Karl Syson

发表

Assembly of α-Glucan by GlgE and GlgB in Mycobacteria and Streptomycetes.

A. Rashid, S. Bornemann, R. Kalscheuer, 2016, Biochemistry.

Structure of the Mycobacterium smegmatis α-maltose-1-phosphate synthase GlgM

C. Stevenson, S. Bornemann, D. Lawson, 2020, Acta crystallographica. Section F, Structural biology communications.

Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an α -glucan pathway

Z. Liu, G. Besra, J. Sacchettini, 2012 .

Dissecting the Kinetic Mechanism of Human Lysine Methyltransferase 2D and Its Interactions with the WRAD2 Complex

A. Gohlke, Karl Syson, S. Caswell, 2022, Biochemistry.

Three Metal Ions Participate in the Reaction Catalyzed by T5 Flap Endonuclease*

J. Tainer, J. Grasby, Nicholas H Williams, 2008, Journal of Biological Chemistry.

The molecular basis for a temperature-sensitive Mycobacterium smegmatis glgE mutant

S. Bornemann, R. Kalscheuer, S. Batey, 2020 .

A temperature-sensitive Mycobacterium smegmatis glgE mutation leads to a loss of GlgE enzyme activity and thermostability and the accumulation of α-maltose-1-phosphate

S. Bornemann, R. Kalscheuer, S. Batey, 2020, bioRxiv.

Metabolic Network for the Biosynthesis of Intra- and Extracellular α-Glucans Required for Virulence of Mycobacterium tuberculosis

W. Jacobs, T. Ioerger, S. Bornemann, 2016, PLoS pathogens.

Trehalose-6-Phosphate-Mediated Toxicity Determines Essentiality of OtsB2 in Mycobacterium tuberculosis In Vitro and in Mice

K. Köhrer, W. Jacobs, T. Ioerger, 2016, PLoS pathogens.

Trehalose and α-glucan mediate distinct abiotic stress responses in Pseudomonas aeruginosa

James K. M. Brown, S. Bornemann, Karl Syson, 2020, bioRxiv.

Structure of Streptomyces Maltosyltransferase GlgE, a Homologue of a Genetically Validated Anti-tuberculosis Target*

K. Chater, M. Rejžek, R. Field, 2011, The Journal of Biological Chemistry.

Enhanced ligand affinity for receptors in which components of the binding site are independently mobile.

C. Hunter, J. Perkins, A. Annila, 2005, Chemistry & biology.

Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an alpha-glucan pathway.

G. Besra, J. Sacchettini, W. Jacobs, 2010, Nature chemical biology.

Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.

A. Hounslow, J. Waltho, Karl Syson, 2005, Structure.

Comparison of the catalytic parameters and reaction specificities of a phage and an archaeal flap endonuclease.

J. Tainer, J. Grasby, Karl Syson, 2007, Journal of molecular biology.

Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis

S. Bornemann, A. Iglesias, Karl Syson, 2015, Biochimica et biophysica acta.

Neutralizing Mutations of Carboxylates That Bind Metal 2 in T5 Flap Endonuclease Result in an Enzyme That Still Requires Two Metal Ions*

J. Tainer, J. Grasby, Nicholas H Williams, 2011, The Journal of Biological Chemistry.

The denatured state under native conditions: a non-native-like collapsed state of N-PGK.

M. Reed, A. Clarke, A. Hounslow, 2006, Journal of molecular biology.

Mycobacterium tuberculosis Maltosyltransferase GlgE, a Genetically Validated Antituberculosis Target, Is Negatively Regulated by Ser/Thr Phosphorylation*

L. Kremer, S. Bornemann, V. Molle, 2013, The Journal of Biological Chemistry.

Phosphorylation Negatively Regulated by Ser/Thr Validated Antituberculosis Target, Is Maltosyltransferase GlgE, a Genetically Mycobacterium tuberculosis Microbiology:

L. Kremer, S. Bornemann, V. Molle, 2013 .

Ligand-bound Structures and Site-directed Mutagenesis Identify the Acceptor and Secondary Binding Sites of Streptomyces coelicolor Maltosyltransferase GlgE*

A. Rashid, C. Stevenson, S. Bornemann, 2016, The Journal of Biological Chemistry.

Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds α-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate

S. Withers, D. Svergun, A. Rashid, 2014, Biochemistry.