Ruby H. P. Law

5.3k total citations · 1 hit paper
89 papers, 3.9k citations indexed

About

Ruby H. P. Law is a scholar working on Molecular Biology, Cancer Research and Immunology. According to data from OpenAlex, Ruby H. P. Law has authored 89 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 20 papers in Cancer Research and 18 papers in Immunology. Recurrent topics in Ruby H. P. Law's work include Protease and Inhibitor Mechanisms (20 papers), Mitochondrial Function and Pathology (12 papers) and ATP Synthase and ATPases Research (11 papers). Ruby H. P. Law is often cited by papers focused on Protease and Inhibitor Mechanisms (20 papers), Mitochondrial Function and Pathology (12 papers) and ATP Synthase and ATPases Research (11 papers). Ruby H. P. Law collaborates with scholars based in Australia, United States and United Kingdom. Ruby H. P. Law's co-authors include James C. Whisstock, Ashley M. Buckle, Phillip I. Bird, Robert N. Pike, Carlos J. Rosado, Ilia Voskoboinik, Christopher G. Langendorf, Joseph A. Trapani, Qingwei Zhang and Michelle A. Dunstone and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Ruby H. P. Law

85 papers receiving 3.8k citations

Hit Papers

An overview of the serpin superfamily. 2006 2026 2012 2019 2006 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ruby H. P. Law Australia 32 1.7k 747 495 483 356 89 3.9k
Stefan Krebs Germany 33 2.6k 1.5× 693 0.9× 402 0.8× 220 0.5× 296 0.8× 134 4.5k
Pablo Fuentes‐Prior Spain 37 2.5k 1.5× 1.1k 1.5× 420 0.8× 780 1.6× 296 0.8× 77 5.0k
Edward R. LaVallie United States 32 3.0k 1.7× 611 0.8× 459 0.9× 505 1.0× 121 0.3× 54 5.3k
Timothy Cardozo United States 33 2.9k 1.7× 714 1.0× 292 0.6× 179 0.4× 267 0.8× 96 4.6k
Youichi Suzuki Japan 25 2.4k 1.4× 1.2k 1.6× 441 0.9× 380 0.8× 338 0.9× 78 5.9k
Kate J. Heesom United Kingdom 39 2.9k 1.7× 415 0.6× 422 0.9× 195 0.4× 201 0.6× 156 5.4k
Tatsuya Abé Japan 34 2.1k 1.2× 589 0.8× 423 0.9× 129 0.3× 127 0.4× 181 4.5k
Michelle A. Dunstone Australia 32 1.2k 0.7× 1.5k 2.0× 107 0.2× 380 0.8× 460 1.3× 51 3.2k
Tatsuya Sawasaki Japan 43 4.1k 2.4× 909 1.2× 196 0.4× 131 0.3× 350 1.0× 209 6.2k
Stephen Bottomley Australia 42 3.1k 1.8× 792 1.1× 1.3k 2.6× 524 1.1× 92 0.3× 139 5.3k

Countries citing papers authored by Ruby H. P. Law

Since Specialization
Citations

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

Fields of papers citing papers by Ruby H. P. Law

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ruby H. P. Law. 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 Ruby H. P. Law. The network helps show where Ruby H. P. Law may publish in the future.

Co-authorship network of co-authors of Ruby H. P. Law

This figure shows the co-authorship network connecting the top 25 collaborators of Ruby H. P. Law. A scholar is included among the top collaborators of Ruby H. P. Law 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 Ruby H. P. Law. Ruby H. P. Law 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.
Yin, Victor, Tomislav Čaval, Vojtěch Franc, et al.. (2023). Proteoform-Resolved Profiling of Plasminogen Activation Reveals Novel Abundant Phosphorylation Site and Primary N-Terminal Cleavage Site. Molecular & Cellular Proteomics. 23(1). 100696–100696. 1 indexed citations
2.
Wu, Guojie, et al.. (2023). Synthesis and Structural Characterization of Macrocyclic Plasmin Inhibitors. ChemMedChem. 18(6). e202200632–e202200632. 1 indexed citations
3.
Quek, Adam J., Nathan Cowieson, Tom T. Caradoc-Davies, et al.. (2023). A High-Throughput Small-Angle X-ray Scattering Assay to Determine the Conformational Change of Plasminogen. International Journal of Molecular Sciences. 24(18). 14258–14258. 2 indexed citations
4.
Dickeson, S. Kent, Mao-fu Sun, Bassem M. Mohammed, et al.. (2022). A mechanism for hereditary angioedema caused by a lysine 311–to–glutamic acid substitution in plasminogen. Blood. 139(18). 2816–2829. 21 indexed citations
5.
White, Andrew M., Simon J. de Veer, Guojie Wu, et al.. (2020). Application and Structural Analysis of Triazole‐Bridged Disulfide Mimetics in Cyclic Peptides. Angewandte Chemie International Edition. 59(28). 11273–11277. 33 indexed citations
6.
White, Andrew M., Simon J. de Veer, Guojie Wu, et al.. (2020). Application and Structural Analysis of Triazole‐Bridged Disulfide Mimetics in Cyclic Peptides. Angewandte Chemie. 132(28). 11369–11373. 8 indexed citations
7.
Yuan, Yue, Damini Singh, Adam J. Quek, et al.. (2019). Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcus pyogenes. Journal of Structural Biology. 208(1). 18–29. 7 indexed citations
8.
Pang, Siew Siew, Charles Bayly-Jones, Mazdak Radjainia, et al.. (2019). The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1. Nature Communications. 10(1). 4288–4288. 62 indexed citations
9.
Swedberg, Joakim E., Guojie Wu, Thomas Durek, et al.. (2018). Highly Potent and Selective Plasmin Inhibitors Based on the Sunflower Trypsin Inhibitor-1 Scaffold Attenuate Fibrinolysis in Plasma. Journal of Medicinal Chemistry. 62(2). 552–560. 28 indexed citations
10.
Barlow, Νicholas, Eleanor W. W. Leung, Billy J. Williams‐Noonan, et al.. (2018). A Cyclic Peptide Inhibitor of the iNOS–SPSB Protein–Protein Interaction as a Potential Anti-Infective Agent. ACS Chemical Biology. 13(10). 2930–2938. 15 indexed citations
11.
Brennan, A. J., Ruby H. P. Law, Paul J. Conroy, et al.. (2018). Perforin proteostasis is regulated through its C2 domain: supra-physiological cell death mediated by T431D-perforin. Cell Death and Differentiation. 25(8). 1517–1529. 4 indexed citations
12.
House, Imran G., Colin M. House, A. J. Brennan, et al.. (2017). Regulation of perforin activation and pre‐synaptic toxicity through C‐terminal glycosylation. EMBO Reports. 18(10). 1775–1785. 28 indexed citations
13.
Spicer, Bradley A., Paul J. Conroy, Ruby H. P. Law, Ilia Voskoboinik, & James C. Whisstock. (2017). Perforin—A key (shaped) weapon in the immunological arsenal. Seminars in Cell and Developmental Biology. 72. 117–123. 22 indexed citations
14.
Dudkina, Natalya V., Bradley A. Spicer, Cyril F. Reboul, et al.. (2016). Structure of the poly-C9 component of the complement membrane attack complex. Nature Communications. 7(1). 10588–10588. 107 indexed citations
15.
Ellisdon, Andrew M., Qingwei Zhang, Travis K. Johnson, et al.. (2014). High resolution structure of cleaved Serpin 42 Da from Drosophila melanogaster. BMC Structural Biology. 14(1). 14–14. 14 indexed citations
16.
Bernal, Jamie Lopez, Olivia Susanto, Misty R. Jenkins, et al.. (2013). Perforin forms transient pores on the target cell plasma membrane to facilitate rapid access of granzymes during killer cell attack. Blood. 121(14). 2659–2668. 190 indexed citations
17.
Rosado, Carlos J., Stephanie C. Kondos, Michael J. Kuiper, et al.. (2008). The MACPF/CDC family of pore-forming toxins. Cellular Microbiology. 10(9). 1765–1774. 218 indexed citations
18.
Law, Ruby H. P. & Phillip Nagley. (2003). Import into Isolated Yeast Mitochondria of Radiolabeled Proteins Synthesized In Vitro. Humana Press eBooks. 37. 293–316.
19.
Devenish, Rodney J., et al.. (1992). Structure/Function Analysis of Yeast Mitochondrial ATP Synthase Subunit 8a. Annals of the New York Academy of Sciences. 671(1). 403–414. 20 indexed citations
20.
Law, Ruby H. P.. (1967). New Forms for Vaccination. BMJ. 2(5547). 314.2–314. 1 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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