Bogdan Polevoda

3.4k total citations
31 papers, 2.8k citations indexed

About

Bogdan Polevoda is a scholar working on Molecular Biology, Oncology and Epidemiology. According to data from OpenAlex, Bogdan Polevoda has authored 31 papers receiving a total of 2.8k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 17 papers in Oncology and 3 papers in Epidemiology. Recurrent topics in Bogdan Polevoda's work include Peptidase Inhibition and Analysis (16 papers), Ubiquitin and proteasome pathways (15 papers) and Cancer-related gene regulation (7 papers). Bogdan Polevoda is often cited by papers focused on Peptidase Inhibition and Analysis (16 papers), Ubiquitin and proteasome pathways (15 papers) and Cancer-related gene regulation (7 papers). Bogdan Polevoda collaborates with scholars based in United States, Norway and Japan. Bogdan Polevoda's co-authors include Fred Sherman, Thomas Arnesen, Kris Gevaert, Petra Van Damme, Johan R. Lillehaug, Joël Vandekerckhove, Rune Evjenth, Niklaas Colaert, Kenny Helsens and Jan Erik Varhaug and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Bogdan Polevoda

31 papers receiving 2.7k citations

Peers

Bogdan Polevoda

ONCOL

SPECT

Willy V. Bienvenut France

Ivan Matić Germany

Aaron Aslanian United States

Adrian Drazic Norway

Pitter F. Huesgen Germany

Tapasree Goswami United States

Ujwal Shinde United States

Erhard Wintersberger Austria

Carlo M. Nalin United States

Thierry Buchou France

Willy V. Bienvenut France

Bogdan Polevoda

1.5k ×0.7

551 ×0.4

ONCOL

135 ×0.6

414 ×2.1

SPECT

237 ×1.3

Citations per year, relative to Bogdan Polevoda Bogdan Polevoda (= 1×) peers Willy V. Bienvenut

Countries citing papers authored by Bogdan Polevoda

Since Specialization

Citations

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

Fields of papers citing papers by Bogdan Polevoda

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Bogdan Polevoda

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

Polevoda, Bogdan, et al.. (2017). DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315. Journal of Biological Chemistry. 292(21). 8642–8656. 9 indexed citations

Polevoda, Bogdan, William M. McDougall, Ryan P. Bennett, Jason D. Salter, & Harold C. Smith. (2016). Structural and functional assessment of APOBEC3G macromolecular complexes. Methods. 107. 10–22. 10 indexed citations

Polevoda, Bogdan, William M. McDougall, Michael Cheung, et al.. (2015). RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates. Nucleic Acids Research. 43(19). 9434–9445. 28 indexed citations

Polevoda, Bogdan, Thomas Arnesen, & Fred Sherman. (2009). A synopsis of eukaryotic Nα-terminal acetyltransferases: nomenclature, subunits and substrates. BMC Proceedings. 3(S6). S2–S2. 95 indexed citations

Polevoda, Bogdan, et al.. (2007). Yeast N^α‐terminal acetyltransferases are associated with ribosomes. Journal of Cellular Biochemistry. 103(2). 492–508. 83 indexed citations

Polevoda, Bogdan & Fred Sherman. (2007). Methylation of proteins involved in translation. Molecular Microbiology. 65(3). 590–606. 119 indexed citations

Polevoda, Bogdan, et al.. (2006). Phenotypes of yeast mutants lacking the mitochondrial protein Pet20p. Yeast. 23(2). 127–139. 7 indexed citations

Polevoda, Bogdan, et al.. (2005). The Yeast Translation Release Factors Mrf1p and Sup45p (eRF1) Are Methylated, Respectively, by the Methyltransferases Mtq1p and Mtq2p. Journal of Biological Chemistry. 281(5). 2562–2571. 52 indexed citations

Polevoda, Bogdan & Fred Sherman. (2003). Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochemical and Biophysical Research Communications. 308(1). 1–11. 92 indexed citations

10.

Polevoda, Bogdan, Thomas S. Cardillo, Timothy C. Doyle, Gurrinder S. Bedi, & Fred Sherman. (2003). Nat3p and Mdm20p Are Required for Function of Yeast NatB Nα-terminal Acetyltransferase and of Actin and Tropomyosin. Journal of Biological Chemistry. 278(33). 30686–30697. 104 indexed citations

11.

Polevoda, Bogdan & Fred Sherman. (2002). The diversity of acetylated proteins.. Genome Biology. 3(5). reviews0006.1–reviews0006.1. 201 indexed citations

12.

Polevoda, Bogdan & Fred Sherman. (2002). N-terminal Acetyltransferases and Sequence Requirements for N-terminal Acetylation of Eukaryotic Proteins. Journal of Molecular Biology. 325(4). 595–622. 381 indexed citations

13.

Polevoda, Bogdan & Fred Sherman. (2001). NatC Nα-terminal Acetyltransferase of Yeast Contains Three Subunits, Mak3p, Mak10p, and Mak31p. Journal of Biological Chemistry. 276(23). 20154–20159. 90 indexed citations

14.

Kimura, Yayoi, Motoko Takaoka, Hidenori Sassa, et al.. (2000). N α-Acetylation and Proteolytic Activity of the Yeast 20 S Proteasome. Journal of Biological Chemistry. 275(7). 4635–4639. 95 indexed citations

15.

Polevoda, Bogdan, Mark R. Martzen, Biswadip Das, Eric M. Phizicky, & Fred Sherman. (2000). Cytochrome c Methyltransferase, Ctm1p, of Yeast. Journal of Biological Chemistry. 275(27). 20508–20513. 45 indexed citations

16.

Polevoda, Bogdan & Fred Sherman. (2000). Nα-terminal Acetylation of Eukaryotic Proteins. Journal of Biological Chemistry. 275(47). 36479–36482. 275 indexed citations

17.

Polevoda, Bogdan. (1999). Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae. The EMBO Journal. 18(21). 6155–6168. 181 indexed citations

18.

Arnold, Randy J., Bogdan Polevoda, James P. Reilly, & Fred Sherman. (1999). The Action of N-terminal Acetyltransferases on Yeast Ribosomal Proteins. Journal of Biological Chemistry. 274(52). 37035–37040. 64 indexed citations

19.

Maines, M D, Bogdan Polevoda, Taha Abdulkadir Çoban, et al.. (1998). Neuronal Overexpression of Heme Oxygenase‐1 Correlates with an Attenuated Exploratory Behavior and Causes an Increase in Neuronal NADPH Diaphorase Staining. Journal of Neurochemistry. 70(5). 2057–2069. 32 indexed citations

20.

Maines, Mahin D., et al.. (1996). Human Biliverdin IXα Reductase is a Zinc‐Metalloprotein. European Journal of Biochemistry. 235(1-2). 372–381. 53 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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