Margaret M. Suhanovsky

714 total citations
15 papers, 475 citations indexed

About

Margaret M. Suhanovsky is a scholar working on Molecular Biology, Ecology and Genetics. According to data from OpenAlex, Margaret M. Suhanovsky has authored 15 papers receiving a total of 475 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 11 papers in Ecology and 5 papers in Genetics. Recurrent topics in Margaret M. Suhanovsky's work include Bacteriophages and microbial interactions (11 papers), RNA and protein synthesis mechanisms (6 papers) and Protein Structure and Dynamics (5 papers). Margaret M. Suhanovsky is often cited by papers focused on Bacteriophages and microbial interactions (11 papers), RNA and protein synthesis mechanisms (6 papers) and Protein Structure and Dynamics (5 papers). Margaret M. Suhanovsky collaborates with scholars based in United States. Margaret M. Suhanovsky's co-authors include Carolyn M. Teschke, Kristin N. Parent, Timothy S. Baker, Long Tu, John E. Johnson, Reza Khayat, Juliana R. Cortines, Alexandra M. Deaconescu, Adam Zlotnick and Andrei T. Alexandrescu and has published in prestigious journals such as Cell, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Margaret M. Suhanovsky

15 papers receiving 472 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Margaret M. Suhanovsky United States	13	355	349	105	87	70	15	475
Asher Hodes United States	6	270 0.8×	297 0.9×	74 0.7×	91 1.0×	50 0.7×	7	414
Kanika Khanna United States	14	365 1.0×	366 1.0×	163 1.6×	102 1.2×	20 0.3×	24	606
Sandrine Brasilès France	10	308 0.9×	233 0.7×	70 0.7×	58 0.7×	34 0.5×	11	348
Elena T. Wright United States	11	304 0.9×	260 0.7×	51 0.5×	64 0.7×	64 0.9×	26	375
Nora A. Linderoth United States	13	220 0.6×	406 1.2×	210 2.0×	38 0.4×	60 0.9×	13	538
L. Liljas Sweden	12	217 0.6×	180 0.5×	56 0.5×	147 1.7×	25 0.4×	19	408
Kathryn Eppler United States	7	296 0.8×	322 0.9×	156 1.5×	58 0.7×	32 0.5×	7	411
Lidia P. Kurochkina Russia	15	701 2.0×	667 1.9×	202 1.9×	123 1.4×	74 1.1×	53	936
Sergey Nazarov Switzerland	12	244 0.7×	256 0.7×	122 1.2×	46 0.5×	33 0.5×	14	550
M. F. Bundule Latvia	6	283 0.8×	234 0.7×	49 0.5×	47 0.5×	66 0.9×	18	393

Countries citing papers authored by Margaret M. Suhanovsky

Since Specialization

Citations

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

Fields of papers citing papers by Margaret M. Suhanovsky

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Margaret M. Suhanovsky. 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 Margaret M. Suhanovsky. The network helps show where Margaret M. Suhanovsky may publish in the future.

Co-authorship network of co-authors of Margaret M. Suhanovsky

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

All Works

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15 of 15 papers shown

Zhang, Cheng, et al.. (2020). Molecular determinants for dsDNA translocation by the transcription-repair coupling and evolvability factor Mfd. Nature Communications. 11(1). 3740–3740. 19 indexed citations

Tripathi, Arti, Joel R. Hoskins, Margaret M. Suhanovsky, et al.. (2019). Structural basis for inhibition of a response regulator of σ^S stability by a ClpXP antiadaptor. Genes & Development. 33(11-12). 718–732. 21 indexed citations

Le, Tung T., Yi Yang, Chuang 创 Tan 谭, et al.. (2018). Mfd Dynamically Regulates Transcription via a Release and Catch-Up Mechanism. Cell. 173(7). 1823–1823. 13 indexed citations

Deaconescu, Alexandra M. & Margaret M. Suhanovsky. (2016). From Mfd to TRCF and Back Again—A Perspective on Bacterial Transcription‐coupled Nucleotide Excision Repair. Photochemistry and Photobiology. 93(1). 268–279. 10 indexed citations

Suhanovsky, Margaret M. & Carolyn M. Teschke. (2015). Nature׳s favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold. Virology. 479-480. 487–497. 89 indexed citations

Rizzo, Alessandro A., Margaret M. Suhanovsky, Matthew L. Baker, et al.. (2014). Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling. Structure. 22(6). 830–841. 38 indexed citations

Suhanovsky, Margaret M. & Carolyn M. Teschke. (2013). An Intramolecular Chaperone Inserted in Bacteriophage P22 Coat Protein Mediates Its Chaperonin-independent Folding. Journal of Biological Chemistry. 288(47). 33772–33783. 13 indexed citations

Zlotnick, Adam, Margaret M. Suhanovsky, & Carolyn M. Teschke. (2012). The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids. Virology. 428(1). 64–69. 15 indexed citations

Rizzo, Alessandro A., et al.. (2012). NMR assignments for the telokin-like domain of bacteriophage P22 coat protein. Biomolecular NMR Assignments. 7(2). 257–260. 8 indexed citations

10.

Suhanovsky, Margaret M. & Carolyn M. Teschke. (2011). Bacteriophage P22 capsid size determination: Roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus. Virology. 417(2). 418–429. 22 indexed citations

11.

Parent, Kristin N., Robert S. Sinkovits, Margaret M. Suhanovsky, et al.. (2010). Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins. Physical Biology. 7(4). 45004–45004. 23 indexed citations

12.

Suhanovsky, Margaret M., et al.. (2010). Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching. Molecular Microbiology. 77(6). 1568–1582. 25 indexed citations

13.

Parent, Kristin N., Reza Khayat, Long Tu, et al.. (2010). P22 Coat Protein Structures Reveal a Novel Mechanism for Capsid Maturation: Stability without Auxiliary Proteins or Chemical Crosslinks. Structure. 18(3). 390–401. 127 indexed citations

14.

Parent, Kristin N., Margaret M. Suhanovsky, & Carolyn M. Teschke. (2007). Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching. Molecular Microbiology. 65(5). 1300–1310. 27 indexed citations

15.

Parent, Kristin N., Margaret M. Suhanovsky, & Carolyn M. Teschke. (2006). Phage P22 Procapsids Equilibrate with Free Coat Protein Subunits. Journal of Molecular Biology. 365(2). 513–522. 25 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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