David H. Margulies

11.3k total citations · 2 hit papers
179 papers, 9.4k citations indexed

About

David H. Margulies is a scholar working on Immunology, Radiology, Nuclear Medicine and Imaging and Molecular Biology. According to data from OpenAlex, David H. Margulies has authored 179 papers receiving a total of 9.4k indexed citations (citations by other indexed papers that have themselves been cited), including 141 papers in Immunology, 58 papers in Radiology, Nuclear Medicine and Imaging and 49 papers in Molecular Biology. Recurrent topics in David H. Margulies's work include Immune Cell Function and Interaction (95 papers), T-cell and B-cell Immunology (95 papers) and Immunotherapy and Immune Responses (65 papers). David H. Margulies is often cited by papers focused on Immune Cell Function and Interaction (95 papers), T-cell and B-cell Immunology (95 papers) and Immunotherapy and Immune Responses (65 papers). David H. Margulies collaborates with scholars based in United States, Japan and Israel. David H. Margulies's co-authors include Ronald N. Germain, Kannan Natarajan, Lisa F. Boyd, Matthew D. Scharff, Roy A. Mariuzza, Malcolm L. Gefter, Glen A. Evans, J G Seidman, Steven Kozlowski and Maripat Corr and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

David H. Margulies

173 papers receiving 9.0k citations

Hit Papers

The Biochemistry and Cell... 1977 2026 1993 2009 1993 1977 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David H. Margulies United States 54 6.9k 2.9k 1.8k 1.0k 906 179 9.4k
John E. Coligan United States 56 6.1k 0.9× 2.3k 0.8× 1.5k 0.8× 1.3k 1.3× 952 1.1× 186 9.1k
Olaf Rötzschke Germany 42 6.8k 1.0× 2.8k 1.0× 1.1k 0.6× 1.2k 1.1× 1.1k 1.2× 104 9.3k
Kirsten Falk Germany 39 7.0k 1.0× 2.8k 1.0× 1.2k 0.7× 1.1k 1.0× 999 1.1× 75 8.8k
Susan K. Pierce United States 53 5.8k 0.8× 3.1k 1.1× 1.2k 0.6× 650 0.6× 815 0.9× 154 9.5k
Yueh‐hsiu Chien United States 46 6.5k 0.9× 1.9k 0.7× 1.5k 0.8× 1.5k 1.5× 641 0.7× 78 8.7k
J L Strominger United States 51 6.4k 0.9× 3.1k 1.1× 1.8k 1.0× 1.1k 1.0× 989 1.1× 101 9.9k
H M Grey United States 48 6.5k 0.9× 3.0k 1.0× 2.4k 1.3× 745 0.7× 1.2k 1.3× 92 8.6k
Ellen S. Vitetta United States 58 6.9k 1.0× 3.7k 1.3× 3.3k 1.8× 1.9k 1.9× 659 0.7× 250 11.4k
Joan C. Gorga United States 28 5.8k 0.9× 2.5k 0.9× 1.9k 1.0× 420 0.4× 640 0.7× 40 8.2k
Mark A. Saper United States 30 6.4k 0.9× 4.7k 1.6× 1.5k 0.8× 654 0.6× 636 0.7× 51 10.7k

Countries citing papers authored by David H. Margulies

Since Specialization
Citations

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

Fields of papers citing papers by David H. Margulies

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David H. Margulies

This figure shows the co-authorship network connecting the top 25 collaborators of David H. Margulies. A scholar is included among the top collaborators of David H. Margulies 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 H. Margulies. David H. Margulies 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.
Margulies, David H., Jiansheng Jiang, Javeed Ahmad, Lisa F. Boyd, & Kannan Natarajan. (2023). Chaperone function in antigen presentation by MHC class I molecules—tapasin in the PLC and TAPBPR beyond. Frontiers in Immunology. 14. 1179846–1179846. 8 indexed citations
2.
Jiang, Jiansheng, Kannan Natarajan, Lisa F. Boyd, et al.. (2017). Crystal structure of a TAPBPR–MHC I complex reveals the mechanism of peptide editing in antigen presentation. Science. 358(6366). 1064–1068. 93 indexed citations
3.
Morozov, Giora I., Huaying Zhao, Michael G. Mage, et al.. (2016). Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing. Proceedings of the National Academy of Sciences. 113(8). E1006–15. 68 indexed citations
4.
Sgourakis, Nikolaos G., et al.. (2015). A Novel MHC-I Surface Targeted for Binding by the MCMV m06 Immunoevasin Revealed by Solution NMR. Journal of Biological Chemistry. 290(48). 28857–28868. 9 indexed citations
5.
Yokoyama, Wayne M., Amy Reichlin, David H. Margulies, & Hamish R.C. Smith. (2015). MHC Class I-Dependent and -Independent NK Cell Specificity. Chemical immunology/Fortschritte der Allergielehre/Progress in allergy/Chemical immunology and allergy. 64. 1–18.
6.
Mage, Michael G., Michael Dolan, Rui Wang, et al.. (2012). The Peptide-Receptive Transition State of MHC Class I Molecules: Insight from Structure and Molecular Dynamics. The Journal of Immunology. 189(3). 1391–1399. 55 indexed citations
7.
Tilahun, Mulualem E., Alan C. Kwan, Kannan Natarajan, et al.. (2011). Chimeric Anti-Staphylococcal Enterotoxin B Antibodies and Lovastatin Act Synergistically to Provide In Vivo Protection against Lethal Doses of SEB. PLoS ONE. 6(11). e27203–e27203. 12 indexed citations
8.
Wang, Rui, Kannan Natarajan, & David H. Margulies. (2009). Structural Basis of the CD8αβ/MHC Class I Interaction: Focused Recognition Orients CD8β to a T Cell Proximal Position. The Journal of Immunology. 183(4). 2554–2564. 87 indexed citations
9.
Tang, Xiaobin, Sriram Narayanan, Giovanna Peruzzi, et al.. (2009). A Single Residue, Arginine 65, Is Critical for the Functional Interaction of Leukocyte-Associated Inhibitory Receptor-1 with Collagens. The Journal of Immunology. 182(9). 5446–5452. 26 indexed citations
10.
Mans, Janet, Zhi Li, L. M. Smith, et al.. (2008). Structure and function of murine cytomegalovirus MHC-I-like molecules: how the virus turned the host defense to its advantage. Immunologic Research. 43(1-3). 264–279. 13 indexed citations
11.
Mans, Janet, Kannan Natarajan, Andrea Balbo, et al.. (2007). Cellular Expression and Crystal Structure of the Murine Cytomegalovirus Major Histocompatibility Complex Class I-like Glycoprotein, m153. Journal of Biological Chemistry. 282(48). 35247–35258. 21 indexed citations
12.
Dam, Julie, R. Guan, K. Natarajan, et al.. (2003). VARIABLE MHC CLASS I ENGAGEMENT BY LY49 NATURAL KILLER CELL RECEPTORS DEMONSTRATED BY THE CRYSTAL STRUCTURE OF LY49C BOUND TO H-2K(B). Langmuir. 20.
13.
Takahashi, Megumi, Yohko Nakagawa, Jian Wang, et al.. (2002). Rapid Induction of Apoptosis in CD8+ HIV-1 Envelope-Specific Murine CTLs by Short Exposure to Antigenic Peptide. The Journal of Immunology. 169(11). 6588–6593. 22 indexed citations
14.
Derby, Michael A., Jian Wang, David H. Margulies, & Jay A. Berzofsky. (2001). Two intermediate-avidity cytotoxic T lymphocyte clones with a disparity between functional avidity and MHC tetramer staining. International Immunology. 13(6). 817–824. 55 indexed citations
15.
Chung, Doo Hyun, Igor M. Belyakov, Michael A. Derby, et al.. (2001). Competitive Inhibition In Vivo and Skewing of the T Cell Repertoire of Antigen-Specific CTL Priming by an Anti-Peptide-MHC Monoclonal Antibody. The Journal of Immunology. 167(2). 699–707. 8 indexed citations
16.
Poláková, K, Daniel Plaksin, Doo Hyun Chung, et al.. (2000). Antibodies Directed Against the MHC-I Molecule H-2Dd Complexed with an Antigenic Peptide: Similarities to a T Cell Receptor with the Same Specificity. The Journal of Immunology. 165(10). 5703–5712. 27 indexed citations
17.
Margulies, David H.. (1997). Interactions of TCRs with MHC-peptide complexes: a quantitative basis for mechanistic models. Current Opinion in Immunology. 9(3). 390–395. 51 indexed citations
18.
Corr, Maripat, Lisa F. Boyd, Sam Frankel, et al.. (1992). Endogenous peptides of a soluble major histocompatibility complex class I molecule, H-2Lds: sequence motif, quantitative binding, and molecular modeling of the complex.. The Journal of Experimental Medicine. 176(6). 1681–1692. 132 indexed citations
19.
Kozlowski, Steven, Maripat Corr, Toshiyuki Takeshita, et al.. (1992). Serum angiotensin-1 converting enzyme activity processes a human immunodeficiency virus 1 gp160 peptide for presentation by major histocompatibility complex class I molecules.. The Journal of Experimental Medicine. 175(6). 1417–1422. 100 indexed citations
20.
McCluskey, James, T I Munitz, Lisa F. Boyd, et al.. (1988). Cell surface expression of the amino-terminal domain of A kappa  alpha. Recognition of an isolated MHC antigenic structure by allospecific T cells but not alloantibodies.. The Journal of Immunology. 140(6). 2081–2089. 9 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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