Nino Campobasso

2.7k total citations
25 papers, 775 citations indexed

About

Nino Campobasso is a scholar working on Molecular Biology, Materials Chemistry and Renewable Energy, Sustainability and the Environment. According to data from OpenAlex, Nino Campobasso has authored 25 papers receiving a total of 775 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 8 papers in Materials Chemistry and 6 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Nino Campobasso's work include Metalloenzymes and iron-sulfur proteins (6 papers), Enzyme Structure and Function (6 papers) and Metabolism and Genetic Disorders (5 papers). Nino Campobasso is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (6 papers), Enzyme Structure and Function (6 papers) and Metabolism and Genetic Disorders (5 papers). Nino Campobasso collaborates with scholars based in United States, United Kingdom and Switzerland. Nino Campobasso's co-authors include Tadhg P. Begley, Cynthia Kinsland, Hsiu‐Ju Chiu, Jason J. Reddick, S.E. Ealick, S. E. Ealick, Fred W. McLafferty, Adolphus P. G. M. van Loon, Sean V. Taylor and Diana M. Downs and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Nino Campobasso

25 papers receiving 767 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Nino Campobasso United States 14 482 135 101 98 98 25 775
G. Obmolova Germany 17 805 1.7× 367 2.7× 257 2.5× 50 0.5× 363 3.7× 20 1.1k
Qingfei Zheng United States 25 977 2.0× 75 0.6× 138 1.4× 40 0.4× 27 0.3× 63 1.5k
Isabelle Correia France 15 680 1.4× 65 0.5× 63 0.6× 11 0.1× 51 0.5× 34 921
Jaru Jancarik United States 16 703 1.5× 301 2.2× 27 0.3× 22 0.2× 79 0.8× 19 902
Mirella Vivoli United Kingdom 15 404 0.8× 115 0.9× 21 0.2× 46 0.5× 88 0.9× 27 581
Rudolf Kaiser Sweden 16 649 1.3× 101 0.7× 82 0.8× 15 0.2× 111 1.1× 28 1.0k
T. Conn Mallett United States 13 684 1.4× 111 0.8× 34 0.3× 8 0.1× 215 2.2× 15 955
Dominic J. B. Hunter Australia 19 731 1.5× 87 0.6× 9 0.1× 83 0.8× 21 0.2× 38 1.2k
I. D’Angelo Canada 16 756 1.6× 107 0.8× 10 0.1× 102 1.0× 18 0.2× 23 1.1k
Virginia L. Rath United States 16 871 1.8× 124 0.9× 31 0.3× 10 0.1× 31 0.3× 23 1.2k

Countries citing papers authored by Nino Campobasso

Since Specialization
Citations

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

Fields of papers citing papers by Nino Campobasso

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Nino Campobasso

This figure shows the co-authorship network connecting the top 25 collaborators of Nino Campobasso. A scholar is included among the top collaborators of Nino Campobasso 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 Nino Campobasso. Nino Campobasso 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.
Reihill, James, Melisa W-Y. Ho, Jeffrey M. Axten, et al.. (2022). A highly selective, cell-permeable furin inhibitor BOS-318 rescues key features of cystic fibrosis airway disease. Cell chemical biology. 29(6). 947–957.e8. 18 indexed citations
2.
Pearce, Kenneth H., Laurie K. Overton, Robert T. Gampe, et al.. (2019). BacMam production and crystal structure of nonglycosylated apo human furin at 1.89 Å resolution. Acta Crystallographica Section F Structural Biology Communications. 75(4). 239–245. 12 indexed citations
3.
Spletstoser, Jared T., Andrew B. Benowitz, Nino Campobasso, et al.. (2019). Discovery of piperazic acid peptide deformylase inhibitors with in vivo activity for respiratory tract and skin infections. Bioorganic & Medicinal Chemistry Letters. 29(16). 2410–2414. 5 indexed citations
4.
Béliveau, François, Sébastien P. Dion, Antoine Désilets, et al.. (2019). Discovery and Development of TMPRSS6 Inhibitors Modulating Hepcidin Levels in Human Hepatocytes. Cell chemical biology. 26(11). 1559–1572.e9. 25 indexed citations
5.
Campobasso, Nino & D.P. Huddler. (2015). Hydrogen deuterium mass spectrometry in drug discovery. Bioorganic & Medicinal Chemistry Letters. 25(18). 3771–3776. 17 indexed citations
6.
Concha, N.O., Angela Smallwood, William G. Bonnette, et al.. (2015). Long-Range Inhibitor-Induced Conformational Regulation of Human IRE1α Endoribonuclease Activity. Molecular Pharmacology. 88(6). 1011–1023. 42 indexed citations
7.
Axten, Jeffrey M., Jesús R. Medina, Charles W. Blackledge, et al.. (2012). Acylprolinamides: A new class of peptide deformylase inhibitors with in vivo antibacterial activity. Bioorganic & Medicinal Chemistry Letters. 22(12). 4028–4032. 5 indexed citations
8.
Totoritis, Rachel D., Chaya Duraiswami, Amy Taylor, et al.. (2011). Understanding the Origins of Time-Dependent Inhibition by Polypeptide Deformylase Inhibitors. Biochemistry. 50(31). 6642–6654. 3 indexed citations
9.
Zuercher, William J., Richard G. Buckholz, Nino Campobasso, et al.. (2010). Discovery of Tertiary Sulfonamides as Potent Liver X Receptor Antagonists. Journal of Medicinal Chemistry. 53(8). 3412–3416. 81 indexed citations
10.
Washburn, David G., Tram H. Hoang, Nino Campobasso, et al.. (2009). Synthesis and SAR of potent LXR agonists containing an indole pharmacophore. Bioorganic & Medicinal Chemistry Letters. 19(4). 1097–1100. 15 indexed citations
11.
Theisen, Michael J., et al.. (2004). 3-hydroxy-3-methylglutaryl–CoA synthase intermediate complex observed in “real-time”. Proceedings of the National Academy of Sciences. 101(47). 16442–16447. 48 indexed citations
12.
Campobasso, Nino, et al.. (2004). Staphylococcus aureus 3-Hydroxy-3-methylglutaryl-CoA Synthase. Journal of Biological Chemistry. 279(43). 44883–44888. 52 indexed citations
13.
Chiu, Hsiu‐Ju, et al.. (2001). Structural Characterization of the Enzyme−Substrate, Enzyme−Intermediate, and Enzyme−Product Complexes of Thiamin Phosphate Synthase,. Biochemistry. 40(34). 10103–10114. 38 indexed citations
14.
Begley, Tadhg P., Diana M. Downs, S. E. Ealick, et al.. (1999). Thiamin biosynthesis in prokaryotes. Archives of Microbiology. 171(5). 293–300. 239 indexed citations
15.
Campobasso, Nino, Colleen A. Costello, Cynthia Kinsland, Tadhg P. Begley, & S.E. Ealick. (1998). Crystal Structure of Thiaminase-I from Bacillus thiaminolyticus at 2.0 Å Resolution,. Biochemistry. 37(45). 15981–15989. 31 indexed citations
16.
Campobasso, Nino, Jakob Begun, Colleen A. Costello, Tadhg P. Begley, & S. E. Ealick. (1998). Crystallization and preliminary X-ray analysis of thiaminase I from Bacillus thiaminolyticus: space group change upon freezing of crystals. Acta Crystallographica Section D Biological Crystallography. 54(3). 448–450. 6 indexed citations
17.
Campobasso, Nino, et al.. (1993). Structure and environment of metal clusters in the nitrogenase molybdenum-iron protein from Clostridium pasteurianum.. 186–195. 1 indexed citations
18.
Christiansen, Jason, Nino Campobasso, Jeffrey T. Bolin, et al.. (1993). Verfeinerung eines Modells für den Nitrogenase-Mo-Fe-Cluster mit Einkristall-Mo- und -Fe-EXAFS. Angewandte Chemie. 105(11). 1661–1663. 2 indexed citations
19.
Chen, Jie, Jason Christiansen, Nino Campobasso, et al.. (1993). Verfeinerung eines Modells für den Nitrogenase‐Mo‐Fe‐Cluster mit Einkristall‐Mo‐ und ‐Fe‐EXAFS. Angewandte Chemie. 105(11). 1661–1663. 11 indexed citations
20.
Cramer, Stephen P., Jie Chen, Jason Christiansen, et al.. (1993). Refinement of a Model for the Nitrogenase MoFe Cluster Using Single‐Crystal Mo and Fe EXAFS. Angewandte Chemie International Edition in English. 32(11). 1592–1594. 34 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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