Jonathan A. King

1.4k total citations
28 papers, 1.1k citations indexed

About

Jonathan A. King is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, Jonathan A. King has authored 28 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 10 papers in Materials Chemistry and 9 papers in Physiology. Recurrent topics in Jonathan A. King's work include Connexins and lens biology (17 papers), Heat shock proteins research (12 papers) and Protein Structure and Dynamics (10 papers). Jonathan A. King is often cited by papers focused on Connexins and lens biology (17 papers), Heat shock proteins research (12 papers) and Protein Structure and Dynamics (10 papers). Jonathan A. King collaborates with scholars based in United States, Mexico and China. Jonathan A. King's co-authors include Eugene Serebryany, Ruhong Zhou, Payel Das, Kelly M. Knee, Oksana A. Sergeeva, Cameron Haase‐Pettingell, Liliana Quintanar, Corie Y. Ralston, Daniel R. Goulet and Paul D. Adams and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Jonathan A. King

28 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jonathan A. King United States	17	924	226	183	177	148	28	1.1k
Takumi Takata Japan	17	679 0.7×	185 0.8×	158 0.9×	154 0.9×	80 0.5×	37	829
Jaya Bhattacharyya United States	15	552 0.6×	121 0.5×	77 0.4×	80 0.5×	56 0.4×	23	721
Bryan M. Dunyak United States	11	616 0.7×	114 0.5×	30 0.2×	50 0.3×	44 0.3×	13	767
Daxin Tang United States	14	526 0.6×	125 0.6×	122 0.7×	17 0.1×	32 0.2×	16	690
Juan Pablo F.C. Rossi Argentina	19	711 0.8×	144 0.6×	67 0.4×	31 0.2×	88 0.6×	77	1.0k
Taleh Yusifov United States	21	468 0.5×	87 0.4×	32 0.2×	44 0.2×	27 0.2×	38	969
Tomoaki Uchiki United States	10	399 0.4×	66 0.3×	79 0.4×	36 0.2×	46 0.3×	11	596
Elizabeth Blachly‐Dyson United States	21	2.2k 2.4×	122 0.5×	432 2.4×	25 0.1×	72 0.5×	24	2.4k
Rosemary A. Staniforth United Kingdom	17	907 1.0×	325 1.4×	46 0.3×	450 2.5×	39 0.3×	26	1.2k
Barry K. Derham United Kingdom	11	400 0.4×	66 0.3×	59 0.3×	50 0.3×	28 0.2×	11	504

Countries citing papers authored by Jonathan A. King

Since Specialization

Citations

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

Fields of papers citing papers by Jonathan A. King

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jonathan A. King. 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 Jonathan A. King. The network helps show where Jonathan A. King may publish in the future.

Co-authorship network of co-authors of Jonathan A. King

This figure shows the co-authorship network connecting the top 25 collaborators of Jonathan A. King. A scholar is included among the top collaborators of Jonathan A. King 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 Jonathan A. King. Jonathan A. King 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

Serebryany, Eugene, et al.. (2023). Copper Reductase Activity and Free Radical Chemistry by Cataract-Associated Human Lens γ-Crystallins. Journal of the American Chemical Society. 145(12). 6781–6797. 13 indexed citations

Kosinski‐Collins, Melissa S., et al.. (2019). Kinetic Stability of Long-Lived Human γ-D and γS Lens Crystallins, Derived in Part from their Domain Interfaces, May Protect against Cataract. Biophysical Journal. 116(3). 321a–322a. 1 indexed citations

Sergeeva, Oksana A., Cameron Haase‐Pettingell, & Jonathan A. King. (2019). Co-expression of CCT subunits hints at TRiC assembly. Cell Stress and Chaperones. 24(6). 1055–1065. 12 indexed citations

Serebryany, Eugene, et al.. (2018). Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease. JBIC Journal of Biological Inorganic Chemistry. 23(7). 1105–1118. 25 indexed citations

Pereira, J.H., R.P. McAndrew, Oksana A. Sergeeva, et al.. (2017). Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy. Scientific Reports. 7(1). 3673–3673. 26 indexed citations

Serebryany, Eugene, Jaie Woodard, Bharat V. Adkar, et al.. (2017). An Internal Disulfide Locks a Misfolded Aggregation-Prone Intermediate in Cataract-Linked Mutants of Human Gamma-D Crystallin. Biophysical Journal. 112(3). 167a–168a. 1 indexed citations

Serebryany, Eugene, Jaie Woodard, Bharat V. Adkar, et al.. (2016). An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin. Journal of Biological Chemistry. 291(36). 19172–19183. 52 indexed citations

Serebryany, Eugene & Jonathan A. King. (2015). Wild-type Human γD-crystallin Promotes Aggregation of Its Oxidation-mimicking, Misfolding-prone W42Q Mutant. Journal of Biological Chemistry. 290(18). 11491–11503. 29 indexed citations

Sergeeva, Oksana A., et al.. (2014). Biochemical Characterization of Mutants in Chaperonin Proteins CCT4 and CCT5 Associated with Hereditary Sensory Neuropathy. Journal of Biological Chemistry. 289(40). 27470–27480. 24 indexed citations

10.

Serebryany, Eugene & Jonathan A. King. (2014). The βγ-crystallins: Native state stability and pathways to aggregation. Progress in Biophysics and Molecular Biology. 115(1). 32–41. 85 indexed citations

11.

Xia, Zhen, Zaixing Yang, Toan Huynh, Jonathan A. King, & Ruhong Zhou. (2013). UV-radiation Induced Disruption of Dry-Cavities in Human γD-crystallin Results in Decreased Stability and Faster Unfolding. Scientific Reports. 3(1). 1560–1560. 38 indexed citations

12.

Yang, Zaixing, Zhen Xia, Toan Huynh, Jonathan A. King, & Ruhong Zhou. (2013). Dissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins. Nanoscale. 6(3). 1797–1807. 11 indexed citations

13.

King, Jonathan A., et al.. (2012). Protein misfolding and aggregation in cataract disease and prospects for prevention. Trends in Molecular Medicine. 18(5). 273–282. 330 indexed citations

14.

Pereira, J.H., Corie Y. Ralston, Nicholai R. Douglas, et al.. (2012). Mechanism of nucleotide sensing in group II chaperonins. The EMBO Journal. 31(19). 3949–3950. 2 indexed citations

15.

Pereira, J.H., Corie Y. Ralston, Nicholai R. Douglas, et al.. (2011). Mechanism of nucleotide sensing in group II chaperonins. The EMBO Journal. 31(3). 731–740. 31 indexed citations

16.

Goulet, Daniel R., Kelly M. Knee, & Jonathan A. King. (2011). Inhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate. Experimental Eye Research. 93(4). 371–381. 18 indexed citations

17.

Pereira, J.H., Corie Y. Ralston, Nicholai R. Douglas, et al.. (2010). Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle. Journal of Biological Chemistry. 285(36). 27958–27966. 58 indexed citations

18.

Knee, Kelly M., Daniel R. Goulet, Junjie Zhang, et al.. (2010). The group II chaperonin Mm‐Cpn binds and refolds human γD crystallin. Protein Science. 20(1). 30–41. 11 indexed citations

19.

Chen, Chau‐Chyun, et al.. (1992). Molecular thermodynamic model to predict the .alpha.-helical secondary structure of polypeptide chains in solution. Biochemistry. 31(43). 10591–10601. 8 indexed citations

20.

Chen, Chau‐Chyun, et al.. (1992). A molecular thermodynamic approach to predict the secondary structure of homopolypeptides in aqueous systems. Biopolymers. 32(10). 1375–1392. 22 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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