John D. Shannon
About
John D. Shannon is a scholar working on Molecular Biology, Genetics and Immunology and Allergy.
According to data from OpenAlex, John D. Shannon has authored 42 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 20 papers in Genetics and 9 papers in Immunology and Allergy. Recurrent topics in John D. Shannon's work include Venomous Animal Envenomation and Studies (18 papers), Biochemical and Structural Characterization (11 papers) and Protease and Inhibitor Mechanisms (9 papers). John D. Shannon is often cited by papers focused on Venomous Animal Envenomation and Studies (18 papers), Biochemical and Structural Characterization (11 papers) and Protease and Inhibitor Mechanisms (9 papers). John D. Shannon collaborates with scholars based in United States, Brazil and Costa Rica. John D. Shannon's co-authors include Jay W. Fox, Michael D. Schaller, Jeffrey D. Hildebrand, J. Thomas Parsons, Richard Vines, Jón B. Bjarnason, J. Thomas Parsons, Eugenia N. Baramova, Li-Guo Jia and Solange M.T. Serrano and has published in prestigious journals such as Journal of Biological Chemistry, Molecular and Cellular Biology and Biochemistry.
In The Last Decade
John D. Shannon
42 papers receiving 4.2k citations
Hit Papers
Peers — A (Enhanced Table)
Peers by citation overlap · career bar shows stage (early→late) cites · hero ref
| Name | h | Career | Trend | Papers | Cites | |||||
|---|---|---|---|---|---|---|---|---|---|---|
| John D. Shannon United States | 28 | 2.2k | 1.6k | 1.5k | 1.1k | 659 | 42 | 4.3k | ||
| Donald Dowbenko United States | 34 | 3.1k 1.4× | 1.3k 0.8× | 401 0.3× | 815 0.7× | 516 0.8× | 50 | 5.5k | ||
| Klaus Ebnet Germany | 38 | 2.7k 1.2× | 925 0.6× | 328 0.2× | 1.1k 1.0× | 64 0.1× | 73 | 5.2k | ||
| Walter Stöcker Germany | 32 | 1.5k 0.7× | 461 0.3× | 457 0.3× | 295 0.3× | 51 0.1× | 70 | 3.4k | ||
| Lars Hellman Sweden | 42 | 2.0k 0.9× | 1.3k 0.9× | 350 0.2× | 587 0.5× | 47 0.1× | 170 | 5.3k | ||
| Vania Braga United Kingdom | 34 | 3.0k 1.3× | 602 0.4× | 272 0.2× | 2.2k 1.9× | 46 0.1× | 68 | 4.4k | ||
| Aura S. Kamiguti United Kingdom | 34 | 1.1k 0.5× | 263 0.2× | 2.5k 1.6× | 109 0.1× | 1.5k 2.2× | 69 | 3.2k | ||
| John A. Martignetti United States | 38 | 3.0k 1.3× | 143 0.1× | 891 0.6× | 187 0.2× | 243 0.4× | 102 | 5.4k | ||
| Takis S. Papas United States | 45 | 5.2k 2.3× | 206 0.1× | 1.6k 1.0× | 344 0.3× | 1.9k 2.8× | 139 | 9.0k | ||
| Charles A. Whittaker United States | 37 | 3.3k 1.5× | 694 0.4× | 662 0.4× | 1.4k 1.2× | 25 0.0× | 72 | 6.0k | ||
| Christine Bessia France | 12 | 1.9k 0.9× | 318 0.2× | 200 0.1× | 284 0.2× | 742 1.1× | 12 | 4.3k |
Countries citing papers authored by John D. Shannon
Since
Specialization
Citations
This map shows the geographic impact of John D. Shannon'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 John D. Shannon with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites John D. Shannon more than expected).
Fields of papers citing papers by John D. Shannon
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by John D. Shannon. 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 John D. Shannon. The network helps show where John D. Shannon may publish in the future.
Co-authorship network of co-authors of John D. Shannon
This figure shows the co-authorship network connecting the top 25 collaborators of John D. Shannon. A scholar is included among the top collaborators of John D. Shannon 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 John D. Shannon. John D. Shannon is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Khromov, Alexander S., Ko Momotani, Li Jin, et al.. (2012). Molecular Mechanism of Telokin-mediated Disinhibition of Myosin Light Chain Phosphatase and cAMP/cGMP-induced Relaxation of Gastrointestinal Smooth Muscle. Journal of Biological Chemistry. 287(25). 20975–20985.
2.
Rucavado, Alexandra, Teresa Escalante, John D. Shannon, José Marı́a Gutiérrez, & Jay W. Fox. (2011). Proteomics of Wound Exudate in Snake Venom-Induced Pathology: Search for Biomarkers To Assess Tissue Damage and Therapeutic Success. Journal of Proteome Research. 10(4). 1987–2005.
3.
Chianese‐Bullock, Kimberly A., et al.. (2009). Multi-peptide vaccines vialed as peptide mixtures can be stable reagents for use in peptide-based immune therapies. Vaccine. 27(11). 1764–1770.
4.
Díaz, Patricia, Gina D’Suze, Víctor Salazar, et al.. (2009). Antibacterial activity of six novel peptides from Tityus discrepans scorpion venom. A fluorescent probe study of microbial membrane Na+ permeability changes. Toxicon. 54(6). 802–817.
5.
Serrano, Solange M.T., Deyu Wang, John D. Shannon, et al.. (2007). Interaction of the cysteine‐rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site‐specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor‐mediated platelet aggregation. FEBS Journal. 274(14). 3611–3621.
6.
Turner, Terry T., et al.. (2006). Testicular Torsion Alters the Presence of Specific Proteins in the Mouse Testis as Well as the Phosphorylation Status of Specific Proteins. Journal of Andrology. 27(2). 285–293.
7.
Serrano, Solange M.T., Junho Kim, Deyu Wang, et al.. (2006). The Cysteine-rich Domain of Snake Venom Metalloproteinases Is a Ligand for von Willebrand Factor A Domains. Journal of Biological Chemistry. 281(52). 39746–39756.
8.
Serrano, Solange M.T., John D. Shannon, Deyu Wang, Antônio Carlos Martins de Camargo, & Jay W. Fox. (2005). A multifaceted analysis of viperid snake venoms by two‐dimensional gel electrophoresis: An approach to understanding venom proteomics. PROTEOMICS. 5(2). 501–510.
9.
Neves‐Ferreira, Ana Gisele C., Jonás Perales, Jay W. Fox, et al.. (2002). Structural and Functional Analyses of DM43, a Snake Venom Metalloproteinase Inhibitor from Didelphis marsupialisSerum. Journal of Biological Chemistry. 277(15). 13129–13137.
10.
Moura‐da‐Silva, Ana M., Maisa S. Della-Casa, Anthony S. David, et al.. (2002). Evidence for heterogeneous forms of the snake venom metalloproteinase jararhagin: a factor contributing to snake venom variability. Archives of Biochemistry and Biophysics. 409(2). 395–401.
11.
Jia, Li-Guo, Xiaoming Wang, John D. Shannon, Jón B. Bjarnason, & Jay W. Fox. (2000). Inhibition of Platelet Aggregation by the Recombinant Cysteine-Rich Domain of the Hemorrhagic Snake Venom Metalloproteinase, Atrolysin A. Archives of Biochemistry and Biophysics. 373(1). 281–286.
12.
Shimokawa, Ken‐ichi, Li-Guo Jia, John D. Shannon, & Jay W. Fox. (1998). Isolation, Sequence Analysis, and Biological Activity of Atrolysin E/D, the Non-RGD Disintegrin Domain fromCrotalus atroxVenom. Archives of Biochemistry and Biophysics. 354(2). 239–246.
13.
Jia, Li-Guo, Xiaoming Wang, John D. Shannon, Jón B. Bjarnason, & Jay W. Fox. (1997). Function of Disintegrin-like/Cysteine-rich Domains of Atrolysin A. Journal of Biological Chemistry. 272(20). 13094–13102.
14.
Richardson, Alan, John D. Shannon, Reid B. Adams, Michael D. Schaller, & J. Thomas Parsons. (1997). Identification of integrin-stimulated sites of serine phosphorylation in FRNK, the separately expressed C-terminal domain of focal adhesion kinase: a potential role for protein kinase A. Biochemical Journal. 324(1). 141–149.
15.
Botos, Istvan, Léonardo Scapozza, John D. Shannon, Jay W. Fox, & Erik Meyer. (1995). Structure-based analysis of inhibitor binding to Ht-d. Acta Crystallographica Section D Biological Crystallography. 51(4). 597–604.
16.
Arruda, L. Karla, Lisa D. Vailes, Barbara J. Mann, et al.. (1995). Molecular Cloning of a Major Cockroach (Blattella germanica) Allergen, Bla g 2. Journal of Biological Chemistry. 270(33). 19563–19568.
17.
Herr, John C., et al.. (1992). Purification and Microsequencing of the Intra-Acrosomal Protein SP-10. Evidence that SP-10 Heterogeneity Results from Endoproteolytic Processes1. Biology of Reproduction. 47(1). 11–20.
18.
Baramova, Eugenia N., John D. Shannon, Jón B. Bjarnason, & Jay W. Fox. (1990). Identification of the Cleavage Sites by a Hemorrhagic Metalloproteinase in Type IV Collagen. Matrix. 10(2). 91–97.
19.
Baramova, Eugenia N., et al.. (1990). Interaction of hemorrhagic metalloproteinases with human .alpha.2-macroglobulin. Biochemistry. 29(4). 1069–1074.
20.
Baramova, Eugenia N., John D. Shannon, Jón B. Bjarnason, & Jay W. Fox. (1989). Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases. Archives of Biochemistry and Biophysics. 275(1). 63–71.
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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