Mark Knapp

3.5k total citations
24 papers, 1.2k citations indexed

About

Mark Knapp is a scholar working on Molecular Biology, Organic Chemistry and Cellular and Molecular Neuroscience. According to data from OpenAlex, Mark Knapp has authored 24 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 4 papers in Organic Chemistry and 3 papers in Cellular and Molecular Neuroscience. Recurrent topics in Mark Knapp's work include PI3K/AKT/mTOR signaling in cancer (7 papers), Biochemical and Molecular Research (4 papers) and Quinazolinone synthesis and applications (4 papers). Mark Knapp is often cited by papers focused on PI3K/AKT/mTOR signaling in cancer (7 papers), Biochemical and Molecular Research (4 papers) and Quinazolinone synthesis and applications (4 papers). Mark Knapp collaborates with scholars based in United States, Switzerland and China. Mark Knapp's co-authors include Bernhard Rupp, Michael C. Phillips, Mark L. Segall, Julie Morrow, Karl H. Weisgraber, Sissel Lund‐Katz, Pascal Furet, Joachim Blanz, Christine Fritsch and Giorgio Caravatti and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nature Communications and Journal of Molecular Biology.

In The Last Decade

Mark Knapp

24 papers receiving 1.2k 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 Knapp United States 17 769 219 140 127 104 24 1.2k
Douglas R. Dougan United States 19 918 1.2× 378 1.7× 293 2.1× 94 0.7× 33 0.3× 32 1.6k
M. Kyle Hadden United States 23 1.3k 1.7× 182 0.8× 264 1.9× 63 0.5× 23 0.2× 77 1.8k
Qingxiang Sun China 20 1.0k 1.3× 55 0.3× 159 1.1× 51 0.4× 62 0.6× 59 1.4k
Jason D. Katz United States 12 946 1.2× 335 1.5× 213 1.5× 57 0.4× 61 0.6× 23 1.9k
Maciej Wieczorek Poland 20 831 1.1× 143 0.7× 243 1.7× 77 0.6× 25 0.2× 83 1.4k
Tong Ying Shun United States 21 686 0.9× 99 0.5× 223 1.6× 39 0.3× 17 0.2× 35 1.4k
George W. Small United States 19 1.1k 1.4× 88 0.4× 338 2.4× 77 0.6× 51 0.5× 32 1.7k
Aisha Shamas‐Din Canada 13 1.5k 1.9× 76 0.3× 220 1.6× 46 0.4× 27 0.3× 17 1.9k
A. K. Wong Australia 17 683 0.9× 210 1.0× 101 0.7× 59 0.5× 24 0.2× 21 1.3k
Sunanda G. Dastidar India 21 618 0.8× 372 1.7× 181 1.3× 45 0.4× 20 0.2× 56 1.4k

Countries citing papers authored by Mark Knapp

Since Specialization
Citations

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

Fields of papers citing papers by Mark Knapp

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark Knapp

This figure shows the co-authorship network connecting the top 25 collaborators of Mark Knapp. A scholar is included among the top collaborators of Mark Knapp 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 Knapp. Mark Knapp 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.
Zvornicanin, Sarah N., Ala M. Shaqra, Qiu Yu J. Huang, et al.. (2023). Crystal Structures of Inhibitor-Bound Main Protease from Delta- and Gamma-Coronaviruses. Viruses. 15(3). 781–781. 5 indexed citations
2.
Shaqra, Ala M., Sarah N. Zvornicanin, Qiu Yu J. Huang, et al.. (2022). Defining the substrate envelope of SARS-CoV-2 main protease to predict and avoid drug resistance. Nature Communications. 13(1). 3556–3556. 73 indexed citations
3.
Fong, Susan, Alexandra Frommlet, Andreas O. Frank, et al.. (2020). A polyomavirus peptide binds to the capsid VP1 pore and has potent antiviral activity against BK and JC polyomaviruses. eLife. 9. 7 indexed citations
4.
Knapp, Mark, Peter Kim, Andreas Hein, et al.. (2020). Preclinical Characterization of MAU868, a Novel Neutralizing Antibody Targeting BK Virus. Journal of the American Society of Nephrology. 31(10S). 720–720. 1 indexed citations
5.
Lu, Yipin, Mark Knapp, Kenneth Crawford, et al.. (2017). Rationally Designed PI3Kα Mutants to Mimic ATR and Their Use to Understand Binding Specificity of ATR Inhibitors. Journal of Molecular Biology. 429(11). 1684–1704. 28 indexed citations
6.
Han, Wooseok, Daniel L. Menezes, Yongjin Xu, et al.. (2016). Discovery of imidazo[1,2-a]-pyridine inhibitors of pan-PI3 kinases that are efficacious in a mouse xenograft model. Bioorganic & Medicinal Chemistry Letters. 26(3). 742–746. 20 indexed citations
7.
Hoegenauer, Klemens, Nicolas Soldermann, Frédéric Stauffer, et al.. (2016). Discovery and Pharmacological Characterization of Novel Quinazoline-Based PI3K Delta-Selective Inhibitors. ACS Medicinal Chemistry Letters. 7(8). 762–767. 49 indexed citations
8.
Honda, Ayako, Edmund Harrington, Iván Cornella‐Taracido, et al.. (2015). Potent, Selective, and Orally Bioavailable Inhibitors of VPS34 Provide Chemical Tools to Modulate Autophagy in Vivo. ACS Medicinal Chemistry Letters. 7(1). 72–76. 40 indexed citations
9.
Fairhurst, Robin A., Marc Gerspacher, Patricia Imbach‐Weese, et al.. (2015). Identification and optimisation of 4,5-dihydrobenzo[1,2-d:3,4-d]bisthiazole and 4,5-dihydrothiazolo[4,5-h]quinazoline series of selective phosphatidylinositol-3 kinase alpha inhibitors. Bioorganic & Medicinal Chemistry Letters. 25(17). 3575–3581. 15 indexed citations
10.
Pecchi, Sabina, Zhi‐Jie Ni, Wooseok Han, et al.. (2013). Structure guided optimization of a fragment hit to imidazopyridine inhibitors of PI3K. Bioorganic & Medicinal Chemistry Letters. 23(16). 4652–4656. 6 indexed citations
11.
Furet, Pascal, Vito Guagnano, Robin A. Fairhurst, et al.. (2013). Discovery of NVP-BYL719 a potent and selective phosphatidylinositol-3 kinase alpha inhibitor selected for clinical evaluation. Bioorganic & Medicinal Chemistry Letters. 23(13). 3741–3748. 350 indexed citations
12.
Pecchi, Sabina, Paul A. Renhowe, Clarke Taylor, et al.. (2010). Identification and structure–activity relationship of 2-morpholino 6-(3-hydroxyphenyl) pyrimidines, a class of potent and selective PI3 kinase inhibitors. Bioorganic & Medicinal Chemistry Letters. 20(23). 6895–6898. 24 indexed citations
13.
Knapp, Mark, Cornelia Bellamacina, Jeremy Murray, & Dirksen E. Bussiere. (2006). Targeting Cancer: The Challenges and Successes of Structure-Based Drug Design Against the Human Purinome. Current Topics in Medicinal Chemistry. 6(11). 1129–1159. 13 indexed citations
14.
Segelke, Brent W., Mark Knapp, Saloumeh Kadkhodayan, Rod Balhorn, & Bernhard Rupp. (2004). Crystal structure of Clostridium botulinum neurotoxin protease in a product-bound state: Evidence for noncanonical zinc protease activity. Proceedings of the National Academy of Sciences. 101(18). 6888–6893. 77 indexed citations
15.
Bott, R., Gina Chan, Grant Ganshaw, et al.. (2003). Do Enzymes Change the Nature of Transition States? Mapping the Transition State for General Acid−Base Catalysis of a Serine Protease. Biochemistry. 42(36). 10545–10553. 16 indexed citations
16.
Krupka, Heike I., et al.. (2002). Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC‐IIα. Protein Science. 11(3). 642–651. 7 indexed citations
17.
Lightstone, Felice C., Anup K. Singh, M.C. Piqueras, et al.. (2000). Identification of Novel Small Molecule Ligands That Bind to Tetanus Toxin. Chemical Research in Toxicology. 13(5). 356–362. 25 indexed citations
18.
Morrow, Julie, Mark L. Segall, Sissel Lund‐Katz, et al.. (2000). Differences in Stability among the Human Apolipoprotein E Isoforms Determined by the Amino-Terminal Domain. Biochemistry. 39(38). 11657–11666. 274 indexed citations
19.
Kadkhodayan, Saloumeh, et al.. (2000). Cloning, Expression, and One-Step Purification of the Minimal Essential Domain of the Light Chain of Botulinum Neurotoxin Type A. Protein Expression and Purification. 19(1). 125–130. 23 indexed citations
20.
Forstner, Michael, Clare Peters‐Libeu, Yvonne M. Newhouse, et al.. (1999). Carboxyl-Terminal Domain of Human Apolipoprotein E: Expression, Purification, and Crystallization. Protein Expression and Purification. 17(2). 267–272. 25 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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