J.I. Salach

719 total citations
10 papers, 538 citations indexed

About

J.I. Salach is a scholar working on Molecular Biology, Electrical and Electronic Engineering and Neurology. According to data from OpenAlex, J.I. Salach has authored 10 papers receiving a total of 538 indexed citations (citations by other indexed papers that have themselves been cited), including 6 papers in Molecular Biology, 3 papers in Electrical and Electronic Engineering and 2 papers in Neurology. Recurrent topics in J.I. Salach's work include Electrochemical sensors and biosensors (3 papers), Microbial metabolism and enzyme function (2 papers) and Metabolism and Genetic Disorders (2 papers). J.I. Salach is often cited by papers focused on Electrochemical sensors and biosensors (3 papers), Microbial metabolism and enzyme function (2 papers) and Metabolism and Genetic Disorders (2 papers). J.I. Salach collaborates with scholars based in United States, Sweden and France. J.I. Salach's co-authors include Walter Weyler, Thomas P. Singer, Alan L. Maycock, Robert H. Abeles, Neal Castagnoli, Christian Paech, R. Seng, Wolfram H. Walker, Edna B. Kearney and R. M. Denney and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Neuroscience and Biochemistry.

In The Last Decade

J.I. Salach

10 papers receiving 502 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J.I. Salach United States 9 242 177 172 93 71 10 538
M. Krueger United States 13 329 1.4× 247 1.4× 232 1.3× 63 0.7× 49 0.7× 19 677
R. Seng United States 12 317 1.3× 100 0.6× 64 0.4× 132 1.4× 98 1.4× 12 598
Sau‐Wah Kwan United States 13 295 1.2× 182 1.0× 95 0.6× 52 0.6× 27 0.4× 17 571
V. Z. Gorkin Russia 13 225 0.9× 144 0.8× 49 0.3× 134 1.4× 72 1.0× 65 471
Anastasia Constantinescu United States 9 309 1.3× 94 0.5× 83 0.5× 186 2.0× 29 0.4× 14 569
A. D'Iorio Canada 14 344 1.4× 145 0.8× 44 0.3× 110 1.2× 43 0.6× 62 688
Shu Wen Li United States 14 174 0.7× 268 1.5× 337 2.0× 38 0.4× 36 0.5× 22 742
Monique Zreika France 10 160 0.7× 102 0.6× 96 0.6× 54 0.6× 36 0.5× 22 421
Carvell H. Williams United Kingdom 12 332 1.4× 236 1.3× 83 0.5× 63 0.7× 39 0.5× 31 714
C.J. Coles United States 12 395 1.6× 125 0.7× 43 0.3× 49 0.5× 36 0.5× 16 599

Countries citing papers authored by J.I. Salach

Since Specialization
Citations

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

Fields of papers citing papers by J.I. Salach

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J.I. Salach

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

All Works

10 of 10 papers shown
1.
Powell, John, Yun‐Pung P. Hsu, Walter Weyler, et al.. (1989). The primary structure of bovine monoamine oxidase type A. Comparison with peptide sequences of bovine monoamine oxidase type B and other flavoenzymes. Biochemical Journal. 259(2). 407–413. 49 indexed citations
2.
Singer, Thomas P., et al.. (1986). Interactions of the neurotoxic amine 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine with monoamine oxidases. Biochemical Journal. 235(3). 785–789. 76 indexed citations
3.
Weyler, Walter & J.I. Salach. (1985). Purification and properties of mitochondrial monoamine oxidase type A from human placenta.. Journal of Biological Chemistry. 260(24). 13199–13207. 133 indexed citations
4.
Hsieh, C-C, et al.. (1985). Immunological uniqueness of human monoamine oxidases A and B: new evidence from studies with monoclonal antibodies to human monoamine oxidase A. Journal of Neuroscience. 5(11). 2874–2881. 49 indexed citations
5.
Paech, Christian, J.I. Salach, & Thomas P. Singer. (1980). Suicide inactivation of monoamine oxidase by trans-phenylcyclopropylamine.. Journal of Biological Chemistry. 255(7). 2700–2704. 52 indexed citations
6.
Maycock, Alan L., Robert H. Abeles, J.I. Salach, & Thomas P. Singer. (1976). The structure of the covalent adduct formed by the interaction of 3-dimethylamino-1-propyne and the flavine of mitochondrial amine oxidase. Biochemistry. 15(1). 114–125. 95 indexed citations
7.
Kearney, Edna B., J.I. Salach, Wolfram H. Walker, R. Seng, & Thomas P. Singer. (1971). Structure of the covalently bound flavin of monoamine oxidase. Biochemical and Biophysical Research Communications. 42(3). 490–496. 37 indexed citations
8.
Walker, Wolfram H., J.I. Salach, M. Gutman, et al.. (1969). Endor studies on the covalently bound flavin at the active center of succinate dehydrogenase. FEBS Letters. 5(3). 237–240. 17 indexed citations
9.
Salach, J.I., Paola Turini, J. Hauber, et al.. (1968). Isolation of phospholipase a isoenzymes from Najanaja venom and their action on membrane-bound enzymes. Biochemical and Biophysical Research Communications. 33(6). 936–941. 29 indexed citations
10.
Salach, J.I., Thomas P. Singer, & Peter Bader. (1967). Conversion of Reduced Nicotinamide-Adenine Dinucleotide Dehydrogenase into Reduced Nicotinamide-Adenine Dinucleotide-Ubiquinone Reductase. Biochemical Journal. 104(2). 22C–24C. 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.

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