M. Sørlie

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Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases

A. Mackenzie, R. Helland, V. Eijsink, 2014, Proceedings of the National Academy of Sciences.

An Oxidative Enzyme Boosting the Enzymatic Conversion of Recalcitrant Polysaccharides

V. Eijsink, S. Horn, M. Sørlie, 2010, Science.

Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens

B. Synstad, P. Sikorski, V. Eijsink, 2006, The FEBS journal.

Novel molecular biological tools for the efficient expression of fungal lytic polysaccharide monooxygenases in Pichia pastoris

A. Glieder, M. Sørlie, Lukas Rieder, 2021, Biotechnology for Biofuels.

Human chitotriosidase-catalyzed hydrolysis of chitosan.

Anne Line Norberg, V. Eijsink, K. Vårum, 2012, Biochemistry.

An investigation of the endocrine disrupting potential of enniatin B using in vitro bioassays.

E. Ropstad, C. Frizzell, L. Connolly, 2015, Toxicology letters.

An in vitro investigation of endocrine disrupting effects of the mycotoxin alternariol.

E. Ropstad, C. Frizzell, C. Elliott, 2013, Toxicology and applied pharmacology.

An in vitro investigation of endocrine disrupting effects of trichothecenes deoxynivalenol (DON), T-2 and HT-2 toxins.

C. Fæste, E. Ropstad, C. Frizzell, 2012, Toxicology letters.

Endocrine disrupting effects of zearalenone, alpha- and beta-zearalenol at the level of nuclear receptor binding and steroidogenesis.

E. Ropstad, C. Frizzell, C. Elliott, 2011, Toxicology letters.

Effect of enzyme processivity on the efficacy of a competitive chitinase inhibitor

V. Eijsink, K. Vårum, M. Sørlie, 2010 .

Antifungal activity of well-defined chito-oligosaccharide preparations against medically relevant yeasts

V. Eijsink, O. Bakke, M. Sørlie, 2019, PloS one.

Processivity and substrate-binding in family 18 chitinases

Anne Line Norberg, V. Eijsink, M. Sørlie, 2012 .

Analysis of noncovalent chitinase-chito-oligosaccharide complexes by infrared-matrix assisted laser desorption ionization and nanoelectrospray ionization mass spectrometry.

Anne Line Norberg, J. Peter-Katalinic, V. Eijsink, 2011, Analytical chemistry.

Natural substrate assay for chitinases using high-performance liquid chromatography: a comparison with existing assays.

S. Gåseidnes, B. Synstad, V. Eijsink, 2007, Analytical biochemistry.

Transkingdom mechanism of MAMP generation by chitotriosidase (CHIT1) feeds oligomeric chitin from fungal pathogens and allergens into TLR2-mediated innate immune sensing

T. Roger, B. Moerschbacher, N. Gow, 2022, bioRxiv.

Mutational effects on transglycosylating activity of family 18 chitinases and construction of a hypertransglycosylating mutant.

V. Eijsink, M. Sørlie, Henrik Zakariassen, 2011, Biochemistry.

Elucidating thermodynamic parameters for electron transfer proteins using isothermal titration calorimetry: application to the nitrogenase Fe protein

L. Seefeldt, M. Sørlie, V. Parker, 2003, JBIC Journal of Biological Inorganic Chemistry.

Adherence inhibition of enteropathogenic Escherichia coli by chitooligosaccharides with specific degrees of acetylation and polymerization.

V. Eijsink, M. Sørlie, R. Hutkins, 2013, Journal of agricultural and food chemistry.

Inhibition of a family 18 chitinase by chitooligosaccharides

V. Eijsink, K. Vårum, M. Sørlie, 2008 .

Reactivity of anthracene in liquid SbCl/sub 3/-AlCl/sub 3/-N-(1-butyl)pyridinium chloride mixtures

D. M. Chapman, A. C. Buchanan, M. Sørlie, 1984 .

Comparative study of two chitin-active and two cellulose-active AA10-type lytic polysaccharide monooxygenases.

V. Eijsink, Zarah Forsberg, M. Sørlie, 2014, Biochemistry.

Chemoenzymatic Synthesis of Chito-oligosaccharides with Alternating N-d-Acetylglucosamine and d-Glucosamine.

S. Withers, J. Madhuprakash, V. Eijsink, 2020, Biochemistry.

Key Residues Affecting Transglycosylation Activity in Family 18 Chitinases: Insights into Donor and Acceptor Subsites.

J. Madhuprakash, A. Podile, B. Dalhus, 2018, Biochemistry.

Thermodynamics of tunnel formation upon substrate binding in a processive glycoside hydrolase.

V. Eijsink, M. Sørlie, A. G. Hamre, 2017, Archives of biochemistry and biophysics.

The effect of the carbohydrate binding module on substrate degradation by the human chitotriosidase.

V. Eijsink, A. Tøndervik, H. Sletta, 2015, Biochimica et biophysica acta.

The directionality of processive enzymes acting on recalcitrant polysaccharides is reflected in the kinetic signatures of oligomer degradation

V. Eijsink, M. Sørlie, A. G. Hamre, 2015, FEBS letters.

Dissecting factors that contribute to ligand-binding energetics for family 18 chitinases

Anne Line Norberg, V. Eijsink, M. Sørlie, 2010 .

Comparative studies of chitinases A, B and C from Serratia marcescens

B. Synstad, V. Eijsink, S. Horn, 2006, Microbiology.

Kinetic Characterization of a Putatively Chitin-Active LPMO Reveals a Preference for Soluble Substrates and Absence of Monooxygenase Activity

V. Eijsink, M. Sørlie, D. Petrović, 2021, ACS catalysis.

Using chitosan to understand chitinases and the role of processivity in the degradation of recalcitrant polysaccharides

V. Eijsink, S. Horn, M. Sørlie, 2020 .

Treatment of recalcitrant crystalline polysaccharides with lytic polysaccharide monooxygenase relieves the need for glycoside hydrolase processivity.

V. Eijsink, M. Sørlie, G. Vaaje-Kolstad, 2019, Carbohydrate research.

The role of active site aromatic residues in substrate degradation by the human chitotriosidase.

V. Eijsink, A. Tøndervik, M. Sørlie, 2016, Biochimica et biophysica acta.

Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase.

M. Sørlie, K. B. Eide, A. G. Hamre, 2015, Carbohydrate research.

Enzyme processivity changes with the extent of recalcitrant polysaccharide degradation

M. Sørlie, P. Väljamäe, Silje B Lorentzen, 2014, FEBS letters.

Analysis of productive binding modes in the human chitotriosidase

V. Eijsink, M. Sørlie, K. B. Eide, 2013, FEBS letters.

Cleavage of cellulose by a CBM33 protein

A. Mackenzie, V. Eijsink, S. Horn, 2011, Protein science : a publication of the Protein Society.

One-electron oxidation of catecholamines generates free radicals with an in vitro toxicity correlating with their lifetime.

T. Flatmark, M. Sørlie, O. Terland, 2006, Free radical biology & medicine.

Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity*

Christina M. Payne, M. Sandgren, G. Mathiesen, 2015, The Journal of Biological Chemistry.

Electron inventory, kinetic assignment (E(n)), structure, and bonding of nitrogenase turnover intermediates with C2H2 and CO.

B. Hoffman, M. Sørlie, Hong-In Lee, 2005, Journal of the American Chemical Society.

Variant MoFe proteins of Azotobacter vinelandii: effects of carbon monoxide on electron paramagnetic resonance spectra generated during enzyme turnover

K. Fisher, M. Sørlie, W. Newton, 2005, JBIC Journal of Biological Inorganic Chemistry.

Use of stopped-flow spectrophotometry to establish midpoint potentials for redox proteins.

L. Seefeldt, M. Sørlie, V. Parker, 2000, Analytical biochemistry.

Characterization of an Intermediate in the Reduction of Acetylene by the Nitrogenase α-Gln195 MoFe Protein by Q-band EPR and 13C,1H ENDOR

B. Hoffman, M. Sørlie, Hong-In Lee, 2000 .

Analytical Tools for Characterizing Cellulose-Active Lytic Polysaccharide Monooxygenases (LPMOs).

V. Eijsink, F. Aachmann, M. Sørlie, 2018, Methods in molecular biology.

DETECTION OF A NEW RADICAL AND FEMO-COFACTOR EPR SIGNAL DURING ACETYLENE REDUCTION BY THE ALPHA -H195Q MUTANT OF NITROGENASE

M. Sørlie, D. Dean, B. Hales, 1999 .

Q-Band ENDOR Studies of the Nitrogenase MoFe Protein under Turnover Conditions: Substrate-Inhibitor-Binding to and Metal-Ion Valencies of the FeMo-Cofactor

B. Hoffman, M. Sørlie, W. Orme-Johnson, 2003 .

Modulation of Lck Function through Multisite Docking to T Cell-specific Adapter Protein*

M. Sørlie, T. Lea, A. Spurkland, 2008, Journal of Biological Chemistry.

a copy of Mechanistic basis of substrate-O2 coupling within a chitin-active lytic polysaccharide monooxygenase: an integrated NMR/EPR study a

G. Davies, V. Eijsink, F. Aachmann, 2020 .

Polysaccharide degradation by lytic polysaccharide monooxygenases.

V. Eijsink, F. Aachmann, Zarah Forsberg, 2019, Current opinion in structural biology.

Kinetic insights into the role of the reductant in H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase

V. Eijsink, M. Sørlie, P. Väljamäe, 2018, The Journal of Biological Chemistry.

Tetrahydrobiopterin as combined electron/proton donor in nitric oxide biosynthesis: cryogenic UV-Vis and EPR detection of reaction intermediates.

B. Mayer, M. Sørlie, S. Marchal, 2005, Methods in enzymology.

CO exchange of the oxyferrous complexes of endothelial nitric-oxide synthase oxygenase domain in the presence of 4-amino-tetrahydrobiopterin.

B. Mayer, M. Sørlie, S. Marchal, 2004, Journal of inorganic biochemistry.

Single-turnover of Nitric-oxide Synthase in the Presence of 4-Amino-tetrahydrobiopterin

B. Mayer, Toru Shimizu, M. Sørlie, 2003, Journal of Biological Chemistry.

Biotransformation of zearalenone and zearalenols to their major glucuronide metabolites reduces estrogenic activity.

E. Ropstad, C. Miles, C. Frizzell, 2015, Toxicology in vitro : an international journal published in association with BIBRA.

Antibiotic saving effect of combination therapy through synergistic interactions between well-characterized chito-oligosaccharides and commercial antifungals against medically relevant yeasts

V. Eijsink, M. Sørlie, P. Gaustad, 2019, PloS one.

Thermodynamic analysis of allosamidin binding to the human chitotriosidase

M. Sørlie, S. Sakuda, K. B. Eide, 2013 .

Determination of substrate binding energies in individual subsites of a family 18 chitinase

Anne Line Norberg, V. Eijsink, M. Sørlie, 2010, FEBS letters.

Oligothiophenes. Part 4: Formation and characterization of stable radicals from novel bis- and tris-bithiophene methanes

M. Sørlie, H. Halvorsen, J. Skramstad, 2007 .

Synthesis and Structure of the Ruthenium(II) Complexes [(eta-C(5)Me(5))Ru(NO)(bipy)](2+) and [(eta-C(5)Me(5))Ru(NO)(dppz)](2+). DNA Cleavage by an Organometallic dppz Complex (bipy = 2,2'-Bipyridine; dppz = Dipyrido[3,2-a:2',3'-c]phenazine).

M. Sørlie, T. K. Schoch, J. L. Hubbard, 1996, Inorganic chemistry.

Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 Chitinases*

M. Sørlie, P. Väljamäe, P. Kuusk, 2015, The Journal of Biological Chemistry.

The Predominant Molecular State of Bound Enzyme Determines the Strength and Type of Product Inhibition in the Hydrolysis of Recalcitrant Polysaccharides by Processive Enzymes*

M. Sørlie, P. Väljamäe, Silja Kuusk, 2015, The Journal of Biological Chemistry.

Inhibition of Fungal Plant Pathogens by Synergistic Action of Chito-Oligosaccharides and Commercially Available Fungicides

Md. Hafizur Rahman, V. Eijsink, M. Sørlie, 2014, PloS one.

Antifungal effect of chito-oligosaccharides with different degrees of polymerization

Md. Hafizur Rahman, M. Sørlie, B. B. Aam, 2014, European Journal of Plant Pathology.

The chitinolytic machinery of Serratia marcescens – a model system for enzymatic degradation of recalcitrant polysaccharides

Morten Sørlie, V. Eijsink, S. Horn, 2013, The FEBS journal.

Aromatic Residues in the Catalytic Center of Chitinase A from Serratia marcescens Affect Processivity, Enzyme Activity, and Biomass Converting Efficiency*

V. Eijsink, S. Horn, K. Vårum, 2009, Journal of Biological Chemistry.

Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides

B. Synstad, G. Vriend, P. Sikorski, 2006, Proceedings of the National Academy of Sciences.

Lytic Polysaccharide Monooxygenases in Enzymatic Processing of Lignocellulosic Biomass

V. Eijsink, S. Horn, M. Sørlie, 2019, ACS Catalysis.

Thermodynamic insights into the role of aromatic residues in chitooligosaccharide binding to the transglycosylating chitinase-D from Serratia proteamaculans.

J. Madhuprakash, A. Podile, V. Eijsink, 2020, Biochimica et biophysica acta. Proteins and proteomics.

Polar residues lining the binding cleft of a Serratia marcescens family 18 chitinase position the substrate for attack and stabilize associative interactions

Christina M. Payne, V. Eijsink, M. Sørlie, 2019, Molecular Physics.

Kinetic relationships with processivity in Serratia marcescens family 18 glycoside hydrolases.

M. Sørlie, A. G. Hamre, 2019, Biochemical and biophysical research communications.

Thermodynamic Relationships with Processivity in Serratia marcescens Family 18 Chitinases.

Christina M. Payne, G. Mathiesen, M. Sørlie, 2015, The journal of physical chemistry. B.

Inhibition of angiogenesis by chitooligosaccharides with specific degrees of acetylation and polymerization.

Anne Line Norberg, Yuguang Du, V. Eijsink, 2012, Carbohydrate polymers.

Mechanistic basis of substrate–O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study

G. Davies, V. Eijsink, F. Aachmann, 2020, Proceedings of the National Academy of Sciences.

Production of Chitooligosaccharides and Their Potential Applications in Medicine

Morten Sørlie, Anne Line Norberg, V. Eijsink, 2010, Marine drugs.

Using SILAC proteomics to investigate the effect of the mycotoxin, alternariol, in the human H295R steroidogenesis model

E. Ropstad, L. Connolly, M. Sørlie, 2014, Cell Biology and Toxicology.

Can we make Chitosan by Enzymatic Deacetylation of Chitin?

V. Eijsink, M. Sørlie, Rianne A. G. Harmsen, 2019, Molecules.

Signatures of activation parameters reveal substrate-dependent rate determining steps in polysaccharide turnover by a family 18 chitinase

V. Eijsink, M. Sørlie, Henrik Zakariassen, 2010 .

The characterization of the glucono-δ-lactone-carboxylic acid equilibrium in the products of chitin-active lytic polysaccharide monooxygenases

V. Eijsink, Y. Stenstrøm, M. Sørlie, 2017 .

Cytosol protein regulation in H295R steroidogenesis model induced by the zearalenone metabolites, α- and β-zearalenol.

E. Ropstad, C. Frizzell, L. Connolly, 2012, Toxicon : official journal of the International Society on Toxinology.

Penetration of Sodium and Bath Constituents into Cathode Carbon Materials Used in Industrial Cells

M. Sørlie, H. A. Øye, C. Krohn, 2013 .

Unraveling the roles of the reductant and free copper ions in LPMO kinetics

V. Eijsink, A. Wentzel, Zarah Forsberg, 2021, Biotechnology for Biofuels.

NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions

V. Eijsink, F. Aachmann, G. Skjåk-Bræk, 2012, Proceedings of the National Academy of Sciences.

Thermodynamic analysis of allosamidin binding to a family 18 chitinase.

V. Eijsink, M. Sørlie, S. Sakuda, 2007, Biochemistry.

Evidence for a protein-protein complex during iron loading into ferritin by ceruloplasmin.

M. Sørlie, S. Aust, C. Reilly, 1998, Archives of biochemistry and biophysics.

Relative quantification of the proteomic changes associated with the mycotoxin zearalenone in the H295R steroidogenesis model.

E. Ropstad, L. Connolly, G. Eriksen, 2011, Toxicon : official journal of the International Society on Toxinology.

The interplay between lytic polysaccharide monooxygenases and glycoside hydrolases.

P. Westh, M. Sørlie, M. B. Keller, 2023, Essays in biochemistry.

Fast and Specific Peroxygenase Reactions Catalyzed by Fungal Mono-Copper Enzymes

V. Eijsink, M. Sørlie, Lukas Rieder, 2021, Biochemistry.

Kinetics of H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase

V. Eijsink, Zarah Forsberg, M. Sørlie, 2017, The Journal of Biological Chemistry.

Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase

M. Sandgren, V. Eijsink, F. Aachmann, 2016, Proceedings of the National Academy of Sciences.

Lytic Polysaccharide Monooxygenase

V. Eijsink, F. Aachmann, Zarah Forsberg, 2015 .

Measuring processivity.

V. Eijsink, S. Horn, K. Vårum, 2012, Methods in enzymology.

Methylation of the N‐terminal histidine protects a lytic polysaccharide monooxygenase from auto‐oxidative inactivation

V. Eijsink, F. Aachmann, M. Sørlie, 2018, Protein science : a publication of the Protein Society.

Hallmarks of Processivity in Glycoside Hydrolases from Crystallographic and Computational Studies of the Serratia marcescens Chitinases

Christina M. Payne, G. Beckham, B. Dalhus, 2012, The Journal of Biological Chemistry.

Kinetics of H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase.

V. Eijsink, Zarah Forsberg, M. Sørlie, 2018, The Journal of Biological Chemistry.

Temperature Stability of Søderberg Anode Pitch

M. Sørlie, 2016 .

The use of isothermal titration calorimetry to determine the thermodynamics of metal ion binding to low-cost sorbents

M. Sørlie, V. Karlsen, E. Heggset, 2010 .

The kinase Itk and the adaptor TSAd change the specificity of the kinase Lck in T cells by promoting the phosphorylation of Tyr192

M. Sørlie, G. Abrahamsen, A. Spurkland, 2014, Science Signaling.

Degradation of chitosans with a family 46 chitosanase from Streptomyces coelicolor A3(2).

V. Eijsink, K. Vårum, M. Sørlie, 2010, Biomacromolecules.

NMR and Fluorescence Spectroscopies Reveal the Preorganized Binding Site in Family 14 Carbohydrate-Binding Module from Human Chitotriosidase

M. Vandevenne, F. Aachmann, M. Sørlie, 2019, ACS omega.

The effect of carbohydrate binding modules and linkers on inhibitor binding to family 18 glycoside hydrolases

M. Sørlie, K. B. Eide, 2018, The Journal of Chemical Thermodynamics.

Human Chitotriosidase Is an Endo-Processive Enzyme

M. Sørlie, P. Väljamäe, Silja Kuusk, 2017, PloS one.

The roles of three Serratia marcescens chitinases in chitin conversion are reflected in different thermodynamic signatures of allosamidin binding.

V. Eijsink, M. Sørlie, S. Sakuda, 2010, The journal of physical chemistry. B.

Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function

M. Galleni, M. Vandevenne, D. Baurain, 2017, Scientific Reports.

Processivity, Substrate Positioning, and Binding: The Role of Polar Residues in a Family 18 Glycoside Hydrolase.

Christina M. Payne, M. Sørlie, Suvamay Jana, 2015, Biochemistry.

Synergistic Antifungal Activity of Chito-Oligosaccharides and Commercial Antifungals on Biofilms of Clinical Candida Isolates

M. Sørlie, P. Gaustad, M. Ganan, 2021, Journal of fungi.

Electrochemical properties of the solvent SbCl/sub 3/-AlCl/sub 3/-N(1-butyl)pyridinium chloride and electrochemical and spectroelectrochemical studies of arene solutes

D. M. Chapman, M. Sørlie, G. Smith, 1984 .

Spectroelectrochemical Study of the Formation of the Radical Cation and Dication of Perylene in Molten Antimony(III) Chloride

M. Sørlie, G. Smith, G. Mamantov, 1981 .

Experimental Comparison of Cathode Rodding Practices

M. Sørlie, K. Rye, L. Caruso, 2013 .

Identification of a high-affinity-binding oligosaccharide by (+) nanoelectrospray quadrupole time-of-flight tandem mass spectrometry of a noncovalent enzyme-ligand complex.

J. Peter-Katalinic, V. Eijsink, M. Sørlie, 2006, Angewandte Chemie.

Structural and Thermodynamic Signatures of Ligand Binding to the Enigmatic Chitinase D of Serratia proteamaculans.

J. Madhuprakash, A. Podile, B. Dalhus, 2019, The journal of physical chemistry. B.

Towards a molecular-level theory of carbohydrate processivity in glycoside hydrolases.

Christina M. Payne, M. Himmel, J. Ståhlberg, 2014, Current opinion in biotechnology.

Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe protein.

B. J. Lemon, J. W. Peters, B. Lemon, 2001, Biochemistry.

Reductants fuel lytic polysaccharide monooxygenase activity in a pH‐dependent manner

V. Eijsink, M. Sørlie, Iván Ayuso-Fernández, 2023, FEBS letters.

Thermodynamic analysis of L-arginine and N omega-hydroxy-L-arginine binding to nitric oxide synthase.

B. Mayer, Toru Shimizu, M. Sørlie, 2008, Biochimica et biophysica acta.

High-pressure studies of the reaction mechanism of nitric-oxide synthase.

B. Mayer, M. Sørlie, S. Marchal, 2006, Biochimica et biophysica acta.

Evidence of Two Distinct Oxygen Complexes of Reduced Endothelial Nitric Oxide Synthase*

B. Mayer, M. Sørlie, S. Marchal, 2004, Journal of Biological Chemistry.

Formation of gas complexes between europium chloride and aluminium chloride above liquid chloroaluminate mixtures

M. Sørlie, H. A. Øye, 1978 .

Aromatic-Mediated Carbohydrate Recognition in Processive Serratia marcescens Chitinases.

Christina M. Payne, G. Beckham, V. Eijsink, 2016, The journal of physical chemistry. B.

Concurrent enzyme reactions and binding events for chitinases interacting with chitosan oligosaccharides monitored by high resolution mass spectrometry

J. Peter-Katalinic, V. Eijsink, M. Sørlie, 2011 .

Antifungal effect of chito-oligosaccharides with different degrees of polymerization

Md. Hafizur Rahman, M. Sørlie, B. B. Aam, 2014, European journal of plant pathology.

Thermodynamic Signatures of Substrate Binding for Three Thermobifida fusca Cellulases with Different Modes of Action.

Christina M. Payne, M. Sørlie, P. Väljamäe, 2019, Biochemistry.

Chitin oligosaccharide binding to a family GH19 chitinase from the moss Bryum coronatum

M. Sørlie, T. Taira, T. Ohnuma, 2011, The FEBS journal.

Structural and functional characterization of the catalytic domain of a cell-wall anchored bacterial lytic polysaccharide monooxygenase from Streptomyces coelicolor

V. Eijsink, Zarah Forsberg, M. Sørlie, 2023, Scientific Reports.

Substrate positioning in chitinase A, a processive chito‐biohydrolase from Serratia marcescens

J. Peter-Katalinic, V. Eijsink, M. Sørlie, 2011, FEBS letters.

Enzyme assay for chitinase catalyzed hydrolysis of tetra-N-acetylchitotetraose by isothermal titration calorimetry

V. Eijsink, M. Sørlie, Inger-Mari Krokeide, 2007 .

Short communication Enzyme assay for chitinase catalyzed hydrolysis of tetra-N-acetylchitotetraose by isothermal titration calorimetry

M. Sørlie, Inger-Mari Krokeide, 2007 .

Effect of baking temperature and anode current density on anode carbon consumption

M. Sørlie, J. Thonstad, S. Rolseth, 1996 .

Heat capacity changes in heme protein–ligand interactions

M. Sørlie, Henrik Zakariassen, 2007 .

Reactive complexes in myoglobin and nitric oxide synthase

B. Mayer, T. Uchida, Toru Shimizu, 2008 .

Changes in the proteome of the H295R steroidogenesis model associated with exposure to the mycotoxin zearalenone and its metabolites, α- and β-zearalenol

E. Ropstad, C. Frizzell, L. Connolly, 2012 .

Crystal structure and thermodynamic dissection of chitin oligosaccharide binding to the LysM module of chitinase-A from Pteris ryukyuensis.

M. Sørlie, T. Numata, T. Taira, 2017, Biochemical and biophysical research communications.

Genomic and Proteomic Study of Andreprevotia ripae Isolated from an Anthill Reveals an Extensive Repertoire of Chitinolytic Enzymes

V. Eijsink, M. Arntzen, T. Hahn, 2021, Journal of proteome research.