Edward A. Burstein

2.6k total citations · 1 hit paper
36 papers, 2.4k citations indexed

About

Edward A. Burstein is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Spectroscopy. According to data from OpenAlex, Edward A. Burstein has authored 36 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 8 papers in Cellular and Molecular Neuroscience and 8 papers in Spectroscopy. Recurrent topics in Edward A. Burstein's work include Protein Interaction Studies and Fluorescence Analysis (15 papers), Protein Structure and Dynamics (10 papers) and Hemoglobin structure and function (6 papers). Edward A. Burstein is often cited by papers focused on Protein Interaction Studies and Fluorescence Analysis (15 papers), Protein Structure and Dynamics (10 papers) and Hemoglobin structure and function (6 papers). Edward A. Burstein collaborates with scholars based in Russia, Belgium and Japan. Edward A. Burstein's co-authors include Eugene A. Permyakov, Yana K. Reshetnyak, Lina P. Kalinichenko, Charles Gerday, Isao Yamazaki, Yukiharu Sawada, Alexander B. Chetverin, V. A. Yashin, Alessandro Finazzi Agrò and S.Yu. Venyaminov and has published in prestigious journals such as Biochemical and Biophysical Research Communications, FEBS Letters and Biophysical Journal.

In The Last Decade

Edward A. Burstein

36 papers receiving 2.2k citations

Hit Papers

FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN P... 1973 2026 1990 2008 1973 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Edward A. Burstein Russia 19 1.7k 425 337 237 199 36 2.4k
Colin Blake United Kingdom 20 3.3k 1.9× 721 1.7× 381 1.1× 274 1.2× 214 1.1× 29 4.4k
Hugo L. Monaco Italy 31 2.2k 1.2× 487 1.1× 514 1.5× 189 0.8× 267 1.3× 84 3.4k
Howard L. Brockman United States 40 3.7k 2.1× 171 0.4× 416 1.2× 325 1.4× 202 1.0× 107 4.6k
Robert Simoni United States 28 2.5k 1.4× 408 1.0× 313 0.9× 197 0.8× 110 0.6× 209 3.4k
B. S. Hartley United Kingdom 24 2.3k 1.3× 562 1.3× 317 0.9× 350 1.5× 95 0.5× 46 3.5k
B S Hartley United Kingdom 20 2.4k 1.4× 449 1.1× 460 1.4× 477 2.0× 124 0.6× 28 3.5k
Yee‐Hsiung Chen Taiwan 19 1.9k 1.1× 263 0.6× 322 1.0× 210 0.9× 108 0.5× 33 2.7k
A. Ian Scott United States 39 3.2k 1.8× 727 1.7× 205 0.6× 322 1.4× 104 0.5× 237 4.7k
Robert M. Bock United States 32 3.2k 1.8× 280 0.7× 337 1.0× 350 1.5× 156 0.8× 92 4.2k
Betty J. Gaffney United States 28 1.3k 0.8× 270 0.6× 206 0.6× 241 1.0× 106 0.5× 68 2.6k

Countries citing papers authored by Edward A. Burstein

Since Specialization
Citations

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

Fields of papers citing papers by Edward A. Burstein

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Edward A. Burstein

This figure shows the co-authorship network connecting the top 25 collaborators of Edward A. Burstein. A scholar is included among the top collaborators of Edward A. Burstein 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 Edward A. Burstein. Edward A. Burstein 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.
Burstein, Edward A., et al.. (2008). Mechanisms involved in proteolytic degradation of globular proteins: The role of local and global fluctuations in the native structure. Molecular Biology. 42(2). 289–301. 1 indexed citations
3.
Linke, Dirk, Joachim Frank, Jürgen Soll, et al.. (2004). Folding Kinetics and Structure of OEP16. Biophysical Journal. 86(3). 1479–1487. 29 indexed citations
4.
Burstein, Edward A., et al.. (2001). Decomposition of Protein Tryptophan Fluorescence Spectra into Log-Normal Components. I. Decomposition Algorithms. Biophysical Journal. 81(3). 1699–1709. 95 indexed citations
5.
Reshetnyak, Yana K. & Edward A. Burstein. (2001). Decomposition of Protein Tryptophan Fluorescence Spectra into Log-Normal Components. II. The Statistical Proof of Discreteness of Tryptophan Classes in Proteins. Biophysical Journal. 81(3). 1710–1734. 127 indexed citations
7.
Andreev, Oleg A., et al.. (2000). The Identification of Tryptophan Residues Responsible for ATP-Induced Increase in Intrinsic Fluorescence of Myosin Subfragment 1. Journal of Biomolecular Structure and Dynamics. 18(1). 113–125. 12 indexed citations
8.
Reshetnyak, Yana K., et al.. (1999). Comparative Study of Recombinant Rat Nucleoside Diphosphate Kinases α and β By Intrinsic Protein Fluorescence. Journal of Biomolecular Structure and Dynamics. 16(4). 955–968. 6 indexed citations
10.
Burstein, Edward A., et al.. (1996). Log‐Normal Description of Fluorescence Spectra of Organic Fluorophores. Photochemistry and Photobiology. 64(2). 316–320. 122 indexed citations
11.
Permyakov, Eugene A., et al.. (1986). Conformational changes in the muscle proteins of cured beef during heating. Meat Science. 16(4). 297–305. 9 indexed citations
12.
Burstein, Edward A., et al.. (1985). Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy. Archives of Biochemistry and Biophysics. 240(2). 781–791. 9 indexed citations
13.
Permyakov, Eugene A., et al.. (1985). Cation binding effects on the pH, thermal and urea denaturation transitions in α-lactalbumin. Biophysical Chemistry. 21(1). 21–31. 110 indexed citations
14.
Kalinichenko, Lina P., et al.. (1983). Comparative study of physicochemical properties of two pike parvalbumins by means of their intrinsic tyrosyl and phenylalanyl fluorescence. Archives of Biochemistry and Biophysics. 227(1). 9–20. 18 indexed citations
15.
Permyakov, Eugene A., et al.. (1983). Sodium and potassium binding to parvalbumins measured by means of intrinsic protein fluorescence. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 749(2). 185–191. 12 indexed citations
16.
Permyakov, Eugene A., et al.. (1982). Intrinsic fluorescence spectra of a tryptophan-containing parvalbumin as a function of thermal, pH and urea denaturation. Biophysical Chemistry. 15(1). 19–26. 15 indexed citations
17.
Permyakov, Eugene A., et al.. (1981). Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Biochemical and Biophysical Research Communications. 100(1). 191–197. 113 indexed citations
18.
Burstein, Edward A., et al.. (1980). Some regularities of dynamic accessibility of buried fluorescent residues to external quenchers in proteins. Archives of Biochemistry and Biophysics. 204(1). 161–166. 27 indexed citations
19.
Burstein, Edward A., et al.. (1979). Study of some physicochemical properties of the neurotoxic complex and its components from the venom of bulgarian sand viper, Vipera ammodytes ammodytes. Biochimica et Biophysica Acta (BBA) - Protein Structure. 577(1). 44–51. 5 indexed citations
20.
Burstein, Edward A., et al.. (1973). FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULES. Photochemistry and Photobiology. 18(4). 263–279. 1068 indexed citations breakdown →

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