W. Mark Abbott

915 total citations
23 papers, 606 citations indexed

About

W. Mark Abbott is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Oncology. According to data from OpenAlex, W. Mark Abbott has authored 23 papers receiving a total of 606 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 8 papers in Radiology, Nuclear Medicine and Imaging and 4 papers in Oncology. Recurrent topics in W. Mark Abbott's work include Viral Infectious Diseases and Gene Expression in Insects (8 papers), Monoclonal and Polyclonal Antibodies Research (8 papers) and Insect Resistance and Genetics (4 papers). W. Mark Abbott is often cited by papers focused on Viral Infectious Diseases and Gene Expression in Insects (8 papers), Monoclonal and Polyclonal Antibodies Research (8 papers) and Insect Resistance and Genetics (4 papers). W. Mark Abbott collaborates with scholars based in United Kingdom, Sweden and Japan. W. Mark Abbott's co-authors include Melissa Damschroder, David C. Lowe, Edward A. McKenzie, Ian W. Taylor, Eileen McCall, Philip G. Strange, Brian Middleton, Graeme Smith, Frank Carey and Raj K. Beri and has published in prestigious journals such as Journal of Molecular Biology, Biochemical Journal and FEBS Letters.

In The Last Decade

W. Mark Abbott

22 papers receiving 580 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
W. Mark Abbott United Kingdom 13 439 128 86 75 71 23 606
Lisa Murphy Ireland 12 382 0.9× 91 0.7× 99 1.2× 79 1.1× 122 1.7× 14 637
Kristen Jensen-Pergakes United States 13 665 1.5× 115 0.9× 199 2.3× 56 0.7× 67 0.9× 15 964
Myriam Gwerder Switzerland 8 364 0.8× 126 1.0× 115 1.3× 50 0.7× 94 1.3× 9 519
R. I. Christopherson Australia 14 604 1.4× 94 0.7× 74 0.9× 70 0.9× 54 0.8× 28 808
Kerstin K. Leuther United States 13 928 2.1× 84 0.7× 130 1.5× 142 1.9× 69 1.0× 19 1.2k
Tetsuo Miyake Japan 10 526 1.2× 73 0.6× 81 0.9× 109 1.5× 51 0.7× 26 701
Guy de Martynoff Belgium 10 422 1.0× 123 1.0× 47 0.5× 124 1.7× 88 1.2× 16 705
Arnaud Briat France 13 235 0.5× 77 0.6× 128 1.5× 119 1.6× 30 0.4× 23 440
Sandrine Guillard United Kingdom 11 580 1.3× 88 0.7× 126 1.5× 39 0.5× 44 0.6× 12 714
Róisín O’Flaherty Ireland 16 606 1.4× 210 1.6× 57 0.7× 99 1.3× 158 2.2× 28 792

Countries citing papers authored by W. Mark Abbott

Since Specialization
Citations

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

Fields of papers citing papers by W. Mark Abbott

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by W. Mark Abbott. 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 W. Mark Abbott. The network helps show where W. Mark Abbott may publish in the future.

Co-authorship network of co-authors of W. Mark Abbott

This figure shows the co-authorship network connecting the top 25 collaborators of W. Mark Abbott. A scholar is included among the top collaborators of W. Mark Abbott 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 W. Mark Abbott. W. Mark Abbott 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.
Phelan, Thomas, Jean Dunne, Niall Conlon, et al.. (2021). Dynamic Assay for Profiling Anti-SARS-CoV-2 Antibodies and Their ACE2/Spike RBD Neutralization Capacity. Viruses. 13(7). 1371–1371. 11 indexed citations
2.
McKenzie, Edward A. & W. Mark Abbott. (2018). Expression of recombinant proteins in insect and mammalian cells. Methods. 147. 40–49. 48 indexed citations
3.
Fisher, David I., et al.. (2017). Use of a protein engineering strategy to overcome limitations in the production of “Difficult to Express” recombinant proteins. Biotechnology and Bioengineering. 114(10). 2348–2359. 20 indexed citations
4.
Thompson, Mark J., L. David Finger, J.E. Debreczeni, et al.. (2016). Cellularly active N-hydroxyurea FEN1 inhibitors block substrate entry to the active site. Nature Chemical Biology. 12(10). 815–821. 56 indexed citations
5.
Abbott, W. Mark, et al.. (2015). Optimisation of a simple method to transiently transfect a CHO cell line in high-throughput and at large scale. Protein Expression and Purification. 116. 113–119. 23 indexed citations
6.
Abbott, W. Mark, Melissa Damschroder, & David C. Lowe. (2014). Current approaches to fine mapping of antigen–antibody interactions. Immunology. 142(4). 526–535. 111 indexed citations
7.
Abbott, W. Mark, Gareth M. Davies, Richard A. Norman, et al.. (2013). Characterization of the complex formed between a potent neutralizing ovine-derived polyclonal anti-TNFα Fab fragment and human TNFα. Bioscience Reports. 33(4). 7 indexed citations
8.
Abbott, W. Mark, et al.. (2012). Co-expression of protein phosphatases in insect cells affects phosphorylation status and expression levels of proteins. Protein Expression and Purification. 83(2). 217–225. 3 indexed citations
9.
Gerhardt, S., Eileen McCall, Liz Flavell, et al.. (2007). Crystal Structures of Human ADAMTS-1 Reveal a Conserved Catalytic Domain and a Disintegrin-like Domain with a Fold Homologous to Cysteine-Rich Domains. Journal of Molecular Biology. 373(4). 891–902. 68 indexed citations
10.
Pengelley, Stuart, David A. Chapman, W. Mark Abbott, et al.. (2006). A suite of parallel vectors for baculovirus expression. Protein Expression and Purification. 48(2). 173–181. 16 indexed citations
11.
McCall, Eileen, et al.. (2005). Improvements to the throughput of recombinant protein expression in the baculovirus/insect cell system. Protein Expression and Purification. 42(1). 29–36. 29 indexed citations
12.
Middleton, Brian, et al.. (2002). Identification of in Vitro Folding Conditions for Procathepsin S and Cathepsin S Using Fractional Factorial Screens. Protein Expression and Purification. 24(2). 242–254. 42 indexed citations
13.
McPheat, Jane, Claire A. Minshull, Nel C. Moore, et al.. (2001). Study of the interaction of the medium chain μ2 subunit of the clathrin-associated adapter protein complex 2 with cytotoxic T-lymphocyte antigen 4 and CD28. Biochemical Journal. 359(2). 427–427. 18 indexed citations
14.
McPheat, Jane, Claire A. Minshull, Nel C. Moore, et al.. (2001). Study of the interaction of the medium chain μ2 subunit of the clathrin-associated adapter protein complex 2 with cytotoxic T-lymphocyte antigen 4 and CD28. Biochemical Journal. 359(2). 427–434. 12 indexed citations
15.
Knäuper, Vera, et al.. (2000). An Analysis of Two Refolding Routes for a C-Terminally Truncated Human Collagenase-3 Expressed in Escherichia coli. Protein Expression and Purification. 19(2). 246–252. 5 indexed citations
16.
Newton, Charles R., William L. McPheat, H.M.H. Carr, et al.. (1994). Cloning and Expression in Murine Erythroleukemia Cells: The Soluble Forms of the Type I and Type II Tumor Necrosis Factor Receptors Fused to an Immunogenic Affinity Tag. Protein Expression and Purification. 5(5). 449–457. 4 indexed citations
17.
Abbott, W. Mark & Philip G. Strange. (1986). Attempts to obtain anti(D2 dopamine receptor) antibodies via the anti-idiotypic route. Biochemical Journal. 238(3). 817–823. 10 indexed citations
18.
Strange, Philip G., et al.. (1985). Isolation and characterization of D2-dopamine receptors. Biochemical Society Transactions. 13(6). 1099–1100. 1 indexed citations
19.
Abbott, W. Mark & Philip G. Strange. (1985). Partial purification of dopamine D2 receptors using lectin affinity columns. Bioscience Reports. 5(4). 303–308. 11 indexed citations
20.
Abbott, W. Mark, Anthony P. Monaco, & Paul S. Russell. (1971). The Effect of Supralethal Amethopterin and Folinic Acid Rescue on Mouse Skin Allograft Survival. Experimental Biology and Medicine. 136(2). 510–513. 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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