Mark J. Forster

1.9k total citations
35 papers, 1.5k citations indexed

About

Mark J. Forster is a scholar working on Molecular Biology, Spectroscopy and Cell Biology. According to data from OpenAlex, Mark J. Forster has authored 35 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 11 papers in Spectroscopy and 10 papers in Cell Biology. Recurrent topics in Mark J. Forster's work include Advanced NMR Techniques and Applications (10 papers), Proteoglycans and glycosaminoglycans research (9 papers) and Glycosylation and Glycoproteins Research (8 papers). Mark J. Forster is often cited by papers focused on Advanced NMR Techniques and Applications (10 papers), Proteoglycans and glycosaminoglycans research (9 papers) and Glycosylation and Glycoproteins Research (8 papers). Mark J. Forster collaborates with scholars based in United Kingdom, Tanzania and Sweden. Mark J. Forster's co-authors include Barbara Mulloy, Christopher Jones, D.B. Davies, Steve W. Homans, Andrew N. Lane, John B. O. Mitchell, Alexander Alex, Janet M. Thornton, Roman A. Laskowski and Edward A. Johnson and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Blood.

In The Last Decade

Mark J. Forster

35 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mark J. Forster United Kingdom 20 1.0k 694 340 138 136 35 1.5k
Robert L. Simmer United States 19 1.4k 1.3× 130 0.2× 261 0.8× 93 0.7× 72 0.5× 25 2.3k
Wouter A. van der Linden Netherlands 24 1.5k 1.4× 234 0.3× 436 1.3× 25 0.2× 72 0.5× 42 2.2k
James C. Myslik United States 10 965 0.9× 546 0.8× 82 0.2× 93 0.7× 71 0.5× 11 1.6k
Sami Mahrus United States 19 1.5k 1.4× 210 0.3× 213 0.6× 65 0.5× 244 1.8× 29 2.3k
Mitsuo Murata Japan 16 998 1.0× 243 0.4× 112 0.3× 100 0.7× 64 0.5× 34 1.6k
Eugene C. Petrella United States 14 1.1k 1.0× 194 0.3× 150 0.4× 30 0.2× 73 0.5× 17 1.6k
Olga Vinogradova United States 27 1.3k 1.3× 474 0.7× 259 0.8× 835 6.1× 131 1.0× 68 2.2k
Martyn C. Botfield United States 22 1.2k 1.2× 147 0.2× 123 0.4× 89 0.6× 66 0.5× 47 2.0k
Andrew G. Stephen United States 32 2.8k 2.7× 406 0.6× 315 0.9× 37 0.3× 43 0.3× 92 3.6k
Ursula Schulze‐Gahmen United States 25 1.8k 1.7× 275 0.4× 209 0.6× 26 0.2× 56 0.4× 38 2.5k

Countries citing papers authored by Mark J. Forster

Since Specialization
Citations

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

Fields of papers citing papers by Mark J. Forster

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark J. Forster

This figure shows the co-authorship network connecting the top 25 collaborators of Mark J. Forster. A scholar is included among the top collaborators of Mark J. Forster 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 Mark J. Forster. Mark J. Forster 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.
Gaulton, Anna, Namrata Kale, Gerard J. P. van Westen, et al.. (2015). A large-scale crop protection bioassay data set. Scientific Data. 2(1). 150032–150032. 19 indexed citations
3.
4.
Harland, Lee, Christopher Larminie, Susanna‐Assunta Sansone, et al.. (2011). Empowering industrial research with shared biomedical vocabularies. Drug Discovery Today. 16(21-22). 940–947. 11 indexed citations
5.
Magagnoli, Claudia, Mark J. Forster, Lauren Allen, et al.. (2011). Structural characterisation, stability and antibody recognition of chimeric NHBA-GNA1030: An investigational vaccine component against Neisseria meningitidis. Vaccine. 30(7). 1330–1342. 9 indexed citations
6.
Mulloy, Barbara & Mark J. Forster. (2008). Application of drug discovery software to the identification of heparin-binding sites on protein surfaces: a computational survey of the 4-helix cytokines. Molecular Simulation. 34(4). 481–489. 24 indexed citations
7.
Robinson, C. Jane, et al.. (2005). Vascular endothelial growth factor (VEGF): modulation of heparin-binding activity and bioactivity by site-directed mutagenesis. 2 indexed citations
8.
Mahoney, David J., Barbara Mulloy, Mark J. Forster, et al.. (2005). Characterization of the Interaction between Tumor Necrosis Factor-stimulated Gene-6 and Heparin. Journal of Biological Chemistry. 280(29). 27044–27055. 82 indexed citations
9.
Forster, Mark J., et al.. (2003). Modeling of welded joints for design against fatigue. Engineering With Computers. 19(2-3). 142–151. 1 indexed citations
10.
Sachchidanand, Sachchidanand, Olivier Lequin, David Staunton, et al.. (2002). Mapping the Heparin-binding Site on the13–14F3 Fragment of Fibronectin. Journal of Biological Chemistry. 277(52). 50629–50635. 44 indexed citations
11.
Forster, Mark J., Barbara Mulloy, & M. V. Nermut. (2000). Molecular modelling study of HIV p17gag (MA) protein shell utilising data from electron microscopy and X-ray crystallography. Journal of Molecular Biology. 298(5). 841–857. 39 indexed citations
12.
Mulloy, Barbara & Mark J. Forster. (2000). Conformation and dynamics of heparin and heparan sulfate. Glycobiology. 10(11). 1147–1156. 254 indexed citations
13.
Forster, Mark J., Anthony Heath, & Muhammad Afzal. (1999). Application of distance geometry to 3D visualization of sequence relationships.. Bioinformatics. 15(1). 89–90. 15 indexed citations
14.
Mulloy, Barbara, Mark J. Forster, Christopher Jones, et al.. (1994). The effect of variation of substitution on the solution conformation of heparin: a spectroscopic and molecular modelling study. Carbohydrate Research. 255. 1–26. 80 indexed citations
15.
Forster, Mark J. & Barbara Mulloy. (1994). Rationalizing nuclear overhauser effect data for compounds adopting multiple‐solution conformations. Journal of Computational Chemistry. 15(2). 155–161. 11 indexed citations
16.
Homans, Steve W. & Mark J. Forster. (1992). Application of restrained minimization, simulated annealing and molecular dynamics simulations for the conformational analysis of oligosaccharides. Glycobiology. 2(2). 143–151. 63 indexed citations
17.
Currie, Felicity, et al.. (1991). N.m.r. and conformational analysis of the capsular polysaccharide from Streptococcus pneumoniae type 4. Carbohydrate Research. 221(1). 95–121. 35 indexed citations
18.
Lane, Andrew N. & Mark J. Forster. (1989). Determination of internal dynamics of deoxyriboses in the DNA hexamer d(CGTACG)2 by 1H NMR. European Biophysics Journal. 17(4). 221–32. 29 indexed citations
19.
Forster, Mark J., Chris Jones, & Barbara Mulloy. (1989). NOEMOL: integrated molecular graphics and the simulation of Nuclear Overhauser effects in NMK spectroscopy. Journal of Molecular Graphics. 7(4). 196–201. 27 indexed citations
20.
Searle, Mark S., Mark J. Forster, B. Birdsall, et al.. (1988). Dynamics of trimethoprim bound to dihydrofolate reductase.. Proceedings of the National Academy of Sciences. 85(11). 3787–3791. 30 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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