John M. Lowenstein

10.2k total citations · 1 hit paper
131 papers, 8.1k citations indexed

About

John M. Lowenstein is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, John M. Lowenstein has authored 131 papers receiving a total of 8.1k indexed citations (citations by other indexed papers that have themselves been cited), including 73 papers in Molecular Biology, 24 papers in Physiology and 23 papers in Cell Biology. Recurrent topics in John M. Lowenstein's work include Biochemical and Molecular Research (21 papers), Adenosine and Purinergic Signaling (19 papers) and Enzyme function and inhibition (18 papers). John M. Lowenstein is often cited by papers focused on Biochemical and Molecular Research (21 papers), Adenosine and Purinergic Signaling (19 papers) and Enzyme function and inhibition (18 papers). John M. Lowenstein collaborates with scholars based in United States, United Kingdom and Belgium. John M. Lowenstein's co-authors include Keith Tornheim, Richard M. Burger, Henri Brunengraber, John Watson, Barbara Setlow, Mireille Boutry, Juan J. Aragón, Vera Schultz, M. N. Goodman and Marie Fang and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

John M. Lowenstein

131 papers receiving 7.5k citations

Hit Papers

Ammonia production in mus... 1972 2026 1990 2008 1972 100 200 300 400 500

Author Peers

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

Author Last Decade Papers Cites
John M. Lowenstein 4.3k 2.0k 1.5k 1.1k 955 131 8.1k
Henri Beaufay 3.9k 0.9× 1.1k 0.6× 1.1k 0.7× 1.1k 1.0× 296 0.3× 67 6.5k
C. De Duve 8.0k 1.8× 3.0k 1.5× 2.1k 1.4× 2.1k 1.8× 652 0.7× 64 13.8k
H G Hers 6.6k 1.5× 2.9k 1.5× 1.8k 1.2× 1.4k 1.2× 540 0.6× 159 12.3k
Paul A. Watkins 7.7k 1.8× 2.3k 1.2× 732 0.5× 2.5k 2.2× 413 0.4× 181 10.7k
Norman S. Radin 6.6k 1.5× 3.0k 1.5× 1.3k 0.8× 720 0.6× 208 0.2× 197 10.8k
Peter L. Pedersen 12.0k 2.8× 1.4k 0.7× 901 0.6× 1.5k 1.3× 272 0.3× 213 15.7k
Junichi Fujii 6.1k 1.4× 1.5k 0.8× 1.2k 0.8× 525 0.5× 300 0.3× 265 11.8k
Robert Salvayre 6.1k 1.4× 3.0k 1.5× 1.6k 1.1× 1.0k 0.9× 327 0.3× 280 13.3k
Michio Ui 6.2k 1.4× 1.4k 0.7× 1.6k 1.0× 239 0.2× 474 0.5× 180 9.4k
Irwin M. Arias 4.4k 1.0× 586 0.3× 895 0.6× 916 0.8× 323 0.3× 196 10.0k

Countries citing papers authored by John M. Lowenstein

Since Specialization
Citations

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

Fields of papers citing papers by John M. Lowenstein

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John M. Lowenstein. 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 John M. Lowenstein. The network helps show where John M. Lowenstein may publish in the future.

Co-authorship network of co-authors of John M. Lowenstein

This figure shows the co-authorship network connecting the top 25 collaborators of John M. Lowenstein. A scholar is included among the top collaborators of John M. Lowenstein 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 John M. Lowenstein. John M. Lowenstein 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.
Lowenstein, John M., et al.. (2024). Carbohydrate Deacetylase Unique to Gut Microbe Bacteroides Reveals Atypical Structure. Biochemistry. 64(1). 180–191. 2 indexed citations
2.
Matsushita, Kenji, Craig N. Morrell, Béatrice Cambien, et al.. (2003). Nitric Oxide Regulates Exocytosis by S-Nitrosylation of N-ethylmaleimide-Sensitive Factor. Cell. 115(2). 139–150. 361 indexed citations
3.
Saura, Marta, Carlos Zaragoza, Richard A. Quick, et al.. (1999). An Antiviral Mechanism of Nitric Oxide. Immunity. 10(1). 21–28. 205 indexed citations
4.
Pawełczyk, Tadeusz & John M. Lowenstein. (1997). The effect of different molecular species of sphingomyelin on phospholipase C δ1 activity. Biochimie. 79(12). 741–748. 5 indexed citations
5.
Pawełczyk, Tadeusz, et al.. (1997). Phospholipase C Isoforms δ1and δ3from Human Fibroblasts. Protein Expression and Purification. 9(2). 262–278. 18 indexed citations
6.
Brenner, Charles, et al.. (1997). Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nature Structural Biology. 4(3). 231–238. 119 indexed citations
8.
Pawełczyk, Tadeusz & John M. Lowenstein. (1993). Inhibition of phospholipase cδ by hexadecylphosphorylcholine and lysophospholipids with antitumor activity. Biochemical Pharmacology. 45(2). 493–497. 29 indexed citations
9.
Gascard, Philippe, Tadeusz Pawełczyk, John M. Lowenstein, & Carl M. Cohen. (1993). The role of inositol phospholipids in the association of band 4.1 with the human erythrocyte membrane. European Journal of Biochemistry. 211(3). 671–681. 29 indexed citations
10.
Pawełczyk, Tadeusz & John M. Lowenstein. (1992). Regulation of phospholipase Cδ activity by sphingomyelin and sphingosine. Archives of Biochemistry and Biophysics. 297(2). 328–333. 29 indexed citations
11.
Rosenthal, Rosalind A. & John M. Lowenstein. (1991). Inhibition of phosphorylation of troponin I in rat heart by adenosine and 5′-chloro-5′-deoxyadenosine. Biochemical Pharmacology. 42(3). 685–692. 8 indexed citations
12.
Haber, Martin T., Tetsuya Fukui, Michael Lebowitz, & John M. Lowenstein. (1991). Activation of phosphoinositide-specific phospholipase Cδ from rat liver by polyamines and basic proteins. Archives of Biochemistry and Biophysics. 288(1). 243–249. 42 indexed citations
13.
Yamazaki, Yukiko, et al.. (1991). 5'-Nucleotidase I from rabbit heart. Biochemistry. 30(6). 1503–1509. 40 indexed citations
14.
Buechler, Kenneth F. & John M. Lowenstein. (1990). The involvement of carnitine intermediates in peroxisomal fatty acid oxidation: A study with 2-bromofatty acids. Archives of Biochemistry and Biophysics. 281(2). 233–238. 32 indexed citations
15.
Lowenstein, John M.. (1990). The Purine Nucleotide Cycle Revised. International Journal of Sports Medicine. 11(S 2). S37–S46. 91 indexed citations
16.
Yamazaki, Yukiko, et al.. (1989). Regulation of Soluble 5′-Nucleotidase I from Rabbit Heart. Advances in experimental medicine and biology. 253B. 107–111. 7 indexed citations
17.
Casey, Patrick J. & John M. Lowenstein. (1987). Inhibition of adenylosuccinate lyase by L-alanosyl-5-aminoimidazole-4-carboxylic acid ribonucleotide (alanosyl-aicor). Biochemical Pharmacology. 36(5). 705–709. 9 indexed citations
18.
Raaka, Bruce M. & John M. Lowenstein. (1981). [42] 2-Bromooctanoate. Methods in enzymology on CD-ROM/Methods in enzymology. 72. 559–577. 4 indexed citations
19.
Lowenstein, John M.. (1972). Ammonia production in muscle and other tissues: the purine nucleotide cycle.. Physiological Reviews. 52(2). 382–414. 557 indexed citations breakdown →
20.
Hughes, D. E., et al.. (1958). The hydroxylation of nicotinic acid by Pseudomonas fluorescens. Biochemical Journal. 69(2). 170–173. 55 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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