Margaret M. Stratton

1.3k total citations
23 papers, 692 citations indexed

About

Margaret M. Stratton is a scholar working on Molecular Biology, Cell Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Margaret M. Stratton has authored 23 papers receiving a total of 692 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 6 papers in Cell Biology and 5 papers in Cellular and Molecular Neuroscience. Recurrent topics in Margaret M. Stratton's work include Protein Kinase Regulation and GTPase Signaling (6 papers), Protein Structure and Dynamics (5 papers) and Neuroscience and Neuropharmacology Research (4 papers). Margaret M. Stratton is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (6 papers), Protein Structure and Dynamics (5 papers) and Neuroscience and Neuropharmacology Research (4 papers). Margaret M. Stratton collaborates with scholars based in United States, China and Japan. Margaret M. Stratton's co-authors include Stewart N. Loh, Howard Schulman, John Kuriyan, Luke H. Chao, Jay T. Groves, Il‐Hyung Lee, Joshua Levitz, Daniel J. Mandell, Oren S. Rosenberg and Tanja Kortemme and has published in prestigious journals such as Cell, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Margaret M. Stratton

23 papers receiving 691 citations

Peers

Margaret M. Stratton
Albert Lin United States
Susan Q. Shen United States
Ranjie Xu United States
Paul S.‐H. Park United States
Margaret M. Stratton
Citations per year, relative to Margaret M. Stratton Margaret M. Stratton (= 1×) peers Géraldine Gouzer

Countries citing papers authored by Margaret M. Stratton

Since Specialization
Citations

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

Fields of papers citing papers by Margaret M. Stratton

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Margaret M. Stratton

This figure shows the co-authorship network connecting the top 25 collaborators of Margaret M. Stratton. A scholar is included among the top collaborators of Margaret M. Stratton 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 Margaret M. Stratton. Margaret M. Stratton 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.
Ma, Xiuquan, David R. Croucher, Elizabeth V. Nguyen, et al.. (2025). Activation of CAMK2 by pseudokinase PEAK1 represents a targetable pathway in triple negative breast cancer. Nature Communications. 16(1). 1871–1871. 3 indexed citations
2.
Yang, Pan, Zishuo Yu, Barbara Ludeke, et al.. (2025). Structural and functional analysis of the Nipah virus polymerase complex. Cell. 188(3). 688–703.e18. 12 indexed citations
3.
Schafer, Johanna M., Marzena Dyba, Sergey G. Tarasov, et al.. (2025). Optimized isolation of enzymatically active ubiquitin E3 ligase E6AP/UBE3A from mammalian cells. Protein Expression and Purification. 228. 106661–106661. 1 indexed citations
4.
Garman, Scott C., et al.. (2024). Ca2+/CaM dependent protein kinase II (CaMKII)α and CaMKIIβ hub domains adopt distinct oligomeric states and stabilities. Protein Science. 33(4). e4960–e4960. 4 indexed citations
5.
Gee, Christine L., Bente Frølund, Margaret M. Stratton, et al.. (2024). Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity. Protein Science. 33(10). e5152–e5152. 1 indexed citations
6.
Russi, Silvia, et al.. (2023). Polymer-based microfluidic device for on-chip counter-diffusive crystallization and in situ X-ray crystallography at room temperature. Lab on a Chip. 23(8). 2075–2090. 13 indexed citations
7.
Sloutsky, Roman, Christl Gaubitz, Edward A. Esposito, et al.. (2022). CaMKII binds both substrates and activators at the active site. Cell Reports. 40(2). 111064–111064. 18 indexed citations
8.
Sloutsky, Roman & Margaret M. Stratton. (2020). Functional implications of CaMKII alternative splicing. European Journal of Neuroscience. 54(8). 6780–6794. 21 indexed citations
9.
Sloutsky, Roman, et al.. (2020). Heterogeneity in human hippocampal CaMKII transcripts reveals allosteric hub-dependent regulation. Science Signaling. 13(641). 28 indexed citations
10.
Esposito, Edward A., et al.. (2020). Characterization of CaMKIIα holoenzyme stability. Protein Science. 29(6). 1524–1534. 19 indexed citations
11.
Saneyoshi, Takeo, Hitomi Matsuno, Akio Suzuki, et al.. (2019). Reciprocal Activation within a Kinase-Effector Complex Underlying Persistence of Structural LTP. Neuron. 102(6). 1199–1210.e6. 79 indexed citations
12.
Ardestani, Goli, et al.. (2019). FRET-based sensor for CaMKII activity (FRESCA): A useful tool for assessing CaMKII activity in response to Ca2+ oscillations in live cells. Journal of Biological Chemistry. 294(31). 11876–11891. 14 indexed citations
13.
Bhattacharyya, Moitrayee, Margaret M. Stratton, Catherine C. Going, et al.. (2016). Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II. eLife. 5. 80 indexed citations
14.
Stratton, Margaret M., Il‐Hyung Lee, Moitrayee Bhattacharyya, et al.. (2014). Correction: Activation-triggered subunit exchange between CaMKII holoenzymes facilitates the spread of kinase activity. eLife. 3. 13 indexed citations
15.
Stratton, Margaret M., Luke H. Chao, Howard Schulman, & John Kuriyan. (2013). Structural studies on the regulation of Ca2+/calmodulin dependent protein kinase II. Current Opinion in Structural Biology. 23(2). 292–301. 68 indexed citations
16.
Chao, Luke H., Margaret M. Stratton, Il‐Hyung Lee, et al.. (2011). A Mechanism for Tunable Autoinhibition in the Structure of a Human Ca2+/Calmodulin- Dependent Kinase II Holoenzyme. Cell. 146(5). 732–745. 194 indexed citations
17.
Stratton, Margaret M. & Stewart N. Loh. (2010). Converting a protein into a switch for biosensing and functional regulation. Protein Science. 20(1). 19–29. 39 indexed citations
18.
Stratton, Margaret M. & Stewart N. Loh. (2010). On the mechanism of protein fold‐switching by a molecular sensor. Proteins Structure Function and Bioinformatics. 78(16). 3260–3269. 18 indexed citations
19.
Stratton, Margaret M., et al.. (2010). Probing local structural fluctuations in myoglobin by size‐dependent thiol‐disulfide exchange. Protein Science. 19(8). 1587–1594. 5 indexed citations
20.
Stratton, Margaret M., Diana M. Mitrea, & Stewart N. Loh. (2008). A Ca2+-Sensing Molecular Switch Based on Alternate Frame Protein Folding. ACS Chemical Biology. 3(11). 723–732. 45 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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