T.M. Gloster

5.0k total citations
72 papers, 3.9k citations indexed

About

T.M. Gloster is a scholar working on Molecular Biology, Organic Chemistry and Biotechnology. According to data from OpenAlex, T.M. Gloster has authored 72 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 62 papers in Molecular Biology, 41 papers in Organic Chemistry and 25 papers in Biotechnology. Recurrent topics in T.M. Gloster's work include Carbohydrate Chemistry and Synthesis (41 papers), Glycosylation and Glycoproteins Research (30 papers) and Enzyme Production and Characterization (23 papers). T.M. Gloster is often cited by papers focused on Carbohydrate Chemistry and Synthesis (41 papers), Glycosylation and Glycoproteins Research (30 papers) and Enzyme Production and Characterization (23 papers). T.M. Gloster collaborates with scholars based in United Kingdom, Canada and United States. T.M. Gloster's co-authors include G.J. Davies, David J. Vocadlo, Bernard Henrissat, Wesley F. Zandberg, David L. Shen, J.P. Turkenburg, Harry J. Gilbert, Linhong Deng, Robert V. Stick and S.M. Roberts and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

T.M. Gloster

68 papers receiving 3.9k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
T.M. Gloster United Kingdom 35 2.9k 1.8k 1.2k 699 518 72 3.9k
Hongzhi Cao China 35 2.4k 0.8× 1.4k 0.8× 339 0.3× 248 0.4× 461 0.9× 105 3.8k
Christelle Breton France 28 2.3k 0.8× 850 0.5× 468 0.4× 262 0.4× 481 0.9× 58 3.1k
Gerlind Sulzenbacher France 28 2.2k 0.7× 754 0.4× 837 0.7× 447 0.6× 83 0.2× 50 3.4k
Stephen G. Withers Canada 15 1.8k 0.6× 1.0k 0.6× 791 0.7× 334 0.5× 145 0.3× 17 2.5k
Antoni Planas Spain 37 2.7k 0.9× 1.5k 0.8× 2.0k 1.7× 1.0k 1.5× 72 0.1× 145 4.3k
Tokuji Ikenaka Japan 42 4.1k 1.4× 1.2k 0.7× 1.4k 1.2× 256 0.4× 512 1.0× 217 5.6k
Shang‐Cheng Hung Taiwan 37 3.6k 1.3× 3.7k 2.0× 323 0.3× 168 0.2× 207 0.4× 132 5.1k
Ramón Hurtado‐Guerrero Spain 34 2.1k 0.7× 965 0.5× 306 0.3× 128 0.2× 531 1.0× 122 3.0k
Peter Orlean United States 31 2.7k 0.9× 587 0.3× 302 0.3× 440 0.6× 345 0.7× 58 3.6k
Günter Legler Germany 35 2.4k 0.8× 2.2k 1.2× 919 0.8× 177 0.3× 131 0.3× 73 3.4k

Countries citing papers authored by T.M. Gloster

Since Specialization
Citations

This map shows the geographic impact of T.M. Gloster's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by T.M. Gloster with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T.M. Gloster more than expected).

Fields of papers citing papers by T.M. Gloster

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by T.M. Gloster. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by T.M. Gloster. The network helps show where T.M. Gloster may publish in the future.

Co-authorship network of co-authors of T.M. Gloster

This figure shows the co-authorship network connecting the top 25 collaborators of T.M. Gloster. A scholar is included among the top collaborators of T.M. Gloster based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with T.M. Gloster. T.M. Gloster is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Hoikkala, Ville, et al.. (2025). A viral SAVED protein with ring nuclease activity degrades the CRISPR second messenger cA4. Biochemical Journal. 482(22). 1707–1719.
2.
Grüschow, Sabine, Katrin Ackermann, S.A. McMahon, et al.. (2024). CRISPR antiphage defence mediated by the cyclic nucleotide-binding membrane protein Csx23. Nucleic Acids Research. 52(6). 2761–2775. 12 indexed citations
3.
Hobbs, Emma, T.M. Gloster, & Leighton Pritchard. (2023). cazy_webscraper: local compilation and interrogation of comprehensive CAZyme datasets. Microbial Genomics. 9(8). 6 indexed citations
4.
Zhu, Wenlong, Sabine Grüschow, S.A. McMahon, et al.. (2021). The CRISPR ancillary effector Can2 is a dual-specificity nuclease potentiating type III CRISPR defence. Nucleic Acids Research. 49(5). 2777–2789. 54 indexed citations
5.
Gloster, T.M., et al.. (2021). Sialidase and Sialyltransferase Inhibitors: Targeting Pathogenicity and Disease. Frontiers in Molecular Biosciences. 8. 705133–705133. 33 indexed citations
6.
Gloster, T.M.. (2020). Exploitation of carbohydrate processing enzymes in biocatalysis. Current Opinion in Chemical Biology. 55. 180–188. 16 indexed citations
7.
8.
Gloster, T.M., et al.. (2018). Linear Eyring Plots Conceal a Change in the Rate-Limiting Step in an Enzyme Reaction. Biochemistry. 57(49). 6757–6761. 19 indexed citations
9.
Stubbs, Keith A., J.P. Bacik, Garrett E. Whitworth, et al.. (2013). The Development of Selective Inhibitors of NagZ: Increased Susceptibility of Gram‐Negative Bacteria to β‐Lactams. ChemBioChem. 14(15). 1973–1981. 33 indexed citations
10.
Cuskin, Fiona, J.E. Flint, T.M. Gloster, et al.. (2012). How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity. Proceedings of the National Academy of Sciences. 109(51). 20889–20894. 102 indexed citations
11.
Thompson, Andrew J., Z. Hakki, Dominic S. Alonzi, et al.. (2012). Structural and mechanistic insight into N-glycan processing by endo-α-mannosidase. Proceedings of the National Academy of Sciences. 109(3). 781–786. 67 indexed citations
12.
Lazarus, Michael B., Jiaoyang Jiang, T.M. Gloster, et al.. (2012). Structural snapshots of the reaction coordinate for O-GlcNAc transferase. Nature Chemical Biology. 8(12). 966–968. 126 indexed citations
13.
Correia, M.A.S., D. Wade Abbott, T.M. Gloster, et al.. (2010). Signature Active Site Architectures Illuminate the Molecular Basis for Ligand Specificity in Family 35 Carbohydrate Binding Module,. Biochemistry. 49(29). 6193–6205. 36 indexed citations
14.
15.
Aguilar‐Moncayo, Matilde, T.M. Gloster, J.P. Turkenburg, et al.. (2009). Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring. Organic & Biomolecular Chemistry. 7(13). 2738–2738. 52 indexed citations
16.
Taylor, Edward J., T.M. Gloster, J.P. Turkenburg, et al.. (2006). Structure and Activity of Two Metal Ion-dependent Acetylxylan Esterases Involved in Plant Cell Wall Degradation Reveals a Close Similarity to Peptidoglycan Deacetylases. Journal of Biological Chemistry. 281(16). 10968–10975. 93 indexed citations
17.
Gloster, T.M., Robert Madsen, & G.J. Davies. (2006). Structural basis for cyclophellitol inhibition of a β-glucosidase. Organic & Biomolecular Chemistry. 5(3). 444–446. 42 indexed citations
18.
Taylor, Edward J., et al.. (2006). Structure of a carbohydrate esterase from Bacillus anthracis. Proteins Structure Function and Bioinformatics. 66(1). 250–252. 23 indexed citations
19.
Gloster, T.M., James M. MacDonald, Chris A. Tarling, et al.. (2004). Structural, Thermodynamic, and Kinetic Analyses of Tetrahydrooxazine-derived Inhibitors Bound to β-Glucosidases. Journal of Biological Chemistry. 279(47). 49236–49242. 39 indexed citations
20.

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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