John D. Harling

6.6k total citations · 2 hit papers
51 papers, 4.1k citations indexed

About

John D. Harling is a scholar working on Molecular Biology, Organic Chemistry and Oncology. According to data from OpenAlex, John D. Harling has authored 51 papers receiving a total of 4.1k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 18 papers in Organic Chemistry and 10 papers in Oncology. Recurrent topics in John D. Harling's work include Protein Degradation and Inhibitors (16 papers), Ubiquitin and proteasome pathways (15 papers) and Multiple Myeloma Research and Treatments (8 papers). John D. Harling is often cited by papers focused on Protein Degradation and Inhibitors (16 papers), Ubiquitin and proteasome pathways (15 papers) and Multiple Myeloma Research and Treatments (8 papers). John D. Harling collaborates with scholars based in United Kingdom, United States and Ireland. John D. Harling's co-authors include Nicholas J. Laping, James F. Callahan, Laramie M. Gaster, Francisco José Nicolás, Alastair D. Reith, Gareth J. Inman, Caroline S. Hill, Eugene T. Grygielko, W. Martin and Christopher Tweed and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

John D. Harling

51 papers receiving 4.0k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

SB-431542 Is a Potent and Specific Inhibitor of Transforming Growth Factor-β Superfamily Type I Activin Receptor-Like Kinase (ALK) Receptors ALK4, ALK5, and ALK7

2002 1.4k citations Gareth J. Inman, Francisco José Nicolás et al. Molecular Pharmacology profile →
Inhibition of Transforming Growth Factor (TGF)-β1–Induced Extracellular Matrix with a Novel Inhibitor of the TGF-β Type I Receptor Kinase Activity: SB-431542

2002 544 citations Nicholas J. Laping, Eugene T. Grygielko et al. Molecular Pharmacology profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
John D. Harling United Kingdom	25	2.9k	903	621	304	266	51	4.1k
Adam P. Silverman United States	21	2.3k 0.8×	1.4k 1.5×	206 0.3×	71 0.2×	121 0.5×	36	3.2k
Jun‐ichi Yamaguchi Japan	19	2.0k 0.7×	471 0.5×	169 0.3×	114 0.4×	764 2.9×	66	3.3k
Dalia Baršytė-Lovejoy Canada	32	4.5k 1.5×	729 0.8×	138 0.2×	510 1.7×	118 0.4×	71	5.1k
Lei Huang China	29	2.6k 0.9×	847 0.9×	150 0.2×	117 0.4×	168 0.6×	84	3.7k
Helga Raab United States	22	1.8k 0.6×	1.7k 1.9×	231 0.4×	97 0.3×	115 0.4×	26	3.8k
Masanobu Komatsu United States	28	1.7k 0.6×	752 0.8×	158 0.3×	69 0.2×	264 1.0×	66	2.9k
Michael A. Erb United States	24	2.5k 0.9×	555 0.6×	111 0.2×	320 1.1×	86 0.3×	49	2.9k
Sonia Franco United States	30	3.0k 1.0×	1.0k 1.2×	138 0.2×	87 0.3×	225 0.8×	59	4.7k
Catrin Pritchard United Kingdom	36	3.9k 1.3×	1.9k 2.1×	195 0.3×	182 0.6×	305 1.1×	88	5.9k
Patrizio Castagnola Italy	27	1.3k 0.5×	404 0.4×	200 0.3×	71 0.2×	221 0.8×	96	3.0k

Countries citing papers authored by John D. Harling

Since Specialization

Citations

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

Fields of papers citing papers by John D. Harling

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John D. Harling

This figure shows the co-authorship network connecting the top 25 collaborators of John D. Harling. A scholar is included among the top collaborators of John D. Harling 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 John D. Harling. John D. Harling is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Vita, Elena De, Daniel Conole, Xinyue Zhang, et al.. (2024). Structure-Guided Design and Optimization of Covalent VHL-Targeted Sulfonyl Fluoride PROTACs. Journal of Medicinal Chemistry. 67(6). 4641–4654. 21 indexed citations

Stevens, Rebecca, Jenni Cryan, Peter Stacey, et al.. (2024). Expanding the reaction toolbox for nanoscale direct-to-biology PROTAC synthesis and biological evaluation. RSC Medicinal Chemistry. 16(3). 1141–1150. 8 indexed citations

Harling, John D. & Christopher P. Tinworth. (2023). A two-faced selectivity solution to target SMARCA2 for cancer therapy. Nature Communications. 14(1). 515–515. 6 indexed citations

Stevens, Rebecca, Afjal H. Miah, Robert P. Law, et al.. (2023). Integrated Direct-to-Biology Platform for the Nanoscale Synthesis and Biological Evaluation of PROTACs. Journal of Medicinal Chemistry. 66(22). 15437–15452. 26 indexed citations

Kounde, Cyrille S., Milon Mondal, Jake L. Greenfield, et al.. (2022). Light-mediated multi-target protein degradation using arylazopyrazole photoswitchable PROTACs (AP-PROTACs). Chemical Communications. 58(78). 10933–10936. 35 indexed citations

Stacey, Peter, Xiao Qing Lewell, Agnieszka Konopacka, et al.. (2021). A Phenotypic Approach for the Identification of New Molecules for Targeted Protein Degradation Applications. SLAS DISCOVERY. 26(7). 885–895. 5 indexed citations

Law, Robert P., João Nunes, Chun‐wa Chung, et al.. (2021). Discovery and Characterisation of Highly Cooperative FAK‐Degrading PROTACs. Angewandte Chemie International Edition. 60(43). 23327–23334. 85 indexed citations

Law, Robert P., João Nunes, Chun‐wa Chung, et al.. (2021). Discovery and Characterisation of Highly Cooperative FAK‐Degrading PROTACs. Angewandte Chemie. 133(43). 23515–23522. 4 indexed citations

Miah, Afjal H., Ian E. Smith, M.D. Rackham, et al.. (2021). Optimization of a Series of RIPK2 PROTACs. Journal of Medicinal Chemistry. 64(17). 12978–13003. 49 indexed citations

10.

Kounde, Cyrille S., Maria M. Shchepinova, Marcel Muelbaier, et al.. (2020). A caged E3 ligase ligand for PROTAC-mediated protein degradation with light. Chemical Communications. 56(41). 5532–5535. 107 indexed citations

11.

Chung, Chun‐wa, Han Dai, Esther Fernández, et al.. (2020). Structural Insights into PROTAC-Mediated Degradation of Bcl-xL. ACS Chemical Biology. 15(9). 2316–2323. 67 indexed citations

12.

Tinworth, Christopher P., Zuni I. Bassi, Marcel Muelbaier, et al.. (2019). PROTAC-Mediated Degradation of Bruton’s Tyrosine Kinase Is Inhibited by Covalent Binding. ACS Chemical Biology. 14(3). 342–347. 134 indexed citations

13.

Nunes, João Soares, Xiao Qing Lewell, John G. Emery, et al.. (2019). Targeting IRAK4 for Degradation with PROTACs. ACS Medicinal Chemistry Letters. 10(7). 1081–1085. 100 indexed citations

14.

Ngala, Robert A., Claire J. Stocker, Anirban Roy, et al.. (2011). A new, highly selective murine peroxisome proliferator‐activated receptor δ agonist increases responsiveness to thermogenic stimuli and glucose uptake in skeletal muscle in obese mice. Diabetes Obesity and Metabolism. 13(5). 455–464. 23 indexed citations

15.

Guo, Jun, John D. Harling, Patrick G. Steel, & Tom M. Woods. (2008). Phosphinates as new electrophilic partners for cross-coupling reactions. Organic & Biomolecular Chemistry. 6(21). 4053–4053. 13 indexed citations

16.

Bamford, Mark J., Nicholas Bailey, Susannah Davies, et al.. (2005). (1H-Imidazo[4,5-c]pyridin-2-yl)-1,2,5-oxadiazol-3-ylamine derivatives: A novel class of potent MSK-1-inhibitors. Bioorganic & Medicinal Chemistry Letters. 15(14). 3402–3406. 30 indexed citations

17.

Grygielko, Eugene T., W. Martin, Christopher Tweed, et al.. (2005). Inhibition of Gene Markers of Fibrosis with a Novel Inhibitor of Transforming Growth Factor-β Type I Receptor Kinase in Puromycin-Induced Nephritis. Journal of Pharmacology and Experimental Therapeutics. 313(3). 943–951. 153 indexed citations

18.

Donohoe, Timothy J., et al.. (2004). An Efficient Synthesis of Lactacystin β‐Lactone. Angewandte Chemie International Edition. 43(17). 2293–2296. 50 indexed citations

19.

Austin, Nigel, Michael S. Hadley, John D. Harling, et al.. (2003). The design of 8,8-Dimethyl[1,6]naphthyridines as potential anticonvulsant agents. Bioorganic & Medicinal Chemistry Letters. 13(10). 1627–1629. 22 indexed citations

20.

Inman, Gareth J., Francisco José Nicolás, James F. Callahan, et al.. (2002). SB-431542 Is a Potent and Specific Inhibitor of Transforming Growth Factor-β Superfamily Type I Activin Receptor-Like Kinase (ALK) Receptors ALK4, ALK5, and ALK7. Molecular Pharmacology. 62(1). 65–74. 1406 indexed citations breakdown →

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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