Andrew Docherty

12.3k total citations · 4 hit papers
101 papers, 10.5k citations indexed

About

Andrew Docherty is a scholar working on Cancer Research, Oncology and Electrical and Electronic Engineering. According to data from OpenAlex, Andrew Docherty has authored 101 papers receiving a total of 10.5k indexed citations (citations by other indexed papers that have themselves been cited), including 56 papers in Cancer Research, 40 papers in Oncology and 27 papers in Electrical and Electronic Engineering. Recurrent topics in Andrew Docherty's work include Protease and Inhibitor Mechanisms (56 papers), Peptidase Inhibition and Analysis (35 papers) and Advanced Fiber Laser Technologies (25 papers). Andrew Docherty is often cited by papers focused on Protease and Inhibitor Mechanisms (56 papers), Peptidase Inhibition and Analysis (35 papers) and Advanced Fiber Laser Technologies (25 papers). Andrew Docherty collaborates with scholars based in United Kingdom, United States and Australia. Andrew Docherty's co-authors include Gillian Murphy, John J. Reynolds, Mark I. Cockett, Paul E. Stephens, Bryan John Smith, Gillian Murphy, Frances Willenbrock, Patrick M. Slocombe, Peter Angel and James P. O’Connell and has published in prestigious journals such as Nature, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Andrew Docherty

101 papers receiving 10.2k citations

Hit Papers

Transforming growth factor beta modulates the expression ... 1985 2026 1998 2012 1987 1985 1992 1998 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Andrew Docherty United Kingdom 49 6.1k 4.1k 3.2k 2.3k 1.9k 101 10.5k
Vera Knäuper United Kingdom 52 6.1k 1.0× 3.7k 0.9× 3.1k 1.0× 2.3k 1.0× 1.8k 0.9× 104 9.7k
Leif R. Lund Denmark 56 5.8k 0.9× 2.9k 0.7× 3.8k 1.2× 2.7k 1.2× 2.1k 1.1× 125 10.5k
Gregory I. Goldberg United States 33 5.8k 0.9× 3.3k 0.8× 2.5k 0.8× 2.1k 0.9× 1.5k 0.8× 46 8.6k
John J. Reynolds United Kingdom 63 5.5k 0.9× 3.5k 0.8× 4.3k 1.4× 1.9k 0.8× 1.8k 0.9× 186 12.6k
Paolo Mignatti United States 40 3.7k 0.6× 2.1k 0.5× 4.5k 1.4× 1.4k 0.6× 1.4k 0.7× 98 8.9k
Stanley Zucker United States 55 4.8k 0.8× 4.2k 1.0× 4.2k 1.3× 1.6k 0.7× 1.1k 0.6× 161 9.6k
Olli Saksela Finland 37 3.2k 0.5× 2.8k 0.7× 5.5k 1.7× 1.5k 0.7× 1.4k 0.7× 82 9.6k
Yves A. DeClerck United States 55 4.3k 0.7× 4.1k 1.0× 3.7k 1.2× 1.1k 0.5× 1.2k 0.6× 127 9.1k
Niels Behrendt Denmark 47 5.3k 0.9× 2.4k 0.6× 2.7k 0.9× 2.9k 1.3× 2.0k 1.0× 109 8.2k
Kaoru Miyazaki Japan 52 3.2k 0.5× 2.4k 0.6× 3.5k 1.1× 1.3k 0.6× 2.3k 1.2× 181 8.3k

Countries citing papers authored by Andrew Docherty

Since Specialization
Citations

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

Fields of papers citing papers by Andrew Docherty

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Andrew Docherty

This figure shows the co-authorship network connecting the top 25 collaborators of Andrew Docherty. A scholar is included among the top collaborators of Andrew Docherty 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 Andrew Docherty. Andrew Docherty 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.
2.
Okusaga, Olukayode, et al.. (2012). Guided entropy mode Rayleigh scattering in optical fibers. Optics Letters. 37(4). 683–683. 21 indexed citations
3.
Zhou, Weimin, Olukayode Okusaga, Etgar Levy, et al.. (2012). Potentials and challenges for the optoelectronic oscillator. Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE. 8255. 82551N–82551N. 5 indexed citations
4.
Weiblen, R. Joseph, Andrew Docherty, Jonathan Hu, & Curtis R. Menyuk. (2010). Calculation of the expected bandwidth for a mid-infrared supercontinuum source based on As_2S_3 chalcogenide photonic crystal fibers. Optics Express. 18(25). 26666–26666. 22 indexed citations
5.
Nisato, Riccardo E., Christian Sirrenberg, Georgina S. Butler, et al.. (2005). Dissecting the Role of Matrix Metalloproteinases (MMP) and Integrin αvβ3 in Angiogenesis In vitro : Absence of Hemopexin C Domain Bioactivity, but Membrane-Type 1-MMP and αvβ3 Are Critical. Cancer Research. 65(20). 9377–9387. 54 indexed citations
6.
Sinkin, O. V., V.S. Grigoryan, J. Zweck, et al.. (2005). Calculation, characterization, and application of the time shift function in wavelength-division-multiplexed return-to-zero systems. Optics Letters. 30(16). 2056–2056. 6 indexed citations
7.
Knäuper, Vera, Margaret L. Patterson, Bryan Ronain Smith, et al.. (2001). The role of exon 5 in fibroblast collagenase (MMP-1) substrate specificity and inhibitor selectivity. European Journal of Biochemistry. 268(6). 1888–1896. 1 indexed citations
9.
Gohlke, U., F. Xavier Gomis‐Rüth, Thomas Crabbe, et al.. (1996). The C‐terminal (haemopexin‐like) domain structure of human gelatinase A (MMP2): structural implications for its function. FEBS Letters. 378(2). 126–130. 75 indexed citations
10.
Chander, Surinder K., Pari Antoniw, Nigel R. A. Beeley, et al.. (1995). An in Vivo Model for Screening Peptidomimetic Inhibitors of Gelatinase A. Journal of Pharmaceutical Sciences. 84(4). 404–409. 10 indexed citations
11.
Williamson, Richard A., Gabriel Martorell, Mark D. Carr, et al.. (1994). Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family. Biochemistry. 33(39). 11745–11759. 84 indexed citations
12.
Crabbe, Thomas, Stanley Zucker, Mark I. Cockett, et al.. (1994). Mutation of the Active Site Glutamic Acid of Human Gelatinase A: Effects on Latency, Catalysis, and the Binding of Tissue Inhibitor of Metalloproteinases-1. Biochemistry. 33(21). 6684–6690. 59 indexed citations
13.
Paterson, Christopher A., et al.. (1994). Recombinant tissue inhibitor of metalloproteinases type 1 suppresses alkali-burn-induced corneal ulceration in rabbits.. PubMed. 35(2). 677–84. 43 indexed citations
14.
Nguyen, Quang, Frances Willenbrock, Mark I. Cockett, et al.. (1994). Different Domain Interactions Are Involved in the Binding of Tissue Inhibitors of Metalloproteinases to Stromelysin-1 and Gelatinase A. Biochemistry. 33(8). 2089–2095. 66 indexed citations
15.
Crabbe, Thomas, James P. O’Connell, Bryan John Smith, & Andrew Docherty. (1994). Reciprocated matrix metalloproteinase activation: A process performed by interstitial collagenase and progelatinase A. Biochemistry. 33(48). 14419–14425. 82 indexed citations
16.
Crabbe, Thomas, Bryan Ronain Smith, James P. O’Connell, & Andrew Docherty. (1994). Human progelatinase A can be activated by matrilysin. FEBS Letters. 345(1). 14–16. 82 indexed citations
17.
Willenbrock, Frances, Thomas Crabbe, Patrick M. Slocombe, et al.. (1993). The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: A kinetic analysis of the inhibition of gelatinase A. Biochemistry. 32(16). 4330–4337. 206 indexed citations
19.
Docherty, Andrew & Gillian Murphy. (1990). The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins.. PubMed. 49 Suppl 1. 469–79. 184 indexed citations
20.
Spurr, Nigel K., Alan C. Gough, John R. Gosden, et al.. (1988). Restriction fragment length polymorphism analysis and assignment of the metalloproteinases stromelysin and collagenase to the long arm of chromosome 11. Genomics. 2(2). 119–127. 48 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026