Michael L. Easterling

2.1k total citations
29 papers, 1.6k citations indexed

About

Michael L. Easterling is a scholar working on Spectroscopy, Computational Mechanics and Molecular Biology. According to data from OpenAlex, Michael L. Easterling has authored 29 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Spectroscopy, 9 papers in Computational Mechanics and 8 papers in Molecular Biology. Recurrent topics in Michael L. Easterling's work include Mass Spectrometry Techniques and Applications (24 papers), Analytical Chemistry and Chromatography (13 papers) and Ion-surface interactions and analysis (9 papers). Michael L. Easterling is often cited by papers focused on Mass Spectrometry Techniques and Applications (24 papers), Analytical Chemistry and Chromatography (13 papers) and Ion-surface interactions and analysis (9 papers). Michael L. Easterling collaborates with scholars based in United States, Germany and Canada. Michael L. Easterling's co-authors include I. Jonathan Amster, Desmond A. Kaplan, Todd H. Mize, Marilyn M. Olmstead, Alan L. Balch, Steven Stevenson, Mary A. Mackey, Jeffrey N. Agar, J. Paige Phillips and Melissa A. Stuart and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Analytical Chemistry.

In The Last Decade

Michael L. Easterling

29 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Michael L. Easterling United States 19 909 665 428 422 138 29 1.6k
Kyle A. Brown United States 22 650 0.7× 765 1.2× 99 0.2× 73 0.2× 44 0.3× 47 1.3k
Brenda L. Schwartz United States 12 790 0.9× 539 0.8× 89 0.2× 122 0.3× 88 0.6× 15 1.0k
Yuichiro Hashimoto Japan 18 426 0.5× 176 0.3× 193 0.5× 218 0.5× 66 0.5× 51 892
L. Chinsky France 23 289 0.3× 832 1.3× 116 0.3× 314 0.7× 14 0.1× 80 1.4k
Christopher Mullen United States 18 820 0.9× 517 0.8× 28 0.1× 117 0.3× 118 0.9× 40 1.1k
Bruno Bellina United Kingdom 20 416 0.5× 377 0.6× 33 0.1× 195 0.5× 61 0.4× 33 857
Boris Neumann Germany 13 173 0.2× 236 0.4× 250 0.6× 257 0.6× 42 0.3× 25 774
David E. Hansen United States 15 111 0.1× 447 0.7× 198 0.5× 157 0.4× 17 0.1× 37 893
Zhuchun Wu United States 15 577 0.6× 586 0.9× 223 0.5× 51 0.1× 78 0.6× 23 1.3k
Suzana Martinović United States 13 626 0.7× 657 1.0× 197 0.5× 75 0.2× 25 0.2× 22 1.0k

Countries citing papers authored by Michael L. Easterling

Since Specialization
Citations

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

Fields of papers citing papers by Michael L. Easterling

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Michael L. Easterling

This figure shows the co-authorship network connecting the top 25 collaborators of Michael L. Easterling. A scholar is included among the top collaborators of Michael L. Easterling 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 Michael L. Easterling. Michael L. Easterling 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.
Mercado, Brandon Q., et al.. (2015). 2‐Aminoethanol Extraction as a Method for Purifying Sc3N@C80 and for Differentiating Classes of Endohedral Fullerenes on the Basis of Reactivity. Chemistry - A European Journal. 21(47). 17035–17043. 16 indexed citations
2.
Salisbury, Joseph P., Yun‐Wei A. Hsu, Jeniffer Quijada, et al.. (2013). A rapid MALDI-TOF mass spectrometry workflow for Drosophila melanogaster differential neuropeptidomics. Molecular Brain. 6(1). 60–60. 10 indexed citations
3.
Liu, Xiaohui, Isaiah Norton, Mark A. Marchionni, et al.. (2013). Molecular imaging of drug transit through the blood-brain barrier with MALDI mass spectrometry imaging. Scientific Reports. 3(1). 2859–2859. 102 indexed citations
4.
Liu, Qian, Michael L. Easterling, & Jeffrey N. Agar. (2013). Resolving Isotopic Fine Structure to Detect and Quantify Natural Abundance- and Hydrogen/Deuterium Exchange-Derived Isotopomers. Analytical Chemistry. 86(1). 820–825. 8 indexed citations
5.
Karabacak, Murat, Michael L. Easterling, Nathalie Y.R. Agar, & Jeffrey N. Agar. (2010). Transformative effects of higher magnetic field in Fourier transform ion cyclotron resonance mass spectrometry. Journal of the American Society for Mass Spectrometry. 21(7). 1218–1222. 9 indexed citations
7.
Mercado, Brandon Q., Melissa A. Stuart, Mary A. Mackey, et al.. (2010). Sc22-O) Trapped in a Fullerene Cage: The Isolation and Structural Characterization of Sc22-O)@Cs(6)-C82and the Relevance of the Thermal and Entropic Effects in Fullerene Isomer Selection. Journal of the American Chemical Society. 132(34). 12098–12105. 103 indexed citations
8.
Mercado, Brandon Q., Marilyn M. Olmstead, Christine M. Beavers, et al.. (2009). A seven atom cluster in a carbon cage, the crystallographically determined structure of Sc43-O)3@Ih-C80. Chemical Communications. 46(2). 279–281. 97 indexed citations
9.
Torres, Matthew P., et al.. (2009). Top-Down Proteomics on a High-field Fourier Transform Ion Cyclotron Resonance Mass Spectrometer. Methods in molecular biology. 492. 215–231. 8 indexed citations
10.
Abzalimov, Rinat R., Desmond A. Kaplan, Michael L. Easterling, & Igor A. Kaltashov. (2009). Protein conformations can be probed in top-down HDX MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling. Journal of the American Society for Mass Spectrometry. 20(8). 1514–1517. 116 indexed citations
11.
Karabacak, Murat, Long Li, Ashutosh Tiwari, et al.. (2008). Sensitive and Specific Identification of Wild Type and Variant Proteins from 8 to 669 kDa Using Top-down Mass Spectrometry. Molecular & Cellular Proteomics. 8(4). 846–856. 71 indexed citations
12.
Kaplan, Desmond A., Ralf Hartmer, J. Paul Speir, et al.. (2008). Electron transfer dissociation in the hexapole collision cell of a hybrid quadrupole‐hexapole Fourier transform ion cyclotron resonance mass spectrometer. Rapid Communications in Mass Spectrometry. 22(3). 271–278. 49 indexed citations
13.
Stevenson, Steven, Mary A. Mackey, Melissa A. Stuart, et al.. (2008). A Distorted Tetrahedral Metal Oxide Cluster inside an Icosahedral Carbon Cage. Synthesis, Isolation, and Structural Characterization of Sc43-O)2@Ih-C80. Journal of the American Chemical Society. 130(36). 11844–11845. 178 indexed citations
14.
Rajabi, Khadijeh, Michael L. Easterling, & Travis D. Fridgen. (2008). Solvation of electrosprayed ions in the accumulation/collision hexapole of a hybrid Q-FTMS. Journal of the American Society for Mass Spectrometry. 20(3). 411–418. 28 indexed citations
15.
Borchers, Christoph H., Roopa Thapar, Evgeniy V. Petrotchenko, et al.. (2006). Combined top-down and bottom-up proteomics identifies a phosphorylation site in stem–loop-binding proteins that contributes to high-affinity RNA binding. Proceedings of the National Academy of Sciences. 103(9). 3094–3099. 36 indexed citations
16.
Easterling, Michael L., Christopher M. Colangelo, Robert A. Scott, & I. Jonathan Amster. (1998). Monitoring Protein Expression in Whole Bacterial Cells with MALDI Time-of-Flight Mass Spectrometry. Analytical Chemistry. 70(13). 2704–2709. 57 indexed citations
17.
Easterling, Michael L., Todd H. Mize, & I. Jonathan Amster. (1997). MALDI FTMS analysis of polymers: improved performance using an open ended cylindrical analyzer cell. International Journal of Mass Spectrometry and Ion Processes. 169-170. 387–400. 18 indexed citations
18.
Easterling, Michael L., et al.. (1997). rf Capacitive coupling with efficient gated trapping in internal matrix-assisted laser desorption ionization fourier transform ion cyclotron resonance. Journal of the American Society for Mass Spectrometry. 8(2). 195–198. 12 indexed citations
19.
Easterling, Michael L., et al.. (1996). A 4.7 Tesla internal MALDI-FTICR instrument for high mass studies: performance and methods. International Journal of Mass Spectrometry and Ion Processes. 157-158. 97–113. 13 indexed citations
20.
Salter, E. Alan, Anthony S. Wierzbicki, Jorge M. Seminario, et al.. (1994). Structure of trans-Rh(PH3)2(CO)X (X = F, Cl) Using Hartree-Fock/MBPT(2) and Density Functional Theory. The Journal of Physical Chemistry. 98(49). 12945–12948. 10 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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