J.B. Bonanno

6.0k total citations · 1 hit paper
81 papers, 4.5k citations indexed

About

J.B. Bonanno is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, J.B. Bonanno has authored 81 papers receiving a total of 4.5k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 23 papers in Materials Chemistry and 16 papers in Organic Chemistry. Recurrent topics in J.B. Bonanno's work include Enzyme Structure and Function (21 papers), Organometallic Complex Synthesis and Catalysis (9 papers) and Cancer-related gene regulation (9 papers). J.B. Bonanno is often cited by papers focused on Enzyme Structure and Function (21 papers), Organometallic Complex Synthesis and Catalysis (9 papers) and Cancer-related gene regulation (9 papers). J.B. Bonanno collaborates with scholars based in United States, Canada and United Kingdom. J.B. Bonanno's co-authors include S.K. Burley, Steven C. Almo, Peter T. Wolczanski, Nahum Sonenberg, Rahul C. Deo, Subramanyam Swaminathan, U.A. Ramagopal, Emil B. Lobkovsky, J.M. Sauder and Gerard Parkin and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

J.B. Bonanno

81 papers receiving 4.4k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin

2009 501 citations P.G. Leiman, Marek Basler et al. Proceedings of the National Academy of Sciences profile →

Peers

J.B. Bonanno

IMMUN

Wulf Blankenfeldt Germany

Owen Johnson United Kingdom

Yan‐Cheng Liu China

Michail N. Isupov United Kingdom

P. John Hart United States

A.M.W.H. Thunnissen Netherlands

Vishal Verma United States

Lothar Esser United States

Andrea Ilari Italy

P.C.E. Moody United Kingdom

Wulf Blankenfeldt Germany

J.B. Bonanno

3.1k ×1.2

599 ×0.8

406 ×0.7

156 ×0.3

292 ×0.7

IMMUN

Citations per year, relative to J.B. Bonanno J.B. Bonanno (= 1×) peers Wulf Blankenfeldt

Countries citing papers authored by J.B. Bonanno

Since Specialization

Citations

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

Fields of papers citing papers by J.B. Bonanno

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J.B. Bonanno. 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 J.B. Bonanno. The network helps show where J.B. Bonanno may publish in the future.

Co-authorship network of co-authors of J.B. Bonanno

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Ketaren, Natalia E., Peter C. Fridy, V.N. Malashkevich, et al.. (2025). Unique mechanisms to increase structural stability and enhance antigen binding in nanobodies. Structure. 33(4). 677–690.e5. 3 indexed citations

Liu, Weifeng, Sarah C. Garrett-Thomson, Goo‐Young Seo, et al.. (2021). HVEM structures and mutants reveal distinct functions of binding to LIGHT and BTLA/CD160. The Journal of Experimental Medicine. 218(12). 20 indexed citations

Wang, Hua, А.А. Федоров, E.V. Fedorov, et al.. (2019). An essential bifunctional enzyme in Mycobacterium tuberculosis for itaconate dissimilation and leucine catabolism. Proceedings of the National Academy of Sciences. 116(32). 15907–15913. 47 indexed citations

Liu, Weifeng, E.V. Fedorov, U.A. Ramagopal, et al.. (2019). Structural Basis of CD160:HVEM Recognition. Structure. 27(8). 1286–1295.e4. 31 indexed citations

Ramagopal, U.A., R. Toro, Mingzhao Zhu, et al.. (2018). Comparison of Alicyclobacillus acidocaldarius o-Succinylbenzoate Synthase to Its Promiscuous N-Succinylamino Acid Racemase/o-Succinylbenzoate Synthase Relatives. Biochemistry. 57(26). 3676–3689. 8 indexed citations

Nemmara, Venkatesh V., Dao Feng Xiang, А.А. Федоров, et al.. (2018). Substrate Profile of the Phosphotriesterase Homology Protein from Escherichia coli. Biochemistry. 57(43). 6219–6227. 7 indexed citations

Kim, Jungwook, Hui Xiao, Yikai Wang, et al.. (2015). Determinants of the CmoB carboxymethyl transferase utilized for selective tRNA wobble modification. Nucleic Acids Research. 43(9). 4602–4613. 24 indexed citations

Liu, Weifeng, Vladimir Vigdorovich, Chenyang Zhan, et al.. (2015). Increased Heterologous Protein Expression in Drosophila S2 Cells for Massive Production of Immune Ligands/Receptors and Structural Analysis of Human HVEM. Molecular Biotechnology. 57(10). 914–922. 9 indexed citations

Burgos, Emmanuel S., Carola Wilczek, Takashi Onikubo, et al.. (2015). Histone H2A and H4 N-terminal Tails Are Positioned by the MEP50 WD Repeat Protein for Efficient Methylation by the PRMT5 Arginine Methyltransferase. Journal of Biological Chemistry. 290(15). 9674–9689. 72 indexed citations

10.

Liu, Weifeng, Chenyang Zhan, P. Rajesh Kumar, et al.. (2014). Mechanistic Basis for Functional Promiscuity in the TNF and TNF Receptor Superfamilies: Structure of the LIGHT:DcR3 Assembly. Structure. 22(9). 1252–1262. 28 indexed citations

11.

Kim, Jungwook, Hui Xiao, J.B. Bonanno, et al.. (2013). Structure-guided discovery of the metabolite carboxy-SAM that modulates tRNA function. Nature. 498(7452). 123–126. 74 indexed citations

12.

Sampathkumar, Parthasarathy, Seung Joong Kim, Paula Upla, et al.. (2013). Structure, Dynamics, Evolution, and Function of a Major Scaffold Component in the Nuclear Pore Complex. Structure. 21(4). 560–571. 50 indexed citations

13.

Schellenberg, Matthew J., Emily M. Gesner, J.B. Bonanno, et al.. (2012). Cas5d processes pre-crRNA and is a member of a larger family of CRISPR RNA endonucleases. RNA. 18(11). 2020–2028. 73 indexed citations

14.

Leiman, P.G., Marek Basler, U.A. Ramagopal, et al.. (2009). Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Proceedings of the National Academy of Sciences. 106(11). 4154–4159. 501 indexed citations breakdown →

15.

Agarwal, Rakhi, J.B. Bonanno, S.K. Burley, & Subramanyam Swaminathan. (2006). Structure determination of an FMN reductase fromPseudomonas aeruginosaPA01 using sulfur anomalous signal. Acta Crystallographica Section D Biological Crystallography. 62(4). 383–391. 39 indexed citations

16.

Romanowski, M.J., J.B. Bonanno, & S.K. Burley. (2002). Crystal structure of the Escherichia coli glucose‐inhibited division protein B (GidB) reveals a methyltransferase fold. Proteins Structure Function and Bioinformatics. 47(4). 563–567. 23 indexed citations

17.

Romanowski, M.J., J.B. Bonanno, & S.K. Burley. (2002). Crystal structure of the Escherichia coli glucose‐inhibited division protein B (GidB) reveals a methyltransferase fold. Proteins Structure Function and Bioinformatics. 47(4). 563–567. 1 indexed citations

18.

Romanowski, M.J., J.B. Bonanno, & S.K. Burley. (2002). Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily. Proteins Structure Function and Bioinformatics. 47(4). 568–571. 47 indexed citations

19.

Deo, Rahul C., J.B. Bonanno, Nahum Sonenberg, & S.K. Burley. (1999). Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein. Cell. 98(6). 835–845. 414 indexed citations

20.

Burley, S.K., Steven C. Almo, J.B. Bonanno, et al.. (1999). Structural genomics: beyond the Human Genome Project. Nature Genetics. 23(2). 151–157. 287 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.

Explore authors with similar magnitude of impact