Mary A. Napier

4.6k total citations · 2 hit papers
44 papers, 3.9k citations indexed

About

Mary A. Napier is a scholar working on Molecular Biology, Pulmonary and Respiratory Medicine and Organic Chemistry. According to data from OpenAlex, Mary A. Napier has authored 44 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 7 papers in Pulmonary and Respiratory Medicine and 6 papers in Organic Chemistry. Recurrent topics in Mary A. Napier's work include Receptor Mechanisms and Signaling (9 papers), Heart Failure Treatment and Management (5 papers) and Chemical Synthesis and Analysis (5 papers). Mary A. Napier is often cited by papers focused on Receptor Mechanisms and Signaling (9 papers), Heart Failure Treatment and Management (5 papers) and Chemical Synthesis and Analysis (5 papers). Mary A. Napier collaborates with scholars based in United States, Belgium and Italy. Mary A. Napier's co-authors include I. Goldberg, Michael T. Lipari, Joseph M. DeSimone, Kevin P. Herlihy, James E. Bear, B M Fendly, J W McLean, Terry Lipari, Richard Vandlen and Axel Ullrich and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Mary A. Napier

44 papers receiving 3.6k citations

Hit Papers

PEGylated PRINT Nanoparti... 2011 2026 2016 2021 2012 2011 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mary A. Napier United States 29 1.8k 658 575 541 471 44 3.9k
David C. Turner United States 42 3.0k 1.6× 616 0.9× 342 0.6× 306 0.6× 425 0.9× 123 5.5k
John Hood United States 30 4.2k 2.3× 1.1k 1.7× 378 0.7× 448 0.8× 410 0.9× 56 7.2k
Gary R. Matsueda United States 38 2.5k 1.4× 442 0.7× 126 0.2× 1.2k 2.2× 122 0.3× 116 5.7k
In-San Kim South Korea 36 2.1k 1.1× 535 0.8× 967 1.7× 265 0.5× 886 1.9× 68 3.8k
Cora‐Ann Schoenenberger Switzerland 31 1.9k 1.0× 491 0.7× 308 0.5× 148 0.3× 966 2.1× 84 4.3k
Andrew I. Minchinton Canada 30 2.0k 1.1× 1.4k 2.1× 824 1.4× 532 1.0× 1.4k 3.0× 103 5.1k
W. Gregory Roberts United States 24 2.5k 1.4× 784 1.2× 1.2k 2.1× 435 0.8× 1.7k 3.7× 30 5.5k
Nadia Carlesso United States 32 2.7k 1.5× 973 1.5× 523 0.9× 232 0.4× 538 1.1× 65 5.5k
Mirco Ponzoni Italy 44 3.4k 1.9× 1.2k 1.8× 669 1.2× 337 0.6× 546 1.2× 174 5.9k
Hiroaki Kodama Japan 32 2.3k 1.3× 1.0k 1.6× 152 0.3× 107 0.2× 166 0.4× 110 4.1k

Countries citing papers authored by Mary A. Napier

Since Specialization
Citations

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

Fields of papers citing papers by Mary A. Napier

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mary A. Napier. 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 Mary A. Napier. The network helps show where Mary A. Napier may publish in the future.

Co-authorship network of co-authors of Mary A. Napier

This figure shows the co-authorship network connecting the top 25 collaborators of Mary A. Napier. A scholar is included among the top collaborators of Mary A. Napier 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 Mary A. Napier. Mary A. Napier 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.
Napier, Mary A., et al.. (2023). Glial-mediated dysregulation of neurodevelopment in Fragile X Syndrome. International review of neurobiology. 173. 187–215. 3 indexed citations
2.
Bruinenberg, Marcel, et al.. (2014). Comparing the Hub-and-Spoke Model Practices of the LifeLines Study in the Netherlands and the H3Africa Initiative. Biopreservation and Biobanking. 12(1). 13–16. 4 indexed citations
3.
George, J., et al.. (2004). Comparison of Xilinx Virtex-II FPGA SEE Sensitivities to Protons and Heavy Ions. ESASP. 536. 273. 3 indexed citations
4.
Thomas, Robert, Allen E. Eckhardt, Mary A. Napier, et al.. (1999). The San Diego Conference Nucleic Acid Technologies in Disease Detection November 17–19, 1999. Clinical Chemistry. 45(11). 2047–2053. 1 indexed citations
5.
Lowe, John B., et al.. (1993). RGD-containing peptides inhibit adhesion of 293 cells transfected with GpIIb/IIIa to fibrinogen. Blood Coagulation & Fibrinolysis. 4(2). 255–262. 1 indexed citations
6.
Lu, Hua Rong, Herman K. Gold, Tsunehiro Yasuda, et al.. (1992). G4120, an Arg-Gly-Asp Containing Pentapeptide, Enhances Arterial Eversion Graft Recanalization with Recombinant Tissue-Type Plasminogen Activator in Dogs. Thrombosis and Haemostasis. 67(6). 686–691. 13 indexed citations
7.
Sarup, Jay, R. M. Johnson, K. L. King, et al.. (1991). Characterization of an anti-p185HER2 monoclonal antibody that stimulates receptor function and inhibits tumor cell growth.. PubMed. 1(2). 72–82. 142 indexed citations
8.
Moyle, Matthew, Mary A. Napier, & J W McLean. (1991). Cloning and expression of a divergent integrin subunit beta 8.. Journal of Biological Chemistry. 266(29). 19650–19658. 153 indexed citations
9.
10.
Fendly, B M, et al.. (1990). Characterization of murine monoclonal antibodies reactive to either the human epidermal growth factor receptor or HER2/neu gene product.. PubMed. 50(5). 1550–8. 348 indexed citations
11.
Bodary, Sarah, Mary A. Napier, & J W McLean. (1989). Expression of recombinant platelet glycoprotein IIbIIIa results in a functional fibrinogen-binding complex. Journal of Biological Chemistry. 264(32). 18859–18862. 73 indexed citations
12.
Maegawa, Hiroshi, Donald A. McClain, Gary R. Freidenberg, et al.. (1988). Properties of a human insulin receptor with a COOH-terminal truncation. II. Truncated receptors have normal kinase activity but are defective in signaling metabolic effects.. Journal of Biological Chemistry. 263(18). 8912–8917. 126 indexed citations
13.
Napier, Mary A., et al.. (1987). Epidermal growth factor receptor tyrosine kinase phosphorylation of glucose-6-phosphate dehydrogenase in vitro. Archives of Biochemistry and Biophysics. 259(2). 296–304. 13 indexed citations
14.
Vandlen, Richard, Karen E. Arcuri, & Mary A. Napier. (1985). Identification of a receptor for atrial natriuretic factor in rabbit aorta membranes by affinity cross-linking.. Journal of Biological Chemistry. 260(20). 10889–10892. 77 indexed citations
15.
Napier, Mary A., Richard Vandlen, G. Albers‐Schönberg, et al.. (1984). Specific membrane receptors for atrial natriuretic factor in renal and vascular tissues.. Proceedings of the National Academy of Sciences. 81(19). 5946–5950. 227 indexed citations
16.
Napier, Mary A., Barton Holmquist, Daniël J. Strydom, & I. Goldberg. (1981). Neocarzinostatin chromophore: purification of the major active form and characterization of its spectral and biological properties. Biochemistry. 20(19). 5602–5608. 34 indexed citations
17.
ALBERS-SCHÖNBERG, GEORG, Ray S. Dewey, Otto D. Hensens, et al.. (1980). Neocarzinostatin: Chemical characterization and partial structure of the non-protein chromophore. Biochemical and Biophysical Research Communications. 95(3). 1351–1356. 42 indexed citations
18.
Goldberg, I., Takumi Hatayama, Lizzy S. Kappen, & Mary A. Napier. (1980). DNA as a Target for a Protein Antibiotic: Molecular Basis of Action. PubMed. 32. 308–322. 1 indexed citations
19.
Napier, Mary A., Barton Holmquist, Daniël J. Strydom, & I. Goldberg. (1979). Neocarzinostatin: Spectral characterization and separation of a non-protein chromophore. Biochemical and Biophysical Research Communications. 89(2). 635–642. 142 indexed citations
20.
Napier, Mary A. & Nortin M. Hadler. (1978). Effect of calcium on structure and function of a hyaluronic acid matrix: Carbon-13 nuclear magnetic resonance analysis and the diffusional behavior of small solutes. Proceedings of the National Academy of Sciences. 75(5). 2261–2265. 33 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026