Judith Murray‐Rust

4.2k total citations
83 papers, 3.4k citations indexed

About

Judith Murray‐Rust is a scholar working on Molecular Biology, Organic Chemistry and Materials Chemistry. According to data from OpenAlex, Judith Murray‐Rust has authored 83 papers receiving a total of 3.4k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Molecular Biology, 28 papers in Organic Chemistry and 13 papers in Materials Chemistry. Recurrent topics in Judith Murray‐Rust's work include Nerve injury and regeneration (7 papers), Protein Kinase Regulation and GTPase Signaling (7 papers) and Magnetism in coordination complexes (6 papers). Judith Murray‐Rust is often cited by papers focused on Nerve injury and regeneration (7 papers), Protein Kinase Regulation and GTPase Signaling (7 papers) and Magnetism in coordination complexes (6 papers). Judith Murray‐Rust collaborates with scholars based in United Kingdom, United States and Sweden. Judith Murray‐Rust's co-authors include Neil Q. McDonald, Peter J. Parker, Carlos F. Ibáñez, Patrick Vallance, James Leiper, Tom L. Blundell, Peter Murray‐Rust, Håkan Persson, Phillip P. Knowles and Gisela Barbany and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Judith Murray‐Rust

81 papers receiving 3.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Judith Murray‐Rust United Kingdom 29 1.7k 693 624 375 330 83 3.4k
Kiichiro Nakajima Japan 32 2.4k 1.4× 880 1.3× 1.1k 1.8× 366 1.0× 589 1.8× 92 4.3k
David B. Glass United States 29 2.6k 1.5× 405 0.6× 418 0.7× 265 0.7× 307 0.9× 46 3.4k
Hervé Coste France 16 3.5k 2.0× 494 0.7× 550 0.9× 465 1.2× 303 0.9× 17 4.8k
J Lacapère France 31 3.1k 1.8× 963 1.4× 512 0.8× 540 1.4× 247 0.7× 117 5.0k
Andrew P. Thomas United Kingdom 37 3.4k 2.0× 657 0.9× 407 0.7× 818 2.2× 311 0.9× 82 5.2k
ISAMI TAKAHASHI Japan 19 3.2k 1.8× 471 0.7× 361 0.6× 605 1.6× 194 0.6× 29 4.6k
T R Hesketh United Kingdom 36 3.1k 1.8× 895 1.3× 665 1.1× 228 0.6× 219 0.7× 66 4.6k
Jacques Pouysségur France 27 3.6k 2.1× 297 0.4× 501 0.8× 411 1.1× 167 0.5× 31 5.5k
Yuliang Ma United States 36 3.8k 2.2× 679 1.0× 711 1.1× 467 1.2× 322 1.0× 58 5.3k
Wolfgang R. Dostmann United States 29 2.6k 1.5× 451 0.7× 816 1.3× 169 0.5× 634 1.9× 58 3.5k

Countries citing papers authored by Judith Murray‐Rust

Since Specialization
Citations

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

Fields of papers citing papers by Judith Murray‐Rust

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Judith Murray‐Rust. 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 Judith Murray‐Rust. The network helps show where Judith Murray‐Rust may publish in the future.

Co-authorship network of co-authors of Judith Murray‐Rust

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

All Works

20 of 20 papers shown
1.
Plaza-Menacho, Iván, Karin Barnouin, K.M. Goodman, et al.. (2014). Oncogenic RET Kinase Domain Mutations Perturb the Autophosphorylation Trajectory by Enhancing Substrate Presentation In trans. Molecular Cell. 53(5). 738–751. 57 indexed citations
2.
Boëda, Batiste, Phillip P. Knowles, David C. Briggs, et al.. (2011). Molecular Recognition of the Tes LIM2–3 Domains by the Actin-related Protein Arp7A. Journal of Biological Chemistry. 286(13). 11543–11554. 35 indexed citations
3.
Mologni, Luca, Roberta Rostagno, Phillip P. Knowles, et al.. (2010). Synthesis, structure–activity relationship and crystallographic studies of 3-substituted indolin-2-one RET inhibitors. Bioorganic & Medicinal Chemistry. 18(4). 1482–1496. 63 indexed citations
4.
Leiper, James, Manasi Nandi, Belén Torondel, et al.. (2007). Disruption of methylarginine metabolism impairs vascular homeostasis. Nature Medicine. 13(2). 198–203. 320 indexed citations
5.
Newman, Matthew, Judith Murray‐Rust, John Lally, et al.. (2005). Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition. The EMBO Journal. 24(5). 895–905. 87 indexed citations
6.
7.
Movahedzadeh, Farahnaz, Debbie A. Smith, Richard A. Norman, et al.. (2003). The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence. Molecular Microbiology. 51(4). 1003–1014. 75 indexed citations
8.
Norman, Richard A., M. McAlister, Judith Murray‐Rust, et al.. (2002). Crystal Structure of Inositol 1-Phosphate Synthase from Mycobacterium tuberculosis, a Key Enzyme in Phosphatidylinositol Synthesis. Structure. 10(3). 393–402. 51 indexed citations
9.
Bourne, Philip E., Judith Murray‐Rust, & Jeremy H. Lakey. (2001). Protein–nucleic acid interactions. Current Opinion in Structural Biology. 11(1). 9–10. 1 indexed citations
10.
Foehr, Erik D., Simona Raffioni, Judith Murray‐Rust, & Ralph Bradshaw. (2001). The Role of Tyrosine Residues in Fibroblast Growth Factor Receptor 1 Signaling in PC12 Cells. Journal of Biological Chemistry. 276(40). 37529–37536. 18 indexed citations
11.
Murray‐Rust, Judith, et al.. (1998). Crystal structure of the C2 domain from protein kinase C-δ. Structure. 6(7). 885–894. 103 indexed citations
12.
Murray‐Rust, Judith, et al.. (1998). Catalysis and regulation Proteins Web alert. Current Opinion in Structural Biology. 8(6). 673–674. 1 indexed citations
13.
Murray‐Rust, Judith, et al.. (1998). Protein—nucleic acid interactions Folding and binding Web alert. Current Opinion in Structural Biology. 8(1). 9–10. 1 indexed citations
14.
Murray‐Rust, Judith, et al.. (1995). The first structure of a receptor tyrosine kinase domain:a further step in understanding the molecular basis of insulin action. Structure. 3(1). 1–6. 18 indexed citations
15.
Murray‐Rust, Judith, et al.. (1994). Nerve growth factor: Structure/function relationships. Protein Science. 3(11). 1901–1913. 54 indexed citations
16.
Bradshaw, Ralph, Tom L. Blundell, Risto Lapatto, Neil Q. McDonald, & Judith Murray‐Rust. (1993). Nerve growth factor revisited. Trends in Biochemical Sciences. 18(2). 48–52. 78 indexed citations
17.
18.
Murray‐Rust, Judith, Tom L. Blundell, Markus Hosang, et al.. (1993). Topological similarities in TGF-β2, PDGF-BB and NGF define a superfamily of polypeptide growth factors. Structure. 1(2). 153–159. 114 indexed citations
19.
Murray‐Rust, Judith, et al.. (1992). Structure and evolution of insulins: Implications for receptor binding. BioEssays. 14(5). 325–331. 60 indexed citations
20.
Ibáñez, Carlos F., Ted Ebendal, Gisela Barbany, et al.. (1992). Disruption of the low affinity receptor-binding site in NGF allows neuronal survival and differentiation by binding to the trk gene product. Cell. 69(2). 329–341. 293 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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