L.S. Beese

8.8k total citations · 4 hit papers
73 papers, 7.1k citations indexed

About

L.S. Beese is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, L.S. Beese has authored 73 papers receiving a total of 7.1k indexed citations (citations by other indexed papers that have themselves been cited), including 68 papers in Molecular Biology, 15 papers in Genetics and 14 papers in Materials Chemistry. Recurrent topics in L.S. Beese's work include DNA Repair Mechanisms (26 papers), DNA and Nucleic Acid Chemistry (21 papers) and Bacterial Genetics and Biotechnology (14 papers). L.S. Beese is often cited by papers focused on DNA Repair Mechanisms (26 papers), DNA and Nucleic Acid Chemistry (21 papers) and Bacterial Genetics and Biotechnology (14 papers). L.S. Beese collaborates with scholars based in United States, France and Germany. L.S. Beese's co-authors include Thomas A. Steitz, Patrick J. Casey, Sean Johnson, Homme W. Hellinga, Victoria Derbyshire, Jonathan M. Friedman, James R. Kiefer, Jeffrey C. Braman, Mao Chen and J.J. Warren and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

L.S. Beese

72 papers receiving 6.9k 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 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism.

1991 904 citations L.S. Beese, Thomas A. Steitz profile →
Structure of DNA Polymerase I Klenow Fragment Bound to Duplex DNA

1993 398 citations L.S. Beese, Thomas A. Steitz et al. profile →
Genetic and Crystallographic Studies of the 3′,5′-Exonucleolytic Site of DNA Polymerase I

1988 303 citations Paul S. Freemont, Mark R. Sanderson et al. profile →
Structure of the Human MutSα DNA Lesion Recognition Complex

2007 279 citations J.J. Warren, Anita Changela et al. profile →

Peers

L.S. Beese

GENET

ONCOL

Lars Abrahmsén Sweden

William A. Beard United States

F.F. Vajdos United States

Gerald Zon United States

Christopher D. Lima United States

D.A.R. Sanders Canada

Mark Bycroft United Kingdom

Daisuke Kohda Japan

Pavol Skubák Netherlands

Bi‐Cheng Wang China

Lars Abrahmsén Sweden

L.S. Beese

3.6k ×0.6

630 ×0.5

GENET

1.3k ×1.6

ONCOL

307 ×0.5

347 ×0.6

Citations per year, relative to L.S. Beese L.S. Beese (= 1×) peers Lars Abrahmsén

Countries citing papers authored by L.S. Beese

Since Specialization

Citations

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

Fields of papers citing papers by L.S. Beese

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of L.S. Beese

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Kumar, S., et al.. (2024). Accurate Identification of Periplasmic Urea-binding Proteins by Structure- and Genome Context-assisted Functional Analysis. Journal of Molecular Biology. 436(22). 168780–168780.

Kumar, S., et al.. (2023). Chromophore carbonyl twisting in fluorescent biosensors encodes direct readout of protein conformations with multicolor switching. Communications Chemistry. 6(1). 168–168. 2 indexed citations

Shi, Yuqian, Homme W. Hellinga, & L.S. Beese. (2017). Interplay of catalysis, fidelity, threading, and processivity in the exo- and endonucleolytic reactions of human exonuclease I. Proceedings of the National Academy of Sciences. 114(23). 6010–6015. 37 indexed citations

Miller, Bill R., L.S. Beese, Carol A. Parish, & Eugene Wu. (2015). The Closing Mechanism of DNA Polymerase I at Atomic Resolution. Structure. 23(9). 1609–1620. 30 indexed citations

Mullen, Daniel G., et al.. (2012). Covalent protein–oligonucleotide conjugates by copper-free click reaction. Bioorganic & Medicinal Chemistry. 20(14). 4532–4539. 39 indexed citations

Orans, Jillian, Michael A. Hast, Ravi R. Iyer, et al.. (2011). Purification, crystallization and preliminary X-ray diffraction analysis of the human mismatch repair protein MutSβ. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(8). 947–952. 3 indexed citations

Orans, Jillian, Ravi Iyer, Michael A. Hast, et al.. (2011). Structures of Human Exonuclease 1 DNA Complexes Suggest a Unified Mechanism for Nuclease Family. Cell. 145(2). 212–223. 130 indexed citations

Hast, Michael A., et al.. (2008). Caged Protein Prenyltransferase Substrates: Tools for Understanding Protein Prenylation. Chemical Biology & Drug Design. 72(3). 171–181. 22 indexed citations

Cuneo, M.J., et al.. (2007). Structure‐based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose‐binding protein. Protein Science. 16(10). 2240–2250. 36 indexed citations

10.

Warren, J.J., Lawrence J. Forsberg, & L.S. Beese. (2006). The structural basis for the mutagenicity of O ⁶ -methyl-guanine lesions. Proceedings of the National Academy of Sciences. 103(52). 19701–19706. 118 indexed citations

11.

Eastman, Richard T., John White, Oliver Hucke, et al.. (2006). Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase. Molecular and Biochemical Parasitology. 152(1). 66–71. 21 indexed citations

12.

Hsu, Gerald W., Xuanwei Huang, Natalia P. Luneva, Nicholas E. Geacintov, & L.S. Beese. (2004). Structure of a High Fidelity DNA Polymerase Bound to a Benzo[a]pyrene Adduct That Blocks Replication. Journal of Biological Chemistry. 280(5). 3764–3770. 68 indexed citations

13.

Johnson, Sean & L.S. Beese. (2004). Structures of Mismatch Replication Errors Observed in a DNA Polymerase. Cell. 116(6). 803–816. 251 indexed citations

14.

Johnson, Sean, Jeffrey S. Taylor, & L.S. Beese. (2003). Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proceedings of the National Academy of Sciences. 100(7). 3895–3900. 253 indexed citations

15.

Long, Stephen B., Patrick J. Casey, & L.S. Beese. (2002). Reaction path of protein farnesyltransferase at atomic resolution. Nature. 419(6907). 645–650. 138 indexed citations

16.

Casey, Patrick J., et al.. (2000). The basis for K-Ras4B binding specificity to protein farnesyl-transferase revealed by 2 Å resolution ternary complex structures. Structure. 8(2). 209–222. 93 indexed citations

17.

Zhou, Ming, Chengzhou Mao, Aida Rodríguez, et al.. (1998). Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon. Acta Crystallographica Section D Biological Crystallography. 54(5). 994–995. 3 indexed citations

18.

Beese, L.S., Jonathan M. Friedman, & Thomas A. Steitz. (1993). Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate. Biochemistry. 32(51). 14095–14101. 146 indexed citations

19.

Lamvik, M. K., et al.. (1989). Correction for specimen movement after acquisition of element‐specific electron microprobe images. Journal of Microscopy. 156(2). 183–190. 4 indexed citations

20.

Steitz, T.A., L.S. Beese, Paul S. Freemont, Jonathan M. Friedman, & Mark R. Sanderson. (1987). Structural Studies of Klenow Fragment: An Enzyme with Two Active Sites. Cold Spring Harbor Symposia on Quantitative Biology. 52(0). 465–471. 33 indexed citations

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