David Hayes

1.4k total citations
32 papers, 967 citations indexed

About

David Hayes is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Biomedical Engineering. According to data from OpenAlex, David Hayes has authored 32 papers receiving a total of 967 indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 10 papers in Radiology, Nuclear Medicine and Imaging and 6 papers in Biomedical Engineering. Recurrent topics in David Hayes's work include Protein purification and stability (11 papers), Monoclonal and Polyclonal Antibodies Research (10 papers) and Muscle Physiology and Disorders (5 papers). David Hayes is often cited by papers focused on Protein purification and stability (11 papers), Monoclonal and Polyclonal Antibodies Research (10 papers) and Muscle Physiology and Disorders (5 papers). David Hayes collaborates with scholars based in United States, Germany and France. David Hayes's co-authors include Walter F. Stafford, Roberto Domínguez, Grzegorz Rębowski, Małgorzata Boczkowska, V. di Napoli, Ikuko Fujiwara, David Chéreau, Aneta Skwarek‐Maruszewska, Philip Graceffa and Thomas D. Pollard and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

David Hayes

32 papers receiving 951 citations

Peers

David Hayes
James J. Hartman United States
Elena G. Yarmola United States
Venkaiah Betapudi United States
Xiangduo Kong United States
Pamela E. Hoppe United States
Sari Tojkander Finland
Joseph F. Kelleher United States
Kenji Tatematsu Japan
Marisan Mejillano United States
Anne L. Hitt United States
James J. Hartman United States
David Hayes
Citations per year, relative to David Hayes David Hayes (= 1×) peers James J. Hartman

Countries citing papers authored by David Hayes

Since Specialization
Citations

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

Fields of papers citing papers by David Hayes

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Hayes

This figure shows the co-authorship network connecting the top 25 collaborators of David Hayes. A scholar is included among the top collaborators of David Hayes 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 Hayes. David Hayes 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.
Bou-Assaf, George M., Michael Brenowitz, Eric S. Day, et al.. (2022). Best Practices for Aggregate Quantitation of Antibody Therapeutics by Sedimentation Velocity Analytical Ultracentrifugation. Journal of Pharmaceutical Sciences. 111(7). 2121–2133. 15 indexed citations
2.
Hayes, David & David Dobnik. (2022). Commentary: Multiplex dPCR and SV-AUC are Promising Assays to Robustly Monitor the Critical Quality Attribute of AAV Drug Product Integrity. Journal of Pharmaceutical Sciences. 111(8). 2143–2148. 11 indexed citations
3.
Wei, Yangjie, et al.. (2021). Determination of the SLAMF1 self-association affinity constant with sedimentation velocity ultracentrifugation. Analytical Biochemistry. 633. 114410–114410. 1 indexed citations
4.
Batys, Piotr, et al.. (2020). Analyzing the weak dimerization of a cellulose binding module by analytical ultracentrifugation. International Journal of Biological Macromolecules. 163. 1995–2004. 10 indexed citations
5.
Stafford, Walter F., et al.. (2018). Pre-clinical Biophysical Characterization of Therapeutic Antibodies in Human Serum by Analytical Ultracentrifugation. Biophysical Journal. 114(3). 64a–65a. 2 indexed citations
6.
Hayes, David, et al.. (2018). Characterization of therapeutic antibodies in the presence of human serum proteins by AU-FDS analytical ultracentrifugation. Analytical Biochemistry. 550. 72–83. 28 indexed citations
7.
Correia, John J., et al.. (2018). AUC Measurements of Diffusion Coefficients of Monoclonal Antibodies in the Presence of Human Serum Proteins. Biophysical Journal. 114(3). 62a–62a. 3 indexed citations
8.
Zhou, Yu, Neel Sharma, Priyanka Gupta, et al.. (2016). GDF11 Treatment Attenuates the Recovery of Skeletal Muscle Function After Injury in Older Rats. The AAPS Journal. 19(2). 431–437. 22 indexed citations
9.
Padyana, Anil K., et al.. (2016). Crystal structure of human GDF11. Acta Crystallographica Section F Structural Biology Communications. 72(3). 160–164. 22 indexed citations
10.
Esfandiary, Reza, David Hayes, Arun Parupudi, et al.. (2013). A systematic multitechnique approach for detection and characterization of reversible self-association during formulation development of therapeutic antibodies. Journal of Pharmaceutical Sciences. 102(9). 3089–3099. 27 indexed citations
11.
Fowler, Susan B., Kenneth G. Miller, David Hayes, et al.. (2013). Monovalent IgG4 molecules. mAbs. 5(3). 406–417. 12 indexed citations
12.
Esfandiary, Reza, David Hayes, Arun Parupudi, et al.. (2012). A Systematic Multitechnique Approach for Detection and Characterization of Reversible Self-Association during Formulation Development of Therapeutic Antibodies. Journal of Pharmaceutical Sciences. 102(1). 62–72. 40 indexed citations
13.
Li, Yi‐Ming, et al.. (2011). Characterization of the Self-Association of Human Interferon-α2b, Albinterferon-α2b, and Pegasys. Journal of Pharmaceutical Sciences. 101(1). 68–80. 17 indexed citations
14.
Campbell, Mel, Wen‐Rong Lie, Jing Zhao, et al.. (2010). Multiplex Analysis of Src Family Kinase Signaling by Microbead Suspension Arrays. Assay and Drug Development Technologies. 8(4). 488–496. 5 indexed citations
15.
Boczkowska, Małgorzata, Grzegorz Rębowski, Maxim V. Petoukhov, et al.. (2008). X-Ray Scattering Study of Activated Arp2/3 Complex with Bound Actin-WCA. Structure. 16(5). 695–704. 61 indexed citations
16.
Lee, Sung Haeng, David Hayes, Grzegorz Rębowski, Isabelle Tardieux, & Roberto Domínguez. (2007). Toxofilin from Toxoplasma gondii forms a ternary complex with an antiparallel actin dimer. Proceedings of the National Academy of Sciences. 104(41). 16122–16127. 25 indexed citations
17.
18.
Lee, Sung Haeng, Astrid Weins, David Hayes, Martin R. Pollak, & Roberto Domínguez. (2007). Crystal Structure of the Actin-Binding Domain of α-Actinin-4 Lys255Glu Mutant Implicated in Focal Segmental Glomerulosclerosis. Journal of Molecular Biology. 376(2). 317–324. 29 indexed citations
19.
Ridgeway, Theresa M., et al.. (1998). An apparatus for membrane‐confined analytical electrophoresis. Electrophoresis. 19(10). 1611–1619. 16 indexed citations
20.
Hayes, David. (1993). Equilibrium electrophoresis: Results from the second prototype. University of New Hampshire Scholars Repository (University of New Hampshire at Manchester). 3 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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