John J. Harding

7.3k total citations · 1 hit paper
140 papers, 5.5k citations indexed

About

John J. Harding is a scholar working on Molecular Biology, Clinical Biochemistry and Physiology. According to data from OpenAlex, John J. Harding has authored 140 papers receiving a total of 5.5k indexed citations (citations by other indexed papers that have themselves been cited), including 104 papers in Molecular Biology, 46 papers in Clinical Biochemistry and 45 papers in Physiology. Recurrent topics in John J. Harding's work include Connexins and lens biology (90 papers), Advanced Glycation End Products research (45 papers) and Biochemical effects in animals (44 papers). John J. Harding is often cited by papers focused on Connexins and lens biology (90 papers), Advanced Glycation End Products research (45 papers) and Biochemical effects in animals (44 papers). John J. Harding collaborates with scholars based in United Kingdom, United States and China. John J. Harding's co-authors include Keith J. Dilley, Elena Ganea, Ruth van Heyningen, Robert Blakytny, H T Beswick, Hong Yan, Barry K. Derham, Hong Yan, Oleg Mirochnitchenko and Anthony J. Bron and has published in prestigious journals such as The Lancet, JAMA and Journal of Biological Chemistry.

In The Last Decade

John J. Harding

138 papers receiving 5.3k 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.

Structural proteins of the mammalian lens: A review with emphasis on changes in development, aging and cataract

1976 421 citations John J. Harding et al. Experimental Eye Research profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
John J. Harding United Kingdom	42	3.6k	1.7k	1.6k	737	529	140	5.5k
Allen Taylor United States	51	4.9k 1.4×	1.6k 0.9×	1.1k 0.7×	1.0k 1.4×	1.6k 3.0×	178	8.0k
Takayuki Ozawa Japan	51	6.4k 1.8×	2.2k 1.3×	1.5k 0.9×	373 0.5×	155 0.3×	316	9.9k
Marjorie F. Lou United States	41	3.3k 0.9×	870 0.5×	939 0.6×	671 0.9×	356 0.7×	123	4.3k
Wolfgang Sperl Austria	50	4.1k 1.2×	2.3k 1.3×	892 0.6×	263 0.4×	72 0.1×	204	6.2k
Venkat N. Reddy United States	41	3.3k 0.9×	686 0.4×	907 0.6×	766 1.0×	833 1.6×	129	4.5k
Walter C. Hubbard United States	50	2.8k 0.8×	270 0.2×	2.3k 1.5×	244 0.3×	215 0.4×	132	7.3k
Ye-Shih Ho United States	36	2.5k 0.7×	375 0.2×	1.1k 0.7×	200 0.3×	157 0.3×	55	5.1k
Kenneth H. Gabbay United States	55	4.0k 1.1×	1.1k 0.6×	2.0k 1.3×	4.0k 5.4×	371 0.7×	116	11.0k
James M. Phang United States	53	4.9k 1.4×	468 0.3×	732 0.5×	565 0.8×	49 0.1×	138	8.4k
Nadja C. de Souza‐Pinto United States	45	5.9k 1.6×	776 0.5×	1.3k 0.8×	299 0.4×	55 0.1×	86	8.1k

Countries citing papers authored by John J. Harding

Since Specialization

Citations

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

Fields of papers citing papers by John J. Harding

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John J. Harding

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Harding, John J. & M. James C. Crabbe. (2024). Post-translational Modifications of Proteins. 1 indexed citations

Sangrigoli, Robert, et al.. (2023). Randomized prospective evaluation of same-day discharge after cryoballoon ablation of atrial fibrillation: results of the EASY PVI study. Journal of Interventional Cardiac Electrophysiology. 66(7). 1601–1607. 8 indexed citations

Su, Wilber, Robert Hoyt, James H. Baker, et al.. (2018). Retrospective review of Arctic Front Advance Cryoballoon Ablation: a multicenter examination of second-generation cryoballoon (RADICOOL trial). Journal of Interventional Cardiac Electrophysiology. 51(3). 199–204. 13 indexed citations

Harding, John J. & Muriel Egerton. (2015). Diabetes, Sex, and Cataract. Developments in ophthalmology. 26. 11–13.

Zhang, Jie, et al.. (2008). Identification of the Primary Targets of Carbamylation in Bovine Lens Proteins by Mass Spectrometry. Current Eye Research. 33(11-12). 963–976. 9 indexed citations

Ganea, Elena & John J. Harding. (2006). Glutathione-Related Enzymes and the Eye. Current Eye Research. 31(1). 1–11. 176 indexed citations

Harding, John J. & Elena Ganea. (2006). Protection against glycation and similar post-translational modifications of proteins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(9). 1436–1446. 31 indexed citations

Lou, Marjorie F., et al.. (2005). Glutathione Reductase from Human Cataract Lenses can be Revived by Reducing Agents and by a Molecular Chaperone, α -Crystallin. Current Eye Research. 30(10). 919–925. 8 indexed citations

Lou, Marjorie F., et al.. (2004). Revival of inactive glyceraldehyde 3-phosphate dehydrogenase in human cataract lenses by reduction. Experimental Eye Research. 79(1). 105–109. 7 indexed citations

10.

Yan, Hong & John J. Harding. (2004). Carnosine protects against the inactivation of esterase induced by glycation and a steroid. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1741(1-2). 120–126. 42 indexed citations

11.

Shyadehi, Akbar Z. & John J. Harding. (2002). Protective effects of ibuprofen and its major metabolites against in vitro inactivation of catalase and fumarase: relevance to cataract. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1587(1). 31–35. 5 indexed citations

12.

Harding, John J., et al.. (2002). The Effect of Modification of α-Crystallin by Prednisolone-21-Hemisuccinate and Fructose 6-Phosphate on Chaperone Activity. Developments in ophthalmology. 35. 150–160. 6 indexed citations

13.

Derham, Barry K., Martinus A.M. van Boekel, Paul J. Muchowski, et al.. (2001). Chaperone function of mutant versions of αA‐ and αB‐crystallin prepared to pinpoint chaperone binding sites. European Journal of Biochemistry. 268(3). 713–721. 55 indexed citations

14.

Blakytny, Robert, et al.. (1997). A spectroscopic study of glycated bovine α-crystallin: investigation of flexibility of the C-terminal extension, chaperone activity and evidence for diglycation. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1343(2). 299–315. 28 indexed citations

15.

Harding, John J., et al.. (1997). Inactivation of glyceraldehyde 3-phosphate dehydrogenase by sugars, prednisolone-21-hemisuccinate, cyanate and other small molecules. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1362(2-3). 232–242. 23 indexed citations

16.

Harding, John J., et al.. (1996). Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, α-crystallin. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1315(3). 176–184. 55 indexed citations

17.

Harding, John J., et al.. (1996). Molecular Masses of Gamma-Crystallins. Ophthalmic Research. 28(2). 131–135. 4 indexed citations

18.

Hsuan, James, John J. Harding, & Anthony J. Bron. (1996). The Penetration of Topical Cysteamine into the Human Eye. Journal of Ocular Pharmacology and Therapeutics. 12(4). 499–502. 5 indexed citations

19.

Riley, M. L. & John J. Harding. (1995). The reaction of methylglyoxal with human and bovine lens proteins. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1270(1). 36–43. 34 indexed citations

20.

Harding, John J., et al.. (1990). The effects of aminoguanidine on the glycation (non-enzymic glycosylation) of lens proteins. Experimental Eye Research. 50(5). 463–467. 57 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.

Explore authors with similar magnitude of impact