Elizabeth A. McCormack

2.4k total citations
21 papers, 1.8k citations indexed

About

Elizabeth A. McCormack is a scholar working on Molecular Biology, Materials Chemistry and Plant Science. According to data from OpenAlex, Elizabeth A. McCormack has authored 21 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 6 papers in Materials Chemistry and 3 papers in Plant Science. Recurrent topics in Elizabeth A. McCormack's work include Heat shock proteins research (11 papers), Protein Structure and Dynamics (10 papers) and RNA and protein synthesis mechanisms (9 papers). Elizabeth A. McCormack is often cited by papers focused on Heat shock proteins research (11 papers), Protein Structure and Dynamics (10 papers) and RNA and protein synthesis mechanisms (9 papers). Elizabeth A. McCormack collaborates with scholars based in United Kingdom, Israel and Spain. Elizabeth A. McCormack's co-authors include Janet Braam, Yu-Chang Tsai, Keith R. Willison, Dale B. Wigley, Carien Dekker, Oliver Willhöft, Gillian Hynes, José L. Carrascosa, Óscar Llorca and José Valpuesta and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Elizabeth A. McCormack

21 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Elizabeth A. McCormack United Kingdom 18 1.4k 654 320 188 81 21 1.8k
Fumiaki Yumoto Japan 17 684 0.5× 352 0.5× 146 0.5× 46 0.2× 84 1.0× 40 1.3k
Felix Willmund Germany 20 1.2k 0.8× 226 0.3× 83 0.3× 217 1.2× 88 1.1× 30 1.3k
Philipp Korber Germany 30 2.4k 1.7× 526 0.8× 110 0.3× 183 1.0× 193 2.4× 49 2.6k
Michael F. Dion United States 8 2.2k 1.5× 422 0.6× 77 0.2× 184 1.0× 298 3.7× 10 2.4k
Marilyn D. Yoder United States 13 822 0.6× 530 0.8× 152 0.5× 192 1.0× 111 1.4× 24 1.3k
Yeon‐Gil Kim South Korea 19 986 0.7× 107 0.2× 121 0.4× 338 1.8× 161 2.0× 41 1.3k
Harm Post Netherlands 17 1.0k 0.7× 175 0.3× 89 0.3× 255 1.4× 69 0.9× 32 1.5k
Éva Klement Hungary 23 897 0.6× 392 0.6× 99 0.3× 141 0.8× 69 0.9× 47 1.2k
Keiko Kubota Japan 16 695 0.5× 456 0.7× 98 0.3× 93 0.5× 60 0.7× 36 1.2k
Michiel Meijer Germany 20 1.7k 1.2× 396 0.6× 60 0.2× 354 1.9× 152 1.9× 23 2.0k

Countries citing papers authored by Elizabeth A. McCormack

Since Specialization
Citations

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

Fields of papers citing papers by Elizabeth A. McCormack

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Elizabeth A. McCormack. 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 Elizabeth A. McCormack. The network helps show where Elizabeth A. McCormack may publish in the future.

Co-authorship network of co-authors of Elizabeth A. McCormack

This figure shows the co-authorship network connecting the top 25 collaborators of Elizabeth A. McCormack. A scholar is included among the top collaborators of Elizabeth A. McCormack 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 Elizabeth A. McCormack. Elizabeth A. McCormack 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.
Jalal, Adam S. B., et al.. (2024). Nucleosome flipping drives kinetic proofreading and processivity by SWR1. Nature. 636(8041). 251–257. 4 indexed citations
2.
Jalal, Adam S. B., Eugene Chua, Shijie Wang, et al.. (2024). Stabilization of the hexasome intermediate during histone exchange by yeast SWR1 complex. Molecular Cell. 84(20). 3871–3884.e9. 5 indexed citations
3.
Willhöft, Oliver, Mohamed Ghoneim, Chia‐Liang Lin, et al.. (2018). Structure and dynamics of the yeast SWR1-nucleosome complex. Science. 362(6411). 118 indexed citations
4.
Ayala, Rafael, Oliver Willhöft, Ricardo Aramayo, et al.. (2018). Structure and regulation of the human INO80–nucleosome complex. Nature. 556(7701). 391–395. 131 indexed citations
5.
Willhöft, Oliver, Elizabeth A. McCormack, Ricardo Aramayo, et al.. (2017). Crosstalk within a functional INO80 complex dimer regulates nucleosome sliding. eLife. 6. 20 indexed citations
6.
Lin, Chia‐Liang, et al.. (2017). Functional characterization and architecture of recombinant yeast SWR1 histone exchange complex. Nucleic Acids Research. 45(12). 7249–7260. 22 indexed citations
7.
Willhöft, Oliver, Rohan Bythell‐Douglas, Elizabeth A. McCormack, & Dale B. Wigley. (2016). Synergy and antagonism in regulation of recombinant human INO80 chromatin remodeling complex. Nucleic Acids Research. 44(17). 8179–8188. 25 indexed citations
8.
Matheshwaran, Saravanan, Jochen Wuerges, Daniel Bose, et al.. (2012). Interactions between the nucleosome histone core and Arp8 in the INO80 chromatin remodeling complex. Proceedings of the National Academy of Sciences. 109(51). 20883–20888. 40 indexed citations
9.
Dekker, Carien, S. Mark Roe, Elizabeth A. McCormack, et al.. (2011). The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins. The EMBO Journal. 30(15). 3078–3090. 80 indexed citations
10.
Nadler-Holly, Michal, Elizabeth A. McCormack, Ester Feldmesser, et al.. (2010). Equivalent Mutations in the Eight Subunits of the Chaperonin CCT Produce Dramatically Different Cellular and Gene Expression Phenotypes. Journal of Molecular Biology. 401(3). 532–543. 76 indexed citations
11.
Altschuler, Gabriel, Carien Dekker, Elizabeth A. McCormack, et al.. (2009). A single amino acid residue is responsible for species‐specific incompatibility between CCT and α‐actin. FEBS Letters. 583(4). 782–786. 14 indexed citations
12.
McCormack, Elizabeth A., et al.. (2009). Yeast Phosducin-Like Protein 2 Acts as a Stimulatory Co-Factor for the Folding of Actin by the Chaperonin CCT via a Ternary Complex. Journal of Molecular Biology. 391(1). 192–206. 27 indexed citations
13.
Hynes, Gillian, et al.. (2008). ATP-Induced Allostery in the Eukaryotic Chaperonin CCT Is Abolished by the Mutation G345D in CCT4 that Renders Yeast Temperature-Sensitive for Growth. Journal of Molecular Biology. 377(2). 469–477. 46 indexed citations
14.
Dekker, Carien, Peter C. Stirling, Elizabeth A. McCormack, et al.. (2008). The interaction network of the chaperonin CCT. The EMBO Journal. 27(13). 1827–1839. 170 indexed citations
15.
Pappenberger, Florian, Elizabeth A. McCormack, & Keith R. Willison. (2006). Quantitative Actin Folding Reactions using Yeast CCT Purified via an Internal Tag in the CCT3/γ Subunit. Journal of Molecular Biology. 360(2). 484–496. 56 indexed citations
16.
McCormack, Elizabeth A., Yu-Chang Tsai, & Janet Braam. (2005). Handling calcium signaling: Arabidopsis CaMs and CMLs. Trends in Plant Science. 10(8). 383–389. 415 indexed citations
17.
McCormack, Elizabeth A. & Janet Braam. (2003). Calmodulins and related potential calcium sensors of Arabidopsis. New Phytologist. 159(3). 585–598. 265 indexed citations
18.
McCormack, Elizabeth A., et al.. (2001). Mutational Screen Identifies Critical Amino Acid Residues of β-Actin Mediating Interaction between Its Folding Intermediates and Eukaryotic Cytosolic Chaperonin CCT. Journal of Structural Biology. 135(2). 185–197. 36 indexed citations
19.
McCormack, Elizabeth A., Óscar Llorca, José L. Carrascosa, José Valpuesta, & Keith R. Willison. (2001). Point Mutations in a Hinge Linking the Small and Large Domains of β-Actin Result in Trapped Folding Intermediates Bound to Cytosolic Chaperonin CCT. Journal of Structural Biology. 135(2). 198–204. 28 indexed citations
20.
Llorca, Óscar, Elizabeth A. McCormack, Gillian Hynes, et al.. (1999). Eukaryotic type II chaperonin CCT interacts with actin through specific subunits. Nature. 402(6762). 693–696. 228 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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