Giuseppe Zanotti

8.7k total citations
235 papers, 6.8k citations indexed

About

Giuseppe Zanotti is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Giuseppe Zanotti has authored 235 papers receiving a total of 6.8k indexed citations (citations by other indexed papers that have themselves been cited), including 143 papers in Molecular Biology, 42 papers in Materials Chemistry and 40 papers in Organic Chemistry. Recurrent topics in Giuseppe Zanotti's work include Enzyme Structure and Function (36 papers), Helicobacter pylori-related gastroenterology studies (28 papers) and Protein Structure and Dynamics (23 papers). Giuseppe Zanotti is often cited by papers focused on Enzyme Structure and Function (36 papers), Helicobacter pylori-related gastroenterology studies (28 papers) and Protein Structure and Dynamics (23 papers). Giuseppe Zanotti collaborates with scholars based in Italy, Germany and United States. Giuseppe Zanotti's co-authors include R. Berni, Roberto Battistutta, Laura Cendron, Hugo L. Monaco, Paola Spadon, Lorenzo A. Pinna, Stefania Sarno, Claudia Folli, E. Papinutto and E. De Moliner and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Giuseppe Zanotti

232 papers receiving 6.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Giuseppe Zanotti Italy	45	4.1k	894	832	643	641	235	6.8k
Enrico Di United States	52	4.8k 1.2×	714 0.8×	445 0.5×	568 0.9×	383 0.6×	241	9.8k
A. D’Arcy Switzerland	41	4.0k 1.0×	958 1.1×	619 0.7×	932 1.4×	286 0.4×	61	7.0k
Malcolm D. Walkinshaw United Kingdom	57	6.2k 1.5×	1.0k 1.2×	1.3k 1.6×	1.4k 2.1×	423 0.7×	285	10.0k
Toshiki Tanaka Japan	42	3.4k 0.8×	671 0.8×	410 0.5×	767 1.2×	497 0.8×	239	6.2k
Jesper V. Møller Denmark	50	6.9k 1.7×	474 0.5×	529 0.6×	820 1.3×	515 0.8×	150	8.8k
Adrian Goldman Finland	44	7.0k 1.7×	1.5k 1.7×	972 1.2×	713 1.1×	236 0.4×	178	10.8k
Kenneth B. Tomer United States	63	5.0k 1.2×	631 0.7×	1.1k 1.3×	605 0.9×	179 0.3×	259	12.4k
Elmar Krieger Netherlands	34	7.1k 1.8×	1.2k 1.4×	805 1.0×	730 1.1×	234 0.4×	45	11.6k
Vladimı́r Saudek Czechia	39	6.0k 1.5×	932 1.0×	647 0.8×	469 0.7×	205 0.3×	96	8.4k
Bruno O. Villoutreix France	49	3.9k 1.0×	439 0.5×	907 1.1×	616 1.0×	333 0.5×	221	8.5k

Countries citing papers authored by Giuseppe Zanotti

Since Specialization

Citations

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

Fields of papers citing papers by Giuseppe Zanotti

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Giuseppe Zanotti

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

Surana, Sunaina, David Villarroel‐Campos, Sergey S. Novoselov, et al.. (2024). The tyrosine phosphatases LAR and PTPRδ act as receptors of the nidogen-tetanus toxin complex. The EMBO Journal. 43(16). 3358–3387. 2 indexed citations

Grinzato, Alessandro, Pascal Albanese, Roberto Marotta, et al.. (2020). High-Light versus Low-Light: Effects on Paired Photosystem II Supercomplex Structural Rearrangement in Pea Plants. International Journal of Molecular Sciences. 21(22). 8643–8643. 14 indexed citations

Zanotti, Giuseppe & Laura Cendron. (2019). Structural Aspects of Helicobacter pylori Antibiotic Resistance. Advances in experimental medicine and biology. 1149. 227–241. 22 indexed citations

Loconte, Valentina, et al.. (2017). Structural characterization of FlgE2 protein from Helicobacter pylori hook. FEBS Journal. 284(24). 4328–4342. 6 indexed citations

Cavazzini, Davide, Guido Grossi, Francesca Vallese, et al.. (2017). A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mycorrhizal fungus Tuber melanosporum. Scientific Reports. 7(1). 7628–7628. 9 indexed citations

Calí, Tito, Laura Luoni, Francesco Zonta, et al.. (2016). The ataxia related G1107D mutation of the plasma membrane Ca 2+ ATPase isoform 3 affects its interplay with calmodulin and the autoinhibition process. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1863(1). 165–173. 22 indexed citations

Giacovazzo, Carmelo, Hugo L. Monaco, Gilberto Artioli, et al.. (2011). Fundamentals of Crystallography. Oxford University Press eBooks. 150 indexed citations

Cendron, Laura, Elisabetta Tasca, Anke Seydel, et al.. (2007). The crystal structure of CagS from the Helicobacter pylori pathogenicity island. Proteins Structure Function and Bioinformatics. 69(2). 440–443. 9 indexed citations

Zanotti, Giuseppe & R. Berni. (2004). Plasma Retinol-Binding Protein: Structure and Interactions with Retinol, Retinoids, and Transthyretin. Vitamins and hormones. 69. 271–295. 123 indexed citations

10.

Folli, Claudia, et al.. (2003). Distinctive binding and structural properties of piscine transthyretin. FEBS Letters. 555(2). 279–284. 24 indexed citations

11.

Platt, Daniel E., Concettina Guerra, Giuseppe Zanotti, & Isidore Rigoutsos. (2003). Global secondary structure packing angle bias in proteins. Proteins Structure Function and Bioinformatics. 53(2). 252–261. 7 indexed citations

12.

Sandei, L., et al.. (2000). Varietal comparison of processing tomato lines.. Informatore Agrario. 56(24). 49–53. 1 indexed citations

13.

Sandei, L., et al.. (2000). Evaluation of the lycopene content in HP (high pigment) processing tomato hybrids.. Informatore Agrario. 56(12). 83–87. 1 indexed citations

14.

Sandei, L., et al.. (2000). Comparison of mid-late and late tomato hybrids.. Informatore Agrario. 56(9). 49–51. 1 indexed citations

15.

Sandei, L., et al.. (2000). Efficacy of a new fungicide for industrial tomatoes.. Informatore Agrario. 56(8). 104–106. 1 indexed citations

16.

Zanotti, Giuseppe. (1999). Muscle fatty acid-binding protein. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1441(2-3). 94–105. 26 indexed citations

17.

Zanotti, Giuseppe, et al.. (1996). Active Site Structural Features for Chemically Modified Forms of Rhodanese. Journal of Biological Chemistry. 271(35). 21054–21061. 45 indexed citations

18.

Ptitsyn, Oleg B., et al.. (1993). Mechanism of pH‐induced release of retinol from retinol‐binding protein. FEBS Letters. 317(3). 181–184. 18 indexed citations

19.

Morelli, Maria Antonietta Castiglione, Annalisa Pastore, Carlo Pedone, et al.. (1991). Conformational study of cyclolinopeptide A. A distance geometry and molecular dynamics approach.. PubMed. 37(2). 81–9. 6 indexed citations

20.

Wieland, T, Barbro Beijer, Annemarie Seeliger, et al.. (1981). Components of the green deathcap toadstool amanita phalloides 59. the spatial structure of phallo toxins. European Journal of Organic Chemistry. 12. 2318–2334. 1 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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