Zahi Damuni

2.5k total citations
36 papers, 2.1k citations indexed

About

Zahi Damuni is a scholar working on Molecular Biology, Cell Biology and Biochemistry. According to data from OpenAlex, Zahi Damuni has authored 36 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 10 papers in Cell Biology and 9 papers in Biochemistry. Recurrent topics in Zahi Damuni's work include Protein Kinase Regulation and GTPase Signaling (8 papers), Biochemical Acid Research Studies (8 papers) and Polyamine Metabolism and Applications (7 papers). Zahi Damuni is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (8 papers), Biochemical Acid Research Studies (8 papers) and Polyamine Metabolism and Applications (7 papers). Zahi Damuni collaborates with scholars based in United States, Canada and Switzerland. Zahi Damuni's co-authors include Mei Li, Anthony Makkinje, Lester J. Reed, Hui Guo, Hong Guo, Margaret Merryfield, Samer W.K. Al-Murrani, John Humphreys, James R. Woodgett and Sunil Reddy and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Zahi Damuni

36 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Zahi Damuni United States 23 1.6k 405 376 260 216 36 2.1k
Nelson Quintana United States 19 1.0k 0.7× 382 0.9× 469 1.2× 164 0.6× 213 1.0× 36 1.9k
Manju Swaroop United States 27 1.5k 1.0× 301 0.7× 298 0.8× 159 0.6× 88 0.4× 42 2.6k
P Sherline United States 25 1.7k 1.1× 315 0.8× 977 2.6× 167 0.6× 74 0.3× 34 2.5k
Lee Carpenter United Kingdom 26 1.7k 1.1× 313 0.8× 695 1.8× 121 0.5× 72 0.3× 36 2.4k
Cassandra Obie United States 16 1.4k 0.9× 185 0.5× 135 0.4× 202 0.8× 345 1.6× 22 1.7k
Philippe A. Parone Switzerland 17 2.1k 1.3× 310 0.8× 211 0.6× 70 0.3× 344 1.6× 22 2.6k
Fumiko Hirose Japan 38 2.9k 1.9× 494 1.2× 367 1.0× 559 2.1× 56 0.3× 84 3.7k
T E Bross United States 13 1.2k 0.8× 205 0.5× 420 1.1× 119 0.5× 49 0.2× 16 1.8k
Ronald J. Uhing United States 20 1.1k 0.7× 220 0.5× 283 0.8× 86 0.3× 57 0.3× 33 1.7k
Elizabeth J. Ackermann United States 18 1.9k 1.2× 250 0.6× 410 1.1× 143 0.6× 57 0.3× 35 2.4k

Countries citing papers authored by Zahi Damuni

Since Specialization
Citations

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

Fields of papers citing papers by Zahi Damuni

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Zahi Damuni

This figure shows the co-authorship network connecting the top 25 collaborators of Zahi Damuni. A scholar is included among the top collaborators of Zahi Damuni 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 Zahi Damuni. Zahi Damuni 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.
Härmälä-Braskén, Ann-Sofi, Andrey Mikhailov, Annika Meinander, et al.. (2003). Type-2A protein phosphatase activity is required to maintain death receptor responsiveness. Oncogene. 22(48). 7677–7686. 35 indexed citations
2.
Lynch, Christopher J., Hisao Fujii, Thomas C. Vary, et al.. (2003). Potential role of leucine metabolism in the leucine-signaling pathway involving mTOR. American Journal of Physiology-Endocrinology and Metabolism. 285(4). E854–E863. 89 indexed citations
3.
Bracchi‐Ricard, Valerie, et al.. (2003). Characterization of a unique aspartate-rich protein of the SET/TAF-family in the human malaria parasite, Plasmodium falciparum, which inhibits protein phosphatase 2A. Molecular and Biochemical Parasitology. 126(2). 239–250. 19 indexed citations
4.
Chen, Yun, Masayuki Matsushita, Angus C. Nairn, et al.. (2001). Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels. Biochemistry. 40(38). 11565–11570. 64 indexed citations
5.
Li, Mei, et al.. (2000). Protein Phosphatase 2A Inhibitors, I1PP2A and I2PP2A, Associate with and Modify the Substrate Specificity of Protein Phosphatase 1. Journal of Biological Chemistry. 275(13). 9209–9214. 41 indexed citations
6.
Al-Murrani, Samer W.K., James R. Woodgett, & Zahi Damuni. (1999). Expression of I2PP2A, an inhibitor of protein phosphatase 2A, induces c-Jun and AP-1 activity. Biochemical Journal. 341(2). 293–293. 16 indexed citations
7.
Li, Mei & Zahi Damuni. (1998). I1 PP2A and I2 PP2A. Humana Press eBooks. 93. 59–66. 33 indexed citations
8.
Li, Mei, Anthony Makkinje, & Zahi Damuni. (1996). The Myeloid Leukemia-associated Protein SET Is a Potent Inhibitor of Protein Phosphatase 2A. Journal of Biological Chemistry. 271(19). 11059–11062. 400 indexed citations
9.
Oyler, George A., Katherine Harris, Rathnagiri Polavarapu, et al.. (1995). Tau phosphorylation in brain slices: pharmacological evidence for convergent effects of protein phosphatases on tau and mitogen-activated protein kinase.. Molecular Pharmacology. 47(4). 745–756. 34 indexed citations
10.
Li, Mei, Hong Guo, & Zahi Damuni. (1995). Purification and Characterization of Two Potent Heat-Stable Protein Inhibitors of Protein Phosphatase 2A from Bovine Kidney. Biochemistry. 34(6). 1988–1996. 187 indexed citations
11.
Makkinje, Anthony, et al.. (1995). Phosphorylation of Eukaryotic Protein Synthesis Initiation Factor 4E by Insulin-stimulated Protamine Kinase. Journal of Biological Chemistry. 270(24). 14824–14828. 36 indexed citations
12.
Damuni, Zahi, et al.. (1994). Autophosphorylation‐activated protein kinase inactivates the protein tyrosine phosphatase activity of protein phosphatase 2A. FEBS Letters. 352(3). 311–314. 22 indexed citations
13.
Damuni, Zahi, et al.. (1994). Okadaic Acid and Microcystin-LR Directly Inhibit the Methylation of Protein Phosphatase 2A by Its Specific Methyltransferase. Biochemical and Biophysical Research Communications. 202(2). 1023–1030. 28 indexed citations
14.
15.
Reddy, Sunil, et al.. (1993). Phosphorylation and activation of protamine kinase by two forms of a myelin basic protein kinase from extracts of bovine kidney cortex. Journal of Biological Chemistry. 268(20). 15298–15304. 9 indexed citations
16.
Damuni, Zahi, et al.. (1992). Protamine kinase phosphorylates eukaryotic protein synthesis initiation factor 4E. Biochemical and Biophysical Research Communications. 183(2). 431–437. 22 indexed citations
17.
Damuni, Zahi. (1990). Inactivation of bovine kidney cytosolic protamine kinase by the catalytic subunit of protein phosphatase 2A. Biochemical and Biophysical Research Communications. 166(1). 449–456. 9 indexed citations
18.
Damuni, Zahi & Lester J. Reed. (1988). [42] Branched-chain α-keto acid dehydrogenase phosphatase and its inhibitor protein from bovine kidney. Methods in enzymology on CD-ROM/Methods in enzymology. 166. 321–329. 6 indexed citations
19.
Reed, Lester J., Zahi Damuni, & Margaret Merryfield. (1985). Regulation of Mammalian Pyruvate and Branched-Chain α-Keto Acid Dehydrogenase Complexes by Phosphorylation — Dephosphorylation. Current topics in cellular regulation. 27. 41–49. 97 indexed citations
20.
Damuni, Zahi, H.Y. Lim Tung, & Lester J. Reed. (1985). Specificity of the heat-stable protein inhibitor of the branched-chain α-keto acid dehydrogenase phosphatase. Biochemical and Biophysical Research Communications. 133(3). 878–883. 10 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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