Roberto Santucci

3.4k total citations
113 papers, 3.0k citations indexed

About

Roberto Santucci is a scholar working on Molecular Biology, Cell Biology and Electrical and Electronic Engineering. According to data from OpenAlex, Roberto Santucci has authored 113 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 70 papers in Molecular Biology, 50 papers in Cell Biology and 21 papers in Electrical and Electronic Engineering. Recurrent topics in Roberto Santucci's work include Hemoglobin structure and function (50 papers), Photosynthetic Processes and Mechanisms (35 papers) and Protein Structure and Dynamics (23 papers). Roberto Santucci is often cited by papers focused on Hemoglobin structure and function (50 papers), Photosynthetic Processes and Mechanisms (35 papers) and Protein Structure and Dynamics (23 papers). Roberto Santucci collaborates with scholars based in Italy, United States and Cuba. Roberto Santucci's co-authors include Federica Sinibaldi, Tommaso Ferri, Laura Fiorucci, Massimo Coletta, Fabio Polticelli, Alessandro Poscia, Franca Ascoli, Paolo Ascenzi, Maurizio Brunori and Giulietta Smulevich and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Roberto Santucci

113 papers receiving 2.9k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Roberto Santucci Italy	30	1.9k	729	696	575	338	113	3.0k
Igor V. Kurnikov United States	30	2.5k 1.4×	608 0.8×	382 0.5×	262 0.5×	377 1.1×	54	3.8k
Victor L. Davidson United States	43	4.9k 2.7×	415 0.6×	805 1.2×	222 0.4×	830 2.5×	223	5.9k
Michael H. Klapper United States	24	1.1k 0.6×	249 0.3×	292 0.4×	197 0.3×	313 0.9×	66	2.1k
James T. Hazzard United States	27	1.1k 0.6×	428 0.6×	238 0.3×	278 0.5×	171 0.5×	46	1.8k
James Terner United States	35	1.3k 0.7×	400 0.5×	646 0.9×	128 0.2×	1.4k 4.1×	69	3.5k
Clinton R. Nishida United States	23	745 0.4×	306 0.4×	167 0.2×	87 0.2×	272 0.8×	31	1.9k
Werner Mäntele Germany	39	2.9k 1.6×	334 0.5×	239 0.3×	303 0.5×	377 1.1×	113	4.1k
Shigetoshi Aono Japan	29	1.6k 0.9×	190 0.3×	1.1k 1.6×	119 0.2×	604 1.8×	129	2.7k
Maria Rosa Moncelli Italy	30	1.1k 0.6×	535 0.7×	61 0.1×	696 1.2×	97 0.3×	85	2.1k
Erik Sedlák Slovakia	25	1.3k 0.7×	215 0.3×	165 0.2×	119 0.2×	223 0.7×	91	1.8k

Countries citing papers authored by Roberto Santucci

Since Specialization

Citations

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

Fields of papers citing papers by Roberto Santucci

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Roberto Santucci

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

All Works

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20 of 20 papers shown

Ciaccio, Chiara, Theo Battista, Manuela Cervelli, et al.. (2017). The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket. Journal of Inorganic Biochemistry. 169. 86–96. 21 indexed citations

Santucci, Roberto, Federica Sinibaldi, Fabio Polticelli, & Laura Fiorucci. (2014). Role of Cardiolipin in Mitochondrial Diseases and Apoptosis. Current Medicinal Chemistry. 21(23). 2702–2714. 29 indexed citations

Ascenzi, Paolo, Chiara Ciaccio, Federica Sinibaldi, Roberto Santucci, & Massimo Coletta. (2011). Peroxynitrite detoxification by horse heart carboxymethylated cytochrome c is allosterically modulated by cardiolipin. Biochemical and Biophysical Research Communications. 415(3). 463–467. 23 indexed citations

Santucci, Roberto, et al.. (2010). Misfolded proteins and neurodegeneration: role of non-native cytochrome c in cell death. Expert Review of Proteomics. 7(4). 507–517. 30 indexed citations

Santucci, Roberto, Federica Sinibaldi, & Laura Fiorucci. (2008). Protein Folding, Unfolding and Misfolding: Role Played by Intermediate States. Mini-Reviews in Medicinal Chemistry. 8(1). 57–62. 22 indexed citations

Sinibaldi, Federica, Barry D. Howes, Giampiero Mei, et al.. (2005). Insights into the role of the histidines in the structure and stability of cytochrome c. JBIC Journal of Biological Inorganic Chemistry. 11(1). 52–62. 20 indexed citations

Abbruzzetti, Stefania, Cristiano Viappiani, Federica Sinibaldi, & Roberto Santucci. (2004). Kinetics of Histidine Dissociation From the Heme Fe(III) in N-fragment (residues 1–56) of Cytochrome c. The Protein Journal. 23(8). 519–527. 7 indexed citations

Sinibaldi, Federica, Barry D. Howes, Laura Fiorucci, et al.. (2004). The 40s ?-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c. JBIC Journal of Biological Inorganic Chemistry. 9(8). 997–1006. 16 indexed citations

Sanctis, Giampiero De, Chiara Ciaccio, Giovanni Francesco Fasciglione, et al.. (2004). Effect of Axial Coordination on the Kinetics of Assembly and Folding of the Two Halves of Horse Heart Cytochrome c. Journal of Biological Chemistry. 279(51). 52860–52868. 3 indexed citations

10.

Lombardi, Angela, Flavia Nastri, Daniela Marasco, et al.. (2003). Design of a New Mimochrome with Unique Topology. Chemistry - A European Journal. 9(22). 5643–5654. 38 indexed citations

11.

Ciaccio, Chiara, Giampiero De Sanctis, Federica Sinibaldi, et al.. (2003). Relationships of Ligand Binding, Redox Properties, and Protonation in Coprinus cinereus Peroxidase. Journal of Biological Chemistry. 278(21). 18730–18737. 6 indexed citations

12.

Sinibaldi, Federica, et al.. (2002). Glycerol-Induced Formation of the Molten Globule from Acid-Denatured Cytochrome c: Implication for Hierarchical Folding. Journal of Protein Chemistry. 21(1). 35–41. 17 indexed citations

13.

Ferri, Tommaso, et al.. (2001). An electrochemical multienzymatic biosensor for determination of cholesterol. Bioelectrochemistry. 54(1). 17–22. 70 indexed citations

14.

Priori, Alberto, Chiara Indiani, Giampiero De Sanctis, et al.. (2000). Anion- and pH-linked conformational transition in horseradish peroxidase. Journal of Inorganic Biochemistry. 79(1-4). 25–30. 6 indexed citations

15.

Coletta, Massimo, Mauro Angeletti, I. Ascone, et al.. (1999). Heterotropic Effectors Exert More Significant Strain on Monoligated than on Unligated Hemoglobin. Biophysical Journal. 76(3). 1532–1536. 13 indexed citations

16.

Santucci, Roberto & Franca Ascoli. (1997). The Soret circular dichroism spectrum as a probe for the heme Fe(III)-Met(80) axial bond in horse cytochrome c. Journal of Inorganic Biochemistry. 68(3). 211–214. 78 indexed citations

17.

Ascenzi, Paolo, Alberto Bertollini, Roberto Santucci, et al.. (1993). Cooperative effect of inositol hexakisphosphate, bezafibrate, and clofibric acid on the spectroscopic properties of the nitric oxide derivative of ferrous human hemoglobin. Journal of Inorganic Biochemistry. 50(4). 263–272. 17 indexed citations

18.

Ascenzi, Paolo, Massimo Coletta, Alessandro Desideri, et al.. (1992). Effect of bezafibrate and clofibric acid on the spectroscopic properties of the nitric oxide derivative of ferrous human hemoglobin. Journal of Inorganic Biochemistry. 48(1). 47–53. 4 indexed citations

19.

Santucci, Roberto, et al.. (1988). Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin. Journal of Inorganic Biochemistry. 32(4). 225–232. 11 indexed citations

20.

Coletta, Massimo, et al.. (1987). Redox properties of components I and IV of trout hemoglobins: kinetic and potentiometric studies. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 915(3). 415–419. 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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