P. Savitsky

4.3k total citations
36 papers, 2.9k citations indexed

About

P. Savitsky is a scholar working on Molecular Biology, Materials Chemistry and Plant Science. According to data from OpenAlex, P. Savitsky has authored 36 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Biology, 7 papers in Materials Chemistry and 6 papers in Plant Science. Recurrent topics in P. Savitsky's work include Protein Degradation and Inhibitors (7 papers), Enzyme Structure and Function (7 papers) and Enzyme-mediated dye degradation (5 papers). P. Savitsky is often cited by papers focused on Protein Degradation and Inhibitors (7 papers), Enzyme Structure and Function (7 papers) and Enzyme-mediated dye degradation (5 papers). P. Savitsky collaborates with scholars based in United Kingdom, Russia and United States. P. Savitsky's co-authors include Stefan Knapp, Toren Finkel, O. Gileadi, P. Filippakopoulos, N. Burgess-Brown, Susanne Müller, James E. Bray, Oliver N. F. King, Wen‐Hwa Lee and A. Barr and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

P. Savitsky

36 papers receiving 2.9k citations

Peers

P. Savitsky

ONCOL

IMMUN

HEMAT

Lora Swenson United States

Arianna Donella‐Deana Italy

Kjeld Norris Denmark

André Strauss Switzerland

Bárbara Guerra Denmark

Stefania Sarno Italy

Paul Taylor Canada

A. Chaikuad Germany

Carla Rozzo Italy

Hollis D. Showalter United States

Lora Swenson United States

P. Savitsky

2.1k ×0.8

364 ×1.0

ONCOL

130 ×0.4

IMMUN

268 ×0.9

HEMAT

123 ×0.6

Citations per year, relative to P. Savitsky P. Savitsky (= 1×) peers Lora Swenson

Countries citing papers authored by P. Savitsky

Since Specialization

Citations

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

Fields of papers citing papers by P. Savitsky

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of P. Savitsky

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

Lambert, Jean‐Philippe, S. Picaud, Takao Fujisawa, et al.. (2018). Interactome Rewiring Following Pharmacological Targeting of BET Bromodomains. Molecular Cell. 73(3). 621–638.e17. 114 indexed citations

Gräslund, S., P. Savitsky, & Susanne Müller. (2017). In Vivo Biotinylation of Antigens in E. coli. Methods in molecular biology. 1586. 337–344. 11 indexed citations

Couñago, Rafael M., C.K. Allerston, P. Savitsky, et al.. (2017). Structural characterization of human Vaccinia-Related Kinases (VRK) bound to small-molecule inhibitors identifies different P-loop conformations. Scientific Reports. 7(1). 7501–7501. 25 indexed citations

Yapp, Clarence, Catherine Rogers, P. Savitsky, Martin Philpott, & Susanne Müller. (2016). Frapid: achieving full automation of FRAP for chemical probe validation. Biomedical Optics Express. 7(2). 422–422. 2 indexed citations

Savitsky, P., T. Krojer, Takao Fujisawa, et al.. (2016). Multivalent Histone and DNA Engagement by a PHD/BRD/PWWP Triple Reader Cassette Recruits ZMYND8 to K14ac-Rich Chromatin. Cell Reports. 17(10). 2724–2737. 68 indexed citations

Newman, J.A., P. Savitsky, C.K. Allerston, et al.. (2015). Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. Nucleic Acids Research. 43(10). 5221–5235. 75 indexed citations

Nguyen, Giang Huong, Thomas S. Dexheimer, Andrew S. Rosenthal, et al.. (2013). A Small Molecule Inhibitor of the BLM Helicase Modulates Chromosome Stability in Human Cells. Chemistry & Biology. 20(1). 55–62. 131 indexed citations

Soundararajan, M., A.K. Roos, P. Savitsky, et al.. (2013). Structures of Down Syndrome Kinases, DYRKs, Reveal Mechanisms of Kinase Activation and Substrate Recognition. Structure. 21(6). 986–996. 124 indexed citations

Keates, Tracy, C.D.O. Cooper, P. Savitsky, et al.. (2011). Expressing the human proteome for affinity proteomics: optimising expression of soluble protein domains and in vivo biotinylation. New Biotechnology. 29(5). 515–525. 20 indexed citations

10.

D’Avanzo, Nazzareno, Wayland W.L. Cheng, Xiaobing Xia, et al.. (2010). Expression and purification of recombinant human inward rectifier K+ (KCNJ) channels in Saccharomyces cerevisiae. Protein Expression and Purification. 71(1). 115–121. 21 indexed citations

11.

Savitsky, P., James E. Bray, C.D.O. Cooper, et al.. (2010). High-throughput production of human proteins for crystallization: The SGC experience. Journal of Structural Biology. 172(1). 3–13. 241 indexed citations

12.

Filippakopoulos, P., Andrew Low, Timothy Sharpe, et al.. (2010). Structural Basis for Par-4 Recognition by the SPRY Domain- and SOCS Box-Containing Proteins SPSB1, SPSB2, and SPSB4. Journal of Molecular Biology. 401(3). 389–402. 56 indexed citations

13.

Barr, A., E. Ugochukwu, Wen‐Hwa Lee, et al.. (2009). Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome. Cell. 136(2). 352–363. 376 indexed citations

14.

Gileadi, O., N. Burgess-Brown, G. Berridge, et al.. (2008). High Throughput Production of Recombinant Human Proteins for Crystallography. Methods in molecular biology. 426. 221–246. 77 indexed citations

15.

Elkins, Jonathan M., E. Papagrigoriou, G. Berridge, et al.. (2007). Structure of PICK1 and other PDZ domains obtained with the help of self‐binding C‐terminal extensions. Protein Science. 16(4). 683–694. 56 indexed citations

16.

Ng, Stanley S., K.L. Kavanagh, M.A. McDonough, et al.. (2007). Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature. 448(7149). 87–91. 263 indexed citations

17.

Kursula, Petri, H. Schüler, S. Flodin, et al.. (2006). Structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue. Acta Crystallographica Section D Biological Crystallography. 62(11). 1294–1299. 10 indexed citations

18.

Savitsky, P. & Toren Finkel. (2002). Redox Regulation of Cdc25C. Journal of Biological Chemistry. 277(23). 20535–20540. 182 indexed citations

19.

Gazaryan, Irina G., T. A. Chubar, О. В. Игнатенко, et al.. (1999). Tryptophanless Recombinant Horseradish Peroxidase: Stability and Catalytic Properties. Biochemical and Biophysical Research Communications. 262(1). 297–301. 18 indexed citations

20.

Тишков, В. И., et al.. (1996). Site‐directed mutagenesis of the formate dehydrogenase active centre: role of the His³³²‐Gln³¹³ pair in enzyme catalysis. FEBS Letters. 390(1). 104–108. 52 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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