329 DOI: 10.1016/S0969-2126(00)80051-9 |
0.493 |
|
| 1999 |
Snijder HJ, Ubarretxena-Belandia I, Blaauw M, Kalk KH, Verheij HM, Egmond MR, Dekker N, Dijkstra BW. Structural evidence for dimerization-regulated activation of an integral membrane phospholipase. Nature. 401: 717-21. PMID 10537112 DOI: 10.1038/44890 |
0.354 |
|
| 1999 |
Ridder IS, Rozeboom HJ, Kalk KH, Dijkstra BW. Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase Journal of Biological Chemistry. 274: 30672-30678. PMID 10521454 DOI: 10.1074/Jbc.274.43.30672 |
0.452 |
|
| 1999 |
Van Santen Y, Benen JAE, Schröter KH, Kalk KH, Armand S, Visser J, Dijkstra BW. 1.68-Å crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis Journal of Biological Chemistry. 274: 30474-30480. PMID 10521427 DOI: 10.1074/Jbc.274.43.30474 |
0.5 |
|
| 1999 |
Oubrie A, Rozeboom HJ, Dijkstra BW. Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex Proceedings of the National Academy of Sciences of the United States of America. 96: 11787-11791. PMID 10518528 DOI: 10.1073/Pnas.96.21.11787 |
0.442 |
|
| 1999 |
Pikkemaat MG, Ridder IS, Rozeboom HJ, Kalk KH, Dijkstra BW, Janssen DB. Crystallographic and kinetic evidence of a collision complex formed during halide import in haloalkane dehalogenase Biochemistry. 38: 12052-12061. PMID 10508409 DOI: 10.1021/Bi990849W |
0.407 |
|
| 1999 |
Oubrie A, Rozeboom HJ, Kalk KH, Olsthoorn AJJ, Duine JA, Dijkstra BW. Structure and mechanism of soluble quinoprotein glucose dehydrogenase Embo Journal. 18: 5187-5194. PMID 10508152 DOI: 10.1093/Emboj/18.19.5187 |
0.411 |
|
| 1999 |
Van Asselt EJ, Thunnissen AMWH, Dijkstra BW. High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment Journal of Molecular Biology. 291: 877-898. PMID 10452894 DOI: 10.1006/Jmbi.1999.3013 |
0.477 |
|
| 1999 |
Ridder IS, Rozeboom HJ, Dijkstra BW. Haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 refined at 1.15 Å resolution Acta Crystallographica Section D: Biological Crystallography. 55: 1273-1290. PMID 10393294 DOI: 10.1107/S090744499900534X |
0.397 |
|
| 1999 |
Oubrie A, Rozeboom HJ, Kalk KH, Duine JA, Dijkstra BW. The 1.7 Å crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat Journal of Molecular Biology. 289: 319-333. PMID 10366508 DOI: 10.1006/Jmbi.1999.2766 |
0.396 |
|
| 1999 |
Uitdehaag JCM, Mosi R, Kalk KH, Van der Veen BA, Dijkhuizen L, Withers SG, Dijkstra BW. X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the α-amylase family Nature Structural Biology. 6: 432-436. PMID 10331869 DOI: 10.1038/8235 |
0.408 |
|
| 1999 |
Nardini M, Ridder IS, Rozeboom HJ, Kalk KH, Rink R, Janssen DB, Dijkstra BW. The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides. The Journal of Biological Chemistry. 274: 14579-86. PMID 10329649 DOI: 10.1074/Jbc.274.21.14579 |
0.536 |
|
| 1999 |
Ridder IS, Dijkstra BW. Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY The Biochemical Journal. 339: Pt 2/-. PMID 10191250 DOI: 10.1042/Bj3390223 |
0.416 |
|
| 1999 |
Nardini M, Ridder I, Rozeboom H, Kalk K, Rink R, Janssen D, Dijkstra B. X-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1 : An enzyme to detoxify harmful epoxides Italian Journal of Biochemistry. 49: 15-15. DOI: 10.2210/Pdb1Ehy/Pdb |
0.528 |
|
| 1999 |
Rink R, Lutje Spelberg JH, Pieters RJ, Kingma J, Nardini M, Kellogg RM, Dijkstra BW, Janssen DB. Mutation of tyrosine residues involved in the alkylation half reaction of epoxide hydrolase from Agrobacterium radiobacter AD1 results in improved enantioselectivity [7] Journal of the American Chemical Society. 121: 7417-7418. DOI: 10.1021/Ja990501O |
0.377 |
|
| 1998 |
Mosi R, Sham H, Uitdehaag JCM, Ruiterkamp R, Dijkstra BW, Withers SG. Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase Biochemistry. 37: 17192-17198. PMID 9860832 DOI: 10.1021/Bi981109A |
0.404 |
|
| 1998 |
Van Montfort RLM, Dijkstra BW. The functional importance of structural differences between the mannitol-specific IIA(mannitol) and the regulatory IIA(nitrogen) Protein Science. 7: 2210-2216. PMID 9792109 DOI: 10.1002/Pro.5560071019 |
0.471 |
|
| 1998 |
Krooshof GH, Ridder IS, Tepper AW, Vos GJ, Rozeboom HJ, Kalk KH, Dijkstra BW, Janssen DB. Kinetic analysis and X-ray structure of haloalkane dehalogenase with a modified halide-binding site. Biochemistry. 37: 15013-23. PMID 9790663 DOI: 10.1021/Bi9815187 |
0.51 |
|
| 1998 |
Van Asselt EJ, Perrakis A, Kalk KH, Lamzin VS, Dijkstra BW. Accelerated X-ray structure elucidation of a 36 kDa muramidase/transglycosylase using wARP Acta Crystallographica Section D: Biological Crystallography. 54: 58-73. PMID 9761817 DOI: 10.1107/S0907444997010330 |
0.4 |
|
| 1998 |
Lang DA, Mannesse ML, de Haas GH, Verheij HM, Dijkstra BW. Structural basis of the chiral selectivity of Pseudomonas cepacia lipase. European Journal of Biochemistry / Febs. 254: 333-40. PMID 9660188 DOI: 10.1046/J.1432-1327.1998.2540333.X |
0.364 |
|
| 1998 |
Bordo D, Van Monfort RLM, Pijning T, Kalk KH, Reizer J, Saier MH, Dijkstra BW. The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli Journal of Molecular Biology. 279: 245-255. PMID 9636714 DOI: 10.1006/Jmbi.1998.1753 |
0.42 |
|
| 1998 |
van Montfort RL, Pijning T, Kalk KH, Hangyi I, Kouwijzer ML, Robillard GT, Dijkstra BW. The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site. Structure (London, England : 1993). 6: 377-88. PMID 9551558 DOI: 10.1016/S0969-2126(98)00039-2 |
0.491 |
|
| 1998 |
Krengel U, Schröter KH, Hoier H, Arkema A, Kalk KH, Zimniak P, Dijkstra BW. Crystal structure of a murine α-class glutathione S-transferase involved in cellular defense against oxidative stress Febs Letters. 422: 285-290. PMID 9498801 DOI: 10.1016/S0014-5793(98)00026-X |
0.46 |
|
| 1998 |
Wind RD, Uitdehaag JCM, Buitelaar RM, Dijkstra BW, Dijkhuizen L. Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1 Journal of Biological Chemistry. 273: 5771-5779. PMID 9488711 DOI: 10.1074/Jbc.273.10.5771 |
0.418 |
|
| 1998 |
Uitdehaag JCM, Dijkstra BW. A strategy for engineering thermostability: the case of cyclodextrin glycosyltransferase Progress in Biotechnology. 15: 317-323. DOI: 10.1016/S0921-0423(98)80047-6 |
0.409 |
|
| 1998 |
Lang DA, Dijkstra BW. Structural investigations of the regio- and enantioselectivity of lipases Chemistry and Physics of Lipids. 93: 115-122. DOI: 10.1016/S0009-3084(98)00035-8 |
0.386 |
|
| 1997 |
Ridder IS, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW. Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate Journal of Biological Chemistry. 272: 33015-33022. PMID 9407083 DOI: 10.1074/Jbc.272.52.33015 |
0.44 |
|
| 1997 |
Lapatto R, Krengel U, Schreuder HA, Arkema A, de Boer B, Kalk KH, Hol WG, Grootenhuis PD, Mulders JW, Dijkema R, Theunissen HJ, Dijkstra BW. X-ray structure of antistasin at 1.9 A resolution and its modelled complex with blood coagulation factor Xa. The Embo Journal. 16: 5151-61. PMID 9311976 DOI: 10.1093/Emboj/16.17.5151 |
0.524 |
|
| 1997 |
Mosi R, He S, Uitdehaag J, Dijkstra BW, Withers SG. Trapping and characterization of the reaction intermediate in cyclodextrin glycosyltransferase by use of activated substrates and a mutant enzyme Biochemistry. 36: 9927-9934. PMID 9245426 DOI: 10.1021/Bi970618U |
0.393 |
|
| 1997 |
Mansfeld J, Vriend G, Dijkstra BW, Veltman OR, Van Den Burg B, Venema G, Ulbrich-Hofmann R, Eijsink VGH. Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond Journal of Biological Chemistry. 272: 11152-11156. PMID 9111013 DOI: 10.1074/Jbc.272.17.11152 |
0.36 |
|
| 1997 |
van Montfort RL, Pijning T, Kalk KH, Reizer J, Saier MH, Thunnissen MM, Robillard GT, Dijkstra BW. The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure (London, England : 1993). 5: 217-25. PMID 9032081 DOI: 10.1016/S0969-2126(97)00180-9 |
0.438 |
|
| 1997 |
Tews I, Terwisscha Van Scheltinga AC, Perrakis A, Wilson KS, Dijkstra BW. Substrate-assisted catalysis unifies two families of chitinolytic enzymes Journal of the American Chemical Society. 119: 7954-7959. DOI: 10.1021/Ja970674I |
0.438 |
|
| 1997 |
Jaeger KE, Schneidinger B, Rosenau F, Werner M, Lang D, Dijkstra BW, Schimossek K, Zonta A, Reetz MT. Bacterial lipases for biotechnological applications Journal of Molecular Catalysis - B Enzymatic. 3: 3-12. DOI: 10.1016/S1381-1177(96)00039-2 |
0.336 |
|
| 1996 |
Fusetti F, Dijkstra BW. Purification and light-scattering analysis of penicillin-binding protein 4 from Escherichia coli Microbial Drug Resistance. 2: 73-76. PMID 9158725 DOI: 10.1089/Mdr.1996.2.73 |
0.368 |
|
| 1996 |
Penninga D, Van Der Veen BA, Knegtel RMA, Van Hijum SAFT, Rozeboom HJ, Kalk KH, Dijkstra BW, Dijkhuizen L. The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 Journal of Biological Chemistry. 271: 32777-32784. PMID 8955113 DOI: 10.1074/Jbc.271.51.32777 |
0.448 |
|
| 1996 |
Krengel U, Dijkstra BW. Three-dimensional structure of endo-1,C4-β-xylanase I from Aspergillus niger: Molecular basis for its low pH optimum Journal of Molecular Biology. 263: 70-78. PMID 8890913 DOI: 10.1006/Jmbi.1996.0556 |
0.409 |
|
| 1996 |
Schanstra JP, Ridder IS, Heimeriks GJ, Rink R, Poelarends GJ, Kalk KH, Dijkstra BW, Janssen DB. Kinetic characterization and X-ray structure of a mutant of haloalkane dehalogenase with higher catalytic activity and modified substrate range Biochemistry. 35: 13186-13195. PMID 8855957 DOI: 10.1021/Bi961151A |
0.511 |
|
| 1996 |
Terwisscha Van Scheltinga AC, Hennig M, Dijkstra BW. The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18 Journal of Molecular Biology. 262: 243-257. PMID 8831791 DOI: 10.1006/Jmbi.1996.0510 |
0.489 |
|
| 1996 |
Van Der Laan JM, Misset O, Mulleners LJSM, Gerritse G, Scheffers HN, Van Schouwen DJ, Teplyakov AV, Dijkstra BW. Structual and functional consequences of engineering the high alkaline serine protease PB92 Advances in Experimental Medicine and Biology. 379: 203-218. PMID 8796325 DOI: 10.1007/978-1-4613-0319-0_22 |
0.343 |
|
| 1996 |
Strokopytov B, Knegtel RMA, Penninga D, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW. Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution. Implications for product specificity Biochemistry. 35: 4241-4249. PMID 8672460 DOI: 10.1021/Bi952339H |
0.468 |
|
| 1996 |
Thunnissen AMWH, Dijkstra BW. Cure for a crisis? Nature Structural Biology. 3: 218-221. PMID 8605620 DOI: 10.1038/Nsb0396-218 |
0.326 |
|
| 1996 |
Knegtel RMA, Wind RD, Rozeboom HJ, Kalk KH, Buitelaar RM, Dijkhuizen L, Dijkstra BW. Crystal structure at 2.3 Å resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1 Journal of Molecular Biology. 256: 611-622. PMID 8604143 DOI: 10.1006/Jmbi.1996.0113 |
0.52 |
|
| 1996 |
Knegtel RM, Strokopytov B, Penninga D, Faber OG, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW. Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products. The Journal of Biological Chemistry. 270: 29256-64. PMID 7493956 DOI: 10.1074/Jbc.270.49.29256 |
0.497 |
|
| 1996 |
Dijkstra BW, Thunnissen AWH, van Asselt E. Structure and mechanism of SLT70, a bacterial muramidase Acta Crystallographica Section a Foundations of Crystallography. 52: C95-C95. DOI: 10.1107/S0108767396095281 |
0.344 |
|
| 1995 |
Ridder IS, Rozeboom HJ, Kingma J, Janssen DB, Dijkstra BW. Crystallization and preliminary x-ray analysis of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 Protein Science. 4: 2619-2620. PMID 8580854 DOI: 10.1002/Pro.5560041220 |
0.375 |
|
| 1995 |
Penninga D, Strokopytov B, Rozeboom HJ, Lawson CL, Dijkstra BW, Bergsma J, Dijkhuizen L. Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity Biochemistry. 34: 3368-3376. PMID 7880832 DOI: 10.1021/Bi00010A028 |
0.451 |
|
| 1995 |
Strokopytov B, Penninga D, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW. X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases Biochemistry. 34: 2234-2240. PMID 7857935 DOI: 10.1021/Bi00007A018 |
0.445 |
|
| 1995 |
Dijkstra BW, Thunnissen AM. 'Holy' proteins. II: The soluble lytic transglycosylase. Current Opinion in Structural Biology. 4: 810-3. PMID 7712284 DOI: 10.1016/0959-440X(94)90261-5 |
0.465 |
|
| 1995 |
Thunnissen MM, Fusetti F, de Boer B, Dijkstra BW. Purification, crystallisation and preliminary X-ray analysis of penicillin binding protein 4 from Escherichia coli, a protein related to class A beta-lactamases. Journal of Molecular Biology. 247: 149-53. PMID 7707365 DOI: 10.1006/Jmbi.1994.0128 |
0.38 |
|
| 1995 |
Ransac S, Blaauw M, Dijkstra BW, Slotboom AT, Boots JW, Verheij HM. Crystallization and preliminary X-ray analysis of a lipase from Staphylococcus hyicus. Journal of Structural Biology. 114: 153-5. PMID 7612398 DOI: 10.1006/Jsbi.1995.1014 |
0.401 |
|
| 1995 |
Blaauw M, Dekker N, Verheij HM, Kalk KH, Dijkstra BW. Crystallization and preliminary X-ray analysis of outer membrane phospholipase A from Escherichia coli. Febs Letters. 373: 10-2. PMID 7589423 DOI: 10.1016/0014-5793(95)01002-V |
0.414 |
|
| 1995 |
Thunnissen AMWH, Rozeboom HJ, Kalk KH, Dijkstra BW. Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism Biochemistry. 34: 12729-12737. PMID 7548026 DOI: 10.1021/Bi00039A032 |
0.492 |
|
| 1995 |
Terwisscha Van Scheltinga AC, Armand S, Kalk KH, Isogai A, Henrissat B, Dijkstra BW. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis Biochemistry. 34: 15619-15623. PMID 7495789 DOI: 10.1021/Bi00048A003 |
0.443 |
|
| 1995 |
Hennig M, Jansonius JN, Terwisscha van Scheltinga AC, Dijkstra BW, Schlesier B. Crystal structure of concanavalin B at 1.65 A resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis. Journal of Molecular Biology. 254: 237-46. PMID 7490746 DOI: 10.1006/Jmbi.1995.0614 |
0.433 |
|
| 1995 |
Thunnissen AMWH, Isaacs NW, Dijkstra BW. The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes Proteins: Structure, Function and Genetics. 22: 245-258. PMID 7479697 DOI: 10.1002/Prot.340220305 |
0.473 |
|
| 1995 |
Dijkhuizen L, Penninga D, Rozeboom HJ, Strokopytov B, Dijkstra BW. Protein engineering of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 Progress in Biotechnology. 10: 165-174. DOI: 10.1016/S0921-0423(06)80101-2 |
0.366 |
|
| 1994 |
Van den Burg B, Dijkstra BW, Vriend G, Van der Vinne B, Venema G, Eijsink VGH. Protein stabilization by hydrophobic interactions at the surface European Journal of Biochemistry. 220: 981-985. PMID 8143751 DOI: 10.1111/J.1432-1033.1994.Tb18702.X |
0.332 |
|
| 1994 |
Thunnissen AM, Dijkstra AJ, Kalk KH, Rozeboom HJ, Engel H, Keck W, Dijkstra BW. Doughnut-shaped structure of a bacterial muramidase revealed by X-ray crystallography. Nature. 367: 750-3. PMID 8107871 DOI: 10.1038/367750A0 |
0.481 |
|
| 1994 |
Lawson CL, van Montfort R, Strokopytov B, Rozeboom HJ, Kalk KH, de Vries GE, Penninga D, Dijkhuizen L, Dijkstra BW. Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form. Journal of Molecular Biology. 236: 590-600. PMID 8107143 DOI: 10.1006/Jmbi.1994.1168 |
0.488 |
|
| 1994 |
Misset O, Gerritse G, Jaeger KE, Winkler U, Colson C, Schanck K, Lesuisse E, Dartois V, Blaauw M, Ransac S, Dijkstra BW. The structure–function relationship of the lipases from Pseudomonas aeruginosa and Bacillus subtilis Protein Engineering. 7: 523-529. PMID 8029207 DOI: 10.1093/Protein/7.4.523 |
0.448 |
|
| 1994 |
Van Montfort RLM, Pijning T, Kalk KH, Schuurman-Wolters GK, Reizer J, Saier MH, Robillard G, Dijkstra BW. Crystallization of enzyme IIB of the cellobiose-specific phosphotransferase system of Escherichia coli Journal of Molecular Biology. 239: 588-590. PMID 8006971 DOI: 10.1006/jmbi.1994.1399 |
0.323 |
|
| 1994 |
Jaeger KE, Ransac S, Dijkstra BW, Colson C, van Heuvel M, Misset O. Bacterial lipases. Fems Microbiology Reviews. 15: 29-63. PMID 7946464 DOI: 10.1111/j.1574-6976.1994.tb00121.x |
0.374 |
|
| 1994 |
Schröter KH, Arkema A, Kester HC, Visser J, Dijkstra BW. Crystallization and preliminary crystallographic characterization of endo-polygalacturonase II from Aspergillus niger. Journal of Molecular Biology. 243: 351-2. PMID 7932761 DOI: 10.1006/Jmbi.1994.1660 |
0.385 |
|
| 1994 |
Terwisscha van Scheltinga AC, Kalk KH, Beintema JJ, Dijkstra BW. Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure (London, England : 1993). 2: 1181-9. PMID 7704528 DOI: 10.1016/S0969-2126(94)00120-0 |
0.484 |
|
| 1994 |
Vicković I, Kalk KH, Drenth J, Dijkstra BW. An optimal strategy for X-ray data collection on macromolecular crystals with position-sensitive detectors Journal of Applied Crystallography. 27: 791-793. DOI: 10.1107/S0021889894004681 |
0.53 |
|
| 1993 |
Verschueren KH, Franken SM, Rozeboom HJ, Kalk KH, Dijkstra BW. Non-covalent binding of the heavy atom compound [Au(CN)2]- at the halide binding site of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. Febs Letters. 323: 267-70. PMID 8500621 DOI: 10.1016/0014-5793(93)81354-3 |
0.42 |
|
| 1993 |
Van Der Laan JM, Teplyakov AV, Lammers AA, Dijkstra BW. Preliminary X-ray study of naproxen esterase from Bacillus subtilis Journal of Molecular Biology. 230: 681-683. PMID 8464077 DOI: 10.1006/Jmbi.1993.1184 |
0.382 |
|
| 1993 |
van den Burg B, Dijkstra BW, van der Vinne B, Stulp BK, Eijsink VG, Venema G. Introduction of disulfide bonds into Bacillus subtilis neutral protease. Protein Engineering. 6: 521-7. PMID 8415578 DOI: 10.1093/Protein/6.5.521 |
0.351 |
|
| 1993 |
Jaeger KE, Ransac S, Koch HB, Ferrato F, Dijkstra BW. Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa. Febs Letters. 332: 143-9. PMID 8405431 DOI: 10.1016/0014-5793(93)80501-K |
0.456 |
|
| 1993 |
Verschueren KH, Kingma J, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW. Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site. Biochemistry. 32: 9031-7. PMID 8369276 DOI: 10.1021/Bi00086A008 |
0.423 |
|
| 1993 |
Verschueren KH, Franken SM, Rozeboom HJ, Kalk KH, Dijkstra BW. Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism. Journal of Molecular Biology. 232: 856-72. PMID 8355275 DOI: 10.1006/Jmbi.1993.1436 |
0.411 |
|
| 1993 |
Thunnissen MM, Franken PA, de Haas GH, Drenth J, Kalk KH, Verheij HM, Dijkstra BW. Crystal structure of a porcine pancreatic phospholipase A2 mutant. A large conformational change caused by the F63V point mutation. Journal of Molecular Biology. 232: 839-55. PMID 8355274 DOI: 10.1006/Jmbi.1993.1435 |
0.642 |
|
| 1993 |
Neumann U, Hofsteenge J, Arkema AH, Dijkstra BW. Crystallization of porcine liver ribonuclease inhibitor a member of the family of proteins containing leucine-rich repeats. Journal of Molecular Biology. 231: 505-8. PMID 8323580 DOI: 10.1006/Jmbi.1993.1299 |
0.417 |
|
| 1993 |
Thunnissen A, Djkistra A, Rozeboom I, Kalk KH, Keck W, Dijkstra BW. Crystal structure of a bacterial muramidase: the soluble lytic transglycosylase fromE. coli Acta Crystallographica Section a Foundations of Crystallography. 49: c110-c111. DOI: 10.1107/S0108767378096816 |
0.416 |
|
| 1992 |
Siezen RJ, de Vos WM, Leunissen JA, Dijkstra BW. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Protein Engineering. 4: 719-37. PMID 1798697 DOI: 10.1093/Protein/4.7.719 |
0.464 |
|
| 1992 |
Eijsink VG, Dijkstra BW, Vriend G, van der Zee JR, Veltman OR, van der Vinne B, van den Burg B, Kempe S, Venema G. The effect of cavity-filling mutations on the thermostability of Bacillus stearothermophilus neutral protease. Protein Engineering. 5: 421-6. PMID 1518790 DOI: 10.1093/Protein/5.5.421 |
0.425 |
|
| 1992 |
Teplyakov AV, Van Der Laan JM, Lammers AA, Kelders H, Kalk KH, Misset O, Mulleners LJSM, Dijkstra BW. Protein engineering of the high-alkaline serine protease pb92 from Bacillus alcalophilus: Functional and structural consequences of mutation at the s4 substrate binding pocket Protein Engineering, Design and Selection. 5: 413-420. PMID 1518789 DOI: 10.1093/Protein/5.5.413 |
0.482 |
|
| 1992 |
Van Der Laan JM, Teplyakov AV, Kelders H, Kalk KH, Misset O, Mulleners LJSM, Dijkstra BW. Crystal structure of the high-alkaline serine protease pb92 from Bacillus alcalophilus Protein Engineering, Design and Selection. 5: 405-411. PMID 1518788 DOI: 10.1093/Protein/5.5.405 |
0.49 |
|
| 1992 |
Thunnissen MM, Franken PA, de Haas GH, Drenth J, Kalk KH, Verheij HM, Dijkstra BW. Site-directed mutagenesis and X-ray crystallography of two phospholipase A2 mutants: Y52F and Y73F. Protein Engineering. 5: 597-603. PMID 1480613 DOI: 10.1093/Protein/5.7.597 |
0.581 |
|
| 1992 |
Lammers LA, Dijkstra BW, van Weeghel RP, Pas HH, Robillard GT. Crystallization of the A-domain of the mannitol transport protein enzyme IImtl. Journal of Molecular Biology. 228: 310-2. PMID 1447792 DOI: 10.1016/0022-2836(92)90511-H |
0.421 |
|
| 1992 |
Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J. The alpha/beta hydrolase fold. Protein Engineering. 5: 197-211. PMID 1409539 DOI: 10.1093/Protein/5.3.197 |
0.44 |
|
| 1990 |
Rozeboom HJ, Budiani A, Beintema JJ, Dijkstra BW. Crystallization of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex. Journal of Molecular Biology. 212: 441-3. PMID 2325127 DOI: 10.1016/0022-2836(90)90321-C |
0.418 |
|
| 1990 |
Thunnissen MM, Kalk KH, Drenth J, Dijkstra BW. Structure of an engineered porcine phospholipase A2 with enhanced activity at 2.1 A resolution. Comparison with the wild-type porcine and Crotalus atrox phospholipase A2. Journal of Molecular Biology. 216: 425-39. PMID 2254938 DOI: 10.1016/S0022-2836(05)80332-8 |
0.579 |
|
| 1990 |
Thunnissen MM, Ab E, Kalk KH, Drenth J, Dijkstra BW, Kuipers OP, Dijkman R, de Haas GH, Verheij HM. X-ray structure of phospholipase A2 complexed with a substrate-derived inhibitor. Nature. 347: 689-91. PMID 2215698 DOI: 10.1038/347689A0 |
0.576 |
|
| 1990 |
Rozeboom HJ, Dijkstra BW, Engel H, Keck W. Crystallization of the soluble lytic transglycosylase from Escherichia coli K12. Journal of Molecular Biology. 212: 557-9. PMID 2184239 DOI: 10.1016/0022-2836(90)90221-7 |
0.412 |
|
| 1990 |
Lawson CL, Bergsma J, Bruinenberg PM, de Vries G, Dijkhuizen L, Dijkstra BW. Maltodextrin-dependent crystallization of cyclomaltodextrin glucanotransferase from Bacillus circulans Journal of Molecular Biology. 214: 807-809. PMID 2143786 DOI: 10.1016/0022-2836(90)90335-J |
0.425 |
|
| 1989 |
Hazes B, Dijkstra BW. Model building of disulfide bonds in proteins with known three-dimensional structure. Protein Engineering. 2: 119-25. PMID 3244694 DOI: 10.1093/Protein/2.2.119 |
0.337 |
|
| 1989 |
Schierbeek AJ, Swarte MB, Dijkstra BW, Vriend G, Read RJ, Hol WG, Drenth J, Betzel C. X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques. Journal of Molecular Biology. 206: 365-79. PMID 2716052 DOI: 10.1016/0022-2836(89)90486-5 |
0.694 |
|
| 1989 |
Kuipers OP, Thunnissen MM, de Geus P, Dijkstra BW, Drenth J, Verheij HM, de Haas GH. Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop. Science (New York, N.Y.). 244: 82-5. PMID 2704992 DOI: 10.1126/Science.2704992 |
0.641 |
|
| 1989 |
Gros P, Fujinaga M, Dijkstra BW, Kalk KH, Hol WG. Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c. Acta Crystallographica. Section B, Structural Science. 45: 488-99. PMID 2688688 DOI: 10.1107/S0108768189006038 |
0.555 |
|
| 1989 |
Van der Klei IJ, Lawson CL, Rozeboom H, Dijkstra BW, Veenhuis M, Harder W, Hol WG. Use of electron microscopy in the examination of lattice defects in crystals of alcohol oxidase. Febs Letters. 244: 213-6. PMID 2494064 DOI: 10.1016/0014-5793(89)81195-0 |
0.565 |
|
| 1988 |
Rozeboom HJ, Kingma J, Janssen DB, Dijkstra BW. Crystallization of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. Journal of Molecular Biology. 200: 611-2. PMID 3398051 DOI: 10.1016/0022-2836(88)90548-7 |
0.404 |
|
| 1988 |
Renetseder R, Dijkstra BW, Huizinga K, Kalk KH, Drenth J. Crystal structure of bovine pancreatic phospholipase A2 covalently inhibited by p-bromo-phenacyl-bromide. Journal of Molecular Biology. 200: 181-8. PMID 3379639 DOI: 10.1016/0022-2836(88)90342-7 |
0.623 |
|
| 1986 |
Renetseder R, Dijkstra BW, Kalk KH, Verpoorte J, Drenth J. Bovine phospholipase A2 crystals soaked in 30% methanol: the first structure determination with a FAST diffractometer at high resolution Acta Crystallographica Section B. 42: 602-605. DOI: 10.1107/S0108768186097677 |
0.552 |
|
| 1985 |
Renetseder R, Brunie S, Dijkstra BW, Drenth J, Sigler PB. A comparison of the crystal structures of phospholipase A2 from bovine pancreas and Crotalus atrox venom. The Journal of Biological Chemistry. 260: 11627-34. PMID 4044572 |
0.632 |
|
| 1984 |
Dijkstra BW, Kalk KH, Drenth J, de Haas GH, Egmond MR, Slotboom AJ. Role of the N-terminus in the interaction of pancreatic phospholipase A2 with aggregated substrates. Properties and crystal structure of transaminated phospholipase A2. Biochemistry. 23: 2759-66. PMID 6466614 DOI: 10.1021/Bi00307A035 |
0.613 |
|
| 1983 |
Dijkstra BW, Renetseder R, Kalk KH, Hol WG, Drenth J. Structure of porcine pancreatic phospholipase A2 at 2.6 A resolution and comparison with bovine phospholipase A2. Journal of Molecular Biology. 168: 163-79. PMID 6876174 DOI: 10.1016/S0022-2836(83)80328-3 |
0.707 |
|
| 1983 |
Dijkstra BW, Weijer WJ, Wierenga RK. Polypeptide chains with similar amino acid sequences but a distinctly different conformation. Bovine and porcine phospholipase A2 Febs Letters. 164: 25-27. PMID 6653783 DOI: 10.1016/0014-5793(83)80011-8 |
0.623 |
|
| 1982 |
Dijkstra BW, Nes CJH, Kalk KH, Brandenburg NP, Hol WCJ, Drenth J. The structure of bovine pancreatic prophospholipase A2 at 3.0 Å resolution Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 38: 793-799. DOI: 10.1107/S0567740882004099 |
0.6 |
|
| 1981 |
Dijkstra BW, Drenth J, Kalk KH. Active site and catalytic mechanism of phospholipase A2. Nature. 289: 604-6. PMID 7464926 DOI: 10.1038/289604A0 |
0.642 |
|
| 1981 |
Dijkstra BW, Kalk KH, Hol WG, Drenth J. Structure of bovine pancreatic phospholipase A2 at 1.7A resolution. Journal of Molecular Biology. 147: 97-123. PMID 7265241 DOI: 10.1016/0022-2836(81)90081-4 |
0.704 |
|
| 1980 |
Verheij HM, Volwerk JJ, Jansen EH, Puyk WC, Dijkstra BW, Drenth J, de Haas GH. Methylation of histidine-48 in pancreatic phospholipase A2. Role of histidine and calcium ion in the catalytic mechanism. Biochemistry. 19: 743-50. PMID 7356955 DOI: 10.1021/Bi00545A021 |
0.564 |
|
| 1978 |
Dijkstra BW, Drenth J, Kalk KH, Vandermaelen PJ. Three-dimensional structure and disulfide bond connections in bovine pancreatic phospholipase A2. Journal of Molecular Biology. 124: 53-60. PMID 712836 DOI: 10.1016/0022-2836(78)90146-8 |
0.617 |
|
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