Profile

Dr Tracey Gloster:
Wellcome Trust Research Fellow

Dr Tracey Gloster

Dr Tracey Gloster
Biomolecular Sciences Building
University of St Andrews
North Haugh
St Andrews
KY16 9ST
Fife
UK

tel: 01334 467245
fax: 01334 462595
room: B209
email: tmg@st-andrews.ac.uk

Related Content:

research@st-andrews
Group webpage

Biology Research Committee
School of Biology
Biomedical Sciences Research Complex
Biology Equality and Diversity Committee

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I am interested in the structure and function of eukaryotic carbohydrate processing enzymes. Obtaining a greater appreciation of how these enzymes assimilate or degrade carbohydrates is important in understanding the biological roles that carbohydrates play in cellular processes, and also how these processes malfunction in a number of diseases, such as cancer, lysosomal storage disorders, and neurodegenerative diseases.

I am currently investigating the enzymes responsible for the degradation of heparan sulphate, a component of the extracellular matrix. Using a combination of approaches, including molecular biology, protein production, X-ray crystallography, enzyme kinetics and cell culture, I aim to gain a greater understanding of these enzymes from a mechanistic and structural perspective. Hopefully this will lead to the development of tools, such as enzyme inhibitors, that can be used to probe the biological functions of the enzymes, and possibly also for therapeutic applications in the longer term.

 



I am interested in the structure and function of eukaryotic carbohydrate processing enzymes. Obtaining a greater appreciation of how these enzymes assimilate or degrade carbohydrates is important in understanding the biological roles that carbohydrates play in cellular processes, and also how these processes malfunction in a number of diseases, such as cancer, lysosomal storage disorders, and neurodegenerative diseases.

I am currently investigating the enzymes responsible for the degradation of heparan sulphate, a component of the extracellular matrix. Using a combination of approaches, including molecular biology, protein production, X-ray crystallography, enzyme kinetics and cell culture, I aim to gain a greater understanding of these enzymes from a mechanistic and structural perspective. Hopefully this will lead to the development of tools, such as enzyme inhibitors, that can be used to probe the biological functions of the enzymes, and possibly also for therapeutic applications in the longer term.

source: symbiosis


Recent Publications:

Recent publications listed in research@st-andrews
Adamson, C, Pengelly, RJ, Kazem Abadi, SS, Chakladar, S, Draper, J, Britton, R, Gloster, TM & Bennet, AJ 2016, 'Structural snapshots for mechanism-based inactivation of a glycoside hydrolase by cyclopropyl-carbasugars' Angewandte Chemie International Edition, vol 55, no. 48, pp. 14978-14982. DOI: 10.1002/anie.201607431
Alteen, MG, Oehler, V, Nemčovičová, I, Wilson, IBH, Vacadlo, DJ & Gloster, TM 2016, 'Mechanism of the human nucleocytoplasmic hexosaminidase D' Biochemistry, vol 55, no. 19, pp. 2753-2747. DOI: 10.1021/acs.biochem.5b01285
He, X, Pierce, O, Haselhorst, T, Kolarich, D, Packer, NH, Gloster, T, Vocadlo, DJ, Qian, Y, Brooks, D & Kermode, AR 2013, 'Characterization and downstream mannose phosphorylation of human recombinant α-L-iduronidase produced in Arabidopsis complex glycan-deficient (cgl) seeds' Plant Biotechnology Journal, vol 11, no. 9, pp. 1034–1043. DOI: 10.1111/pbi.12096
Stubbs, KA, Bacik, J-P, Perley-Robertson, GE, Whitworth, GE, Gloster, TM, Vocadlo, DJ & Mark, BL 2013, 'The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to β-lactams' ChemBioChem, vol 14, no. 15, pp. 1973-1981. DOI: 10.1002/cbic.201300395