James I. Salach

1.9k total citations
23 papers, 1.6k citations indexed

About

James I. Salach is a scholar working on Molecular Biology, Neurology and Physiology. According to data from OpenAlex, James I. Salach has authored 23 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 6 papers in Neurology and 6 papers in Physiology. Recurrent topics in James I. Salach's work include Parkinson's Disease Mechanisms and Treatments (6 papers), Amino Acid Enzymes and Metabolism (5 papers) and Electrochemical sensors and biosensors (5 papers). James I. Salach is often cited by papers focused on Parkinson's Disease Mechanisms and Treatments (6 papers), Amino Acid Enzymes and Metabolism (5 papers) and Electrochemical sensors and biosensors (5 papers). James I. Salach collaborates with scholars based in United States, Hungary and Israel. James I. Salach's co-authors include Thomas P. Singer, Rona R. Ramsay, Walter Weyler, R. Seng, Jahan Dadgar, Neal Castagnoli, Anthony J. Trevor, Edna B. Kearney, János Nagy and Wolfram H. Walker and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Brain Research.

In The Last Decade

James I. Salach

22 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
James I. Salach United States 18 724 702 643 187 179 23 1.6k
C. W. Abell United States 7 437 0.6× 457 0.7× 503 0.8× 116 0.6× 96 0.5× 11 1.2k
I Vyas United States 6 990 1.4× 509 0.7× 822 1.3× 65 0.3× 180 1.0× 10 1.6k
Tsutomu Takahashi Japan 25 635 0.9× 784 1.1× 747 1.2× 101 0.5× 188 1.1× 121 2.1k
Norio Kaneda Japan 26 288 0.4× 1.1k 1.6× 529 0.8× 112 0.6× 174 1.0× 97 2.2k
R.W. Von Korff United States 16 131 0.2× 714 1.0× 271 0.4× 171 0.9× 254 1.4× 34 1.3k
Mohammad I. Sabri United States 21 351 0.5× 748 1.1× 628 1.0× 112 0.6× 241 1.3× 62 2.0k
Yves Agid France 6 717 1.0× 581 0.8× 511 0.8× 148 0.8× 290 1.6× 6 1.5k
Byoung Boo Seo United States 25 925 1.3× 1.9k 2.7× 677 1.1× 97 0.5× 372 2.1× 37 3.1k
Michael E. Bembenek United States 13 231 0.3× 676 1.0× 275 0.4× 95 0.5× 97 0.5× 31 1.4k
Roberto Hodara United States 12 1.0k 1.4× 995 1.4× 493 0.8× 227 1.2× 1.1k 6.3× 13 2.6k

Countries citing papers authored by James I. Salach

Since Specialization
Citations

This map shows the geographic impact of James 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 James 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 James I. Salach more than expected).

Fields of papers citing papers by James I. Salach

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of James I. Salach. A scholar is included among the top collaborators of James 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 James I. Salach. James I. Salach 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.
Tan, Anthony K., Walter Weyler, James I. Salach, & Thomas P. Singer. (1991). Differences in substrate specificities of monoamine oxidase A from human liver and placenta. Biochemical and Biophysical Research Communications. 181(3). 1084–1088. 20 indexed citations
2.
Weyler, Walter, et al.. (1990). Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FAD. Biochemical and Biophysical Research Communications. 173(3). 1205–1211. 44 indexed citations
3.
Salach, James I. & Walter Weyler. (1987). [73] Preparation of the flavin-containing aromatic amine oxidases of human placenta and beef liver. Methods in enzymology on CD-ROM/Methods in enzymology. 142. 627–637. 42 indexed citations
4.
Ramsay, Rona R., Andrzej Kowal, Michael K. Johnson, James I. Salach, & Thomas P. Singer. (1987). The inhibition site of MPP+, the neurotoxic bioactivation product of 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine is near the Q-binding site of NADH dehydrogenase. Archives of Biochemistry and Biophysics. 259(2). 645–649. 95 indexed citations
5.
Ramsay, Rona R., James I. Salach, & Thomas P. Singer. (1986). Uptake of the neurotoxin 1-methyl-4-phenylpyridine (MPP+) by mitochondria and its relation to the inhibition of the mitochondrial oxidation of NAD+-linked substrates by MPP+. Biochemical and Biophysical Research Communications. 134(2). 743–748. 225 indexed citations
6.
Singer, Thomas P., James I. Salach, & Donald V. Crabtree. (1985). Reversible inhibition and mechanism-based irreversible inactivation of monoamine oxidases by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Biochemical and Biophysical Research Communications. 127(2). 707–712. 63 indexed citations
7.
Salach, James I., Thomas P. Singer, Neal Castagnoli, & Anthony J. Trevor. (1984). Oxidation of the neurotoxic amine 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) by monoamine oxidases A and B and suicide inactivation of the enzymes by MPTP. Biochemical and Biophysical Research Communications. 125(2). 831–835. 167 indexed citations
8.
Weyler, Walter & James I. Salach. (1981). Iron content and spectral properties of highly purified bovine liver monoamine oxidase. Archives of Biochemistry and Biophysics. 212(1). 147–153. 44 indexed citations
9.
Salach, James I., Kristina Detmer, & Moussa B. H. Youdim. (1979). The Reaction of Bovine and Rat Liver Monoamine Oxidase with [14C]-Clorgyline and [14C]-Deprenyl. Molecular Pharmacology. 16(1). 234–241. 61 indexed citations
10.
Salach, James I.. (1979). Monoamine oxidase from beef liver mitochondria: Simplified isolation procedure, properties, and determination of its cysteinyl flavin content. Archives of Biochemistry and Biophysics. 192(1). 128–137. 117 indexed citations
11.
Salach, James I.. (1978). [49] Preparation of monoamine oxidase from beef liver mitochondria. Methods in enzymology on CD-ROM/Methods in enzymology. 53. 495–501. 49 indexed citations
12.
Salach, James I. & Thomas P. Singer. (1974). Activation of Succinate Dehydrogenase by FMNH2 and by Photoreduction. Journal of Biological Chemistry. 249(12). 3765–3767. 7 indexed citations
13.
Salach, James I., et al.. (1973). Essentiality of coenzyme Q for the oxidation of α-glycerophosphate by pig brain mitochondria. Archives of Biochemistry and Biophysics. 157(1). 133–144. 13 indexed citations
14.
Salach, James I., R. Seng, H.D. Tisdale, & Thomas P. Singer. (1971). Phospholipase A of Snake Venoms. Journal of Biological Chemistry. 246(2). 340–347. 49 indexed citations
15.
Kearney, Edna B., James I. Salach, Wolfram H. Walker, et al.. (1971). The Covalently‐Bound Flavin of Hepatic Monoamine Oxidase. European Journal of Biochemistry. 24(2). 321–327. 163 indexed citations
16.
Salach, James I., Paola Turini, R. Seng, J. Hauber, & Thomas P. Singer. (1971). Phospholipase A of Snake Venoms. Journal of Biological Chemistry. 246(2). 331–339. 92 indexed citations
17.
Salach, James I., H.D. Tisdale, Thomas P. Singer, & Peter Bader. (1967). Inhibitors of NADH-ubiquinone reductase from mitochondria. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 143(1). 281–284. 8 indexed citations
18.
Salach, James I., Thomas P. Singer, & Peter Bader. (1967). Studies on the Respiratory Chain-linked Reduced Nicotinamide Adenine Dinucleotide Dehydrogenase. Journal of Biological Chemistry. 242(20). 4555–4562. 18 indexed citations
19.
Salach, James I., Edna B. Kearney, & Thomas P. Singer. (1964). Further Studies on the Labile Flavin Adenine Dinucleotide of Heart Muscle Preparations. Nature. 201(4923). 1027–1028. 1 indexed citations
20.
Cremona, Terenzio, Edna B. Kearney, James I. Salach, & Thomas P. Singer. (1963). Labile Flavin Adenine Dinucleotide of Heart Muscle Preparations. Nature. 200(4910). 958–959. 4 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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