S.E. Greasley

3.6k total citations · 1 hit paper
25 papers, 935 citations indexed

About

S.E. Greasley is a scholar working on Molecular Biology, Oncology and Infectious Diseases. According to data from OpenAlex, S.E. Greasley has authored 25 papers receiving a total of 935 indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 6 papers in Oncology and 5 papers in Infectious Diseases. Recurrent topics in S.E. Greasley's work include Biochemical and Molecular Research (14 papers), Enzyme Structure and Function (5 papers) and Porphyrin Metabolism and Disorders (4 papers). S.E. Greasley is often cited by papers focused on Biochemical and Molecular Research (14 papers), Enzyme Structure and Function (5 papers) and Porphyrin Metabolism and Disorders (4 papers). S.E. Greasley collaborates with scholars based in United States, United Kingdom and Israel. S.E. Greasley's co-authors include Ian A. Wilson, G. Peter Beardsley, Rose Ann Ferre, Dennis W. Wolan, Patricia A. Horton, Chuangxing Guo, Dale L. Boger, M. Catherine Johnson, Liming Dong and Joseph Marakovits and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

S.E. Greasley

25 papers receiving 912 citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Structural basis for the in vitro efficacy of nirmatrelvir against SARS-CoV-2 variants

2022 114 citations S.E. Greasley, Stephen Noell et al. Journal of Biological Chemistry profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
S.E. Greasley United States	19	726	165	153	142	115	25	935
Salvatore Di Maro Italy	25	755 1.0×	227 1.4×	260 1.7×	61 0.4×	83 0.7×	63	1.3k
Guixian Jin United States	15	714 1.0×	108 0.7×	264 1.7×	59 0.4×	90 0.8×	21	1.1k
Barbara Saxty United Kingdom	16	689 0.9×	81 0.5×	201 1.3×	146 1.0×	48 0.4×	33	1.1k
Mei-Chu Lo United States	11	750 1.0×	117 0.7×	132 0.9×	57 0.4×	77 0.7×	19	957
Dirksen E. Bussiere United States	20	1.4k 1.9×	242 1.5×	273 1.8×	64 0.5×	54 0.5×	37	1.7k
Joseph Marakovits United States	10	657 0.9×	168 1.0×	349 2.3×	177 1.2×	99 0.9×	12	1.0k
Jonathan H. Shrimp United States	14	613 0.8×	85 0.5×	304 2.0×	111 0.8×	84 0.7×	25	982
M.J. Romanowski United States	21	1.0k 1.4×	101 0.6×	261 1.7×	45 0.3×	95 0.8×	37	1.4k
Jakob Fuhrmann United States	20	947 1.3×	123 0.7×	219 1.4×	66 0.5×	40 0.3×	27	1.4k
L. Tresaugues Sweden	16	771 1.1×	60 0.4×	334 2.2×	31 0.2×	35 0.3×	22	1.1k

Countries citing papers authored by S.E. Greasley

Since Specialization

Citations

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

Fields of papers citing papers by S.E. Greasley

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of S.E. Greasley

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

Brodsky, Oleg, Patrick Bingham, Wade Diehl, et al.. (2025). Modulation of the substrate preference of a MYST acetyltransferase by a scaffold protein. Journal of Biological Chemistry. 301(3). 108262–108262. 1 indexed citations

Greasley, S.E., Stephen Noell, Olga Plotnikova, et al.. (2022). Structural basis for the in vitro efficacy of nirmatrelvir against SARS-CoV-2 variants. Journal of Biological Chemistry. 298(6). 101972–101972. 114 indexed citations breakdown →

Guo, Chuangxing, Xinjun Hou, Liming Dong, et al.. (2014). Structure-based design of novel human Pin1 inhibitors (III): Optimizing affinity beyond the phosphate recognition pocket. Bioorganic & Medicinal Chemistry Letters. 24(17). 4187–4191. 38 indexed citations

Guo, Chuangxing, Angelica Linton, Mehran Jalaie, et al.. (2013). Discovery of 2-((1H-benzo[d]imidazol-1-yl)methyl)-4H-pyrido[1,2-a]pyrimidin-4-ones as novel PKM2 activators. Bioorganic & Medicinal Chemistry Letters. 23(11). 3358–3363. 42 indexed citations

Liu, Shenping, Mark Ammirati, Xi Song, et al.. (2012). Insights into Mechanism of Glucokinase Activation. Journal of Biological Chemistry. 287(17). 13598–13610. 56 indexed citations

Le, Phuong, Hengmiao Cheng, Sacha Ninkovic, et al.. (2012). Design and synthesis of a novel pyrrolidinyl pyrido pyrimidinone derivative as a potent inhibitor of PI3Kα and mTOR. Bioorganic & Medicinal Chemistry Letters. 22(15). 5098–5103. 26 indexed citations

Guo, Chuangxing, Susan E. Kephart, Martha A. Ornelas, et al.. (2011). Discovery of 3-aryloxy-lactam analogs as potent androgen receptor full antagonists for treating castration resistant prostate cancer. Bioorganic & Medicinal Chemistry Letters. 22(2). 1230–1236. 11 indexed citations

Johnson, M. Catherine, Qiyue Hu, Laura Lingardo, et al.. (2011). Novel isoquinolone PDK1 inhibitors discovered through fragment-based lead discovery. Journal of Computer-Aided Molecular Design. 25(7). 689–698. 15 indexed citations

Dong, Liming, Joseph Marakovits, Xinjun Hou, et al.. (2010). Structure-based design of novel human Pin1 inhibitors (II). Bioorganic & Medicinal Chemistry Letters. 20(7). 2210–2214. 70 indexed citations

10.

Vernier, William F., Wesley K. M. Chong, David A. Rewolinski, et al.. (2010). Thioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV: Structure-based drug design, synthesis, and biological evaluation. Bioorganic & Medicinal Chemistry. 18(9). 3307–3319. 39 indexed citations

11.

Liu, Kevin K.‐C., Xiao‐Jun Huang, Shubha Bagrodia, et al.. (2010). Quinazolines with intra-molecular hydrogen bonding scaffold (iMHBS) as PI3K/mTOR dual inhibitors. Bioorganic & Medicinal Chemistry Letters. 21(4). 1270–1274. 26 indexed citations

12.

Guo, Chuangxing, Xinjun Hou, Liming Dong, et al.. (2009). Structure-based design of novel human Pin1 inhibitors (I). Bioorganic & Medicinal Chemistry Letters. 19(19). 5613–5616. 91 indexed citations

13.

Cheong, Cheom‐Gil, Dennis W. Wolan, S.E. Greasley, et al.. (2004). Crystal Structures of Human Bifunctional Enzyme Aminoimidazole-4-carboxamide Ribonucleotide Transformylase/IMP Cyclohydrolase in Complex with Potent Sulfonyl-containing Antifolates. Journal of Biological Chemistry. 279(17). 18034–18045. 42 indexed citations

14.

Wolan, Dennis W., S.E. Greasley, Mark J. Wall, Stephen J. Benkovic, & Ian A. Wilson. (2003). Structure of Avian AICAR Transformylase with a Multisubstrate Adduct Inhibitor β-DADF Identifies the Folate Binding Site^,. Biochemistry. 42(37). 10904–10914. 20 indexed citations

15.

Greasley, S.E., Patricia A. Horton, Joseph Ramcharan, et al.. (2001). Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis.. Nature Structural Biology. 8(5). 402–406. 72 indexed citations

16.

Greasley, S.E., Thomas H. Marsilje, Hui Cai, et al.. (2001). Unexpected Formation of an Epoxide-Derived Multisubstrate Adduct Inhibitor on the Active Site of GAR Transformylase^,. Biochemistry. 40(45). 13538–13547. 35 indexed citations

17.

Reyes, Vicente M., S.E. Greasley, E.A. Stura, G. Peter Beardsley, & Ian A. Wilson. (2000). Crystallization and preliminary crystallographic investigations of avian 5-aminoimidazole-4-carboxamide ribonucleotide transformylase–inosine monophosphate cyclohydrolase expressed inEscherichia coli. Acta Crystallographica Section D Biological Crystallography. 56(8). 1051–1054. 3 indexed citations

18.

Su, Ying, M M Yamashita, S.E. Greasley, et al.. (1998). A pH-dependent stabilization of an active site loop observed from low and high ph crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 Å. Journal of Molecular Biology. 281(3). 485–499. 26 indexed citations

19.

Greasley, S.E., Harren Jhoti, Carmel G. Teahan, et al.. (1995). The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms. Nature Structural & Molecular Biology. 2(9). 797–806. 89 indexed citations

20.

Greasley, S.E., Harren Jhoti, Amanda Fensome, et al.. (1994). Crystallization and Preliminary X-ray Diffraction Studies on ADP-ribosylation Factor 1. Journal of Molecular Biology. 244(5). 651–653. 2 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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