Roberta Chiaraluce

2.1k total citations
64 papers, 1.7k citations indexed

About

Roberta Chiaraluce is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Roberta Chiaraluce has authored 64 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 44 papers in Molecular Biology, 26 papers in Materials Chemistry and 18 papers in Biochemistry. Recurrent topics in Roberta Chiaraluce's work include Enzyme Structure and Function (26 papers), Amino Acid Enzymes and Metabolism (17 papers) and Protein Structure and Dynamics (13 papers). Roberta Chiaraluce is often cited by papers focused on Enzyme Structure and Function (26 papers), Amino Acid Enzymes and Metabolism (17 papers) and Protein Structure and Dynamics (13 papers). Roberta Chiaraluce collaborates with scholars based in Italy, United Kingdom and Netherlands. Roberta Chiaraluce's co-authors include Valerio Consalvi, Roberto Scandurra, Laura Politi, Alessandra Pasquo, Mario De Rosa, R Scandurra, K.L. Britton, Patrick J. Baker, P.J. Artymiuk and Paul C. Engel and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Roberta Chiaraluce

64 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Roberta Chiaraluce Italy	22	1.1k	590	275	192	168	64	1.7k
Valerio Consalvi Italy	22	1.2k 1.1×	599 1.0×	285 1.0×	204 1.1×	171 1.0×	76	1.9k
Paul M. Horowitz United States	28	1.5k 1.3×	531 0.9×	421 1.5×	75 0.4×	206 1.2×	114	2.3k
R. Berni Italy	29	1.8k 1.6×	288 0.5×	142 0.5×	65 0.3×	97 0.6×	80	2.4k
Gèrhard Kopperschläger Germany	23	1.6k 1.5×	451 0.8×	116 0.4×	108 0.6×	167 1.0×	106	2.3k
Paul V. Attwood Australia	32	2.0k 1.8×	614 1.0×	428 1.6×	50 0.3×	113 0.7×	93	3.0k
Brian J. Bahnson United States	27	1.3k 1.2×	422 0.7×	180 0.7×	62 0.3×	124 0.7×	58	2.0k
Eberhard Hofmann Germany	21	1.6k 1.5×	371 0.6×	173 0.6×	106 0.6×	191 1.1×	138	2.4k
Karsten Niefind Germany	29	2.4k 2.2×	830 1.4×	210 0.8×	258 1.3×	598 3.6×	93	3.3k
Chen‐Lu Tsou China	25	1.5k 1.3×	547 0.9×	63 0.2×	133 0.7×	120 0.7×	60	1.9k
Laurence Serre France	22	1.5k 1.3×	285 0.5×	63 0.2×	83 0.4×	145 0.9×	44	2.1k

Countries citing papers authored by Roberta Chiaraluce

Since Specialization

Citations

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

Fields of papers citing papers by Roberta Chiaraluce

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Roberta Chiaraluce

This figure shows the co-authorship network connecting the top 25 collaborators of Roberta Chiaraluce. A scholar is included among the top collaborators of Roberta Chiaraluce 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 Roberta Chiaraluce. Roberta Chiaraluce 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

Petrosino, Maria, Alessandra Pasquo, Paola Turina, et al.. (2023). The complex impact of cancer-related missense mutations on the stability and on the biophysical and biochemical properties of MAPK1 and MAPK3 somatic variants. Human Genomics. 17(1). 95–95. 2 indexed citations

Petrosino, Maria, Alessandra Pasquo, Roberta Chiaraluce, et al.. (2021). Analysis and Interpretation of the Impact of Missense Variants in Cancer. International Journal of Molecular Sciences. 22(11). 5416–5416. 44 indexed citations

Fiorillo, Annarita, Maria Petrosino, Andrea Ilari, et al.. (2018). The phosphoglycerate kinase 1 variants found in carcinoma cells display different catalytic activity and conformational stability compared to the native enzyme. PLoS ONE. 13(7). e0199191–e0199191. 20 indexed citations

Demurtas, Olivia Costantina, Silvia Massa, Paola Di Bonito, et al.. (2016). Production of functional, stable, unmutated recombinant human papillomavirus E6 oncoprotein: implications for HPV-tumor diagnosis and therapy. Journal of Translational Medicine. 14(1). 224–224. 13 indexed citations

Pasquo, Alessandra, et al.. (2013). Effect of Single Amino Acid Substitution Observed in Cancer on Pim-1 Kinase Thermodynamic Stability and Structure. PLoS ONE. 8(6). e64824–e64824. 22 indexed citations

Giordano, Cesare, Anna Sansone, Annalisa Masi, et al.. (2011). Inhibition of Amyloid Peptide Fragment Aβ_25–35 Fibrillogenesis and Toxicity by N‐Terminal β‐Amino Acid‐Containing Esapeptides: Is Taurine Moiety Essential for In Vivo Effects?. Chemical Biology & Drug Design. 79(1). 30–37. 16 indexed citations

Villani, Maria Elena, Veronica Morea, Valerio Consalvi, et al.. (2008). Humanization of a highly stable single-chain antibody by structure-based antigen-binding site grafting. Molecular Immunology. 45(9). 2474–2485. 16 indexed citations

Giorgi, Alessandra, Giuseppina Mignogna, Giuliano Bellapadrona, et al.. (2008). The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi. Archives of Biochemistry and Biophysics. 478(1). 69–74. 47 indexed citations

Chiaraluce, Roberta, Rita Florio, Sebastiana Angelaccio, et al.. (2007). Tertiary structure in 7.9 m guanidinium chloride − the role of Glu53 and Asp287 in Pyrococcus furiosus endo‐β‐1,3‐glucanase. FEBS Journal. 274(23). 6167–6179. 3 indexed citations

10.

Desiderio, Angiola, Rosella Franconi, Marián López, et al.. (2001). A semi-synthetic repertoire of intrinsically stable antibody fragments derived from a single-framework scaffold 1 1Edited by J. Kahn. Journal of Molecular Biology. 310(3). 603–615. 63 indexed citations

11.

Chiaraluce, Roberta, Valerio Consalvi, Stefano Cavallo, et al.. (2000). The unusual dodecameric ferritin from Listeria innocua dissociates below pH 2.0. European Journal of Biochemistry. 267(18). 5733–5741. 25 indexed citations

12.

Tavladoraki, Paraskevi, Alessandra Girotti, Marcello Donini, et al.. (1999). A single‐chain antibody fragment is functionally expressed in the cytoplasm of bothEscherichia coliand transgenic plants. European Journal of Biochemistry. 262(2). 617–624. 42 indexed citations

13.

Scandurra, R, Valerio Consalvi, Roberta Chiaraluce, Laura Politi, & Paul C. Engel. (1998). Protein thermostability in extremophiles. Biochimie. 80(11). 933–941. 109 indexed citations

14.

Consalvi, Valerio, Roberta Chiaraluce, Stefania Millevoi, et al.. (1996). Refolding Pathway and Association Intermediates of Glutamate Dehydrogenase from the Hyperthermophile Pyrococcus furiosus. European Journal of Biochemistry. 239(3). 679–685. 13 indexed citations

15.

Britton, K.L., P.J. Artymiuk, Patrick J. Baker, et al.. (1995). The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure. 3(11). 1147–1158. 364 indexed citations

16.

Maras, Bruno, Roberta Chiaraluce, Valerio Consalvi, et al.. (1994). The amino acid sequence of glutamate dehydrogenase fromPyrococcus furiosus, a hyperthermophilic archaebacterium. Journal of Protein Chemistry. 13(2). 253–259. 19 indexed citations

17.

Consalvi, Valerio, et al.. (1991). Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus. European Journal of Biochemistry. 202(3). 1189–1196. 88 indexed citations

18.

Consalvi, Valerio, Roberta Chiaraluce, Laura Politi, et al.. (1991). Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. European Journal of Biochemistry. 196(2). 459–467. 65 indexed citations

19.

Politi, Laura, et al.. (1989). Oxalate, phosphate and sulphate determination in serum and urine by ion chromatography. Clinica Chimica Acta. 184(2). 155–165. 28 indexed citations

20.

Ricci, Giorgio, Roberta Chiaraluce, Giuseppina Pitari, et al.. (1989). Photooxidation of hypotaurine to taurine in the presence of flavins.. Journal of Nutritional Science and Vitaminology. 35(2). 143–153. 3 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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