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Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe proteinHallmarks of Processivity in Glycoside Hydrolases from Crystallographic and Computational Studies of the Serratia marcescens ChitinasesNMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactionsStructural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenasesStructural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate SpecificityDegradation of chitosans with a family 46 chitosanase from Streptomyces coelicolor A3(2).An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides.Analysis of noncovalent chitinase-chito-oligosaccharide complexes by infrared-matrix assisted laser desorption ionization and nanoelectrospray ionization mass spectrometry.Inhibition of fungal plant pathogens by synergistic action of chito-oligosaccharides and commercially available fungicides.Human Chitotriosidase Is an Endo-Processive Enzyme.Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase.Production of chitooligosaccharides and their potential applications in medicineThe chitinolytic machinery of Serratia marcescens--a model system for enzymatic degradation of recalcitrant polysaccharides.Towards a molecular-level theory of carbohydrate processivity in glycoside hydrolases.Expression and characterization of endochitinase C from Serratia marcescens BJL200 and its purification by a one-step general chitinase purification method.Thermodynamic analysis of allosamidin binding to a family 18 chitinase.The predominant molecular state of bound enzyme determines the strength and type of product inhibition in the hydrolysis of recalcitrant polysaccharides by processive enzymesAnalysis of productive binding modes in the human chitotriosidase.Identification of a high-affinity-binding oligosaccharide by (+) nanoelectrospray quadrupole time-of-flight tandem mass spectrometry of a noncovalent enzyme-ligand complex.Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens.Human chitotriosidase-catalyzed hydrolysis of chitosan.Chitin oligosaccharide binding to a family GH19 chitinase from the moss Bryum coronatum.Mutational effects on transglycosylating activity of family 18 chitinases and construction of a hypertransglycosylating mutant.The roles of three Serratia marcescens chitinases in chitin conversion are reflected in different thermodynamic signatures of allosamidin binding.Cleavage of cellulose by a CBM33 protein.An in vitro investigation of endocrine disrupting effects of the mycotoxin alternariol.Adherence inhibition of enteropathogenic Escherichia coli by chitooligosaccharides with specific degrees of acetylation and polymerization.An in vitro investigation of endocrine disrupting effects of trichothecenes deoxynivalenol (DON), T-2 and HT-2 toxins.Inhibition of angiogenesis by chitooligosaccharides with specific degrees of acetylation and polymerization.Cytosol protein regulation in H295R steroidogenesis model induced by the zearalenone metabolites, α- and β-zearalenol.Endocrine disrupting effects of zearalenone, alpha- and beta-zearalenol at the level of nuclear receptor binding and steroidogenesis.Modulation of Lck function through multisite docking to T cell-specific adapter protein.Natural substrate assay for chitinases using high-performance liquid chromatography: a comparison with existing assays.The kinase Itk and the adaptor TSAd change the specificity of the kinase Lck in T cells by promoting the phosphorylation of Tyr192.Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 ChitinasesDetermination of substrate binding energies in individual subsites of a family 18 chitinase.Elucidating thermodynamic parameters for electron transfer proteins using isothermal titration calorimetry: application to the nitrogenase Fe protein.Evidence of two distinct oxygen complexes of reduced endothelial nitric oxide synthase.Comparative study of two chitin-active and two cellulose-active AA10-type lytic polysaccharide monooxygenases.
P50
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P50
description
researcher ORCID ID = 0000-0001-7259-6710
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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Morten Sørlie
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P214
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P31
P496
0000-0001-7259-6710
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viaf-7018149296209080670004