Giuseppe Inesi

14.5k total citations · 2 hit papers
217 papers, 12.2k citations indexed

About

Giuseppe Inesi is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Cellular and Molecular Neuroscience. According to data from OpenAlex, Giuseppe Inesi has authored 217 papers receiving a total of 12.2k indexed citations (citations by other indexed papers that have themselves been cited), including 179 papers in Molecular Biology, 62 papers in Cardiology and Cardiovascular Medicine and 30 papers in Cellular and Molecular Neuroscience. Recurrent topics in Giuseppe Inesi's work include Ion channel regulation and function (103 papers), Ion Transport and Channel Regulation (43 papers) and Cardiac electrophysiology and arrhythmias (42 papers). Giuseppe Inesi is often cited by papers focused on Ion channel regulation and function (103 papers), Ion Transport and Channel Regulation (43 papers) and Cardiac electrophysiology and arrhythmias (42 papers). Giuseppe Inesi collaborates with scholars based in United States, Japan and Italy. Giuseppe Inesi's co-authors include Yutaka Sagara, Chikashi Toyoshima, David E. Lewis, M. Kurzmack, Leopoldo de Meis, Carlota Sumbilla, Michele Chiesi, Carol Coan, David M. Clarke and Tip W. Loo and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Giuseppe Inesi

214 papers receiving 11.5k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Location of high affinity Ca2 +-binding sites within the predicted transmembrahe domain of the sarco-plasmic reticulum Ca2+-ATPase

1989 496 citations Giuseppe Inesi et al. profile →
Phospholipid orientation in sacroplasmic membranes: Spin-label ESR and proton NMR studies

1972 385 citations Giuseppe Inesi et al. profile →

Peers

Giuseppe Inesi

CCM

CMN

PHYSI

Edward J. Cragoe United States

Yasunobu Okada Japan

Chikashi Toyoshima Japan

Arnold Schwartz United States

T J Rink United Kingdom

Claude B. Klee United States

John T. Penniston United States

Michihiko Tada Japan

J.F. Kuo United States

Nieng Yan China

Edward J. Cragoe United States

Giuseppe Inesi

8.3k ×0.8

1.4k ×0.5

CCM

2.8k ×1.7

CMN

760 ×0.5

1.8k ×1.9

PHYSI

Citations per year, relative to Giuseppe Inesi Giuseppe Inesi (= 1×) peers Edward J. Cragoe

Countries citing papers authored by Giuseppe Inesi

Since Specialization

Citations

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

Fields of papers citing papers by Giuseppe Inesi

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Giuseppe Inesi

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Prasad, Anand & Giuseppe Inesi. (2011). Calcineurin a Subunit Silencing Reduces Serca2 Expression in Cardiac Myocytes. Biophysical Journal. 100(3). 85a–85a.

Prasad, Anand & Giuseppe Inesi. (2011). Regulation and rate limiting mechanisms of Ca2+ ATPase (SERCA2) expression in cardiac myocytes. Molecular and Cellular Biochemistry. 361(1-2). 85–96. 14 indexed citations

Bartolommei, Gianluca, Francesco Tadini‐Buoninsegni, Maria Rosa Moncelli, et al.. (2011). The Ca2+-ATPase (SERCA1) Is Inhibited by 4-Aminoquinoline Derivatives through Interference with Catalytic Activation by Ca2+, Whereas the ATPase E2 State Remains Functional. Journal of Biological Chemistry. 286(44). 38383–38389. 10 indexed citations

Tadini‐Buoninsegni, Francesco, Gianluca Bartolommei, Maria Rosa Moncelli, et al.. (2010). ATP dependent charge movement in ATP7B Cu⁺‐ATPase is demonstrated by pre‐steady state electrical measurements. FEBS Letters. 584(22). 4619–4622. 30 indexed citations

Pilankatta, Rajendra, David E. Lewis, Christopher M. Adams, & Giuseppe Inesi. (2009). High Yield Heterologous Expression of Wild-type and Mutant Cu+-ATPase (ATP7B, Wilson Disease Protein) for Functional Characterization of Catalytic Activity and Serine Residues Undergoing Copper-dependent Phosphorylation. Journal of Biological Chemistry. 284(32). 21307–21316. 29 indexed citations

Inesi, Giuseppe, David E. Lewis, Chikashi Toyoshima, Ayami Hirata, & Leopoldo de Meis. (2007). Conformational Fluctuations of the Ca2+-ATPase in the Native Membrane Environment. Journal of Biological Chemistry. 283(2). 1189–1196. 57 indexed citations

Ma, Hailun, Giuseppe Inesi, & Chikashi Toyoshima. (2003). Substrate-induced Conformational Fit and Headpiece Closure in the Ca2+ATPase (SERCA). Journal of Biological Chemistry. 278(31). 28938–28943. 40 indexed citations

Sumbilla, Carlota, et al.. (2002). The Slippage of the Ca2+ Pump and Its Control by Anions and Curcumin in Skeletal and Cardiac Sarcoplasmic Reticulum. Journal of Biological Chemistry. 277(16). 13900–13906. 46 indexed citations

Inesi, Giuseppe, Zhongsen Zhang, & David E. Lewis. (2002). Cooperative Setting for Long-Range Linkage of Ca2+ Bindingand ATP Synthesis in the Ca2+ ATPase. Biophysical Journal. 83(5). 2327–2332. 24 indexed citations

10.

Ma, Hailun, et al.. (1999). Overlapping Effects of S3 Stalk Segment Mutations on the Affinity of Ca²⁺-ATPase (SERCA) for Thapsigargin and Cyclopiazonic Acid. Biochemistry. 38(47). 15522–15527. 28 indexed citations

11.

Zhang, Lilin, et al.. (1998). Specific Substitutions at Amino Acid 256 of the Sarcoplasmic/Endoplasmic Reticulum Ca2+ Transport ATPase Mediate Resistance to Thapsigargin in Thapsigargin-resistant Hamster Cells. Journal of Biological Chemistry. 273(6). 3542–3546. 46 indexed citations

12.

Malak, Henryk, et al.. (1995). Synthesis and interaction of fluorescent thapsigargin derivatives with the sarcoplasmic reticulum ATPase membrane-bound region. Biochemistry. 34(15). 5137–5142. 15 indexed citations

13.

Yu, Xiang & Giuseppe Inesi. (1995). Variable Stoichiometric Efficiency of Ca2+ and Sr2+ Transport by the Sarcoplasmic Reticulum ATPase. Journal of Biological Chemistry. 270(9). 4361–4367. 78 indexed citations

14.

Inesi, Giuseppe & Yutaka Sagara. (1994). Specific inhibitors of intracellular Ca2+ transport ATPases. The Journal of Membrane Biology. 141(1). 1–6. 147 indexed citations

15.

Inesi, Giuseppe, et al.. (1992). Long‐Range Intramolecular Linked Functions in Activation and Inhibition of SERCA ATPases^a. Annals of the New York Academy of Sciences. 671(1). 32–48. 29 indexed citations

16.

Fernández-Belda, Francisco, Francisco Garcı́a-Carmona, & Giuseppe Inesi. (1988). Accelerating effect of ATP on calcium binding to sarcoplasmic reticulum ATPase. Archives of Biochemistry and Biophysics. 260(1). 118–124. 8 indexed citations

17.

Teruel, José A. & Giuseppe Inesi. (1988). Roles of phosphorylation and nucleotide binding domains in calcium transport by sarcoplasmic reticulum adenosine triphosphatase. Biochemistry. 27(16). 5885–5890. 23 indexed citations

18.

Lundblad, Arne, H Gonzalez‐Serratos, Giuseppe Inesi, Julia C. Swanson, & Paul Paolini. (1986). Patterns of sarcomere activation, temperature dependence, and effect of ryanodine in chemically skinned cardiac fibers.. The Journal of General Physiology. 87(6). 885–905. 13 indexed citations

19.

Scarpa, Antonio, et al.. (1972). The Effect of Calcium Ionophores on Fragmented Sarcoplasmic Reticulum. The Journal of General Physiology. 60(6). 735–749. 187 indexed citations

20.

Haugaard, Niels, Marilyn E. Hess, Joseph Shanfeld, Giuseppe Inesi, & W. R. Kukovetz. (1961). THE DETERMINATION OF PHOSPHORYLASE ACTIVITY IN PERFUSED RAT HEART. Journal of Pharmacology and Experimental Therapeutics. 131(2). 137–142. 11 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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