David M. LeMaster

5.0k total citations · 2 hit papers
92 papers, 4.2k citations indexed

About

David M. LeMaster is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, David M. LeMaster has authored 92 papers receiving a total of 4.2k indexed citations (citations by other indexed papers that have themselves been cited), including 71 papers in Molecular Biology, 36 papers in Spectroscopy and 26 papers in Materials Chemistry. Recurrent topics in David M. LeMaster's work include Protein Structure and Dynamics (43 papers), Enzyme Structure and Function (25 papers) and Mass Spectrometry Techniques and Applications (22 papers). David M. LeMaster is often cited by papers focused on Protein Structure and Dynamics (43 papers), Enzyme Structure and Function (25 papers) and Mass Spectrometry Techniques and Applications (22 papers). David M. LeMaster collaborates with scholars based in United States, Sweden and France. David M. LeMaster's co-authors include J.R. Horton, Wayne A. Hendrickson, Frederic M. Richards, Griselda Hernández, Hans Eklund, Suresh Katti, Diana M. Kushlan, Janet S. Anderson, Benoı̂t Chabot and Joan A. Steitz and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

David M. LeMaster

92 papers receiving 4.1k citations

Hit Papers

Selenomethionyl proteins produced for analysis by multiwa... 1990 2026 2002 2014 1990 1990 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David M. LeMaster United States 29 3.3k 1.3k 1.1k 422 304 92 4.2k
Heinz Rüterjans Germany 37 3.1k 1.0× 946 0.7× 864 0.8× 267 0.6× 307 1.0× 144 4.2k
Daiwen Yang Singapore 38 3.3k 1.0× 953 0.7× 1.3k 1.2× 358 0.8× 191 0.6× 151 4.4k
Jonathan P. Waltho United Kingdom 45 4.6k 1.4× 1.3k 1.0× 720 0.7× 448 1.1× 264 0.9× 143 6.0k
David D. Boehr United States 21 3.3k 1.0× 1.1k 0.8× 611 0.6× 305 0.7× 266 0.9× 61 4.0k
William M. Westler United States 41 3.4k 1.1× 865 0.7× 1.3k 1.2× 304 0.7× 322 1.1× 146 5.6k
Frans A. A. Mulder Denmark 38 4.1k 1.3× 1.4k 1.0× 1.5k 1.4× 434 1.0× 281 0.9× 109 5.4k
Anthony Mittermaier Canada 31 3.0k 0.9× 865 0.7× 1.0k 0.9× 236 0.6× 131 0.4× 89 3.8k
Magnus Wolf‐Watz Sweden 24 2.9k 0.9× 1.3k 1.0× 522 0.5× 401 1.0× 205 0.7× 56 3.6k
Frank Löhr Germany 41 4.3k 1.3× 678 0.5× 818 0.8× 768 1.8× 409 1.3× 150 6.1k
Edvards Liepinsh Latvia 30 2.6k 0.8× 859 0.7× 849 0.8× 217 0.5× 191 0.6× 96 4.0k

Countries citing papers authored by David M. LeMaster

Since Specialization
Citations

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

Fields of papers citing papers by David M. LeMaster

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David M. LeMaster. 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 David M. LeMaster. The network helps show where David M. LeMaster may publish in the future.

Co-authorship network of co-authors of David M. LeMaster

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

All Works

20 of 20 papers shown
1.
Hernández, Griselda & David M. LeMaster. (2016). Quantifying protein dynamics in the ps–ns time regime by NMR relaxation. Journal of Biomolecular NMR. 66(3). 163–174. 4 indexed citations
2.
Tang, Yijin, et al.. (2012). UDP-Glucuronosyltransferase-mediated Metabolic Activation of the Tobacco Carcinogen 2-Amino-9H-pyrido[2,3-b]indole. Journal of Biological Chemistry. 287(18). 14960–14972. 17 indexed citations
3.
Anderson, Janet S., Griselda Hernández, & David M. LeMaster. (2009). Backbone conformational dependence of peptide acidity. Biophysical Chemistry. 141(1). 124–130. 16 indexed citations
4.
Anderson, Janet S., Griselda Hernández, & David M. LeMaster. (2008). A Billion-fold Range in Acidity for the Solvent-Exposed Amides of Pyrococcus furiosus Rubredoxin. Biochemistry. 47(23). 6178–6188. 34 indexed citations
5.
Hernández, Griselda & David M. LeMaster. (2008). NMR Analysis of Native-State Protein Conformational Flexibility by Hydrogen Exchange. Methods in molecular biology. 490. 285–310. 5 indexed citations
6.
LeMaster, David M., Janet S. Anderson, & Griselda Hernández. (2007). Spatial distribution of dielectric shielding in the interior of Pyrococcus furiosus rubredoxin as sampled in the subnanosecond timeframe by hydrogen exchange. Biophysical Chemistry. 129(1). 43–48. 13 indexed citations
7.
LeMaster, David M., Janet S. Anderson, & Griselda Hernández. (2007). Normal carbon acid referencing for protein amide hydrogen exchange. Magnetic Resonance in Chemistry. 45(7). 601–604. 1 indexed citations
8.
LeMaster, David M., Janet S. Anderson, Limin Wang, et al.. (2007). NMR and X-ray analysis of structural additivity in metal binding site-swapped hybrids of rubredoxin. BMC Structural Biology. 7(1). 81–81. 1 indexed citations
9.
Anderson, Janet S., David M. LeMaster, & Griselda Hernández. (2006). Electrostatic Potential Energy within a Protein Monitored by Metal Charge-Dependent Hydrogen Exchange. Biophysical Journal. 91(11). L93–L95. 8 indexed citations
10.
LeMaster, David M. & Griselda Hernández. (2006). Additivity of Differential Conformational Dynamics in Hyperthermophile/Mesophile Rubredoxin Chimeras as Monitored by Hydrogen Exchange. ChemBioChem. 7(12). 1886–1889. 3 indexed citations
11.
LeMaster, David M., Michael G. Minnich, Patrick J. Parsons, Janet S. Anderson, & Griselda Hernández. (2006). Tetrathiolate coordination of germanium(IV) in a protein active site. Journal of Inorganic Biochemistry. 100(8). 1410–1412. 12 indexed citations
12.
LeMaster, David M. & Griselda Hernández. (2005). Additivity in Both Thermodynamic Stability and Thermal Transition Temperature for Rubredoxin Chimeras via Hybrid Native Partitioning. Structure. 13(8). 1153–1163. 10 indexed citations
13.
Hernández, Griselda, et al.. (2004). Increased peptide deformylase activity for N-formylmethionine processing of proteins overexpressed in Escherichia coli: application to homogeneous rubredoxin production. Protein Expression and Purification. 36(1). 100–105. 20 indexed citations
15.
LeMaster, David M.. (1997). Assessment of protein solution versus crystal structure determination using spin- diffusion-suppressed NOE and heteronuclear relaxation data. Journal of Biomolecular NMR. 9(1). 79–93. 4 indexed citations
16.
LeMaster, David M., et al.. (1993). The Use of Cystathionine γ-Synthase in the Production of α and Chiral β Deuterated Amino Acids. Analytical Biochemistry. 215(2). 211–215. 16 indexed citations
17.
Katti, Suresh, David M. LeMaster, & Hans Eklund. (1990). Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. Journal of Molecular Biology. 212(1). 167–184. 524 indexed citations breakdown →
19.
LeMaster, David M.. (1990). Uniform and Selective Deuteration in Two-Dimensional NMR of Proteins. PubMed. 19(1). 243–266. 41 indexed citations
20.
LeMaster, David M., et al.. (1988). Protein dynamics and distance determination by NOE measurements. FEBS Letters. 236(1). 71–76. 51 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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