Henry D. Bellamy

1.7k total citations
40 papers, 1.4k citations indexed

About

Henry D. Bellamy is a scholar working on Molecular Biology, Materials Chemistry and Radiation. According to data from OpenAlex, Henry D. Bellamy has authored 40 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 21 papers in Materials Chemistry and 6 papers in Radiation. Recurrent topics in Henry D. Bellamy's work include Enzyme Structure and Function (18 papers), Protein Structure and Dynamics (10 papers) and Photosynthetic Processes and Mechanisms (8 papers). Henry D. Bellamy is often cited by papers focused on Enzyme Structure and Function (18 papers), Protein Structure and Dynamics (10 papers) and Photosynthetic Processes and Mechanisms (8 papers). Henry D. Bellamy collaborates with scholars based in United States, France and Japan. Henry D. Bellamy's co-authors include F. Scott Mathews, Edward H. Snell, Florence Lederer, P. H. Bethge, David B. Neau, Benjamin Perman, Craig W. Vander Kooi, Daniel J. Leahy, Louis W. Lim and Annie Glatigny and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Henry D. Bellamy

40 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Henry D. Bellamy United States 23 1.0k 400 168 167 111 40 1.4k
David E. Timm United States 27 1.2k 1.1× 434 1.1× 145 0.9× 147 0.9× 73 0.7× 49 2.0k
S.J. Harrop Australia 27 2.0k 2.0× 514 1.3× 194 1.2× 292 1.7× 148 1.3× 57 3.0k
Koji Inaka Japan 22 959 0.9× 541 1.4× 140 0.8× 121 0.7× 215 1.9× 75 1.6k
Timothy D. Fenn United States 23 1.2k 1.2× 442 1.1× 139 0.8× 327 2.0× 110 1.0× 30 1.8k
Herbert L. Axelrod United States 21 1.2k 1.2× 317 0.8× 151 0.9× 105 0.6× 79 0.7× 42 1.6k
Axel J. Scheidig Germany 26 1.8k 1.8× 368 0.9× 295 1.8× 452 2.7× 170 1.5× 79 2.5k
Christoph von Ballmoos Switzerland 30 2.0k 2.0× 172 0.4× 285 1.7× 134 0.8× 141 1.3× 69 2.6k
Salam Al‐Karadaghi Sweden 34 2.7k 2.7× 702 1.8× 250 1.5× 434 2.6× 94 0.8× 78 3.2k
M. Roy United States 26 1.7k 1.7× 577 1.4× 63 0.4× 116 0.7× 185 1.7× 69 2.6k
Antonio Dı́az-Quintana Spain 32 2.3k 2.2× 184 0.5× 278 1.7× 157 0.9× 98 0.9× 89 2.9k

Countries citing papers authored by Henry D. Bellamy

Since Specialization
Citations

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

Fields of papers citing papers by Henry D. Bellamy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Henry D. Bellamy. 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 Henry D. Bellamy. The network helps show where Henry D. Bellamy may publish in the future.

Co-authorship network of co-authors of Henry D. Bellamy

This figure shows the co-authorship network connecting the top 25 collaborators of Henry D. Bellamy. A scholar is included among the top collaborators of Henry D. Bellamy 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 Henry D. Bellamy. Henry D. Bellamy 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.
Frankel, Laurie K., Henry D. Bellamy, Larry Sallans, et al.. (2014). Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II. Proceedings of the National Academy of Sciences. 111(45). 16178–16183. 29 indexed citations
2.
Ruggli, Nicolas, Markus Gerber, Jon-Duri Tratschin, et al.. (2013). The Structure of Classical Swine Fever Virus Npro: A Novel Cysteine Autoprotease and Zinc-Binding Protein Involved in Subversion of Type I Interferon Induction. PLoS Pathogens. 9(10). e1003704–e1003704. 29 indexed citations
3.
Frankel, Laurie K., Larry Sallans, Henry D. Bellamy, et al.. (2013). Radiolytic Mapping of Solvent-Contact Surfaces in Photosystem II of Higher Plants. Journal of Biological Chemistry. 288(32). 23565–23572. 23 indexed citations
4.
Roy, Amitava, Eizi Morikawa, Henry D. Bellamy, et al.. (2010). Status of the Center for Advanced Microstructures and Devices (CAMD)—2010. Nuclear Instruments and Methods in Physics Research Section A Accelerators Spectrometers Detectors and Associated Equipment. 649(1). 15–18. 5 indexed citations
5.
Bellamy, Henry D., et al.. (2009). Crystal Structure of the GTPase-activating Protein-related Domain from IQGAP1. Journal of Biological Chemistry. 284(22). 14857–14865. 49 indexed citations
6.
Árnason, Úlfur, et al.. (2008). Conventionally stained and C-banded karyotypes of a female blue whale. Hereditas. 102(2). 251–253. 6 indexed citations
7.
Kooi, Craig W. Vander, et al.. (2007). Structural basis for ligand and heparin binding to neuropilin B domains. Proceedings of the National Academy of Sciences. 104(15). 6152–6157. 185 indexed citations
8.
Zhao, Yonghong, et al.. (2006). The crystal structure of the E. coli stress protein YciF. Protein Science. 15(11). 2605–2611. 22 indexed citations
9.
Bellamy, Henry D., et al.. (2005). Advances in digital topography for characterizing imperfections in protein crystals. Journal of Applied Crystallography. 38(3). 512–519. 7 indexed citations
10.
Soares, Alexei S., et al.. (2004). First results of digital topography applied to macromolecular crystals. Journal of Applied Crystallography. 37(3). 481–485. 8 indexed citations
11.
Snell, Edward H., et al.. (2003). Macromolecular Crystal Quality. Methods in enzymology on CD-ROM/Methods in enzymology. 368. 268–288. 16 indexed citations
12.
Zhao, Yonghong, et al.. (2003). The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites. Protein Science. 12(10). 2303–2311. 27 indexed citations
13.
Vahedi‐Faridi, Ardeschir, et al.. (2003). Physical and structural studies on the cryocooling of insulin crystals. Acta Crystallographica Section D Biological Crystallography. 59(12). 2169–2182. 10 indexed citations
14.
Vahedi‐Faridi, Ardeschir, et al.. (2001). A test of macromolecular crystallization in microgravity: large well ordered insulin crystals. Acta Crystallographica Section D Biological Crystallography. 57(8). 1204–1207. 31 indexed citations
15.
Bellamy, Henry D., et al.. (2000). The high-mosaicity illusion: revealing the true physical characteristics of macromolecular crystals. Acta Crystallographica Section D Biological Crystallography. 56(8). 986–995. 25 indexed citations
16.
Segelke, Brent W., Michael Forstner, S. Trakhanov, et al.. (2000). Conformational flexibility in the apolipoprotein E amino‐terminal domain structure determined from three new crystal forms: Implications for lipid binding. Protein Science. 9(5). 886–897. 41 indexed citations
17.
Fee, James A., Duncan E. McRee, Pamela A. Williams, et al.. (1999). The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution.. Nature Structural Biology. 6(6). 509–516. 105 indexed citations
18.
Crane, Brian R., Henry D. Bellamy, & E.D. Getzoff. (1997). Multiwavelength Anomalous Diffraction of Sulfite Reductase Hemoprotein: Making the Most of MAD Data. Acta Crystallographica Section D Biological Crystallography. 53(1). 8–22. 6 indexed citations
19.
Bellamy, Henry D., R. P. Phizackerley, S. Michael Soltis, & H. Hope. (1994). An open-flow cryogenic cooler for single-crystal diffraction experiments. Journal of Applied Crystallography. 27(6). 967–970. 8 indexed citations
20.
Mercolino, Thomas J., Henry D. Bellamy, & F. Scott Mathews. (1980). A preliminary crystallographic study of β-glucuronidase from rat preputial gland. Journal of Molecular Biology. 139(3). 557–560. 1 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

Breakdown of academic impact, for papers by David E. Timm Breakdown of academic impact, for papers by S.J. Harrop Breakdown of academic impact, for papers by Koji Inaka Breakdown of academic impact, for papers by Timothy D. Fenn Breakdown of academic impact, for papers by Herbert L. Axelrod Breakdown of academic impact, for papers by Axel J. Scheidig Breakdown of academic impact, for papers by Christoph von Ballmoos Breakdown of academic impact, for papers by Salam Al‐Karadaghi Breakdown of academic impact, for papers by M. Roy Breakdown of academic impact, for papers by Antonio Dı́az-Quintana
Rankless by CCL
2026