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Tracey Gloster

Tracey Gloster
Born
Tracey Maureen Gloster
Alma materUniversity of Warwick (BSc)
University of York (PhD)
Scientific career
FieldsStructural biology
Chemical biology
Glycobiology
Carbohydrate processing enzymes[1]
InstitutionsUniversity of St Andrews
Simon Fraser University
ThesisTransition state mimicry in glycoside hydrolysis (2005)
Doctoral advisorGideon Davies[2]
Websiterisweb.st-andrews.ac.uk/portal/en/persons/tracey-gloster(d02c38ef-6020-455d-8ec5-d72eeb81ad64).html Edit this at Wikidata

Tracey Maureen Gloster is a chemist at the University of St Andrews UK.[1][3] Her research interests are in structural biology, chemical biology, glycobiology and carbohydrate processing enzymes.[1]

Education

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Gloster studied biochemistry at University of Warwick, graduating in 2002[4] and then moved to University of York where she was awarded a PhD in chemistry in 2005 for research supervised by Gideon Davies.[2][5]

Career and research

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In her early career she was funded by the Wellcome Trust, initially with a Henry Wellcome post-doctoral fellowship held between 2008 and 2011 at Simon Fraser University, Canada, where she worked with David Vocadlo,[4][6] and then a Wellcome Trust Research Career Development fellowship in 2012 when she joined the University of St Andrews, Scotland. As of 2022 she holds the position of Reader.[7]

Her research is about all aspects of enzymes that deal with carbohydrates within eukaryotes.[7] Carbohydrates are made from a very wide range of sugar molecules that can be attached to each and other molecules in diverse ways. These glycosylations can have profound consequences for the roles and activities of the molecules and can result in disease if the cell does not process them correctly. Identifying the location and nature of glycosylations is technically challenging, in addition to the challenge of linking them to functions. Gloster has applied inhibitors to gain more understanding about exactly how they work, including describing a new class of glycosyltransferase inhibitors.[5] The techniques that Gloster uses includes ones based around cells, including molecular biology and cell cultures, as well as biophysical methods such as enzyme kinetics, X-ray crystallography and isothermal titration calorimetry.[8]

Publications

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Gloster is the author or co-author of over 50 scientific publications.[1][3] They include:

Awards and honours

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Gloster was awarded the Biochemical Society early career research award in 2012,[15] the L’Oreal UK and Ireland Fellowship For Women In Science Fellowship in 2013[7] and she was awarded the Dextra Medal by the Royal Society of Chemistry in 2019 for her work in carbohydrate chemistry largely conducted in the UK within 15 years of gaining a PhD.

She serves as a member of the Royal Society International Exchanges Committee between 2017 - 2022.[16] She serves as treasurer of the Royal Society of Chemistry Carbohydrate Interest Group.[17] She chairs one of the review panels that judge requests to use the Diamond Light Source.[18]

She is a member of the Young Academy of Scotland.[7]

References

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  1. ^ a b c d Tracey Gloster publications indexed by Google Scholar Edit this at Wikidata
  2. ^ a b Gloster, Tracey Maureen (2005). Transition state mimicry in glycoside hydrolysis. york.ac.uk (PhD thesis). The University of York. OCLC 1063339504. EThOS uk.bl.ethos.533533.
  3. ^ a b Tracey Gloster publications from Europe PubMed Central
  4. ^ a b "User:Tracey Gloster". cazypedia.org. CAZypedia: carbohydrate active enzymes. Retrieved 2 September 2020.
  5. ^ a b "Early Career Research Awards – researchers within 5 years of their PhD: Molecular Structure and Function Dr Tracey Gloster" (PDF). portlandpress.com. Portland Press. Retrieved 2 September 2020.
  6. ^ "Dissection of O-glycosylation of nuclear and cytoplasmic proteins". wellcome.ac.uk. The Wellcome Trust. Retrieved 3 September 2020.
  7. ^ a b c d "Tracey Gloster". youngacademyofscotland.org.uk. RSE Young Academy of Scotland. Retrieved 2 September 2020.
  8. ^ "Tracey Gloster". st-andrews.ac.uk. University of St Andrews. Retrieved 3 September 2020.
  9. ^ Januka S Athukoralage; Stephen A McMahon; Changyi Zhang; et al. (15 January 2020). "An anti-CRISPR viral ring nuclease subverts type III CRISPR immunity". Nature. 577 (7791): 572–575. doi:10.1038/S41586-019-1909-5. ISSN 1476-4687. PMC 6986909. PMID 31942067. Wikidata Q92669532.
  10. ^ Tracey M Gloster (20 March 2020). "Exploitation of carbohydrate processing enzymes in biocatalysis". Current Opinion in Chemical Biology. 55: 180–188. doi:10.1016/J.CBPA.2020.01.015. ISSN 1367-5931. PMID 32203896. Wikidata Q90594642.
  11. ^ Weiwu Ren; Robert Pengelly; Marco Farren-Dai; et al. (13 August 2018). "Revealing the mechanism for covalent inhibition of glycoside hydrolases by carbasugars at an atomic level". Nature Communications. 9 (1): 3243. Bibcode:2018NatCo...9.3243R. doi:10.1038/S41467-018-05702-7. ISSN 2041-1723. PMC 6089974. PMID 30104598. Wikidata Q58786771. (erratum)
  12. ^ Laura Griffin; Tracey Gloster (24 July 2017). "The Enzymatic Degradation of Heparan Sulfate". Protein and Peptide Letters. doi:10.2174/0929866524666170724113452. ISSN 0929-8665. PMID 28741461. Wikidata Q39456712.
  13. ^ Tracey M Gloster (19 September 2014). "Advances in understanding glycosyltransferases from a structural perspective". Current Opinion in Structural Biology. 28: 131–141. doi:10.1016/J.SBI.2014.08.012. ISSN 0959-440X. PMC 4330554. PMID 25240227. Wikidata Q38252791.
  14. ^ Tracey M Gloster; David J Vocadlo (18 July 2012). "Developing inhibitors of glycan processing enzymes as tools for enabling glycobiology". Nature Chemical Biology. 8 (8): 683–694. doi:10.1038/NCHEMBIO.1029. ISSN 1552-4450. PMID 22810773. Wikidata Q38027408.
  15. ^ "2012 Award Winners". biochemistry.org. The Biochemical Society. Retrieved 2 September 2020.
  16. ^ "Tracey Gloster". royalsociety.org. The Royal Society. Retrieved 2 September 2020.
  17. ^ "Carbohydrate Group". rsc.org. Royal Society of Chemistry. Retrieved 2 October 2020.
  18. ^ "Apply for Beamtime - Peer Review". diamond.ac.uk. Retrieved 2 September 2020.