David Meininger

1.5k total citations
22 papers, 1.2k citations indexed

About

David Meininger is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Hematology. According to data from OpenAlex, David Meininger has authored 22 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 5 papers in Radiology, Nuclear Medicine and Imaging and 5 papers in Hematology. Recurrent topics in David Meininger's work include Blood Coagulation and Thrombosis Mechanisms (5 papers), Monoclonal and Polyclonal Antibodies Research (5 papers) and Enzyme Structure and Function (3 papers). David Meininger is often cited by papers focused on Blood Coagulation and Thrombosis Mechanisms (5 papers), Monoclonal and Polyclonal Antibodies Research (5 papers) and Enzyme Structure and Function (3 papers). David Meininger collaborates with scholars based in United States, Canada and Switzerland. David Meininger's co-authors include Elizabeth A. Komives, Christopher E. White, Sophia Siu, Nigel P.C. Walker, Michael J. Hunter, Maurizio Pellecchia, Daniel S. Sem, R M Jack, Brian P. Lipsky and Molly D. Smithgall and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

David Meininger

22 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
David Meininger United States	19	689	216	192	165	124	22	1.2k
James P. Thomas United States	17	781 1.1×	120 0.6×	86 0.4×	100 0.6×	350 2.8×	30	1.6k
Nobuya Ishii United States	20	1.4k 2.0×	197 0.9×	47 0.2×	162 1.0×	802 6.5×	49	2.2k
Takumi Shiraishi Japan	22	1.4k 2.1×	373 1.7×	67 0.3×	165 1.0×	390 3.1×	94	2.1k
Sang Min Lim South Korea	19	948 1.4×	56 0.3×	63 0.3×	36 0.2×	281 2.3×	50	1.5k
Qiong Wu China	20	820 1.2×	86 0.4×	66 0.3×	224 1.4×	248 2.0×	92	1.5k
Johannes Kreuzer United States	15	801 1.2×	242 1.1×	35 0.2×	140 0.8×	277 2.2×	25	1.5k
Zhi‐Guang Huang China	19	1.5k 2.1×	197 0.9×	74 0.4×	180 1.1×	246 2.0×	110	2.3k
Anilkumar Gopalakrishnapillai United States	18	747 1.1×	113 0.5×	233 1.2×	74 0.4×	256 2.1×	64	1.4k
Yutaka Emoto United States	15	1.4k 2.0×	253 1.2×	45 0.2×	57 0.3×	295 2.4×	18	1.7k
Kenichi Higashino Japan	24	775 1.1×	420 1.9×	61 0.3×	218 1.3×	115 0.9×	35	1.6k

Countries citing papers authored by David Meininger

Since Specialization

Citations

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

Fields of papers citing papers by David Meininger

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Meininger

This figure shows the co-authorship network connecting the top 25 collaborators of David Meininger. A scholar is included among the top collaborators of David Meininger 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 David Meininger. David Meininger is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Hamblett, Kevin J., Carl J. Kozlosky, Sophia Siu, et al.. (2015). AMG 595, an Anti-EGFRvIII Antibody–Drug Conjugate, Induces Potent Antitumor Activity against EGFRvIII-Expressing Glioblastoma. Molecular Cancer Therapeutics. 14(7). 1614–1624. 82 indexed citations

Gunawardane, Ruwanthi N., Derek E. Piper, Sophia Siu, et al.. (2015). Agonistic Human Antibodies Binding to Lecithin-Cholesterol Acyltransferase Modulate High Density Lipoprotein Metabolism. Journal of Biological Chemistry. 291(6). 2799–2811. 25 indexed citations

Piper, Derek E., William G. Romanow, Ruwanthi N. Gunawardane, et al.. (2015). The high-resolution crystal structure of human LCAT. Journal of Lipid Research. 56(9). 1711–1719. 37 indexed citations

Wang, Zhulun, Xiaoshan Min, Shou-Hua Xiao, et al.. (2013). Molecular Basis of Sphingosine Kinase 1 Substrate Recognition and Catalysis. Structure. 21(5). 798–809. 146 indexed citations

Yang, Xiaoyu, Wei Xu, Sabrina A. Benchaar, et al.. (2013). Developability studies before initiation of process development. mAbs. 5(5). 787–794. 90 indexed citations

Meininger, David, Leeanne Zalameda, Yichin Liu, et al.. (2011). Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814(12). 1947–1954. 88 indexed citations

Pearson, Josh T., Sophia Siu, David Meininger, Larry C. Wienkers, & Dan A. Rock. (2010). In Vitro Modulation of Cytochrome P450 Reductase Supported Indoleamine 2,3-Dioxygenase Activity by Allosteric Effectors Cytochromeb₅and Methylene Blue. Biochemistry. 49(12). 2647–2656. 24 indexed citations

Carter, Jane, Jue Zhang, Haruki Hasegawa, et al.. (2009). Fusion partners can increase the expression of recombinant interleukins via transient transfection in 2936E cells. Protein Science. 19(2). 357–362. 22 indexed citations

Palmer, Gaby, Brian P. Lipsky, Molly D. Smithgall, et al.. (2008). The IL-1 receptor accessory protein (AcP) is required for IL-33 signaling and soluble AcP enhances the ability of soluble ST2 to inhibit IL-33. Cytokine. 42(3). 358–364. 150 indexed citations

10.

Tu, Hua, Jay P. Powers, Jinsong Liu, et al.. (2008). Distinctive molecular inhibition mechanisms for selective inhibitors of human 11β-hydroxysteroid dehydrogenase type 1. Bioorganic & Medicinal Chemistry. 16(19). 8922–8931. 30 indexed citations

11.

Herter, Sylvia, Derek E. Piper, Wade H. Aaron, et al.. (2005). Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers. Biochemical Journal. 390(1). 125–136. 152 indexed citations

12.

Sem, Daniel S., Stephen M. Coutts, Qing Dong, et al.. (2004). Systems-Based Design of Bi-Ligand Inhibitors of Oxidoreductases. Chemistry & Biology. 11(2). 185–194. 29 indexed citations

13.

Pellecchia, Maurizio, et al.. (2002). NMR-based structural characterization of large protein-ligand interactions. Journal of Biomolecular NMR. 22(2). 165–173. 86 indexed citations

14.

Meininger, David, Mark Rance, Melissa A. Starovasnik, Wayne J. Fairbrother, & Nicholas J. Skelton. (2000). Characterization of the Binding Interface between the E-Domain of Staphylococcal Protein A and an Antibody Fv-Fragment. Biochemistry. 39(6). 1541–1541. 1 indexed citations

15.

Meininger, David, Mark Rance, Melissa A. Starovasnik, Wayne J. Fairbrother, & Nicholas J. Skelton. (1999). Characterization of the Binding Interface between the E-Domain of Staphylococcal Protein A and an Antibody Fv-Fragment. Biochemistry. 39(1). 26–36. 23 indexed citations

16.

Gleeson, Martin A., Christopher E. White, David Meininger, & Elizabeth A. Komives. (1998). Generation of Protease-Deficient Strains and Their Use in Heterologous Protein Expression. Methods in molecular biology. 103. 81–94. 72 indexed citations

17.

Hunter, Michael J., et al.. (1997). Structure of the fifth EGF-like domain of thrombomodulin: an EGF-like domain with a novel disulfide-bonding pattern 1 1Edited by P. E. Wright. Journal of Molecular Biology. 273(4). 913–926. 26 indexed citations

18.

Meininger, David, Michael J. Hunter, & Elizabeth A. Komives. (1995). Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin. Protein Science. 4(9). 1683–1695. 17 indexed citations

19.

Lougheed, Julie C., et al.. (1995). Thrombin inhibition by cyclic peptides from thrombomodulin. Protein Science. 4(4). 773–780. 14 indexed citations

20.

White, Christopher E., et al.. (1995). Large-scale expression, purification and characterization of small fragments of thrombomodulin: the roles of the sixth domain and of methionine 388. Protein Engineering Design and Selection. 8(11). 1177–1187. 59 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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