Joseph Kraut

9.0k total citations · 6 hit papers
55 papers, 7.8k citations indexed

About

Joseph Kraut is a scholar working on Molecular Biology, Materials Chemistry and Electrical and Electronic Engineering. According to data from OpenAlex, Joseph Kraut has authored 55 papers receiving a total of 7.8k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 17 papers in Materials Chemistry and 9 papers in Electrical and Electronic Engineering. Recurrent topics in Joseph Kraut's work include Enzyme Structure and Function (16 papers), Photosynthetic Processes and Mechanisms (15 papers) and DNA and Nucleic Acid Chemistry (9 papers). Joseph Kraut is often cited by papers focused on Enzyme Structure and Function (16 papers), Photosynthetic Processes and Mechanisms (15 papers) and DNA and Nucleic Acid Chemistry (9 papers). Joseph Kraut collaborates with scholars based in United States and United Kingdom. Joseph Kraut's co-authors include M.R. Sawaya, H. Pelletier, Samuel H. Wilson, Richard A. Alden, Amalendra Kumar, Christine Schubert Wright, Jens J. Birktoft, H Pelletier, Rajendra Prasad and J. Ernest Villafranca and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Joseph Kraut

55 papers receiving 7.4k citations

Hit Papers

STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYM... 1969 2026 1988 2007 1994 1992 1997 1994 1997 200 400 600

Peers

Joseph Kraut
Phil Evans United Kingdom
Raymond L. Blakley United States
J. Kraut United States
S.E. Ealick United States
B.C. Finzel United States
Simon E. V. Phillips United Kingdom
Duncan E. McRee United States
Pavol Skubák Netherlands
Phil Evans United Kingdom
Joseph Kraut
Citations per year, relative to Joseph Kraut Joseph Kraut (= 1×) peers Phil Evans

Countries citing papers authored by Joseph Kraut

Since Specialization
Citations

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

Fields of papers citing papers by Joseph Kraut

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Joseph Kraut

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph Kraut. A scholar is included among the top collaborators of Joseph Kraut 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 Joseph Kraut. Joseph Kraut 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.
Sawaya, M.R. & Joseph Kraut. (1997). Loop and Subdomain Movements in the Mechanism of Escherichia coli Dihydrofolate Reductase:  Crystallographic Evidence,. Biochemistry. 36(3). 586–603. 555 indexed citations breakdown →
2.
Beard, William A., Wendy P. Osheroff, Rajendra Prasad, et al.. (1996). Enzyme-DNA Interactions Required for Efficient Nucleotide Incorporation and Discrimination in Human DNA Polymerase β. Journal of Biological Chemistry. 271(21). 12141–12144. 155 indexed citations
4.
Miller, Mark A., Lois Geren, Gye Won Han, et al.. (1996). Identifying the Physiological Electron Transfer Site of Cytochrome c Peroxidase by Structure-Based Engineering. Biochemistry. 35(3). 667–673. 19 indexed citations
5.
Reyes, Vicente M., M.R. Sawaya, Katherine A. Brown, & Joseph Kraut. (1995). Isomorphous Crystal Structures of Escherichia coli Dihydrofolate Reductase Complexed with Folate, 5-Deazafolate, and 5,10-Dideazatetrahydrofolate: Mechanistic Implications. Biochemistry. 34(8). 2710–2723. 63 indexed citations
6.
Hahm, Seung, Mark A. Miller, Lois Geren, et al.. (1994). Reaction of Horse Cytochrome c with the Radical and the Oxyferryl Heme in Cytochrome c Peroxidase Compound I. Biochemistry. 33(6). 1473–1480. 27 indexed citations
7.
McTigue, Michele, Jay F. Davies, Bernard T. Kaufman, & Joseph Kraut. (1992). Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin. Biochemistry. 31(32). 7264–7273. 61 indexed citations
8.
Vitello, Lidia B., James E. Erman, Mark A. Miller, J. Matthew Mauro, & Joseph Kraut. (1992). Effect of Asp-235 .fwdarw. Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase. Biochemistry. 31(46). 11524–11535. 46 indexed citations
9.
Brown, Katherine A. & Joseph Kraut. (1992). Exploring the molecular mechanism of dihydrofolate reductase. Faraday Discussions. 93(93). 217–217. 41 indexed citations
10.
Fishel, Laurence A., J. Matthew Mauro, Mark A. Miller, et al.. (1991). Compound I radical in site-directed mutants of cytochrome c peroxidase as probed by electron paramagnetic resonance and electron-nuclear double resonance. Biochemistry. 30(7). 1986–1996. 88 indexed citations
11.
Bystroff, Christopher & Joseph Kraut. (1991). Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry. 30(8). 2227–2239. 169 indexed citations
12.
Bajorath, Jürgen, David H. Kitson, George Fitzgerald, et al.. (1991). Electron redistribution on binding of a substrate to an enzyme: Folate and dihydrofolate reductase. Proteins Structure Function and Bioinformatics. 9(3). 217–224. 31 indexed citations
14.
Vitello, Lidia B., James E. Erman, J. Matthew Mauro, & Joseph Kraut. (1990). Characterization of the hydrogen peroxide - enzyme reaction for two cytochrome c peroxidase mutants. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1038(1). 90–97. 24 indexed citations
15.
Satterlee, James D., James E. Erman, J. Matthew Mauro, & Joseph Kraut. (1990). Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235 .fwdarw. Asn-235 mutant. Biochemistry. 29(37). 8797–8804. 30 indexed citations
16.
Davies, Jay F., Tavner J. Delcamp, Neal J. Prendergast, et al.. (1990). Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate. Biochemistry. 29(40). 9467–9479. 159 indexed citations
17.
Howell, Elizabeth E., J. Ernest Villafranca, Mark S. Warren, Stuart J. Oatley, & Joseph Kraut. (1986). Functional Role of Aspartic Acid-27 in Dihydrofolate Reductase Revealed by Mutagenesis. Science. 231(4742). 1123–1128. 204 indexed citations
18.
Kraut, Joseph, et al.. (1968). Low-resolution electron-density and anomalous-scattering-density maps of Chromatium high-potential iron protein. Journal of Molecular Biology. 35(3). 503–512. 70 indexed citations
19.
Alden, Richard A., Joseph Kraut, & Teddy G. Traylor. (1967). Hybridization, conjugation, and bond lengths. An experimental test. The Journal of Physical Chemistry. 71(7). 2379–2380. 4 indexed citations
20.
Kraut, Joseph. (1954). The sedimentation of sodium polymethacrylate. Journal of Polymer Science. 14(74). 222–224. 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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