Tom D. Heightman

10.0k total citations · 1 hit paper
54 papers, 4.0k citations indexed

About

Tom D. Heightman is a scholar working on Molecular Biology, Organic Chemistry and Hematology. According to data from OpenAlex, Tom D. Heightman has authored 54 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 22 papers in Organic Chemistry and 8 papers in Hematology. Recurrent topics in Tom D. Heightman's work include Protein Degradation and Inhibitors (14 papers), Histone Deacetylase Inhibitors Research (13 papers) and Epigenetics and DNA Methylation (9 papers). Tom D. Heightman is often cited by papers focused on Protein Degradation and Inhibitors (14 papers), Histone Deacetylase Inhibitors Research (13 papers) and Epigenetics and DNA Methylation (9 papers). Tom D. Heightman collaborates with scholars based in United Kingdom, United States and Switzerland. Tom D. Heightman's co-authors include Andrea Vasella, Christopher N. Johnson, Honorine Lebraud, David J. Wright, Stefan Knapp, O. Fedorov, Martin Philpott, Anthony Tumber, David J. Procter and S. Picaud and has published in prestigious journals such as Journal of the American Chemical Society, Angewandte Chemie International Edition and The EMBO Journal.

In The Last Decade

Tom D. Heightman

54 papers receiving 3.9k citations

Hit Papers

Recent Insights into Inhibition, Structure, and Mechanism... 1999 2026 2008 2017 1999 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tom D. Heightman United Kingdom 30 3.0k 1.7k 441 427 408 54 4.0k
Mitsuhiro Kinoshita Japan 33 1.9k 0.6× 1.8k 1.0× 229 0.5× 143 0.3× 162 0.4× 177 3.5k
John D. McCarter United States 26 1.8k 0.6× 1.2k 0.7× 802 1.8× 66 0.2× 177 0.4× 47 2.7k
André White United States 20 1.0k 0.3× 559 0.3× 283 0.6× 166 0.4× 195 0.5× 26 1.7k
Joseph W. Becker United States 29 2.2k 0.7× 546 0.3× 134 0.3× 85 0.2× 486 1.2× 37 3.0k
Yu Rao China 43 2.9k 1.0× 2.8k 1.6× 49 0.1× 521 1.2× 1.1k 2.6× 118 5.9k
Kathryn M. Koeller United States 19 2.7k 0.9× 1.3k 0.8× 169 0.4× 45 0.1× 380 0.9× 24 3.2k
Ian P. Street Australia 31 1.9k 0.6× 998 0.6× 418 0.9× 31 0.1× 366 0.9× 57 3.0k
Alexander Adibekian United States 39 3.1k 1.1× 1.7k 1.0× 109 0.2× 44 0.1× 485 1.2× 95 4.4k
Jef K. De Brabander United States 37 2.1k 0.7× 1.8k 1.1× 487 1.1× 41 0.1× 440 1.1× 97 4.6k
Manuel Martín‐Lomas Spain 38 3.1k 1.0× 2.7k 1.6× 424 1.0× 50 0.1× 58 0.1× 182 4.3k

Countries citing papers authored by Tom D. Heightman

Since Specialization
Citations

This map shows the geographic impact of Tom D. Heightman'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 Tom D. Heightman with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Tom D. Heightman more than expected).

Fields of papers citing papers by Tom D. Heightman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Tom D. Heightman. 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 Tom D. Heightman. The network helps show where Tom D. Heightman may publish in the future.

Co-authorship network of co-authors of Tom D. Heightman

This figure shows the co-authorship network connecting the top 25 collaborators of Tom D. Heightman. A scholar is included among the top collaborators of Tom D. Heightman 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 Tom D. Heightman. Tom D. Heightman 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.
Tamanini, Emiliano, Ildiko M. Buck, Gianni Chessari, et al.. (2017). Discovery of a Potent Nonpeptidomimetic, Small-Molecule Antagonist of Cellular Inhibitor of Apoptosis Protein 1 (cIAP1) and X-Linked Inhibitor of Apoptosis Protein (XIAP). Journal of Medicinal Chemistry. 60(11). 4611–4625. 57 indexed citations
2.
Lebraud, Honorine, et al.. (2016). In-gel activity-based protein profiling of a clickable covalent ERK1/2 inhibitor. Molecular BioSystems. 12(9). 2867–2874. 18 indexed citations
3.
Hewings, David S., et al.. (2016). Isoxazole‐Derived Amino Acids are Bromodomain‐Binding Acetyl‐Lysine Mimics: Incorporation into Histone H4 Peptides and Histone H3. Angewandte Chemie International Edition. 55(29). 8353–8357. 18 indexed citations
4.
Hewings, David S., et al.. (2016). Isoxazole‐Derived Amino Acids are Bromodomain‐Binding Acetyl‐Lysine Mimics: Incorporation into Histone H4 Peptides and Histone H3. Angewandte Chemie. 128(29). 8493–8497. 5 indexed citations
5.
Rooney, Timothy P. C., P. Filippakopoulos, O. Fedorov, et al.. (2014). A Series of Potent CREBBP Bromodomain Ligands Reveals an Induced‐Fit Pocket Stabilized by a Cation–π Interaction. Angewandte Chemie. 126(24). 6240–6244. 13 indexed citations
6.
Rooney, Timothy P. C., P. Filippakopoulos, O. Fedorov, et al.. (2014). A Series of Potent CREBBP Bromodomain Ligands Reveals an Induced‐Fit Pocket Stabilized by a Cation–π Interaction. Angewandte Chemie International Edition. 53(24). 6126–6130. 93 indexed citations
7.
Kanno, Tomohiko, Yuka Kanno, Gary LeRoy, et al.. (2014). BRD4 assists elongation of both coding and enhancer RNAs by interacting with acetylated histones. Nature Structural & Molecular Biology. 21(12). 1047–1057. 239 indexed citations
8.
Patel, Mira C., Matthew D. Smith, Anup Dey, et al.. (2013). BRD4 Coordinates Recruitment of Pause Release Factor P-TEFb and the Pausing Complex NELF/DSIF To Regulate Transcription Elongation of Interferon-Stimulated Genes. Molecular and Cellular Biology. 33(12). 2497–2507. 136 indexed citations
9.
Nimura, Keisuke, Tomohiko Tamura, Tomohiko Kanno, et al.. (2013). WHSC1 links transcription elongation to HIRA‐mediated histone H3.3 deposition. The EMBO Journal. 32(17). 2392–2406. 50 indexed citations
10.
Philpott, Martin, Jing Yang, O. Fedorov, et al.. (2011). Bromodomain-peptide displacement assays for interactome mapping and inhibitor discovery. Molecular BioSystems. 7(10). 2899–2908. 107 indexed citations
11.
Chang, Kai‐Hsuan, Oliver N. F. King, Anthony Tumber, et al.. (2011). Inhibition of Histone Demethylases by 4‐Carboxy‐2,2′‐Bipyridyl Compounds. ChemMedChem. 6(5). 759–764. 61 indexed citations
12.
Heightman, Tom D.. (2011). Therapeutic prospects for epigenetic modulation. Expert Opinion on Therapeutic Targets. 15(6). 729–740. 22 indexed citations
13.
Thalhammer, Armin, Jasmin Mecinović, Christoph Loenarz, et al.. (2010). Inhibition of the histone demethylase JMJD2E by 3-substituted pyridine 2,4-dicarboxylates. Organic & Biomolecular Chemistry. 9(1). 127–135. 48 indexed citations
14.
Kawamura, Akane, Anthony Tumber, Nathan R. Rose, et al.. (2010). Development of homogeneous luminescence assays for histone demethylase catalysis and binding. Analytical Biochemistry. 404(1). 86–93. 51 indexed citations
15.
Niesen, F., Lena Schultz, Ajit Jadhav, et al.. (2010). High-Affinity Inhibitors of Human NAD+-Dependent 15-Hydroxyprostaglandin Dehydrogenase: Mechanisms of Inhibition and Structure-Activity Relationships. PLoS ONE. 5(11). e13719–e13719. 29 indexed citations
16.
Healy, Shannon, Tom D. Heightman, Laura Hohmann, David C. Schriemer, & Roy A. Gravel. (2009). Nonenzymatic biotinylation of histone H2A. Protein Science. 18(2). 314–328. 24 indexed citations
17.
Heightman, Tom D., David F. Corbett, Gregor J. Macdonald, et al.. (2008). Identification of small molecule agonists of the motilin receptor. Bioorganic & Medicinal Chemistry Letters. 18(24). 6423–6428. 11 indexed citations
18.
Kerrigan, Nessan J., et al.. (2004). Development of a solid-phase ‘asymmetric resin-capture–release’ process: application of an ephedrine chiral resin in an approach to γ-butyrolactones. Organic & Biomolecular Chemistry. 2(17). 2476–2482. 34 indexed citations
19.
Watson, Jeannette M., C. Roberts, Claire M. Scott, et al.. (2001). SB‐272183, a selective 5‐HT1A, 5‐HT1B and 5‐HT1D receptor antagonist in native tissue. British Journal of Pharmacology. 133(6). 797–806. 15 indexed citations
20.
Hilge, M., Sergio M. Gloor, W. Rypniewski, et al.. (1998). High-resolution native and complex structures of thermostable β-mannanase from Thermomonospora fusca – substrate specificity in glycosyl hydrolase family 5. Structure. 6(11). 1433–1444. 149 indexed citations

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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