S.N. Borisova

2.0k total citations
28 papers, 1.5k citations indexed

About

S.N. Borisova is a scholar working on Molecular Biology, Hematology and Physiology. According to data from OpenAlex, S.N. Borisova has authored 28 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 14 papers in Hematology and 8 papers in Physiology. Recurrent topics in S.N. Borisova's work include Blood groups and transfusion (14 papers), Glycosylation and Glycoproteins Research (12 papers) and Erythrocyte Function and Pathophysiology (7 papers). S.N. Borisova is often cited by papers focused on Blood groups and transfusion (14 papers), Glycosylation and Glycoproteins Research (12 papers) and Erythrocyte Function and Pathophysiology (7 papers). S.N. Borisova collaborates with scholars based in Canada, Denmark and Germany. S.N. Borisova's co-authors include Mirosław Cygler, Stephen V. Evans, Monica M. Palcic, Luke Masson, Roland Brousseau, Paweł Grochulski, Marianne Pusztai‐Carey, Jean-Louis Schwartz, Nina O.L. Seto and Michael G. Hahn and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

S.N. Borisova

27 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
S.N. Borisova Canada	15	1.2k	347	250	248	247	28	1.5k
Noboru Tomiya United States	21	1.4k 1.2×	37 0.1×	505 2.0×	178 0.7×	35 0.1×	42	1.6k
Leslie Evans United Kingdom	15	755 0.6×	139 0.4×	30 0.1×	95 0.4×	66 0.3×	19	1.2k
Francis X. Sullivan United States	14	1.2k 1.1×	22 0.1×	260 1.0×	141 0.6×	73 0.3×	15	1.7k
Julio J. Caramelo Argentina	23	1.3k 1.1×	27 0.1×	218 0.9×	568 2.3×	29 0.1×	48	2.0k
Cecilia Díaz Costa Rica	25	1.1k 1.0×	80 0.2×	61 0.2×	109 0.4×	51 0.2×	59	2.1k
Ken-ichi Nakayama Japan	22	1.2k 1.0×	45 0.1×	205 0.8×	336 1.4×	18 0.1×	40	1.5k
André Verbert France	26	1.5k 1.3×	23 0.1×	597 2.4×	402 1.6×	33 0.1×	81	1.8k
Joan L. Arolas Spain	18	688 0.6×	59 0.2×	37 0.1×	164 0.7×	64 0.3×	43	1.0k
Nina O.L. Seto Canada	17	686 0.6×	17 0.0×	337 1.3×	40 0.2×	353 1.4×	25	1.0k
F. J. Kezdy United States	16	503 0.4×	59 0.2×	80 0.3×	114 0.5×	21 0.1×	18	998

Countries citing papers authored by S.N. Borisova

Since Specialization

Citations

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

Fields of papers citing papers by S.N. Borisova

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by S.N. Borisova. 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 S.N. Borisova. The network helps show where S.N. Borisova may publish in the future.

Co-authorship network of co-authors of S.N. Borisova

This figure shows the co-authorship network connecting the top 25 collaborators of S.N. Borisova. A scholar is included among the top collaborators of S.N. Borisova 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 S.N. Borisova. S.N. Borisova 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

Borisova, S.N., et al.. (2019). Development Parameters of Pneumatic Slotted Sprayers for Treatment Potato Tubers. International Journal of Innovative Technology and Exploring Engineering. 2(9). 1200–1203.

Polakowski, Robert, Natisha L. Rose, Ruixiang Blake Zheng, et al.. (2016). Glycosyltransfer in mutants of putative catalytic residue Glu303 of the human ABO(H) A and B blood group glycosyltransferases GTA and GTB proceeds through a labile active site. Glycobiology. 27(4). 370–380. 10 indexed citations

Meloncelli, Peter J., Ruixiang Blake Zheng, Omid Haji‐Ghassemi, et al.. (2015). High Resolution Structures of the Human ABO(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in a Stepwise Manner. Journal of Biological Chemistry. 290(45). 27040–27052. 15 indexed citations

Alfaro, Javier A., et al.. (2013). pH-induced conformational changes in human ABO(H) blood group glycosyltransferases confirm the importance of electrostatic interactions in the formation of the semi-closed state. Glycobiology. 24(3). 237–246. 6 indexed citations

Alfaro, Javier A., et al.. (2012). Sequence-dependent effects of cryoprotectants on the active sites of the human ABO(H) blood group A and B glycosyltransferases. Acta Crystallographica Section D Biological Crystallography. 68(3). 268–276. 9 indexed citations

Fisher, S. Zoë, Andrey Kovalevsky, S.N. Borisova, et al.. (2011). Preliminary joint neutron time-of-flight and X-ray crystallographic study of human ABO(H) blood group A glycosyltransferase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(2). 258–262. 3 indexed citations

Polakowski, Robert, Joel T. Weadge, Nina O.L. Seto, et al.. (2010). Cysteine-to-Serine Mutants Dramatically Reorder the Active Site of Human ABO(H) Blood Group B Glycosyltransferase without Affecting Activity: Structural Insights into Cooperative Substrate Binding. Journal of Molecular Biology. 402(2). 399–411. 11 indexed citations

Brooks, Cory L., Andrea Schietinger, S.N. Borisova, et al.. (2010). Antibody recognition of a unique tumor-specific glycopeptide antigen. Proceedings of the National Academy of Sciences. 107(22). 10056–10061. 70 indexed citations

Alfaro, Javier A., Ruixiang Blake Zheng, Mattias Persson, et al.. (2008). ABO(H) Blood Group A and B Glycosyltransferases Recognize Substrate via Specific Conformational Changes. Journal of Biological Chemistry. 283(15). 10097–10108. 75 indexed citations

10.

Persson, Mattias, James A. Letts, Bahram Hosseini‐Maaf, et al.. (2007). Structural Effects of Naturally Occurring Human Blood Group B Galactosyltransferase Mutations Adjacent to the DXD Motif. Journal of Biological Chemistry. 282(13). 9564–9570. 16 indexed citations

11.

Letts, James A., et al.. (2007). The effect of heavy atoms on the conformation of the active-site polypeptide loop in human ABO(H) blood-group glycosyltransferase B. Acta Crystallographica Section D Biological Crystallography. 63(8). 860–865. 10 indexed citations

12.

Letts, James A., Natisha L. Rose, Y. Fang, et al.. (2005). Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B Glycosyltransferases. Journal of Biological Chemistry. 281(6). 3625–3632. 35 indexed citations

13.

Borisova, S.N., Nina O.L. Seto, Ruixiang Blake Zheng, et al.. (2004). Structural Basis for the Inactivity of Human Blood Group O2 Glycosyltransferase. Journal of Biological Chemistry. 280(1). 525–529. 52 indexed citations

14.

Nguyen, Hoa, Nina O.L. Seto, Ye Cai, et al.. (2003). The Influence of an Intramolecular Hydrogen Bond in Differential Recognition of Inhibitory Acceptor Analogs by Human ABO(H) Blood Group A and B Glycosyltransferases. Journal of Biological Chemistry. 278(49). 49191–49195. 29 indexed citations

15.

Marcus, Sandra L., Robert Polakowski, Nina O.L. Seto, et al.. (2003). A Single Point Mutation Reverses the Donor Specificity of Human Blood Group B-synthesizing Galactosyltransferase. Journal of Biological Chemistry. 278(14). 12403–12405. 80 indexed citations

16.

Seto, Nina O.L., S.N. Borisova, Adam Szpacenko, et al.. (2002). The structural basis for specificity in human ABO(H) blood group biosynthesis. Nature Structural Biology. 9(9). 685–690. 179 indexed citations

17.

Schrag, Joseph D., John Bergeron, Yunge Li, et al.. (2001). The Structure of Calnexin, an ER Chaperone Involved in Quality Control of Protein Folding. Molecular Cell. 8(3). 633–644. 309 indexed citations

18.

Borisova, S.N., et al.. (2001). Antibody recognition of a conformational epitope in a peptide antigen: Fv-peptide complex of an antibody fragment specific for the mutant EGF receptor, EGFRvIII. Journal of Molecular Biology. 308(5). 883–893. 11 indexed citations

19.

Hahn, Michael G., S.N. Borisova, Joseph D. Schrag, et al.. (1998). Identification and Crystallization of a Protease-Resistant Core of Calnexin That Retains Biological Activity. Journal of Structural Biology. 123(3). 260–264. 6 indexed citations

20.

Grochulski, Paweł, Luke Masson, S.N. Borisova, et al.. (1995). Bacillus thuringiensisCrylA(a) Insecticidal Toxin: Crystal Structure and Channel Formation. Journal of Molecular Biology. 254(3). 447–464. 430 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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