Roberta B. Nowak

1.8k total citations
43 papers, 1.3k citations indexed

About

Roberta B. Nowak is a scholar working on Molecular Biology, Physiology and Pulmonary and Respiratory Medicine. According to data from OpenAlex, Roberta B. Nowak has authored 43 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 19 papers in Physiology and 14 papers in Pulmonary and Respiratory Medicine. Recurrent topics in Roberta B. Nowak's work include Erythrocyte Function and Pathophysiology (19 papers), Blood properties and coagulation (13 papers) and Connexins and lens biology (12 papers). Roberta B. Nowak is often cited by papers focused on Erythrocyte Function and Pathophysiology (19 papers), Blood properties and coagulation (13 papers) and Connexins and lens biology (12 papers). Roberta B. Nowak collaborates with scholars based in United States, United Kingdom and Japan. Roberta B. Nowak's co-authors include Velia M. Fowler, David S. Gokhin, Catherine Cheng, Ryan Littlefield, Caroline R. McKeown, Sawako Yamashiro, Sumiko Kimura, Alyson S. Smith, Ionita Ghiran and Sondip K. Biswas and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nature Communications and The Journal of Cell Biology.

In The Last Decade

Roberta B. Nowak

41 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Roberta B. Nowak United States 24 847 429 308 276 171 43 1.3k
David A. Tumbarello United Kingdom 22 882 1.0× 521 1.2× 140 0.5× 128 0.5× 54 0.3× 33 1.7k
D Drenckhahn Germany 15 697 0.8× 399 0.9× 282 0.9× 126 0.5× 165 1.0× 18 1.5k
Jeffrey A. Spencer United States 14 1.1k 1.3× 213 0.5× 116 0.4× 232 0.8× 164 1.0× 15 1.6k
Vera B. Dugina Russia 24 718 0.8× 711 1.7× 71 0.2× 121 0.4× 135 0.8× 51 1.7k
Yumiko Kano Japan 13 541 0.6× 706 1.6× 108 0.4× 138 0.5× 76 0.4× 20 1.1k
Krishnakumar Kizhatil United States 16 591 0.7× 324 0.8× 326 1.1× 78 0.3× 64 0.4× 22 1.1k
Virginia Haurigot Spain 24 1.3k 1.5× 153 0.4× 438 1.4× 123 0.4× 16 0.1× 35 2.0k
Eugene Tkachenko United States 21 1.0k 1.2× 983 2.3× 130 0.4× 64 0.2× 104 0.6× 25 1.8k
Keisuke Sako Japan 13 846 1.0× 511 1.2× 95 0.3× 131 0.5× 58 0.3× 16 1.4k

Countries citing papers authored by Roberta B. Nowak

Since Specialization
Citations

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

Fields of papers citing papers by Roberta B. Nowak

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Roberta B. Nowak. 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 Roberta B. Nowak. The network helps show where Roberta B. Nowak may publish in the future.

Co-authorship network of co-authors of Roberta B. Nowak

This figure shows the co-authorship network connecting the top 25 collaborators of Roberta B. Nowak. A scholar is included among the top collaborators of Roberta B. Nowak 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 Roberta B. Nowak. Roberta B. Nowak 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.
Gnanapragasam, Merlin Nithya, Peng Jiang, Preeti Patel, et al.. (2025). KLF1 coordinates specialized transcriptional networks required to maintain the integrity of terminal erythropoiesis. Journal of Cell Science. 138(21).
2.
Georges, Romain O., Hugo Sepúlveda, Eric C. Johnson, et al.. (2022). Acute deletion of TET enzymes results in aneuploidy in mouse embryonic stem cells through decreased expression of Khdc3. Nature Communications. 13(1). 6230–6230. 9 indexed citations
3.
Nowak, Roberta B., Haleh Alimohamadi, Kersi Pestonjamasp, Padmini Rangamani, & Velia M. Fowler. (2022). Nanoscale dynamics of actin filaments in the red blood cell membrane skeleton. Molecular Biology of the Cell. 33(3). ar28–ar28. 13 indexed citations
4.
Liang, Raymond, Vijay Menon, Jiajing Qiu, et al.. (2021). Mitochondrial localization and moderated activity are key to murine erythroid enucleation. Blood Advances. 5(10). 2490–2504. 18 indexed citations
5.
Alimohamadi, Haleh, Alyson S. Smith, Roberta B. Nowak, Velia M. Fowler, & Padmini Rangamani. (2020). Non-uniform distribution of myosin-mediated forces governs red blood cell membrane curvature through tension modulation. PLoS Computational Biology. 16(5). e1007890–e1007890. 34 indexed citations
6.
Smith, Alyson S., Roberta B. Nowak, Sitong Zhou, et al.. (2018). Myosin IIA interacts with the spectrin-actin membrane skeleton to control red blood cell membrane curvature and deformability. Proceedings of the National Academy of Sciences. 115(19). E4377–E4385. 85 indexed citations
7.
Cheng, Catherine, et al.. (2018). Tropomyosin 3.5 protects the F-actin networks required for tissue biomechanical properties. Journal of Cell Science. 131(23). 24 indexed citations
8.
Sui, Zhenhua, David S. Gokhin, Roberta B. Nowak, et al.. (2017). Stabilization of F-actin by tropomyosin isoforms regulates the morphology and mechanical behavior of red blood cells. Molecular Biology of the Cell. 28(19). 2531–2542. 14 indexed citations
9.
Cheng, Catherine, Roberta B. Nowak, & Velia M. Fowler. (2016). The lens actin filament cytoskeleton: Diverse structures for complex functions. Experimental Eye Research. 156. 58–71. 54 indexed citations
10.
Gokhin, David S., et al.. (2015). Dynamic actin filaments control the mechanical behavior of the human red blood cell membrane. Molecular Biology of the Cell. 26(9). 1699–1710. 44 indexed citations
11.
Liang, Raymond, Genís Campreciós, Yan Kou, et al.. (2015). A Systems Approach Identifies Essential FOXO3 Functions at Key Steps of Terminal Erythropoiesis. PLoS Genetics. 11(10). e1005526–e1005526. 52 indexed citations
12.
Biswas, Sondip K., Roberta B. Nowak, Velia M. Fowler, & Woo-Kuen Lo. (2013). The Tropomodulin1-Actin Network and CP49 Beaded Filaments Regulate Formation of Undulating Aquaporin Junctions in Mouse Lens Fiber Cells. Investigative Ophthalmology & Visual Science. 54(15). 5734–5734. 1 indexed citations
13.
Sui, Zhenhua, Roberta B. Nowak, Andrea Bacconi, et al.. (2013). Tropomodulin3-null mice are embryonic lethal with anemia due to impaired erythroid terminal differentiation in the fetal liver. Blood. 123(5). 758–767. 43 indexed citations
14.
Yamashiro, Sawako, David S. Gokhin, Sumiko Kimura, Roberta B. Nowak, & Velia M. Fowler. (2012). Tropomodulins: Pointed‐end capping proteins that regulate actin filament architecture in diverse cell types. Cytoskeleton. 69(6). 337–370. 102 indexed citations
15.
Gokhin, David S., Roberta B. Nowak, Albert C. Chen, et al.. (2012). Tmod1 and CP49 Synergize to Control the Fiber Cell Geometry, Transparency, and Mechanical Stiffness of the Mouse Lens. PLoS ONE. 7(11). e48734–e48734. 55 indexed citations
16.
Nowak, Roberta B., et al.. (2011). Tropomodulin3-Null Mice Are Embryonic Lethal with Anemia and Impaired Definitive Erythropoiesis in the Fetal Liver. Blood. 118(21). 1036–1036. 1 indexed citations
17.
Leonard, Michelle, Ping Zhang, Ahmad Cader, et al.. (2010). Modulation of N-cadherin junctions and their role as epicenters of differentiation-specific actin regulation in the developing lens. Developmental Biology. 349(2). 363–377. 33 indexed citations
18.
Nowak, Roberta B., et al.. (2009). A Nebulin Ruler Does Not Dictate Thin Filament Lengths. Biophysical Journal. 96(5). 1856–1865. 73 indexed citations
19.
McKeown, Caroline R., et al.. (2008). Tropomodulin1 Is Required in the Heart but Not the Yolk Sac for Mouse Embryonic Development. Circulation Research. 103(11). 1241–1248. 42 indexed citations
20.
Lee, Soo‐Kyung, Linda W. Jurata, Roberta B. Nowak, et al.. (2005). The LIM domain-only protein LMO4 is required for neural tube closure. Molecular and Cellular Neuroscience. 28(2). 205–214. 50 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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