David L. Budd

1.0k total citations
16 papers, 864 citations indexed

About

David L. Budd is a scholar working on Cell Biology, Molecular Biology and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, David L. Budd has authored 16 papers receiving a total of 864 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Cell Biology, 11 papers in Molecular Biology and 3 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in David L. Budd's work include Hemoglobin structure and function (13 papers), Protein Structure and Dynamics (7 papers) and Electron Spin Resonance Studies (3 papers). David L. Budd is often cited by papers focused on Hemoglobin structure and function (13 papers), Protein Structure and Dynamics (7 papers) and Electron Spin Resonance Studies (3 papers). David L. Budd collaborates with scholars based in United States, Japan and Germany. David L. Budd's co-authors include Gerd N. La Mar, Kevin M. Smith, Kevin C. Langry, G. N. LA MAR, Thomas G. Spiro, So Yung Choi, Harold M. Goff, David B. Viscio, K. Gersonde and H. Sick and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Biochemistry.

In The Last Decade

David L. Budd

16 papers receiving 778 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David L. Budd United States 12 628 506 191 166 166 16 864
J. G. Beetlestone Nigeria 15 635 1.0× 436 0.9× 256 1.3× 193 1.2× 74 0.4× 37 867
Bernard Alpert France 21 654 1.0× 890 1.8× 185 1.0× 127 0.8× 190 1.1× 68 1.3k
Yi Dou United States 18 810 1.3× 710 1.4× 195 1.0× 282 1.7× 96 0.6× 21 1.1k
George N. Phillips United States 4 561 0.9× 577 1.1× 124 0.6× 166 1.0× 114 0.7× 6 749
Karen D. Egeberg United States 10 1.0k 1.6× 900 1.8× 269 1.4× 283 1.7× 98 0.6× 10 1.3k
Masako Nagai Japan 17 477 0.8× 449 0.9× 147 0.8× 180 1.1× 70 0.4× 45 794
Vandna Sharma United States 13 507 0.8× 538 1.1× 194 1.0× 457 2.8× 97 0.6× 27 1.1k
Nai Teng Yu Hong Kong 11 353 0.6× 379 0.7× 106 0.6× 89 0.5× 128 0.8× 13 612
George V. Woodrow United States 8 291 0.5× 287 0.6× 98 0.5× 71 0.4× 106 0.6× 9 456
E. W. Findsen United States 14 327 0.5× 325 0.6× 68 0.4× 90 0.5× 201 1.2× 39 649

Countries citing papers authored by David L. Budd

Since Specialization
Citations

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

Fields of papers citing papers by David L. Budd

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David L. Budd

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

All Works

16 of 16 papers shown
1.
Mar, Gerd N. La, Robert D. Johnson, Jón Hauksson, et al.. (1993). Nuclear magnetic resonance investigation of the electronic structure of deoxymyoglobin. Journal of the American Chemical Society. 115(10). 3869–3876. 18 indexed citations
2.
Mar, Gerd N. La, et al.. (1989). Proton NMR study of the influence on iron oxidation/ligation/spin state on the heme orientational preference in myoglobin. Biochemical and Biophysical Research Communications. 158(2). 462–468. 9 indexed citations
3.
Choi, So Yung, Thomas G. Spiro, Kevin C. Langry, et al.. (1982). Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins. Journal of the American Chemical Society. 104(16). 4345–4351. 270 indexed citations
4.
Mar, Gerd N. La, Richard R. Anderson, David L. Budd, et al.. (1981). Proton nuclear magnetic resonance investigation of the nature of solution conformational equilibriums of monomeric insect deoxyhemoglobins. Biochemistry. 20(15). 4429–4436. 30 indexed citations
5.
Mar, Gerd N. La, David L. Budd, Kevin M. Smith, & Kevin C. Langry. (1980). Nuclear magnetic resonance of high-spin ferric hemoproteins. Assignment of proton resonances in met-aquo myoglobins using deuterium-labeled hemes. Journal of the American Chemical Society. 102(6). 1822–1827. 76 indexed citations
6.
MAR, G. N. LA, David L. Budd, Kevin M. Smith, & Kevin C. Langry. (1980). ChemInform Abstract: NUCLEAR MAGNETIC RESONANCE OF HIGH‐SPIN FERRIC HEMOPROTEINS. ASSIGNMENT OF PROTON RESONANCES IN MET‐AQUO MYOGLOBINS USING DEUTERIUM‐LABELED HEMES. Chemischer Informationsdienst. 11(25). 3 indexed citations
7.
Mar, Gerd N. La, David L. Budd, & Kevin M. Smith. (1980). Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins. Biochimica et Biophysica Acta (BBA) - Protein Structure. 622(2). 210–218. 24 indexed citations
8.
Mar, Gerd N. La, Kiyoshi Nagai, Thomas Jue, et al.. (1980). Assignment of proximal histidyl imidazole exchangeable proton NMR resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee. Biochemical and Biophysical Research Communications. 96(3). 1172–1177. 38 indexed citations
9.
Mar, Gerd N. La & David L. Budd. (1979). Proton NMR study of model substrate binding in hemoproteins. Intercalation of mercuric triiodide in sperm whale met-aquo myoglobin. Biochimica et Biophysica Acta (BBA) - Protein Structure. 581(2). 201–209. 5 indexed citations
10.
Budd, David L., et al.. (1979). Proton NMR study of high-spin ferric natural porphyrin derivatives as models of methemoproteins. Journal of the American Chemical Society. 101(20). 6091–6096. 75 indexed citations
11.
MAR, G. N. LA, David L. Budd, David B. Viscio, Kevin M. Smith, & Kevin C. Langry. (1978). Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins.. Proceedings of the National Academy of Sciences. 75(12). 5755–5759. 125 indexed citations
12.
Mar, Gerd N. La, David B. Viscio, David L. Budd, & K. Gersonde. (1978). Carbon-13-iron-57 spin coupling as a new structural probe on hemoproteins. Carbon-13 nmr spectrum of iron-57-enriched carbonyl myoglobin. Biochemical and Biophysical Research Communications. 82(1). 19–23. 13 indexed citations
13.
Mar, Gerd N. La, David L. Budd, H. Sick, & K. Gersonde. (1978). Acid Bohr effects in myoglobin characterized by proton NMR hyperfine shifts and oxygen binding studies. Biochimica et Biophysica Acta (BBA) - Protein Structure. 537(2). 270–283. 37 indexed citations
14.
Mar, Gerd N. La, David L. Budd, & Harold M. Goff. (1977). Assignment of proximal histidine proton nmr peaks in myoglobin and hemoglobin. Biochemical and Biophysical Research Communications. 77(1). 104–110. 93 indexed citations
15.
Hsieh, D.P.H., et al.. (1975). 13C nuclear magnetic resonance spectra of aflatoxin B1 derived from acetate. Tetrahedron. 31(7). 661–663. 8 indexed citations
16.
Mar, Gerd N. La & David L. Budd. (1974). Elucidation of the solution conformation of the A ring in vitamin D using proton coupling constants and a shift reagent. Journal of the American Chemical Society. 96(23). 7317–7324. 40 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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