Ghent University Academic Bibliography

Disulfide bridges as essential elements for the thermostability of lytic polysaccharide monooxygenase LPMO10C from Streptomyces coelicolor

Magali Tanghe (UGent) , Barbara Danneels (UGent) , Matthias Last, Koen Beerens (UGent) , Ingeborg Stals (UGent) and Tom Desmet (UGent)

(2017) PROTEIN ENGINEERING DESIGN & SELECTION. 30(5). p.401-408

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Sequence determinants of nucleotide binding in Sucrose Synthase : improving the affinity of a bacterial Sucrose Synthase for UDP by introducing plant residues

Margo Diricks (UGent) , Alexander Gutmann, Simon Debacker, Griet Dewitte (UGent) , Bernd Nidetzky and Tom Desmet (UGent)

(2017) PROTEIN ENGINEERING DESIGN & SELECTION. 30(3). p.143-150

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Increasing the thermostability of sucrose phosphorylase by a combination of sequence- and structure-based mutagenesis

An Cerdobbel (UGent) , Karel De Winter (UGent) , Dirk Aerts (UGent) , Remko Kuipers, Henk-Jan Joosten, Wim Soetaert (UGent) and Tom Desmet (UGent)

(2011) PROTEIN ENGINEERING DESIGN & SELECTION. 24(11). p.829-834

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Thermostabilization of an esterase by alignment-guided focussed directed evolution

Helge Jochens, Dirk Aerts (UGent) and Uwe Bornscheuer

(2010) PROTEIN ENGINEERING DESIGN & SELECTION. 23(12). p.903-909

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PH1-derived bivalent bibodies and trivalent tribodies bind differentially to shed and tumour cell-associated MUC1

Steve Schoonooghe (UGent) , Ingrid Burvenich, Liesbet Vervoort (UGent) , Filip De Vos (UGent) , Nico Mertens (UGent) and Johan Grooten (UGent)

(2010) PROTEIN ENGINEERING DESIGN & SELECTION. 23(9). p.721-728

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Creating lactose phosphorylase enzymes by directed evolution of cellobiose phosphorylase

Manu De Groeve, Miet De Baere (UGent) , Lieve Hoflack (UGent) , Tom Desmet (UGent) , Erick Vandamme (UGent) and Wim Soetaert (UGent)

(2009) PROTEIN ENGINEERING DESIGN & SELECTION. 22(7). p.393-399

Academic Bibliography

Disulfide bridges as essential elements for the thermostability of lytic polysaccharide monooxygenase LPMO10C from Streptomyces coelicolor

Sequence determinants of nucleotide binding in Sucrose Synthase : improving the affinity of a bacterial Sucrose Synthase for UDP by introducing plant residues

Increasing the thermostability of sucrose phosphorylase by a combination of sequence- and structure-based mutagenesis

Thermostabilization of an esterase by alignment-guided focussed directed evolution

PH1-derived bivalent bibodies and trivalent tribodies bind differentially to shed and tumour cell-associated MUC1

Creating lactose phosphorylase enzymes by directed evolution of cellobiose phosphorylase

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