Tina Izard

6.8k total citations · 2 hit papers
75 papers, 4.5k citations indexed

About

Tina Izard is a scholar working on Molecular Biology, Cell Biology and Immunology and Allergy. According to data from OpenAlex, Tina Izard has authored 75 papers receiving a total of 4.5k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 35 papers in Cell Biology and 13 papers in Immunology and Allergy. Recurrent topics in Tina Izard's work include Cellular Mechanics and Interactions (28 papers), Cell Adhesion Molecules Research (13 papers) and Enzyme Structure and Function (10 papers). Tina Izard is often cited by papers focused on Cellular Mechanics and Interactions (28 papers), Cell Adhesion Molecules Research (13 papers) and Enzyme Structure and Function (10 papers). Tina Izard collaborates with scholars based in United States, France and United Kingdom. Tina Izard's co-authors include Erumbi S. Rangarajan, Marina Candido Primi, Michalina Janiszewska, Philippe R.J. Bois, David T. Brown, Clemens Vonrhein, Robert A. Borgon, G. Bricogne, Michael C. Lawrence and Guy Tran Van Nhieu and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Tina Izard

75 papers receiving 4.5k citations

Hit Papers

SARS-CoV-2 spike-protein D614G mutation increases virion ... 2020 2026 2022 2024 2020 2020 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tina Izard United States 34 2.2k 1.2k 714 522 454 75 4.5k
Virgil L. Woods United States 50 3.7k 1.7× 659 0.6× 646 0.9× 351 0.7× 441 1.0× 121 6.5k
Stefan T. Arold Saudi Arabia 42 3.2k 1.4× 660 0.6× 634 0.9× 394 0.8× 442 1.0× 172 5.8k
Isabelle Maridonneau‐Parini France 49 2.4k 1.1× 1.3k 1.1× 937 1.3× 786 1.5× 664 1.5× 123 6.6k
Penelope E. Stein United Kingdom 27 2.2k 1.0× 620 0.5× 238 0.3× 367 0.7× 220 0.5× 48 4.5k
Deborah Fass Israel 39 3.8k 1.7× 1.5k 1.3× 1.0k 1.4× 261 0.5× 71 0.2× 84 6.8k
Robert Karlsson Sweden 31 4.2k 1.9× 338 0.3× 202 0.3× 325 0.6× 265 0.6× 65 6.1k
Robert Esnouf United Kingdom 34 3.8k 1.7× 491 0.4× 2.0k 2.8× 496 1.0× 219 0.5× 76 6.7k
Hideharu Ishida Japan 48 6.2k 2.8× 1.1k 1.0× 286 0.4× 386 0.7× 462 1.0× 376 8.2k
Raymond J. Owens United Kingdom 46 3.8k 1.7× 364 0.3× 699 1.0× 489 0.9× 352 0.8× 177 6.3k
Bo Åkerström Sweden 36 2.1k 0.9× 698 0.6× 375 0.5× 168 0.3× 159 0.4× 119 4.5k

Countries citing papers authored by Tina Izard

Since Specialization
Citations

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

Fields of papers citing papers by Tina Izard

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Tina Izard. 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 Tina Izard. The network helps show where Tina Izard may publish in the future.

Co-authorship network of co-authors of Tina Izard

This figure shows the co-authorship network connecting the top 25 collaborators of Tina Izard. A scholar is included among the top collaborators of Tina Izard 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 Tina Izard. Tina Izard 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.
Izard, Tina. (2025). Environmental Toxicants and Their Disruption of Integrin Signaling in Lipid Rafts. BioEssays. 47(5). e202400276–e202400276. 3 indexed citations
2.
Nwachukwu, J.C., Yingwei Hou, Jian Min, et al.. (2024). Asymmetric allostery in estrogen receptor-α homodimers drives responses to the ensemble of estrogens in the hormonal milieu. Proceedings of the National Academy of Sciences. 121(24). e2321344121–e2321344121. 4 indexed citations
3.
Rangarajan, Erumbi S., et al.. (2024). High-resolution snapshots of the talin auto-inhibitory states suggest roles in cell adhesion and signaling. Nature Communications. 15(1). 9270–9270. 3 indexed citations
4.
Rangarajan, Erumbi S., et al.. (2023). Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments. Communications Biology. 6(1). 276–276. 3 indexed citations
5.
Gupta, Jyoti, Erumbi S. Rangarajan, Regina B. Troyanovsky, et al.. (2023). Plakophilin-3 Binds the Membrane and Filamentous Actin without Bundling F-Actin. International Journal of Molecular Sciences. 24(11). 9458–9458. 1 indexed citations
6.
Patil, Dipak N., Shikha Singh, Timothy S. Strutzenberg, et al.. (2022). Cryo-EM structure of human GPR158 receptor coupled to the RGS7-Gβ5 signaling complex. Science. 375(6576). 86–91. 37 indexed citations
7.
Primi, Marina Candido, Erumbi S. Rangarajan, Dipak N. Patil, & Tina Izard. (2021). Conformational flexibility determines the Nf2/merlin tumor suppressor functions. SHILAP Revista de lepidopterología. 12. 100074–100074. 9 indexed citations
8.
Janiszewska, Michalina, Marina Candido Primi, & Tina Izard. (2020). Cell adhesion in cancer: Beyond the migration of single cells. Journal of Biological Chemistry. 295(8). 2495–2505. 418 indexed citations breakdown →
9.
Rangarajan, Erumbi S., Marina Candido Primi, Lesley A. Colgan, et al.. (2020). A distinct talin2 structure directs isoform specificity in cell adhesion. Journal of Biological Chemistry. 295(37). 12885–12899. 12 indexed citations
10.
Zhang, Lizhou, Cody B. Jackson, Huihui Mou, et al.. (2020). SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity. Nature Communications. 11(1). 6013–6013. 662 indexed citations breakdown →
11.
Bou‐Nader, Charles, Nathalie Carayol, Nicole Quenech’Du, et al.. (2019). Shigella IpaA Binding to Talin Stimulates Filopodial Capture and Cell Adhesion. Cell Reports. 26(4). 921–932.e6. 14 indexed citations
12.
Rangarajan, Erumbi S. & Tina Izard. (2013). Dimer asymmetry defines α-catenin interactions. Nature Structural & Molecular Biology. 20(2). 188–193. 92 indexed citations
13.
Yogesha, S.D., Erumbi S. Rangarajan, Clemens Vonrhein, G. Bricogne, & Tina Izard. (2012). Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin. Protein Science. 21(4). 583–588. 11 indexed citations
14.
Rangarajan, Erumbi S., Jun Hyuck Lee, S.D. Yogesha, & Tina Izard. (2010). A Helix Replacement Mechanism Directs Metavinculin Functions. PLoS ONE. 5(5). e10679–e10679. 30 indexed citations
15.
Ramarao, Nalini, Christophe Le Clainche, Tina Izard, et al.. (2007). Capping of actin filaments by vinculin activated by the Shigella IpaA carboxyl‐terminal domain. FEBS Letters. 581(5). 853–857. 36 indexed citations
16.
Bois, Philippe R.J., Brendan P. O’Hara, Daniel Nietlispach, John Kirkpatrick, & Tina Izard. (2006). The Vinculin Binding Sites of Talin and α-Actinin Are Sufficient to Activate Vinculin. Journal of Biological Chemistry. 281(11). 7228–7236. 109 indexed citations
17.
Izard, Tina & Clemens Vonrhein. (2004). Structural Basis for Amplifying Vinculin Activation by Talin. Journal of Biological Chemistry. 279(26). 27667–27678. 86 indexed citations
19.
Izard, Tina, Arie Geerlof, Ann Lewendon, & John J. Barker. (1999). Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli. Acta Crystallographica Section D Biological Crystallography. 55(6). 1226–1228. 9 indexed citations
20.
Cullis, Paul M., et al.. (1999). Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli. Acta Crystallographica Section D Biological Crystallography. 55(7). 1368–1369. 3 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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