Lesa J. Beamer

3.8k total citations
66 papers, 3.0k citations indexed

About

Lesa J. Beamer is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Lesa J. Beamer has authored 66 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 56 papers in Molecular Biology, 27 papers in Materials Chemistry and 12 papers in Genetics. Recurrent topics in Lesa J. Beamer's work include Enzyme Structure and Function (27 papers), Biochemical and Molecular Research (19 papers) and Protein Structure and Dynamics (18 papers). Lesa J. Beamer is often cited by papers focused on Enzyme Structure and Function (27 papers), Biochemical and Molecular Research (19 papers) and Protein Structure and Dynamics (18 papers). Lesa J. Beamer collaborates with scholars based in United States, Canada and Poland. Lesa J. Beamer's co-authors include David Eisenberg, Carl O. Pabo, Stephen F. Carroll, Mark Hannink, C.A. Regni, Michael T. Henzl, Shih‐Ching Lo, Peter A. Tipton, Kyle M. Stiers and Donna Zhang and has published in prestigious journals such as Science, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Lesa J. Beamer

64 papers receiving 3.0k citations

Peers

Lesa J. Beamer

IMMUN

GENET

K.P. Battaile United States

Young Ho Jeon South Korea

Amir Aharoni Israel

Daniel Lim United States

Alessandro Paiardini Italy

Nina M. Haste United States

Takashi Ohtsuki Japan

Xuejun C. Zhang China

Fabrizia Fusetti Netherlands

Yee‐Hsiung Chen Taiwan

K.P. Battaile United States

Lesa J. Beamer

2.1k ×0.9

266 ×0.6

216 ×0.5

IMMUN

232 ×0.6

527 ×1.6

GENET

Citations per year, relative to Lesa J. Beamer Lesa J. Beamer (= 1×) peers K.P. Battaile

Countries citing papers authored by Lesa J. Beamer

Since Specialization

Citations

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

Fields of papers citing papers by Lesa J. Beamer

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Lesa J. Beamer. 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 Lesa J. Beamer. The network helps show where Lesa J. Beamer may publish in the future.

Co-authorship network of co-authors of Lesa J. Beamer

This figure shows the co-authorship network connecting the top 25 collaborators of Lesa J. Beamer. A scholar is included among the top collaborators of Lesa J. Beamer 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 Lesa J. Beamer. Lesa J. Beamer 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

Mitchum, Melissa G., et al.. (2024). Key structural role of a conserved cis-proline revealed by the P285S variant of soybean serine hydroxymethyltransferase 8. Biochemical Journal. 481(21). 1557–1568.

Korasick, David A., et al.. (2023). Structural and functional analysis of two SHMT8 variants associated with soybean cyst nematode resistance. FEBS Journal. 291(2). 323–337. 5 indexed citations

Beamer, Lesa J.. (2020). Enzyme dysfunction at atomic resolution: Disease-associated variants of human phosphoglucomutase-1. Biochimie. 183. 44–48. 5 indexed citations

Stiers, Kyle M., et al.. (2020). A missense variant remote from the active site impairs stability of human phosphoglucomutase 1. Journal of Inherited Metabolic Disease. 43(4). 861–870. 2 indexed citations

Korasick, David A., Pramod Kaitheri Kandoth, John J. Tanner, Melissa G. Mitchum, & Lesa J. Beamer. (2020). Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode. Journal of Biological Chemistry. 295(11). 3708–3718. 18 indexed citations

Stiers, Kyle M., et al.. (2019). Synthesis, Derivatization, and Structural Analysis of Phosphorylated Mono-, Di-, and Trifluorinated d-Gluco-heptuloses by Glucokinase: Tunable Phosphoglucomutase Inhibition. ACS Omega. 4(4). 7029–7037. 9 indexed citations

Stiers, Kyle M., et al.. (2019). Inhibitory Evaluation of αPMM/PGM from Pseudomonas aeruginosa: Chemical Synthesis, Enzyme Kinetics, and Protein Crystallographic Study. The Journal of Organic Chemistry. 84(15). 9627–9636. 9 indexed citations

Stiers, Kyle M., et al.. (2019). Structural and dynamical description of the enzymatic reaction of a phosphohexomutase. Structural Dynamics. 6(2). 24703–24703. 6 indexed citations

Stiers, Kyle M., et al.. (2017). Phosphorylation-Dependent Effects on the Structural Flexibility of Phosphoglucosamine Mutase from Bacillus anthracis. ACS Omega. 2(11). 8445–8452. 6 indexed citations

10.

Muenks, Andrew, Kyle M. Stiers, & Lesa J. Beamer. (2017). Sequence-structure relationships, expression profiles, and disease-associated mutations in the paralogs of phosphoglucomutase 1. PLoS ONE. 12(8). e0183563–e0183563. 18 indexed citations

11.

Xu, Jia, Ying‐Ying Lee, Lesa J. Beamer, & Steven R. Van Doren. (2015). Phosphorylation in the Catalytic Cleft Stabilizes and Attracts Domains of a Phosphohexomutase. Biophysical Journal. 108(2). 325–337. 15 indexed citations

12.

Wang, Lili, Timothy A. Lewis, Yanling Zhang, et al.. (2013). The identification and characterization of non-reactive inhibitor of Keap1-Nrf2 interaction through HTS using a fluorescence polarization assay. Europe PMC (PubMed Central). 19(7). 204–204. 7 indexed citations

13.

Lee, Ying‐Ying, et al.. (2013). Identification of an essential active‐site residue in the α‐d‐phosphohexomutase enzyme superfamily. FEBS Journal. 280(11). 2622–2632. 11 indexed citations

14.

Lo, Shih‐Ching, et al.. (2006). Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling. The EMBO Journal. 25(15). 3605–3617. 461 indexed citations

15.

Beamer, Lesa J., et al.. (2005). Conserved solvent and side-chain interactions in the 1.35 Å structure of the Kelch domain of Keap1. Acta Crystallographica Section D Biological Crystallography. 61(10). 1335–1342. 35 indexed citations

16.

Regni, C.A., et al.. (2004). Evolutionary trace analysis of the α‐D‐phosphohexomutase superfamily. Protein Science. 13(8). 2130–2138. 81 indexed citations

17.

Zhang, Donna, et al.. (2004). Crystal Structure of the Kelch Domain of Human Keap1. Journal of Biological Chemistry. 279(52). 54750–54758. 191 indexed citations

18.

Regni, C.A., Peter A. Tipton, & Lesa J. Beamer. (2002). Crystal Structure of PMM/PGM. Structure. 10(2). 269–279. 69 indexed citations

19.

Regni, C.A., Peter A. Tipton, & Lesa J. Beamer. (2000). Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase fromPseudomonas aeruginosa. Acta Crystallographica Section D Biological Crystallography. 56(6). 761–762. 15 indexed citations

20.

Stowell, Michael H. B., S. Michael Soltis, Caroline Kisker, et al.. (1996). A simple device for studying macromolecular crystals under moderate gas pressures (0.1–10 MPa). Journal of Applied Crystallography. 29(5). 608–613. 21 indexed citations

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