M. Nielsen

发表

Roles of multiple surface sites, long substrate binding clefts, and carbohydrate binding modules in the action of amylolytic enzymes on polysaccharide substrates

B. Svensson, M. Willemoës, R. Haser, 2008 .

Crystal Structures of the Catalytic Domain of Arabidopsis thaliana Starch Synthase IV, of Granule Bound Starch Synthase From CLg1 and of Granule Bound Starch Synthase I of Cyanophora paradoxa Illustrate Substrate Recognition in Starch Synthases

S. Ball, M. Palcic, J. A. Cuesta-Seijo, 2018, Front. Plant Sci..

The Role of Cysteine Residues in Redox Regulation and Protein Stability of Arabidopsis thaliana Starch Synthase 1

A. Blennow, M. A. Glaring, M. Palcic, 2015, PloS one.

α-Amylases. Interaction with polysaccharide substrates, proteinaceous inhibitors and regulatory proteins

B. Svensson, A. Blennow, K. Maeda, 2008 .

An enzyme family reunion — similarities, differences and eccentricities in actions on α-glucans

B. Svensson, A. Blennow, R. Haser, 2008, Biologia.

Interactions between Barley α-Amylases, Substrates, Inhibitors and Regulatory Proteins

B. Svensson, M. Willemoës, K. Maeda, 2006 .

Surface binding sites (SBSs), mechanism and regulation of enzymes degrading amylopectin and α-limit dextrins.

B. Svensson, M. Willemoës, P. Hägglund, 2013 .

Surface binding sites in amylase have distinct roles in recognition of starch structure motifs and degradation.

B. Svensson, A. Blennow, D. Cockburn, 2015, International journal of biological macromolecules.

Waxy and non-waxy barley cultivars exhibit differences in the targeting and catalytic activity of GBSS1a

A. Blennow, M. Palcic, K. Hebelstrup, 2017, Journal of experimental botany.

Barley callus: a model system for bioengineering of starch in cereals

A. Blennow, K. Hebelstrup, Massimiliano Carciofi, 2012, Plant Methods.

Two secondary carbohydrate binding sites on the surface of barley alpha-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules.

B. Svensson, S. Bozonnet, M. Abou Hachem, 2009, Biochemistry.

Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity.

M. Palcic, L. Marri, Sophie R. Beeren, 2013, Acta crystallographica. Section D, Biological crystallography.

Substrate and Metal Ion Promiscuity in Mannosylglycerate Synthase*

L. Tailford, H. Gilbert, G. Davies, 2011, The Journal of Biological Chemistry.

New insight into structure/function relationships in plant alpha-amylase family GH13 members.

Š. Janeček, B. Svensson, A. Blennow, 2010 .

The ‘pair of sugar tongs’ site on the non‐catalytic domain C of barley α‐amylase participates in substrate binding and activity

B. Svensson, M. Willemoës, R. Haser, 2007, The FEBS journal.

In vitro Biochemical Characterization of All Barley Endosperm Starch Synthases

M. S. Motawia, W. Willats, M. Palcic, 2016, Front. Plant Sci..

Multi‐site substrate binding and interplay in barley α‐amylase 1

B. Svensson, R. Haser, S. Bozonnet, 2008, FEBS letters.

Substrate and Metal Ion Promiscuity in Mannosylglycerate Synthase*

L. Tailford, H. Gilbert, G. Davies, 2011, The Journal of Biological Chemistry.