Roberto Boggio

1.3k total citations
21 papers, 982 citations indexed

About

Roberto Boggio is a scholar working on Molecular Biology, Oncology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Roberto Boggio has authored 21 papers receiving a total of 982 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 6 papers in Oncology and 4 papers in Cellular and Molecular Neuroscience. Recurrent topics in Roberto Boggio's work include Histone Deacetylase Inhibitors Research (8 papers), Protein Degradation and Inhibitors (8 papers) and Peptidase Inhibition and Analysis (6 papers). Roberto Boggio is often cited by papers focused on Histone Deacetylase Inhibitors Research (8 papers), Protein Degradation and Inhibitors (8 papers) and Peptidase Inhibition and Analysis (6 papers). Roberto Boggio collaborates with scholars based in Italy, United States and United Kingdom. Roberto Boggio's co-authors include Susanna Chiocca, Riccardo Colombo, Giulio Draetta, Ronald T. Hay, Andreas Weiss, Christian Seiser, Douglas Macdonald, Edward J. Wild, Blair R. Leavitt and Rainer Kühn 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

Roberto Boggio

21 papers receiving 971 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Roberto Boggio Italy 16 785 275 169 137 129 21 982
Donald E. Spratt United States 17 814 1.0× 78 0.3× 212 1.3× 92 0.7× 144 1.1× 43 1.1k
Ernest Knight United States 10 646 0.8× 113 0.4× 92 0.5× 112 0.8× 32 0.2× 18 871
Jessica Robert France 7 1.1k 1.4× 83 0.3× 287 1.7× 87 0.6× 22 0.2× 8 1.3k
Nathan J. Moerke United States 10 948 1.2× 87 0.3× 93 0.6× 90 0.7× 33 0.3× 15 1.2k
Prasanna Venkatraman India 12 599 0.8× 229 0.8× 76 0.4× 34 0.2× 61 0.5× 36 808
Key-Sun Kim South Korea 12 426 0.5× 58 0.2× 154 0.9× 139 1.0× 25 0.2× 17 717
Heeseon An United States 16 731 0.9× 46 0.2× 128 0.8× 37 0.3× 59 0.5× 19 1.1k
Raymond Mak United States 6 1.2k 1.6× 56 0.2× 68 0.4× 53 0.4× 92 0.7× 8 1.4k
S. Ahn South Korea 21 2.7k 3.4× 63 0.2× 199 1.2× 82 0.6× 16 0.1× 41 2.9k
Kimiko Tsutsui Japan 20 930 1.2× 146 0.5× 256 1.5× 27 0.2× 76 0.6× 38 1.1k

Countries citing papers authored by Roberto Boggio

Since Specialization
Citations

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

Fields of papers citing papers by Roberto Boggio

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Roberto Boggio

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

All Works

20 of 20 papers shown
1.
Bresciani, Alberto, Roberto Boggio, Cristina Cariulo, et al.. (2018). Quantifying autophagy using novel LC3B and p62 TR-FRET assays. PLoS ONE. 13(3). e0194423–e0194423. 34 indexed citations
2.
Fodale, Valentina, Roberto Boggio, Cristina Cariulo, et al.. (2017). Validation of Ultrasensitive Mutant Huntingtin Detection in Human Cerebrospinal Fluid by Single Molecule Counting Immunoassay. Journal of Huntington s Disease. 6(4). 349–361. 38 indexed citations
3.
Cariulo, Cristina, Margherita Verani, Roberto Boggio, et al.. (2017). Phosphorylation of huntingtin at residue T3 is decreased in Huntington’s disease and modulates mutant huntingtin protein conformation. Proceedings of the National Academy of Sciences. 114(50). E10809–E10818. 50 indexed citations
4.
Thaler, Florian, Raffaella Amici, Agnese Abate, et al.. (2015). Synthesis, biological characterization and molecular modeling insights of spirochromanes as potent HDAC inhibitors. European Journal of Medicinal Chemistry. 108. 53–67. 28 indexed citations
5.
Wild, Edward J., Roberto Boggio, Douglas R. Langbehn, et al.. (2015). Quantification of mutant huntingtin protein in cerebrospinal fluid from Huntington’s disease patients. Journal of Clinical Investigation. 125(5). 1979–1986. 173 indexed citations
6.
7.
Fodale, Valentina, Margherita Verani, Cristina Cariulo, et al.. (2014). Polyglutamine- and Temperature-Dependent Conformational Rigidity in Mutant Huntingtin Revealed by Immunoassays and Circular Dichroism Spectroscopy. PLoS ONE. 9(12). e112262–e112262. 34 indexed citations
8.
Valente, Sérgio, Daniela Trisciuoglio, Maria Tardugno, et al.. (2013). tert‐Butylcarbamate‐Containing Histone Deacetylase Inhibitors: Apoptosis Induction, Cytodifferentiation, and Antiproliferative Activities in Cancer Cells. ChemMedChem. 8(5). 800–811. 17 indexed citations
9.
Thaler, Florian, Mario Varasi, Agnese Abate, et al.. (2013). Synthesis and biological characterization of spiro[2H-(1,3)-benzoxazine-2,4′-piperidine] based histone deacetylase inhibitors. European Journal of Medicinal Chemistry. 64. 273–284. 14 indexed citations
10.
Thaler, Florian, Mario Varasi, Andrea Colombo, et al.. (2012). Spiro[chromane‐2,4′‐piperidine]‐Based Histone Deacetylase Inhibitors with Improved in vivo Activity. ChemMedChem. 7(4). 709–721. 11 indexed citations
11.
Varasi, Mario, Florian Thaler, Agnese Abate, et al.. (2011). Discovery, Synthesis, and Pharmacological Evaluation of Spiropiperidine Hydroxamic Acid Based Derivatives as Structurally Novel Histone Deacetylase (HDAC) Inhibitors. Journal of Medicinal Chemistry. 54(8). 3051–3064. 45 indexed citations
12.
Thaler, Florian, Mario Varasi, Andrea Colombo, et al.. (2010). Synthesis and Biological Characterization of Amidopropenyl Hydroxamates as HDAC Inhibitors. ChemMedChem. 5(8). 1359–1372. 13 indexed citations
13.
Riising, Eva M., Roberto Boggio, Susanna Chiocca, Kristian Helin, & Diego Pasini. (2008). The Polycomb Repressive Complex 2 Is a Potential Target of SUMO Modifications. PLoS ONE. 3(7). e2704–e2704. 50 indexed citations
14.
Pirali, Tracey, Francesca Pagliai, Ciro Mercurio, et al.. (2008). Triazole-Modified Histone Deacetylase Inhibitors As a Rapid Route to Drug Discovery. Journal of Combinatorial Chemistry. 10(5). 624–627. 22 indexed citations
15.
Boggio, Roberto, et al.. (2007). Targeting SUMO E1 to Ubiquitin Ligases. Journal of Biological Chemistry. 282(21). 15376–15382. 71 indexed citations
16.
Boggio, Roberto & Susanna Chiocca. (2006). Viruses and sumoylation: recent highlights. Current Opinion in Microbiology. 9(4). 430–436. 76 indexed citations
17.
Boggio, Roberto & Susanna Chiocca. (2005). Gam1 and the SUMO Pathway. Cell Cycle. 4(4). 533–535. 18 indexed citations
18.
Boggio, Roberto, Riccardo Colombo, Ronald T. Hay, Giulio Draetta, & Susanna Chiocca. (2004). A Mechanism for Inhibiting the SUMO Pathway. Molecular Cell. 16(4). 549–561. 153 indexed citations
19.
Chiocca, Susanna, Riccardo Colombo, Roberto Boggio, et al.. (2002). Histone Deacetylase 1 Inactivation by an Adenovirus Early Gene Product. Current Biology. 12(7). 594–598. 39 indexed citations
20.
Lutz, Raymond P., et al.. (1971). Dual reaction pathways in an open-chain Cope rearrangement. Journal of the American Chemical Society. 93(16). 3985–3990. 13 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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