Jennifer Lamb

2.0k total citations
11 papers, 1.4k citations indexed

About

Jennifer Lamb is a scholar working on Cell Biology, Molecular Biology and Biophysics. According to data from OpenAlex, Jennifer Lamb has authored 11 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Cell Biology, 5 papers in Molecular Biology and 4 papers in Biophysics. Recurrent topics in Jennifer Lamb's work include Cellular Mechanics and Interactions (5 papers), Advanced Fluorescence Microscopy Techniques (4 papers) and Force Microscopy Techniques and Applications (2 papers). Jennifer Lamb is often cited by papers focused on Cellular Mechanics and Interactions (5 papers), Advanced Fluorescence Microscopy Techniques (4 papers) and Force Microscopy Techniques and Applications (2 papers). Jennifer Lamb collaborates with scholars based in United States and Denmark. Jennifer Lamb's co-authors include Paul A. Janmey, Søren Hvidt, Thomas P. Stossel, Philip G. Allen, Juan‐José Ventura, Richard A. Flavell, Roger J. Davis, Paul Matsudaira, Patricia Hess and Connie M. Corcoran and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Molecular Cell.

In The Last Decade

Jennifer Lamb

11 papers receiving 1.3k citations

Peers

Jennifer Lamb
Magnus Edlund United States
Mazen Sidani United States
Zhiqi Sun China
Chungho Kim South Korea
Eleanor Kable Australia
Kathryn M. Eisenmann United States
Magnus Edlund United States
Jennifer Lamb
Citations per year, relative to Jennifer Lamb Jennifer Lamb (= 1×) peers Magnus Edlund

Countries citing papers authored by Jennifer Lamb

Since Specialization
Citations

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

Fields of papers citing papers by Jennifer Lamb

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jennifer Lamb

This figure shows the co-authorship network connecting the top 25 collaborators of Jennifer Lamb. A scholar is included among the top collaborators of Jennifer Lamb 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 Jennifer Lamb. Jennifer Lamb is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

11 of 11 papers shown
1.
Godin-Heymann, Nadia, Lindsey Ulkus, Brian W. Brannigan, et al.. (2008). The T790M “gatekeeper” mutation in EGFR mediates resistance to low concentrations of an irreversible EGFR inhibitor. Molecular Cancer Therapeutics. 7(4). 874–879. 163 indexed citations
2.
Bearss, David J., Cory L. Grand, Jennifer Lamb, Maxwell R. Lloyd, & Hariprasad Vankayalapati. (2006). 414 POSTER Discovery and characterization of a small molecule inhibitor for pim-1 kinase. European Journal of Cancer Supplements. 4(12). 127–127. 2 indexed citations
3.
Ventura, Juan‐José, Norman J. Kennedy, Jennifer Lamb, Richard A. Flavell, & Roger J. Davis. (2003). c-Jun NH 2 -Terminal Kinase Is Essential for the Regulation of AP-1 by Tumor Necrosis Factor. Molecular and Cellular Biology. 23(8). 2871–2882. 137 indexed citations
4.
Lamb, Jennifer, Juan‐José Ventura, Patricia Hess, Richard A. Flavell, & Roger J. Davis. (2003). JunD Mediates Survival Signaling by the JNK Signal Transduction Pathway. Molecular Cell. 11(6). 1479–1489. 216 indexed citations
5.
Stappenbeck, Thaddeus S., et al.. (1994). Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks.. Journal of Biological Chemistry. 269(47). 29351–29354. 107 indexed citations
6.
Lamb, Jennifer, et al.. (1993). Selective binding of gelsolin to actin monomers containing ADP. Journal of Biological Chemistry. 268(19). 14202–14207. 34 indexed citations
7.
Lamb, Jennifer, et al.. (1993). Modulation of gelsolin function. Activation at low pH overrides Ca2+ requirement.. Journal of Biological Chemistry. 268(12). 8999–9004. 98 indexed citations
8.
Janmey, Paul A., Jennifer Lamb, Philip G. Allen, & Paul Matsudaira. (1992). Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin.. Journal of Biological Chemistry. 267(17). 11818–11823. 189 indexed citations
9.
Janmey, Paul A., Søren Hvidt, George Oster, et al.. (1990). Effect of ATP on actin filament stiffness. Nature. 347(6288). 95–99. 118 indexed citations
10.
Janmey, Paul A., Søren Hvidt, Jennifer Lamb, & Thomas P. Stossel. (1990). Resemblance of actin-binding protein/actin gels to covalently crosslinked networks. Nature. 345(6270). 89–92. 206 indexed citations
11.
Janmey, Paul A., Søren Hvidt, Joyce Peetermans, et al.. (1988). Viscoelasticity of F-actin and F-actin/gelsolin complexes. Biochemistry. 27(21). 8218–8227. 90 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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