Ninian J. Blackburn

7.0k total citations
141 papers, 5.7k citations indexed

About

Ninian J. Blackburn is a scholar working on Inorganic Chemistry, Molecular Biology and Oncology. According to data from OpenAlex, Ninian J. Blackburn has authored 141 papers receiving a total of 5.7k indexed citations (citations by other indexed papers that have themselves been cited), including 72 papers in Inorganic Chemistry, 62 papers in Molecular Biology and 52 papers in Oncology. Recurrent topics in Ninian J. Blackburn's work include Metal-Catalyzed Oxygenation Mechanisms (68 papers), Metal complexes synthesis and properties (46 papers) and Trace Elements in Health (37 papers). Ninian J. Blackburn is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (68 papers), Metal complexes synthesis and properties (46 papers) and Trace Elements in Health (37 papers). Ninian J. Blackburn collaborates with scholars based in United States, United Kingdom and Finland. Ninian J. Blackburn's co-authors include Martina Ralle, Kenneth D. Karlin, Richard W. Strange, Megan M. McEvoy, Gnana S. Siluvai, Svetlana Lutsenko, Judith P. Klinman, Shulamit Jaron, Peter F. Knowles and Yi Lu 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

Ninian J. Blackburn

140 papers receiving 5.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Ninian J. Blackburn United States	47	2.4k	2.1k	1.8k	1.4k	1.2k	141	5.7k
Anthony G. Wedd Australia	45	2.3k 1.0×	1.1k 0.5×	1.5k 0.9×	1.3k 0.9×	2.4k 2.0×	181	6.8k
James A. Fee United States	44	2.1k 0.9×	3.0k 1.4×	606 0.3×	381 0.3×	797 0.6×	125	5.5k
James W. Whittaker United States	42	2.8k 1.2×	2.1k 1.0×	1.2k 0.7×	248 0.2×	819 0.7×	91	5.8k
Katherine J. Franz United States	41	775 0.3×	1.5k 0.7×	1.3k 0.8×	1.1k 0.8×	1.5k 1.2×	103	5.6k
Richard W. Strange United Kingdom	40	1.1k 0.5×	2.0k 1.0×	532 0.3×	517 0.4×	1.1k 0.9×	115	4.6k
Timothy E. Machonkin United States	15	1.4k 0.6×	890 0.4×	921 0.5×	376 0.3×	722 0.6×	22	3.8k
Zhiguang Xiao Australia	33	483 0.2×	828 0.4×	869 0.5×	1.2k 0.9×	575 0.5×	98	3.3k
Michael P. Hendrich United States	47	4.2k 1.8×	1.9k 0.9×	1.8k 1.0×	182 0.1×	2.7k 2.2×	147	7.2k
Wojciech Bal Poland	49	502 0.2×	3.8k 1.8×	2.3k 1.3×	2.2k 1.6×	995 0.8×	207	8.1k
Dean E. Wilcox United States	33	546 0.2×	1.3k 0.6×	888 0.5×	582 0.4×	584 0.5×	80	3.7k

Countries citing papers authored by Ninian J. Blackburn

Since Specialization

Citations

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

Fields of papers citing papers by Ninian J. Blackburn

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ninian J. Blackburn

This figure shows the co-authorship network connecting the top 25 collaborators of Ninian J. Blackburn. A scholar is included among the top collaborators of Ninian J. Blackburn 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 Ninian J. Blackburn. Ninian J. Blackburn 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

Bandarian, Vahe, et al.. (2025). The binuclear copper state of peptidylglycine monooxygenase visualized through a selenium-substituted peptidyl-homocysteine complex. Dalton Transactions. 54(12). 4941–4955. 1 indexed citations

Leone, Philippe, Ninian J. Blackburn, Sam Horrell, et al.. (2024). Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features. Dalton Transactions. 53(4). 1794–1808. 3 indexed citations

Bandarian, Vahe, et al.. (2024). Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure. Journal of the American Chemical Society. 146(8). 5074–5080. 9 indexed citations

Kincannon, William M., et al.. (2023). Peptide Selenocysteine Substitutions Reveal Direct Substrate–Enzyme Interactions at Auxiliary Clusters in Radical S-Adenosyl-l-methionine Maturases. Journal of the American Chemical Society. 145(18). 10167–10177. 7 indexed citations

Grasso, Michael, Ye‐Jin Kim, Stefanie D. Boyd, et al.. (2021). The copper chaperone CCS facilitates copper binding to MEK1/2 to promote kinase activation. Journal of Biological Chemistry. 297(6). 101314–101314. 60 indexed citations

Blackburn, Ninian J., et al.. (2016). Substrate-Induced Carbon Monoxide Reactivity Suggests Multiple Enzyme Conformations at the Catalytic Copper M-Center of Peptidylglycine Monooxygenase. Biochemistry. 55(48). 6652–6661. 15 indexed citations

Barry, Amanda N., et al.. (2011). The Lumenal Loop Met672–Pro707 of Copper-transporting ATPase ATP7A Binds Metals and Facilitates Copper Release from the Intramembrane Sites. Journal of Biological Chemistry. 286(30). 26585–26594. 33 indexed citations

Blackburn, Ninian J.. (2010). A Tale of Two Metals. Chemistry & Biology. 17(1). 8–9. 4 indexed citations

Andruzzi, Luisa, Michiko Nakano, Mark J. Nilges, & Ninian J. Blackburn. (2005). Spectroscopic Studies of Metal Binding and Metal Selectivity in Bacillus subtilis BSco, a Homologue of the Yeast Mitochondrial Protein Sco1p. Journal of the American Chemical Society. 127(47). 16548–16558. 50 indexed citations

10.

Bauman, Andrew T., et al.. (2005). The Hydrogen Peroxide Reactivity of Peptidylglycine Monooxygenase Supports a Cu(II)-Superoxo Catalytic Intermediate. Journal of Biological Chemistry. 281(7). 4190–4198. 50 indexed citations

11.

Ralle, Martina, Marina Verkhovskaya, Joel E. Morgan, et al.. (1999). Coordination of Cu_B in Reduced and CO-Liganded States of Cytochrome bo₃ from Escherichia coli. Is Chloride Ion a Cofactor?. Biochemistry. 38(22). 7185–7194. 42 indexed citations

12.

Obias, Honorio V., Gino P. F. van Strijdonck, Dong-Heon Lee, et al.. (1998). Heterobinucleating Ligand-Induced Structural and Chemical Variations in [(L)Fe^III−O−Cu^II]⁺ μ-Oxo Complexes. Journal of the American Chemical Society. 120(37). 9696–9697. 38 indexed citations

13.

Reedy, Brian & Ninian J. Blackburn. (1994). Preparation and Characterization of Half-Apo Dopamine-.beta.-hydroxylase by Selective Removal of CuA. Identification of a Sulfur Ligand at the Dioxygen Binding Site by EXAFS and FTIR Spectroscopy. Journal of the American Chemical Society. 116(5). 1924–1931. 70 indexed citations

14.

Blackburn, Ninian J., Richard W. Strange, Robert T. Carr, & Stephen J. Benkovic. (1992). X-ray absorption studies of the copper-dependent phenylalanine hydroxylase from Chromobacterium violaceum. Comparison of the copper coordination in oxidized and dithionite-reduced enzymes. Biochemistry. 31(23). 5298–5303. 18 indexed citations

15.

Mahroof‐Tahir, Mohammad, et al.. (1992). New thermally stable hydroperoxo- and peroxo-copper complexes. Inorganic Chemistry. 31(14). 3001–3003. 53 indexed citations

16.

Blackburn, Ninian J., Richard W. Strange, J. Reedijk, et al.. (1989). X-ray absorption edge spectroscopy of copper(I) complexes. Coordination geometry of copper(I) in the reduced forms of copper proteins and their derivatives with carbon monoxide. Inorganic Chemistry. 28(7). 1349–1357. 63 indexed citations

17.

Karlin, Kenneth D., Phalguni Ghosh, Richard W. Cruse, et al.. (1988). Dioxygen-copper reactivity: generation, characterization, and reactivity of a hydroperoxodicopper(II) complex. Journal of the American Chemical Society. 110(20). 6769–6780. 105 indexed citations

18.

Blackburn, Ninian J., S.S. Hasnain, Norman Binsted, et al.. (1984). An extended-X-ray-absorption-fine-structure study of bovine erythrocyte superoxide dismutase in aqueous solution. Direct evidence for three-co-ordinate Cu(I) in reduced enzyme. Biochemical Journal. 219(3). 985–990. 80 indexed citations

19.

Hasnain, S.S., G. P. Diakun, Peter F. Knowles, et al.. (1984). Direct structural information for the copper site of dopamine β-mono-oxygenase obtained by using extended X-ray-absorption fine structure. Biochemical Journal. 221(2). 545–548. 27 indexed citations

20.

Blackburn, Ninian J., S.S. Hasnain, G. P. Diakun, et al.. (1983). An extended X-ray-absorption-fine-structure study of the copper and zinc sites of freeze-dried bovine superoxide dismutase. Biochemical Journal. 213(3). 765–768. 25 indexed citations

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