Publikationer av Christina Divne
Refereegranskade
Artiklar
[1]
V. Furlanetto et al., "Structural and Functional Characterization of a Gene Cluster Responsible for Deglycosylation of C-glucosyl Flavonoids and Xanthonoids by Deinococcus aerius," Journal of Molecular Biology, vol. 436, no. 9, 2024.
[2]
V. Furlanetto och C. Divne, "LolA and LolB from the plant-pathogen Xanthomonas campestris forms a stable heterodimeric complex in the absence of lipoprotein," Frontiers in Microbiology, vol. 14, 2023.
[3]
S.-C. Chang et al., "The Gram-positive bacterium Romboutsia ilealis harbors a polysaccharide synthase that can produce (1,3;1,4)-β-D-glucans," Nature Communications, vol. 14, no. 1, 2023.
[4]
A. Kostelac et al., "Biochemical Characterization of Pyranose Oxidase from Streptomyces canus-Towards a Better Understanding of Pyranose Oxidase Homologues in Bacteria," International Journal of Molecular Sciences, vol. 23, no. 21, 2022.
[5]
K. M. Kasmaei et al., "Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state," Frontiers in Microbiology, vol. 13, 2022.
[6]
D. Kalyani et al., "A homodimeric bacterial exo-β-1,3-glucanase derived from moose rumen microbiome shows a structural framework similar to yeast exo-β-1,3-glucanases," Enzyme and microbial technology, vol. 143, 2021.
[7]
D. Kalyani et al., "Crystal structure of a homotrimeric verrucomicrobial exo-beta-1,4-mannosidase active in the hindgut of the wood-feeding termite Reticulitermes flavipes," JOURNAL OF STRUCTURAL BIOLOGY-X, vol. 5, s. 100048, 2021.
[8]
D. Humer et al., "Potential of unglycosylated horseradish peroxidase variants for enzyme prodrug cancer therapy," Biomedicine and Pharmacotherapy, vol. 142, 2021.
[9]
R. Gandini et al., "A Transmembrane Crenarchaeal Mannosyltransferase Is Involved in N-Glycan Biosynthesis and Displays an Unexpected Minimal Cellulose-Synthase-like Fold," Journal of Molecular Biology, vol. 432, no. 16, s. 4658-4672, 2020.
[10]
X. Xu et al., "Evolutionary engineering in Saccharomyces cerevisiae reveals a TRK1-dependent potassium influx mechanism for propionic acid tolerance.," Biotechnology for Biofuels, vol. 12, 2019.
[11]
J. Quehenberger et al., "Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum.," International Journal of Molecular Sciences, vol. 20, no. 1, 2019.
[12]
T. Reichenbach et al., "Structural and biochemical characterization of the Cutibacterium acnes exo-β-1,4-mannosidase that targets the N-glycan core of host glycoproteins.," PLOS ONE, vol. 13, no. 9, 2018.
[13]
R. Gandini et al., "Structural basis for dolichylphosphate mannose biosynthesis," Nature Communications, vol. 8, no. 1, 2017.
[14]
N. Hassan et al., "Engineering a thermostable Halothermothrix orenii beta-glucosidase for improved galacto-oligosaccharide synthesis," Applied Microbiology and Biotechnology, vol. 100, no. 8, s. 3533-3543, 2016.
[15]
N. Hassan et al., "Biochemical and structural characterization of a thermostable beta-glucosidase from Halothermothrix orenii for galacto-oligosaccharide synthesis," Applied Microbiology and Biotechnology, vol. 99, no. 4, s. 1731-1744, 2015.
[16]
Y. Wang et al., "Biochemical characterization of the novel endo-β-mannanase AtMan5-2 from Arabidopsis thaliana," Plant Science, vol. 241, s. 151-163, 2015.
[17]
N. Hassan et al., "High-resolution crystal structure of a polyextreme GH43 glycosidase from Halothermothrix orenii with alpha-L-arabinofuranosidase activity," Acta Crystallographica Section F : Structural Biology Communications, vol. 71, no. Pt 3, s. 338-45, 2015.
[18]
T.-C. Tan et al., "Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation," Nature Communications, vol. 6, s. 7542-7542, 2015.
[19]
E. Ullmann et al., "A novel cytosolic NADH : quinone oxidoreductase from Methanothermobacter marburgensis," Bioscience Reports, vol. 34, s. 893-904, 2014.
[20]
T. C. Tan et al., "Structural Basis for Binding of Fluorinated Glucose and Galactose to Trametes multicolor Pyranose 2-Oxidase Variants with Improved Galactose Conversion," PLOS ONE, vol. 9, no. 1, 2014.
[21]
N. Hassan et al., "Crystal structures of Phanerochaete chrysosporium pyranose 2-oxidase suggest that the N-terminus acts as a propeptide that assists in homotetramer assembly," FEBS Open Bio, vol. 3, s. 496-504, 2013.
[22]
T. C. Tan et al., "The 1.6 Å Crystal Structure of Pyranose Dehydrogenase from Agaricus meleagris Rationalizes Substrate Specificity and Reveals a Flavin Intermediate," PLOS ONE, vol. 8, no. 1, 2013.
[23]
T.-C. Tan, D. Haltrich och C. Divne, "Regioselective Control of beta-D-Glucose Oxidation by Pyranose 2-Oxidase Is Intimately Coupled to Conformational Degeneracy," Journal of Molecular Biology, vol. 409, no. 4, s. 588-600, 2011.
[24]
W. Pitsawong et al., "A Conserved Active-site Threonine Is Important for Both Sugar and Flavin Oxidations of Pyranose 2-Oxidase," Journal of Biological Chemistry, vol. 285, no. 13, s. 9697-9705, 2010.
[25]
T.-C. Tan et al., "H-Bonding and Positive Charge at the N(5)/O(4) Locus Are Critical for Covalent Flavin Attachment in Trametes Pyranose 2-Oxidase," Journal of Molecular Biology, vol. 402, no. 3, s. 578-594, 2010.
[26]
O. Spadiut et al., "Importance of the gating segment in the substrate-recognition loop of pyranose 2-oxidase," The FEBS Journal, vol. 277, no. 13, s. 2892-2909, 2010.
[27]
F. Gullfot et al., "The crystal structure of XG-34, an evolved xyloglucan-specific carbohydrate-binding module," Proteins : Structure, Function, and Bioinformatics, vol. 78, no. 3, s. 785-789, 2010.
[28]
O. Spadiut et al., "A thermostable triple mutant of pyranose 2-oxidase from Trametes multicolor with improved properties for biotechnological applications.," Biotechnology Journal, vol. 4, no. 4, s. 525-534, 2009.
[29]
O. Spadiut et al., "Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design," The FEBS Journal, vol. 276, no. 3, s. 776-792, 2009.
[30]
C. Salaheddin et al., "Probing active-site residues of pyranose 2-oxidase from Trametes multicolor by semi-rational protein design.," Biotechnology Journal, vol. 4, no. 4, s. 535-543, 2009.
[31]
J. M. Eklöf et al., "The crystal structure of the outer membrane lipoprotein YbhC from Escherichia coli sheds new light on the phylogeny of carbohydrate esterase family 8," Proteins : Structure, Function, and Bioinformatics, vol. 76, no. 4, s. 1029-1036, 2009.
[32]
T.-C. Tan et al., "Crystal structure of the polyextremophilic alpha-amylase AmyB from Halothermothrix orenii : Details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch," Journal of Molecular Biology, vol. 378, no. 4, s. 852-870, 2008.
[33]
A. S. Rajangam et al., "MAP20, a Microtubule-Associated Protein in the Secondary Cell Walls of Hybrid Aspen, Is a Target of the Cellulose Synthesis Inhibitor 2,6-Dichlorobenzonitrile," Plant Physiology, vol. 148, no. 3, s. 1283-1294, 2008.
[34]
R. Kittl et al., "Molecular cloning of three pyranose dehydrogenase-encoding genes from Agaricus meleagris and analysis of their expression by real-time RT-PCR," Current Genetics, vol. 53, no. 2, s. 117-127, 2008.
[35]
O. Spadiut et al., "Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase from Trametes multicolor," Biocatalysis and Biotransformation, vol. 26, no. 1-2, s. 120-127, 2008.
[36]
T.-H. Nguyen et al., "Characterization and molecular cloning of a heterodimeric beta-galactosidase from the probiotic strain Lactobacillus acidophilus R22," FEMS Microbiology Letters, vol. 269, no. 1, s. 136-144, 2007.
[37]
M. Kujawa et al., "Properties of pyranose dehydrogenase purified from the litter-degrading fungus Agaricus xanthoderma," The FEBS Journal, vol. 274, no. 3, s. 879-894, 2007.
[38]
M. Zamocky et al., "Cellobiose dehydrogenase - A flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi," Current protein and peptide science, vol. 7, no. 3, s. 255-280, 2006.
[39]
M. Kujawa et al., "Structural basis for substrate binding and regioselective oxidation of monosaccharides at C3 by pyranose 2-oxidase," Journal of Biological Chemistry, vol. 281, no. 46, s. 35104-35115, 2006.
[40]
M. Kujawa et al., "Pyranose oxidase from Trametes multicolour : application in biocatalysis," Journal of Biotechnology, vol. 118, s. 89-89, 2005.
[41]
M. Zamocky et al., "Ancestral gene fusion in cellobiose dehydrogenases reflects a specific evolution of GMC oxidoreductases in fungi," Gene, vol. 338, no. 1, s. 1-14, 2004.
[42]
M. Hallberg et al., "Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase," Journal of Molecular Biology, vol. 341, no. 3, s. 781-796, 2004.
[43]
B. M. Hällberg et al., "Crystallization and preliminary X-ray diffraction analysis of pyranose 2-oxidase from the white-rot fungus Trametes multicolor," Acta Crystallographica Section D : Biological Crystallography, vol. 60, s. 197-199, 2004.
[44]
E. Master et al., "Recombinant Expression and Enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides," Biochemistry, vol. 43, no. 31, s. 10080-10089, 2004.
[45]
F. A. J. Rotsaert et al., "Biophysical and structural analysis of a novel heme b iron ligation in the flavocytochrome cellobiose dehydrogenase," Journal of Biological Chemistry, vol. 278, no. 35, s. 33224-33231, 2003.
[46]
I. von Ossowski et al., "Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Ce17A. A comparison with Phanerochaete chrysosporium Cel7D," Journal of Molecular Biology, vol. 333, no. 4, s. 817-829, 2003.
[47]
B. M. Hallberg et al., "Mechanism of the reductive half-reaction in cellobiose dehydrogenase," Journal of Biological Chemistry, vol. 278, no. 9, s. 7160-7166, 2003.
[48]
M. G. Mason et al., "The heme domain of cellobiose oxidoreductase : a one-electron reducing system," Biochimica et Biophysica Acta - Bioenergetics, vol. 1604, no. 1, s. 47-54, 2003.
[49]
B. M. Hallberg et al., "Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase," Journal of Molecular Biology, vol. 315, no. 3, s. 421-434, 2002.
[50]
D. Becker et al., "Engineering of a glycosidase Family 7 cellobiohydrolase to more alkaline pH optimum : the pH behaviour of Trichoderma reesei CeI7A and its E223S/A224H/L225V/T226A/D262G mutant," Biochemical Journal, vol. 356, s. 19-30, 2001.
[51]
M. Yoshida et al., "Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris," Bioscience, biotechnology and biochemistry, vol. 65, no. 9, s. 2050-2057, 2001.
[52]
J. Stahlberg et al., "Structural basis for enantiomer binding and separation of a common beta-blocker : Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution," Journal of Molecular Biology, vol. 305, no. 1, s. 79-93, 2001.
[53]
B. M. Hallberg et al., "A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase," Structure, vol. 8, no. 1, s. 79-88, 2000.
[54]
L. F. Mackenzie et al., "Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 angstrom resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate," Biochemical Journal, vol. 335, s. 409-416, 1998.
[55]
C. Divne et al., "High-resolution crystal structures reveal how a cellulose chain is bound in the 50 angstrom long tunnel of cellobiohydrolase I from Trichoderma reesei," Journal of Molecular Biology, vol. 275, no. 2, s. 309-325, 1998.
[56]
G. Henriksson et al., "Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1," Biochemical Journal, vol. 324, s. 833-838, 1997.
[57]
H. Henriksson et al., "The catalytic amino-acid residues in the active site of cellobiohydrolase 1 are involved in chiral recognition," Journal of Biotechnology, vol. 57, no. 1-3, s. 115-125, 1997.
[58]
G. J. Kleywegt et al., "The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 angstrom resolution, and a comparison with related enzymes," Journal of Molecular Biology, vol. 272, no. 3, s. 383-397, 1997.
[59]
J. Stahlberg et al., "Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei," Journal of Molecular Biology, vol. 264, no. 2, s. 337-349, 1996.
[60]
M. RAICES et al., "Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium," FEBS Letters, vol. 369, no. 2-3, s. 233-238, 1995.
[61]
T. TEERI et al., "HYDROLYSIS OF CRYSTALLINE CELLULOSE BY NATIVE AND ENGINEERED TRICHODERMA-REESEI CELLULASES," Abstracts of Papers of the American Chemical Society, vol. 207, s. 21-AGFD, 1994.
[62]
C. DIVNE et al., "THE 3-DIMENSIONAL CRYSTAL-STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE-I FROM TRICHODERMA-REESEI," Science, vol. 265, no. 5171, s. 524-528, 1994.
[63]
C. Divne et al., "CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDIES ON THE CORE PROTEINS OF CELLOBIOHYDROLASE-I AND ENDOGLUCANASE-I FROM TRICHODERMA-REESEI," Journal of Molecular Biology, vol. 234, no. 3, s. 905-907, 1993.
Konferensbidrag
[64]
M. Kujawa et al., "Properties of pyranose dehydrogenase purified from Agaricus xanthoderma," i 13th Ruropean Congress on Biotechnology (ECB 13), SEP 16-19, 2007, Barcelona, SPAIN, 2007, s. S225-S225.
[65]
T. T. Teeri et al., "Trichoderma reesei cellobiohydrolases : why so efficient on crystalline cellulose?," i 664th Meeting of the Biochemical-Society, DEC 15-17, 1997, UNIV READING, READING, ENGLAND, 1998, s. 173-178.
Icke refereegranskade
Övriga
[66]
[67]
Y. Wang et al., "Biochemical characterization of the novel endo-β-mannanase AtMan5-2 from Arabidopsis thaliana," (Manuskript).
[68]
V. Furlanetto et al., "Deglycosylation of C-glycosylflavonoids by the plant endophyte Microbacterium testaceum," (Manuskript).
[69]
N. Hassan et al., "Engineering a polyextremophilic Halothermothrix orenii β-glucosidase for improved galacto-oligosaccharide synthesis," (Manuskript).
[70]
[71]
Y. Wang et al., "Investigating the function and biochemical properties of Arabidopsis mannanase 5-6," (Manuskript).
[72]
T. Reichenbach et al., "Is Pyrococcus furiosus dolichylphosphate mannose synthase moonlighting as a biogenic flippase for dolichylphosphate mannose?," (Manuskript).
[73]
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