C. Vaccaro

455 total citations
16 papers, 385 citations indexed

About

C. Vaccaro is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, C. Vaccaro has authored 16 papers receiving a total of 385 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 6 papers in Materials Chemistry and 4 papers in Cell Biology. Recurrent topics in C. Vaccaro's work include Enzyme Structure and Function (6 papers), Protein Structure and Dynamics (4 papers) and Hemoglobin structure and function (4 papers). C. Vaccaro is often cited by papers focused on Enzyme Structure and Function (6 papers), Protein Structure and Dynamics (4 papers) and Hemoglobin structure and function (4 papers). C. Vaccaro collaborates with scholars based in Italy, Belarus and Canada. C. Vaccaro's co-authors include Roberto Nucci, Marco Moracci, Ferdinando Febbraio, Maura Rossi, Raffaella Briante, Mosé Rossi, F. La Cara, Miriam Rossi, M. Patumi and Francesco La Cara and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Journal of Agricultural and Food Chemistry.

In The Last Decade

C. Vaccaro

16 papers receiving 367 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
C. Vaccaro Italy	9	242	113	107	63	56	16	385
M. Trop Israel	9	230 1.0×	43 0.4×	85 0.8×	41 0.7×	61 1.1×	20	420
Dae-Ook Kang South Korea	11	229 0.9×	108 1.0×	57 0.5×	16 0.3×	38 0.7×	37	348
Jana Dostálová Czechia	10	156 0.6×	86 0.8×	21 0.2×	10 0.2×	84 1.5×	25	433
Susan Heffron United States	8	320 1.3×	36 0.3×	65 0.6×	43 0.7×	28 0.5×	8	460
Imen Aissa Tunisia	12	230 1.0×	104 0.9×	32 0.3×	12 0.2×	49 0.9×	25	394
Paul Sauve France	13	295 1.2×	17 0.2×	46 0.4×	37 0.6×	14 0.3×	20	442
P. Nordin United States	12	258 1.1×	46 0.4×	154 1.4×	18 0.3×	53 0.9×	32	523
Yoshikiyo Sakakibara Japan	13	292 1.2×	22 0.2×	86 0.8×	21 0.3×	19 0.3×	18	451
Masugu Kamei Japan	8	246 1.0×	83 0.7×	45 0.4×	7 0.1×	36 0.6×	14	362
Coralie Bompard-Gilles Belgium	6	227 0.9×	22 0.2×	120 1.1×	47 0.7×	24 0.4×	6	324

Countries citing papers authored by C. Vaccaro

Since Specialization

Citations

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

Fields of papers citing papers by C. Vaccaro

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of C. Vaccaro

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

All Works

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16 of 16 papers shown

Febbraio, Ferdinando, Annapaola Andolfo, Fabio Tanfani, et al.. (2004). Thermal Stability and Aggregation of Sulfolobus solfataricus β-Glycosidase Are Dependent upon the N-∈-Methylation of Specific Lysyl Residues. Journal of Biological Chemistry. 279(11). 10185–10194. 35 indexed citations

Briante, Raffaella, M. Patumi, Ferdinando Febbraio, et al.. (2002). Changes in phenolic and enzymatic activities content during fruit ripening in two Italian cultivars of Olea europaea L.. Plant Science. 162(5). 791–798. 66 indexed citations

Shames, Alexander I., Roberto Nucci, Sabato D’Auria, et al.. (2000). EPR spin labeling study of conformational transitions of β-glycosidase from the hyperthermophilic archaeonSulfolobus solfataricus expressed inEscherichia coli. Applied Magnetic Resonance. 18(4). 515–526. 3 indexed citations

Briante, Raffaella, Sabato D’Auria, Ferdinando Febbraio, et al.. (1999). Purification and Characterization of a Lipoxygenase Enzyme from Durum Wheat Semolina. Journal of Agricultural and Food Chemistry. 47(5). 1924–1931. 24 indexed citations

D’Auria, Sabato, Alessandra Morana, Ferdinando Febbraio, et al.. (1996). Functional and Structural Properties of the Homogeneous β-Glycosidase from the Extreme Thermoacidophilic ArchaeonSulfolobus solfataricusExpressed inSaccharomyces cerevisiae. Protein Expression and Purification. 7(3). 299–308. 20 indexed citations

Moracci, Marco, Roberto Nucci, Ferdinando Febbraio, et al.. (1995). Expression and extensive characterization of a β-glycosidase from the extreme thermoacidophilic archaeon Sulfolobus solfataricus in Escherichia coli: Authenticity of the recombinant enzyme. Enzyme and Microbial Technology. 17(11). 992–997. 67 indexed citations

Patumi, M., G. Fontanazza, Roberto Nucci, & C. Vaccaro. (1994). PRELIMINARY STUDIES ON ISOENZYMATIC AND ENZYMATIC ACTIVITIES ISOLATED FROM OLIVE PLANTS.. Acta Horticulturae. 95–97. 3 indexed citations

Nucci, Roberto, et al.. (1993). Exo‐glucosidase activity and substrate specificity of the beta‐glycosidase isolated from the extreme thermophile Sulfolobus solfataricus. Biotechnology and Applied Biochemistry. 17(2). 239–250. 85 indexed citations

Whitehead, Edward P., Roberto Nucci, C. Vaccaro, & Mosé Rossi. (1991). Hill coefficient ratios give binding ratios of allosteric enzyme effectors; inhibition, activation, and squatting in deoxycytidylate aminohydrolase (EC 3.5.4.12). Archives of Biochemistry and Biophysics. 289(1). 12–18. 3 indexed citations

10.

Nucci, Roberto, Carlo A. Raia, C. Vaccaro, Mosé Rossi, & Edward P. Whitehead. (1991). Allosteric modifier and substrate binding of donkey deoxycytidylate aminohydrolase (EC 3.5.4.12). Archives of Biochemistry and Biophysics. 289(1). 19–25. 10 indexed citations

11.

Rossi, Miriam, J. Bouchard, Simonetta Bartolucci, et al.. (1986). 5-AZA-2′-Deoxycytidine Synergistic action with Thymidine on Leukemic Cells and Interaction of 5-AZA-dCMP with dCMP Deaminase. Advances in experimental medicine and biology. 195 Pt B. 157–163. 6 indexed citations

12.

Rossi, Miriam, et al.. (1984). Kinetic interaction of 5-AZA-2'-deoxycytidine-5'-monophosphate and its 5'-triphosphate with deoxycytidylate deaminase.. Molecular Pharmacology. 25(3). 436–440. 25 indexed citations

13.

Nucci, Roberto, et al.. (1983). Analysis of competition for substrate sites in an allosteric enzyme with co‐operative kinetics. European Journal of Biochemistry. 137(3). 421–427. 6 indexed citations

14.

Raia, Carlo A., et al.. (1982). Reversal of the effect of the allosteric ligands of dCMP-aminohydrolase and stabilization of the enzyme in the T form. Journal of Molecular Biology. 157(3). 557–570. 6 indexed citations

15.

Nucci, Roberto, et al.. (1978). Freezing of dCMP aminohydrolase in the activated conformation by glutaraldehyde. Journal of Molecular Biology. 124(1). 133–145. 24 indexed citations

16.

Cervone, Felice, et al.. (1974). The Role of the Sulphydryl Groups of Spleen Deoxycytidylate Aminohydrolase. European Journal of Biochemistry. 46(2). 401–405. 2 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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