J. Peisach

16.8k total citations · 3 hit papers
258 papers, 13.8k citations indexed

About

J. Peisach is a scholar working on Molecular Biology, Biophysics and Cell Biology. According to data from OpenAlex, J. Peisach has authored 258 papers receiving a total of 13.8k indexed citations (citations by other indexed papers that have themselves been cited), including 138 papers in Molecular Biology, 73 papers in Biophysics and 66 papers in Cell Biology. Recurrent topics in J. Peisach's work include Electron Spin Resonance Studies (72 papers), Hemoglobin structure and function (64 papers) and Photosynthetic Processes and Mechanisms (52 papers). J. Peisach is often cited by papers focused on Electron Spin Resonance Studies (72 papers), Hemoglobin structure and function (64 papers) and Photosynthetic Processes and Mechanisms (52 papers). J. Peisach collaborates with scholars based in United States, Italy and Japan. J. Peisach's co-authors include W. E. Blumberg, Susan Band Horwitz, W. B. Mims, Richard M. Burger, Jonathan H. Freedman, Edward A. Sausville, Jonathan B. Wittenberg, Maria Rosa Ciriolo, John McCracken and E. A. Rachmilewitz and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

J. Peisach

258 papers receiving 12.9k citations

Hit Papers

Structural implications d... 1974 2026 1991 2008 1974 1989 1981 250 500 750 1000

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
J. Peisach 7.1k 2.7k 2.5k 2.3k 2.0k 258 13.8k
Helmut Beinert 9.9k 1.4× 915 0.3× 1.7k 0.7× 2.7k 1.2× 2.2k 1.1× 228 17.4k
Lucia Banci 9.9k 1.4× 2.8k 1.0× 1.6k 0.6× 2.3k 1.0× 2.9k 1.5× 430 19.9k
Joan Selverstone Valentine 8.8k 1.2× 2.0k 0.7× 1.3k 0.5× 4.3k 1.8× 4.2k 2.2× 247 23.1k
Andrew J. Thomson 5.5k 0.8× 1.4k 0.5× 1.4k 0.6× 2.1k 0.9× 2.0k 1.0× 311 13.2k
Robert J. P. Williams 6.6k 0.9× 976 0.4× 1.9k 0.7× 1.2k 0.5× 3.0k 1.5× 372 13.4k
Astrid Gräslund 10.7k 1.5× 2.4k 0.9× 563 0.2× 2.7k 1.2× 1.4k 0.7× 349 16.0k
Douglas C. Rees 13.8k 1.9× 3.4k 1.3× 1.7k 0.7× 4.6k 2.0× 5.0k 2.5× 231 27.2k
Elizabeth D. Getzoff 7.6k 1.1× 873 0.3× 1.1k 0.4× 1.8k 0.8× 1.5k 0.8× 149 14.4k
Thomas G. Spiro 10.7k 1.5× 1.6k 0.6× 6.5k 2.6× 4.3k 1.9× 6.2k 3.2× 520 24.6k
P. Nordlund 10.6k 1.5× 2.6k 1.0× 1.1k 0.4× 3.2k 1.4× 2.0k 1.0× 181 15.4k

Countries citing papers authored by J. Peisach

Since Specialization
Citations

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

Fields of papers citing papers by J. Peisach

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J. Peisach

This figure shows the co-authorship network connecting the top 25 collaborators of J. Peisach. A scholar is included among the top collaborators of J. Peisach 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 J. Peisach. J. Peisach 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.
Vergara, Alessandro, Antonello Merlino, Cinzia Verde, et al.. (2009). Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins. Biophysical Journal. 97(3). 866–874. 24 indexed citations
2.
Hirota, Shun, Mariano Beltramini, Paolo Di Muro, et al.. (2008). Molecular Basis of the Bohr Effect in Arthropod Hemocyanin. Journal of Biological Chemistry. 283(46). 31941–31948. 15 indexed citations
3.
Giordano, Daniela, Alessandro Vergara, J. Peisach, et al.. (2007). Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus. Gene. 406(1-2). 58–68. 15 indexed citations
4.
Das, Tapan K., Stephen M. G. Duff, Robert D. Hill, et al.. (1999). The Heme Environment in Barley Hemoglobin. Journal of Biological Chemistry. 274(7). 4207–4212. 44 indexed citations
5.
Parast, Camran V., et al.. (1995). Hydrogen Exchange of the Glycyl Radical of Pyruvate Formate-Lyase Is Catalyzed by Cysteine 419. Biochemistry. 34(8). 2393–2399. 62 indexed citations
6.
Magliozzo, Richard S., Luigi Bubacco, John McCracken, et al.. (1995). Cu(II) coordination in arthropod and mollusk green half-methemocyanins analyzed by electron spin-echo envelope modulation spectroscopy. Biochemistry. 34(5). 1513–1523. 15 indexed citations
7.
Balasubramanian, Shankar, Robert T. Carr, Christopher J. Bender, J. Peisach, & Stephen J. Benkovic. (1993). Histidines 138 and 143 are Copper Binding Ligands in Chromobacterium Violaceum Phenylalanine Hydroxylase. Advances in experimental medicine and biology. 338. 67–70. 3 indexed citations
9.
10.
Ikeda‐Saito, Masao, et al.. (1992). Hydrogen bonding to the bound dioxygen in oxy cobaltous myoglobin reduces the superhyperfine coupling to the proximal histidine. Biochemistry. 31(32). 7274–7281. 16 indexed citations
11.
Lu, Jinfeng, et al.. (1992). Pulsed EPR studies of the type 2 copper binding site in the mercury derivative of laccase. Biochemistry. 31(27). 6265–6272. 18 indexed citations
13.
Zer, Hagit, Jonathan H. Freedman, J. Peisach, & Mordechai Chevion. (1991). Inverse correlation between resistance towards copper and towards the redox-cycling compound paraquat: A study in copper-tolerant hepatocytes in tissue culture. Free Radical Biology and Medicine. 11(1). 9–16. 12 indexed citations
14.
Magliozzo, Richard S., J. Peisach, & Maria Rosa Ciriolo. (1989). Transfer RNA is cleaved by activated bleomycin.. Molecular Pharmacology. 35(4). 428–432. 54 indexed citations
15.
Cunningham, Richard P., Hitomi Asahara, Janet F. Bank, et al.. (1989). Endonuclease III is an iron-sulfur protein. Biochemistry. 28(10). 4450–4455. 174 indexed citations
16.
Mondovı̀, Bruno, Laura Morpurgo, Enzo Agostinelli, et al.. (1987). A comparison of the local environment of Cu(II) in native and half‐Cu‐depleted bovine serum amine oxidase. European Journal of Biochemistry. 168(3). 503–507. 11 indexed citations
17.
Pickart, Loren, Jonathan H. Freedman, J. Peisach, et al.. (1980). Growth-modulating plasma tripeptide may function by facilitating copper uptake into cells. Nature. 288(5792). 715–717. 147 indexed citations
18.
Sausville, Edward A., J. Peisach, & Susan Band Horwitz. (1976). A role for ferrous ion and oxygen in the degradation of DNA by bleomycin. Biochemical and Biophysical Research Communications. 73(3). 814–822. 241 indexed citations
19.
Peisach, J. & W. E. Blumberg. (1969). A Mechanism for the Action of Penicillamine in the Treatment of Wilson’s Disease. Molecular Pharmacology. 5(2). 200–209. 66 indexed citations
20.
Peisach, J., Philip Aisen, & W. E. Blumberg. (1966). The biochemistry of copper : proceedings of the symposium on copper in biological systems held at arden house, Harriman, New York, September 8-10, 1965. Academic Press eBooks. 21 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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