Robert Sabatini

1.5k total citations
33 papers, 1.1k citations indexed

About

Robert Sabatini is a scholar working on Epidemiology, Molecular Biology and Public Health, Environmental and Occupational Health. According to data from OpenAlex, Robert Sabatini has authored 33 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Epidemiology, 21 papers in Molecular Biology and 14 papers in Public Health, Environmental and Occupational Health. Recurrent topics in Robert Sabatini's work include Trypanosoma species research and implications (26 papers), Research on Leishmaniasis Studies (14 papers) and Biochemical and Molecular Research (7 papers). Robert Sabatini is often cited by papers focused on Trypanosoma species research and implications (26 papers), Research on Leishmaniasis Studies (14 papers) and Biochemical and Molecular Research (7 papers). Robert Sabatini collaborates with scholars based in United States, Netherlands and United Kingdom. Robert Sabatini's co-authors include Piet Borst, Stephen L. Hajduk, Rudo Kieft, Laura Cliffe, T. Nicolai Siegel, Mike Cross, Susan Madison‐Antenucci, Jacques H. van Boom, Victoria W. Pollard and Yinsheng Wang and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Robert Sabatini

33 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert Sabatini United States 20 781 678 316 119 101 33 1.1k
Samson O. Obado United Kingdom 14 539 0.7× 687 1.0× 366 1.2× 114 1.0× 108 1.1× 22 953
Simone Leal United States 6 731 0.9× 1.2k 1.8× 473 1.5× 101 0.8× 52 0.5× 7 1.3k
Federico Rojas United Kingdom 14 327 0.4× 582 0.9× 341 1.1× 152 1.3× 60 0.6× 20 713
Bernd Schimanski Switzerland 18 736 0.9× 868 1.3× 449 1.4× 107 0.9× 73 0.7× 31 1.1k
T. Baltz France 21 387 0.5× 852 1.3× 552 1.7× 107 0.9× 169 1.7× 36 1.0k
Jane C. Hines United States 19 665 0.9× 460 0.7× 228 0.7× 36 0.3× 51 0.5× 29 848
Zhu‐Hong Li United States 19 539 0.7× 352 0.5× 181 0.6× 58 0.5× 258 2.6× 31 890
Gowthaman Ramasamy United States 14 335 0.4× 433 0.6× 422 1.3× 69 0.6× 122 1.2× 21 733
Agda M. Simpson United States 24 1.1k 1.5× 915 1.3× 351 1.1× 127 1.1× 107 1.1× 32 1.5k
Atashi Anupama United States 12 492 0.6× 539 0.8× 301 1.0× 57 0.5× 59 0.6× 14 728

Countries citing papers authored by Robert Sabatini

Since Specialization
Citations

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

Fields of papers citing papers by Robert Sabatini

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert Sabatini

This figure shows the co-authorship network connecting the top 25 collaborators of Robert Sabatini. A scholar is included among the top collaborators of Robert Sabatini 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 Robert Sabatini. Robert Sabatini 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.
Kieft, Rudo, Yang Zhang, Haidong Yan, Robert J. Schmitz, & Robert Sabatini. (2023). Knockout of protein phosphatase 1 in Leishmania major reveals its role during RNA polymerase II transcription termination. Nucleic Acids Research. 51(12). 6208–6226. 7 indexed citations
2.
Zhang, Yang & Robert Sabatini. (2023). Leishmania PNUTS discriminates between PP1 catalytic subunits through an RVxF–ΦΦ–F motif and polymorphisms in the PP1 C-tail and catalytic domain. Journal of Biological Chemistry. 299(12). 105432–105432. 1 indexed citations
3.
Kieft, Rudo, Yang Zhang, Alexandre P. Marand, et al.. (2020). Identification of a novel base J binding protein complex involved in RNA polymerase II transcription termination in trypanosomes. PLoS Genetics. 16(2). e1008390–e1008390. 26 indexed citations
4.
Reynolds, David L., Brigitte T. Hofmeister, Laura Cliffe, et al.. (2016). Base J represses genes at the end of polycistronic gene clusters in Leishmania major by promoting RNAP II termination. Molecular Microbiology. 101(4). 559–574. 20 indexed citations
5.
Reynolds, David M., Brigitte T. Hofmeister, Laura Cliffe, et al.. (2016). Histone H3 Variant Regulates RNA Polymerase II Transcription Termination and Dual Strand Transcription of siRNA Loci in Trypanosoma brucei. PLoS Genetics. 12(1). e1005758–e1005758. 42 indexed citations
6.
Cliffe, Laura, et al.. (2015). Base J glucosyltransferase does not regulate the sequence specificity of J synthesis in trypanosomatid telomeric DNA. Molecular and Biochemical Parasitology. 204(2). 77–80. 2 indexed citations
7.
Liu, Shuo, et al.. (2014). Identification of the Glucosyltransferase That Converts Hydroxymethyluracil to Base J in the Trypanosomatid Genome. Journal of Biological Chemistry. 289(29). 20273–20282. 43 indexed citations
8.
Cliffe, Laura, et al.. (2012). JBP1 and JBP2 Proteins Are Fe2+/2-Oxoglutarate-dependent Dioxygenases Regulating Hydroxylation of Thymidine Residues in Trypanosome DNA. Journal of Biological Chemistry. 287(24). 19886–19895. 34 indexed citations
9.
10.
Cipriano, Michael J., et al.. (2007). Telomeric co-localization of the modified base J and contingency genes in the protozoan parasite Trypanosoma cruzi. Nucleic Acids Research. 35(19). 6367–6377. 19 indexed citations
11.
Yu, Zhong, Paul-André Genest, Bas ter Riet, et al.. (2007). The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase. Nucleic Acids Research. 35(7). 2107–2115. 73 indexed citations
12.
Kieft, Rudo, et al.. (2005). A minor fraction of base J in kinetoplastid nuclear DNA is bound by the J-binding protein 1. Molecular and Biochemical Parasitology. 143(1). 111–115. 14 indexed citations
13.
Wood, Zachary A., Robert Sabatini, & Stephen L. Hajduk. (2004). RNA Ligase. Molecular Cell. 13(4). 455–456. 7 indexed citations
14.
Cross, Mike, Rudo Kieft, Robert Sabatini, et al.. (2002). J‐binding protein increases the level and retention of the unusual base J in trypanosome DNA. Molecular Microbiology. 46(1). 37–47. 40 indexed citations
15.
Sabatini, Robert, Nico J. Meeuwenoord, Jacques H. van Boom, & Piet Borst. (2002). Site-specific Interactions of JBP with Base and Sugar Moieties in Duplex J-DNA. Journal of Biological Chemistry. 277(31). 28150–28156. 21 indexed citations
16.
Sabatini, Robert, Nico J. Meeuwenoord, Jacques H. van Boom, & Piet Borst. (2002). Recognition of Base J in Duplex DNA by J-binding Protein. Journal of Biological Chemistry. 277(2). 958–966. 33 indexed citations
17.
Cross, Mike, Rudo Kieft, Robert Sabatini, et al.. (1999). The modified base J is the target for a novelDNA-binding protein in kinetoplastid protozoans. The EMBO Journal. 18(22). 6573–6581. 61 indexed citations
18.
Sabatini, Robert, Brian K. Adler, Susan Madison‐Antenucci, Michael T. McManus, & Stephen L. Hajduk. (1998). Biochemical Methods for Analysis of Kinetoplastid RNA Editing. Methods. 15(1). 15–26. 14 indexed citations
19.
Sabatini, Robert & Stephen L. Hajduk. (1995). RNA Ligase and Its Involvement in Guide RNA/mRNA Chimera Formation. Journal of Biological Chemistry. 270(13). 7233–7240. 99 indexed citations
20.
Lacey, James C., Nalinie S. Wickramasinghe, & Robert Sabatini. (1992). Preferential hydrophobic interactions are responsible for a preference of D-amino acids in the aminoacylation of 5′-AMP with hydrophobic amino acids. Cellular and Molecular Life Sciences. 48(4). 379–383. 12 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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