Glynis Johnson

1.6k total citations
37 papers, 1.4k citations indexed

About

Glynis Johnson is a scholar working on Pharmacology, Molecular Biology and Computational Theory and Mathematics. According to data from OpenAlex, Glynis Johnson has authored 37 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Pharmacology, 15 papers in Molecular Biology and 15 papers in Computational Theory and Mathematics. Recurrent topics in Glynis Johnson's work include Cholinesterase and Neurodegenerative Diseases (20 papers), Computational Drug Discovery Methods (15 papers) and Nicotinic Acetylcholine Receptors Study (10 papers). Glynis Johnson is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (20 papers), Computational Drug Discovery Methods (15 papers) and Nicotinic Acetylcholine Receptors Study (10 papers). Glynis Johnson collaborates with scholars based in South Africa, United Kingdom and Canada. Glynis Johnson's co-authors include Samuel W. Moore, Soraya Bardien, William Haylett, Shameemah Abrahams, Jonathan Carr, Peter Jacobs, E. Nassau, L.R. Purves, P. Anne Underwood and Heather R. Luckarift and has published in prestigious journals such as Journal of Clinical Investigation, Biomaterials and Biochemical Journal.

In The Last Decade

Glynis Johnson

36 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Glynis Johnson South Africa 17 564 405 320 174 152 37 1.4k
Sadiq Umar India 24 234 0.4× 631 1.6× 46 0.1× 224 1.3× 128 0.8× 60 1.9k
Ming‐Ching Kao Taiwan 26 475 0.8× 1.1k 2.7× 33 0.1× 70 0.4× 205 1.3× 72 2.1k
Dileep Kumar India 22 216 0.4× 405 1.0× 138 0.4× 182 1.0× 39 0.3× 79 1.2k
Junsoo Park South Korea 26 104 0.2× 763 1.9× 110 0.3× 93 0.5× 121 0.8× 83 1.8k
Yuzhong Zheng China 27 346 0.6× 1.1k 2.7× 76 0.2× 38 0.2× 262 1.7× 119 2.1k
Simona Pace Germany 24 374 0.7× 487 1.2× 35 0.1× 230 1.3× 102 0.7× 58 1.5k
Wu H China 24 232 0.4× 954 2.4× 84 0.3× 61 0.4× 226 1.5× 181 2.0k
Susana G. Guerreiro Portugal 15 95 0.2× 494 1.2× 62 0.2× 57 0.3× 224 1.5× 34 1.4k
Juan Cabezas‐Herrera Spain 25 373 0.7× 839 2.1× 221 0.7× 93 0.5× 95 0.6× 69 1.6k
Vishakha Singh India 23 84 0.1× 560 1.4× 89 0.3× 90 0.5× 112 0.7× 38 1.3k

Countries citing papers authored by Glynis Johnson

Since Specialization
Citations

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

Fields of papers citing papers by Glynis Johnson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Glynis Johnson

This figure shows the co-authorship network connecting the top 25 collaborators of Glynis Johnson. A scholar is included among the top collaborators of Glynis Johnson 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 Glynis Johnson. Glynis Johnson 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
2.
Kinnear, Craig, Brigitte Glanzmann, Glenda Durrheim, et al.. (2017). Exome sequencing identifies a novel TTC37 mutation in the first reported case of Trichohepatoenteric syndrome (THE-S) in South Africa. BMC Medical Genetics. 18(1). 26–26. 13 indexed citations
3.
Johnson, Glynis. (2016). The α/β Hydrolase Fold Proteins of Mycobacterium tuberculosis, with Reference to their Contribution to Virulence. Current Protein and Peptide Science. 18(3). 190–210. 26 indexed citations
4.
Johnson, Glynis & Samuel W. Moore. (2012). Why has butyrylcholinesterase been retained? Structural and functional diversification in a duplicated gene. Neurochemistry International. 61(5). 783–797. 72 indexed citations
5.
Johnson, Glynis & Samuel W. Moore. (2011). The carboxylesterase/cholinesterase gene family in invertebrate deuterostomes. Comparative Biochemistry and Physiology Part D Genomics and Proteomics. 7(2). 83–93. 13 indexed citations
6.
Johnson, Glynis, et al.. (2008). Non‐enzymatic developmental functions of acetylcholinesterase – the question of redundancy. FEBS Journal. 275(20). 5129–5138. 8 indexed citations
7.
Johnson, Glynis & Samuel W. Moore. (2008). Investigations into the development of catalytic activity in anti‐acetylcholinesterase idiotypic and anti‐idiotypic antibodies. Journal of Molecular Recognition. 22(3). 188–196. 5 indexed citations
8.
Moore, Samuel W. & Glynis Johnson. (2005). Acetylcholinesterase in Hirschsprung?s disease. Pediatric Surgery International. 21(4). 255–263. 55 indexed citations
9.
Johnson, Glynis & Samuel W. Moore. (2005). The Peripheral Anionic Site of Acetylcholinesterase: Structure, Functions and Potential Role in Rational Drug Design. Current Pharmaceutical Design. 12(2). 217–225. 257 indexed citations
10.
Johnson, Glynis & Samuel W. Moore. (2004). Functional idiotypic mimicry of an adhesion‐ and differentiation‐promoting site on acetylcholinesterase. Journal of Cellular Biochemistry. 91(5). 999–1009. 5 indexed citations
11.
Johnson, Glynis & Samuel W. Moore. (2004). Identification of a structural site on acetylcholinesterase that promotes neurite outgrowth and binds laminin-1 and collagen IV. Biochemical and Biophysical Research Communications. 319(2). 448–455. 46 indexed citations
12.
Johnson, Glynis & Samuel W. Moore. (2002). Catalytic antibodies with acetylcholinesterase activity. Journal of Immunological Methods. 269(1-2). 13–28. 8 indexed citations
13.
Johnson, Glynis & Samuel W. Moore. (2002). Idiotypic mimicry of a catalytic antibody active site. Molecular Immunology. 39(5-6). 273–288. 9 indexed citations
14.
Johnson, Glynis & Samuel W. Moore. (2000). Cholinesterase-like catalytic antibodies: reaction with substrates and inhibitors. Molecular Immunology. 37(12-13). 707–719. 21 indexed citations
15.
Johnson, Glynis & Samuel W. Moore. (2000). Localization of a Novel Adhesion-Promoting Site on Acetylcholinesterase Using Catalytic Antiacetylcholinesterase Antibodies Displaying Cholinesterase-like Activity. Applied Biochemistry and Biotechnology. 83(1-3). 131–144. 8 indexed citations
16.
Johnson, Glynis & Samuel W. Moore. (1999). The Adhesion Function on Acetylcholinesterase Is Located at the Peripheral Anionic Site. Biochemical and Biophysical Research Communications. 258(3). 758–762. 76 indexed citations
17.
Johnson, Glynis, Samuel W. Moore, & L.R. Purves. (1995). Acetylcholinesterase of human intestinal tissue affected by Hirschsprung's disease: effect of magnesium chloride on isoforms. Clinica Chimica Acta. 243(2). 115–128. 4 indexed citations
18.
Johnson, Glynis & Samuel W. Moore. (1995). Anti‐acetylcholinesterase antibodies display cholinesterase‐like activity. European Journal of Immunology. 25(1). 25–29. 16 indexed citations
20.
Purves, L.R., et al.. (1988). Properties of the transferrin associated with rat intestinal mucosa. Biochimica et Biophysica Acta (BBA) - General Subjects. 966(3). 318–327. 10 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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