N.L. Samara

964 total citations
18 papers, 666 citations indexed

About

N.L. Samara is a scholar working on Molecular Biology, Organic Chemistry and Immunology. According to data from OpenAlex, N.L. Samara has authored 18 papers receiving a total of 666 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 3 papers in Organic Chemistry and 3 papers in Immunology. Recurrent topics in N.L. Samara's work include Glycosylation and Glycoproteins Research (8 papers), Ubiquitin and proteasome pathways (4 papers) and Carbohydrate Chemistry and Synthesis (3 papers). N.L. Samara is often cited by papers focused on Glycosylation and Glycoproteins Research (8 papers), Ubiquitin and proteasome pathways (4 papers) and Carbohydrate Chemistry and Synthesis (3 papers). N.L. Samara collaborates with scholars based in United States, Japan and France. N.L. Samara's co-authors include Wei Yang, Cynthia Wolberger, Xiangbin Zhang, Tingting Yao, Ajit B. Datta, Christopher Berndsen, Robert E. Cohen, Chia‐Lung Li, Yuki Onishi and Kaoru Sugasawa and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

N.L. Samara

17 papers receiving 660 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
N.L. Samara United States 11 547 93 74 64 45 18 666
Thomas Vercruysse Belgium 13 448 0.8× 108 1.2× 56 0.8× 68 1.1× 23 0.5× 25 643
Nigar D. Babayeva United States 16 809 1.5× 89 1.0× 125 1.7× 110 1.7× 31 0.7× 27 982
Maarten Jacquemyn Belgium 11 457 0.8× 99 1.1× 59 0.8× 94 1.5× 46 1.0× 19 610
W. Mark Abbott United Kingdom 13 439 0.8× 46 0.5× 75 1.0× 86 1.3× 35 0.8× 23 606
Mary Christie Australia 10 504 0.9× 45 0.5× 44 0.6× 34 0.5× 57 1.3× 21 583
Simon Messing United States 15 634 1.2× 67 0.7× 62 0.8× 64 1.0× 106 2.4× 27 814
Emiko Uchikawa United States 12 418 0.8× 42 0.5× 30 0.4× 54 0.8× 35 0.8× 18 609
Mikhail I. Dobrikov United States 16 503 0.9× 118 1.3× 125 1.7× 101 1.6× 29 0.6× 30 693
Petra Parizek Switzerland 10 551 1.0× 30 0.3× 52 0.7× 61 1.0× 46 1.0× 11 637
Sandrine Guillard United Kingdom 11 580 1.1× 22 0.2× 39 0.5× 126 2.0× 39 0.9× 12 714

Countries citing papers authored by N.L. Samara

Since Specialization
Citations

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

Fields of papers citing papers by N.L. Samara

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of N.L. Samara

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

All Works

18 of 18 papers shown
1.
Samara, N.L.. (2025). Decoding the complex substrate specificities of GalNAc-Ts. Glycobiology. 35(11).
2.
Hassan, Sergio A., et al.. (2024). An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase. Science Advances. 10(9). eadj8829–eadj8829. 10 indexed citations
3.
Tomita, Tadakimi, et al.. (2024). A Toxoplasma gondii O-glycosyltransferase that modulates bradyzoite cyst wall rigidity is distinct from host homologues. Nature Communications. 15(1). 3792–3792. 5 indexed citations
4.
Collins, Jason C., Xiang Chen, Nicholas Balanda, et al.. (2024). Shared and distinct mechanisms of UBA1 inactivation across different diseases. The EMBO Journal. 43(10). 1919–1946. 26 indexed citations
5.
Oldoni, Federico, Antoine Rimbert, E Tian, et al.. (2022). A novel role for GalNAc-T2 dependent glycosylation in energy homeostasis. Molecular Metabolism. 60. 101472–101472. 7 indexed citations
6.
Syed, Zulfeqhar A., E Tian, N.L. Samara, et al.. (2021). Furin cleavage of the SARS-CoV-2 spike is modulated by O -glycosylation. Proceedings of the National Academy of Sciences. 118(47). 102 indexed citations
7.
Zhang, Liping, Zulfeqhar A. Syed, Negin P. Martin, et al.. (2021). O‐glycosylation of the novel SARS‐CoV‐2 coronavirus spike protein influences furin cleavage. The FASEB Journal. 35(S1). 1 indexed citations
8.
Ji, Suena, Zulfeqhar A. Syed, Thomas Gerken, et al.. (2020). Differential splicing of the lectin domain of an O-glycosyltransferase modulates both peptide and glycopeptide preferences. Journal of Biological Chemistry. 295(35). 12525–12536. 8 indexed citations
9.
Wu, Jinjun, N.L. Samara, Isao Kuraoka, & Wei Yang. (2019). Evolution of Inosine-Specific Endonuclease V from Bacterial DNase to Eukaryotic RNase. Molecular Cell. 76(1). 44–56.e3. 33 indexed citations
10.
Mahajan, Sai Pooja, et al.. (2019). The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its function. Proceedings of the National Academy of Sciences. 116(41). 20404–20410. 18 indexed citations
11.
Ji, Suena, N.L. Samara, Ping Zhang, et al.. (2018). A molecular switch orchestrates enzyme specificity and secretory granule morphology. Nature Communications. 9(1). 3508–3508. 33 indexed citations
12.
Samara, N.L. & Wei Yang. (2018). Cation trafficking propels RNA hydrolysis. Nature Structural & Molecular Biology. 25(8). 715–721. 42 indexed citations
13.
Samara, N.L., Yang Gao, Jinjun Wu, & Wei Yang. (2017). Detection of Reaction Intermediates in Mg 2+ -Dependent DNA Synthesis and RNA Degradation by Time-Resolved X-Ray Crystallography. Methods in enzymology on CD-ROM/Methods in enzymology. 592. 283–327. 15 indexed citations
14.
Gołębiowski, Filip, Chia‐Lung Li, Yuki Onishi, et al.. (2016). Tripartite DNA Lesion Recognition and Verification by XPC, TFIIH, and XPA in Nucleotide Excision Repair. The FASEB Journal. 30(S1). 2 indexed citations
15.
Li, Chia‐Lung, Filip Gołębiowski, Yuki Onishi, et al.. (2015). Tripartite DNA Lesion Recognition and Verification by XPC, TFIIH, and XPA in Nucleotide Excision Repair. Molecular Cell. 59(6). 1025–1034. 123 indexed citations
16.
Samara, N.L., Alison E. Ringel, & Cynthia Wolberger. (2012). A Role for Intersubunit Interactions in Maintaining SAGA Deubiquitinating Module Structure and Activity. Structure. 20(8). 1414–1424. 23 indexed citations
17.
Samara, N.L. & Cynthia Wolberger. (2011). A new chapter in the transcription SAGA. Current Opinion in Structural Biology. 21(6). 767–774. 40 indexed citations
18.
Samara, N.L., Ajit B. Datta, Christopher Berndsen, et al.. (2010). Structural Insights into the Assembly and Function of the SAGA Deubiquitinating Module. Science. 328(5981). 1025–1029. 178 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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