I. Burns

518 total citations
16 papers, 436 citations indexed

About

I. Burns is a scholar working on Molecular Biology, Organic Chemistry and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, I. Burns has authored 16 papers receiving a total of 436 indexed citations (citations by other indexed papers that have themselves been cited), including 5 papers in Molecular Biology, 4 papers in Organic Chemistry and 4 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in I. Burns's work include Boron Compounds in Chemistry (4 papers), Radiopharmaceutical Chemistry and Applications (3 papers) and Asymmetric Hydrogenation and Catalysis (3 papers). I. Burns is often cited by papers focused on Boron Compounds in Chemistry (4 papers), Radiopharmaceutical Chemistry and Applications (3 papers) and Asymmetric Hydrogenation and Catalysis (3 papers). I. Burns collaborates with scholars based in United Kingdom, Denmark and United States. I. Burns's co-authors include Anthony F. Hill, Trevor J. Greenhough, A.K. Shrive, Nathaniel W. Alcock, Andrew J. P. White, David J. Williams, James D. E. T. Wilton‐Ely, Uday Kishore, Peter Strong and P.J. Rizkallah and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

I. Burns

15 papers receiving 409 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
I. Burns United Kingdom 12 199 105 95 89 79 16 436
Raquel Bartolomé-Casado Spain 12 254 1.3× 94 0.9× 147 1.5× 290 3.3× 11 0.1× 18 775
Fang Yuan China 10 120 0.6× 37 0.4× 127 1.3× 48 0.5× 11 0.1× 21 443
Davide Carta Italy 14 195 1.0× 24 0.2× 200 2.1× 23 0.3× 44 0.6× 35 535
Ayoung Pyo South Korea 13 179 0.9× 36 0.3× 96 1.0× 28 0.3× 13 0.2× 26 417
Francesca Paganelli Italy 16 103 0.5× 80 0.8× 284 3.0× 52 0.6× 16 0.2× 33 630
Qingcui Wu China 9 105 0.5× 24 0.2× 300 3.2× 80 0.9× 24 0.3× 16 565
Jennifer L. Hess United States 10 48 0.2× 82 0.8× 89 0.9× 23 0.3× 16 0.2× 18 352
Michael Harris United States 10 179 0.9× 86 0.8× 91 1.0× 63 0.7× 14 0.2× 23 374
A.I. Guce United States 7 103 0.5× 57 0.5× 132 1.4× 124 1.4× 6 0.1× 8 394
Katrin Splith Germany 13 160 0.8× 21 0.2× 396 4.2× 78 0.9× 22 0.3× 29 746

Countries citing papers authored by I. Burns

Since Specialization
Citations

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

Fields of papers citing papers by I. Burns

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by I. Burns. 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 I. Burns. The network helps show where I. Burns may publish in the future.

Co-authorship network of co-authors of I. Burns

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

All Works

16 of 16 papers shown
1.
Moeller, Jesper B., I. Burns, Anders Schlosser, et al.. (2023). Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs. Journal of Biological Chemistry. 300(1). 105552–105552. 1 indexed citations
2.
Paterson, Janet M., et al.. (2019). Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine. Journal of Biological Chemistry. 294(45). 17155–17165. 3 indexed citations
3.
Clark, Howard, Rose‐Marie Mackay, Alastair Watson, et al.. (2018). Structural definition of hSP-D recognition of Salmonella enterica LPS inner core oligosaccharides reveals alternative binding modes for the same LPS. PLoS ONE. 13(6). e0199175–e0199175. 16 indexed citations
4.
Shrive, A.K., Jesper B. Moeller, I. Burns, et al.. (2013). Crystal Structure of the Tetrameric Fibrinogen-like Recognition Domain of Fibrinogen C Domain Containing 1 (FIBCD1) Protein. Journal of Biological Chemistry. 289(5). 2880–2887. 23 indexed citations
5.
Williams, Robert J. P., et al.. (2013). Structural studies of C-reactive protein. Acta Crystallographica Section A Foundations of Crystallography. 69(a1). s317–s317.
6.
Shrive, A.K., I. Burns, Hui‐Ting Chou, et al.. (2009). Crystal Structures of Limulus SAP-Like Pentraxin Reveal Two Molecular Aggregations. Journal of Molecular Biology. 386(5). 1240–1254. 18 indexed citations
7.
Shrive, A.K., I. Burns, Janet M. Paterson, et al.. (2009). Structural Characterisation of Ligand-Binding Determinants in Human Lung Surfactant Protein D: Influence of Asp325. Journal of Molecular Biology. 394(4). 776–788. 20 indexed citations
8.
MacCarthy, Eugene, I. Burns, Ilgiz Irnazarow, et al.. (2008). Serum CRP-like protein profile in common carp Cyprinus carpio challenged with Aeromonas hydrophila and Escherichia coli lipopolysaccharide. Developmental & Comparative Immunology. 32(11). 1281–1289. 33 indexed citations
9.
Shrive, A.K., Peter Strong, Uday Kishore, et al.. (2003). High-resolution Structural Insights into Ligand binding and Immune Cell Recognition by Human Lung Surfactant Protein D. Journal of Molecular Biology. 331(2). 509–523. 93 indexed citations
10.
Bownes, Mary, et al.. (2002). Drosophila yolk protein produced in E. coli is accumulated by mosquito ovaries. Insect Molecular Biology. 11(5). 487–496. 14 indexed citations
11.
Burns, I., et al.. (1999). Polyazolyl Chelate Chemistry. 7.1Reactivity of the Complexes [MCl(PPh3)2{HB(pz)3}] (M = Ru, Os; pz = Pyrazol-1-yl). Organometallics. 18(8). 1504–1516. 66 indexed citations
12.
Burns, I., Anthony F. Hill, Andrew J. P. White, David J. Williams, & James D. E. T. Wilton‐Ely. (1998). Polyazolyl Chelate Chemistry. 6.1Bidentate Coordination of HB(pz)3(pz = Pyrazol-1-yl) to Ruthenium and Osmium:  Crystal Structure of [RuH(CO)(PPh3)22-HB(pz)3}]. Organometallics. 17(8). 1552–1557. 29 indexed citations
13.
Burns, I., Anthony F. Hill, & David J. Williams. (1996). Ruthenatetraboranes:  Molecular Structure of [Ru(B3H8)(PPh3){κ3-HB(pz)3}] (pz = Pyrazol-1-yl). Inorganic Chemistry. 35(9). 2685–2687. 20 indexed citations
14.
Burns, I., et al.. (1992). Synthesis and reactivity of hydrido, halogeno, and σ-organyl ruthenatetraboranes: Crystal structure of [RuH(B3H8)(CO)(PPh3)2]. Journal of Organometallic Chemistry. 425(1-2). C8–C10. 11 indexed citations
15.
Alcock, Nathaniel W., et al.. (1992). Synthesis and reactivity of ruthenatetraboranes: molecular structure of [RuH(B3H8)(CO)(PPh3)2]. Inorganic Chemistry. 31(22). 4606–4610. 15 indexed citations
16.
Alcock, Nathaniel W., et al.. (1992). Ruthenatetraboranes: synthesis of [Ru(B3H8)(PPh3)}HB(pz)3}] and crystal structure of [RuCl(PPh3)2{HB(pz)3}] (pz = pyrazol-1-yl). Inorganic Chemistry. 31(13). 2906–2908. 74 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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